Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O52552
|
RIFK_AMYMS
|
MNARKAPEFPAWPQYDDAERNGLVRALEQGQWWRMGGDEVNSFEREFAAHHGAAHALAVTNGTHALELALQVMGVGPGTEVIVPAFTFISSSQAAQRLGAVTVPVDVDAATYNLDPEAVAAAVTPRTKVIMPVHMAGLMADMDALAKISADTGVPLLQDAAHAHGARWQGKRVGELDSIATFSFQNGKLMTAGEGGAVVFPDGETEKYETAFLRHSCGRPRDDRRYFHKIAGSNMRLNEFSASVLRAQLARLDEQIAVRDERWTLLSRLLGAIDGVVPQGGDVRADRNSHYMAMFRIPGLTEERRNALVDRLVEAGLPAFAAFRAIYRTDAFWELGAPDESVDAIARRCPNTDAISSDCVWLHHRVLLAGEPELHATAEIIADAVARA
|
2.6.1.-; 4.2.1.144
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10433690, ECO:0000269|PubMed:9497318}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:10433690, ECO:0000269|PubMed:9497318};
|
antibiotic biosynthetic process [GO:0017000]; polysaccharide biosynthetic process [GO:0000271]
| null |
dTDP-4-amino-4,6-dideoxygalactose transaminase activity [GO:0019180]; lyase activity [GO:0016829]; pyridoxal phosphate binding [GO:0030170]
|
PF01041;
|
3.90.1150.10;3.40.640.10;
|
DegT/dnrJ/eryC1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=5-deoxy-5-amino-3-dehydroshikimate = 3-amino-5-hydroxybenzoate + H(+) + H2O; Xref=Rhea:RHEA:35771, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71959, ChEBI:CHEBI:71963; EC=4.2.1.144; Evidence={ECO:0000269|PubMed:21081954, ECO:0000269|PubMed:9497318}; CATALYTIC ACTIVITY: Reaction=L-glutamine + UDP-3-oxo-alpha-D-glucose = 2-oxoglutaramate + UDP-alpha-D-kanosamine; Xref=Rhea:RHEA:35775, ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:71964, ChEBI:CHEBI:71965; Evidence={ECO:0000305|PubMed:21081954};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.164 mM for 5-amino-5-deoxy-3-dehydroshikimate {ECO:0000269|PubMed:9497318}; KM=0.122 mM for 5-amino-5-deoxy-3-dehydroshikimate {ECO:0000269|PubMed:21081954}; Note=kcat is 6.82 sec(-1) for AHBA synthase activity. {ECO:0000269|PubMed:21081954};
|
PATHWAY: Antibiotic biosynthesis; rifamycin B biosynthesis. {ECO:0000269|PubMed:21081954}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 for AHBA synthase activity. Retains its activity over a broad range of pH. Over 84% of the maximum activity of AHBA synthase is maintained over a pH range from 7.0 to 9.0. {ECO:0000269|PubMed:9497318};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 33 degrees Celsius for AHBA synthase activity. Retains its activity over a broad range of temperature. Over 84% of the maximum activity of AHBA synthase is maintained over a temperature range from 28 to 50 degrees Celsius. {ECO:0000269|PubMed:9497318};
|
FUNCTION: Catalyzes the dehydration and aromatization of 5-amino-5-deoxy-3-dehydroshikimate (aminoDHS) to 3-amino-5-hydroxybenzoate (AHBA), a compound that then serves as the starter unit for the assembly of a polyketide during the biosynthesis of rifamycin B and other ansamycin antibiotics. Cannot utilize 5-deoxy-5-amino-3-dehydroquinate (aminoDHQ), 5-deoxy-5-aminoshikimate (aminoSA), quinate, 3-dehydroquinate, or 3-dehydroshikimate (DHS) as substrate. {ECO:0000269|PubMed:21081954, ECO:0000269|PubMed:9497318}.; FUNCTION: In a complex with RifL, RifK may have a second function in the AHBA pathway, acting as a transaminase introducing the nitrogen into the first pathway intermediate, UDP-3-keto-D-glucose, to give UDP-kanosamine. Appears to use glutamine as the nitrogen donor; NH(4)(+) or asparagine are 30% less effective as nitrogen donors and neither glutamate nor aspartate show activity. {ECO:0000269|PubMed:21081954}.
|
Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei)
|
O52582
|
CDR_STAA8
|
MPKIVVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRRYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVSVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLNERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEINAINGNEITFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGFLGNNIVKFFDYTFASVGVKPNELKQFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRQILRAAAVGKEGADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK
|
1.8.1.14
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16981688}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:16981688};
| null | null |
CoA-disulfide reductase (NADP) activity [GO:0050451]; flavin adenine dinucleotide binding [GO:0050660]; NADP binding [GO:0050661]; protein disulfide isomerase activity [GO:0003756]
|
PF07992;PF02852;
|
3.30.390.30;3.50.50.60;
|
Class-III pyridine nucleotide-disulfide oxidoreductase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:14705, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62209; EC=1.8.1.14;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for NADPH; KM=11 uM for CoA disulfide; KM=140 uM for 3'-dephospho-CoA disulfide; KM=80 uM for 4,4'-diphosphopantethine; KM=1100 uM for CoA glutathione mixed disulfide;
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.0.;
| null |
FUNCTION: Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. Is also active with other disulfide substrates containing at least one 4'-phosphopantethienyl moiety such as 4,4'-diphosphopantethine, but is not able to reduce oxidized glutathione, cystine, pantethine, or H(2)O(2).
|
Staphylococcus aureus (strain NCTC 8325 / PS 47)
|
O52623
|
SOPE_SALTM
|
MTKITLSPQNFRIQKQETTLLKEKSTEKNSLAKSILAVKNHFIELRSKLSERFISHKNTESSATHFHRGSASEGRAVLTNKVVKDFMLQTLNDIDIRGSASKDPAYASQTREAILSAVYSKNKDQCCNLLISKGINIAPFLQEIGEAAKNAGLPGTTKNDVFTPSGAGANPFITPLISSANSKYPRMFINQHQQASFKIYAEKIIMTEVAPLFNECAMPTPQQFQLILENIANKYIQNTP
| null | null |
actin cytoskeleton organization [GO:0030036]
|
extracellular region [GO:0005576]
|
GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF05364;PF07487;
|
1.10.4120.10;
|
GEF (guanine exchange factor) SopE family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9482928}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS).
| null | null | null | null | null |
FUNCTION: Activator for both CDC42 and RAC1 by directly engaging these Rho GTPases and acting as potent guanine nucleotide exchange factor (GEF). This activation results in actin cytoskeleton rearrangements and stimulates membrane ruffling, promoting bacterial entry into non-phagocytic cells. Also activates MAPK8, indicating that it is capable of stimulating signaling pathways that can lead to nuclear responses. Chaperone InvB is required for secretion and translocation of SopE. {ECO:0000269|PubMed:11440999, ECO:0000269|PubMed:31285585, ECO:0000269|PubMed:9630225}.
|
Salmonella typhimurium
|
O52646
|
DNRD_STRGJ
|
MSEQIAAVRRMVEAYNTGKTDDVADYIHPEYMNPGTLEFTSLRGPELFAINVAWVKKTFSEEARLEEVGIEERADWVRARLVLYGRHVGEMVGMAPTGRLFSGEQIHLLHFVDGKIHHHRDWPDYQGTYRQLGEPWPETEHRRP
|
5.5.1.23
| null |
antibiotic biosynthetic process [GO:0017000]; daunorubicin biosynthetic process [GO:1901771]; doxorubicin metabolic process [GO:0044598]
| null |
intramolecular lyase activity [GO:0016872]
|
PF07366;
|
3.10.450.50;
|
Polyketide cyclase DnrD family
| null | null |
CATALYTIC ACTIVITY: Reaction=methyl aklanonate = aklaviketone; Xref=Rhea:RHEA:37879, ChEBI:CHEBI:77988, ChEBI:CHEBI:77994; EC=5.5.1.23;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for nogalonic acid methyl ester {ECO:0000269|PubMed:16414075}; Note=kcat is 1 sec(-1) for cyclization with nogalonic acid methyl ester.;
|
PATHWAY: Antibiotic biosynthesis; daunorubicin biosynthesis.; PATHWAY: Antibiotic biosynthesis; carminomycin biosynthesis.; PATHWAY: Antibiotic biosynthesis; rhodomycin biosynthesis.; PATHWAY: Antibiotic biosynthesis; aclacinomycin biosynthesis.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:16414075};
| null |
FUNCTION: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the cyclization of aklanonic acid methyl ester to yield aklaviketone. It is also able to use nogalonic acid methyl ester as substrate, but produces exclusively auraviketone with C9-R stereochemistry. {ECO:0000269|PubMed:10658662, ECO:0000269|PubMed:16414075}.
|
Streptomyces galilaeus
|
O52681
|
HYDC_THEMA
|
MERHFEKVEEILKKYGYKRENLIKILLEIQEIYRYLPEDVINYVSTAMGIPPAKIYGVATFYAQFSLKPKGKYTIMVCDGTACHMAGSPEVLKAIEEETGLTPGNVTEDLMFSLDQVGCLGACALAPVMVINGEVYGNLTADKVKEILRKIKEKERESANV
|
1.12.1.4
|
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:27396836}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:Q56221};
| null |
cytoplasm [GO:0005737]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]
|
PF01257;
|
3.40.30.10;1.10.10.1590;
|
Complex I 24 kDa subunit family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19411328}.
|
CATALYTIC ACTIVITY: Reaction=2 H2 + NAD(+) + 2 oxidized [2Fe-2S]-[ferredoxin] = 3 H(+) + NADH + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30279, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.12.1.4; Evidence={ECO:0000269|PubMed:19411328}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30281; Evidence={ECO:0000269|PubMed:19411328};
| null | null | null | null |
FUNCTION: Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2) (PubMed:19411328). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2) (PubMed:19411328). The gamma subunit might be the site where reduced ferredoxin is oxidized (PubMed:19411328). {ECO:0000269|PubMed:19411328}.
|
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
|
O52793
|
EVAA_AMYOR
|
MSSFVVPSLTAVRPRDHHDYADRIALSAATTDGVQMRTEDVRAWIAERRDANVFHVERIPFADLDQWWFEGVTGNLVHRSGRFFTIEGLHVIEHDGPHGDGPYREWQQPVIRQPEVGILGILAKEFDGVLHFLMQAKMEPGNPNLVQLSPTVQATRSNYTKAHGGTNVKLIEYFAPPDPERVIVDVLQAEQGSWFFRKSNRNMIVETVDDVPLWDDFCWLTLGQIAELMHEDETINMNSRSVLSCLPYQDITPRALFSDVQLLSWFTNERSRHDVRVRRIPLADVCGWKQGAEEIEHEDGRYFKVLAVAVKGSNREKISWTQPLVESVDLGVVAFLVRKIDGVPHVLVQARVDGGFLDTVELAPTVQCTPLNYAHLPAEERPPFLDLVQNAPRSRIRYEAIHSEEGGRFLGVRARYLVIDADEAIDPPPGYAWVTPAQLTALTRHGHYVNVEARTLLACINAAAAQPRGGA
|
4.2.1.159
| null |
antibiotic biosynthetic process [GO:0017000]
| null |
lyase activity [GO:0016829]
|
PF03559;
|
3.90.79.40;
|
Hexose 2,3-dehydratase family
| null | null |
CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:47972, ChEBI:CHEBI:15377, ChEBI:CHEBI:57649, ChEBI:CHEBI:84540; EC=4.2.1.159; Evidence={ECO:0000269|PubMed:11035791, ECO:0000269|PubMed:23473392};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=56 uM for dTDP-glucose {ECO:0000269|PubMed:23473392}; Vmax=4 umol/min/mg enzyme for dTDP-glucose {ECO:0000269|PubMed:23473392};
|
PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:11035791}.
| null | null |
FUNCTION: Involved in the biosynthesis of the 2,3,6-trideoxysugar L-epivancosamine, the terminal sugar added to the aglycone scaffold of chloroeremomycin, a member of the glycopeptide antibiotics vancomycin family. Catalyzes the removal of the hydroxyl group at position C-2 of the hexose ring of dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose, and the oxidation of the hydroxyl group at position C-3 to form a carbonyl functionality. The product of the reaction, dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose, is a highly unstable diketosugar, which spontaneously forms dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose. {ECO:0000269|PubMed:11035791, ECO:0000269|PubMed:23473392}.
|
Amycolatopsis orientalis (Nocardia orientalis)
|
O52958
|
KPRS_THEKO
|
MFLLGSGGKHFEDELRNAGAKILEVEIKRFPDGEKYVRVMGNGDEATVVSSTFYPQDEKIVELLLLGDALREKGFEKLKLVVPYFAYSRQDRVTKDGEPISVRAVMRALGIYYEELYIFDTHNPETLRFFPGKAVNVSPARVIGEYFREKLGDGLVLAPDKGALERARAVAEVLGLEYSHFEKRRISPTEVEMHPVDVDVKGKNVLIVDDIISTGGTMVRAAELLRKLGAKKIYVSATHGVFAEGAIERVSRAVDELAVTNTIPTPVSRISIVPELLKLE
|
2.7.6.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00583}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00583};
|
5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; phosphorylation [GO:0016310]; purine nucleotide biosynthetic process [GO:0006164]; ribonucleoside monophosphate biosynthetic process [GO:0009156]
|
cytoplasm [GO:0005737]; ribose phosphate diphosphokinase complex [GO:0002189]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; ribose phosphate diphosphokinase activity [GO:0004749]
|
PF14572;PF13793;
|
3.40.50.2020;
|
Ribose-phosphate pyrophosphokinase family, Class III (archaeal) subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
|
CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|Ref.1};
| null |
PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00583}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|Ref.1};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Half-life of the enzyme activity is 55 minutes at 70 degrees Celsius. {ECO:0000269|Ref.1};
|
FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). It can also use CTP and GTP as substrates in addition to ATP. {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|Ref.1}.
|
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
|
O53166
|
ACNA_MYCTU
|
MTSKSVNSFGAHDTLKVGEKSYQIYRLDAVPNTAKLPYSLKVLAENLLRNEDGSNITKDHIEAIANWDPKAEPSIEIQYTPARVVMQDFTGVPCIVDLATMREAIADLGGNPDKVNPLAPADLVIDHSVIADLFGRADAFERNVEIEYQRNGERYQFLRWGQGAFDDFKVVPPGTGIVHQVNIEYLASVVMTRDGVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFRLTGEIQPGVTATDVVLTVTEMLRQHGVVGKFVEFYGEGVAEVPLANRATLGNMSPEFGSTAAIFPIDEETIKYLRFTGRTPEQVALVEAYAKAQGMWHDPKHEPEFSEYLELNLSDVVPSIAGPKRPQDRIALAQAKSTFREQIYHYVGNGSPDSPHDPHSKLDEVVEETFPASDPGQLTFANDDVATDETVHSAAAHADGRVSNPVRVKSDELGEFVLDHGAVVIAAITSCTNTSNPEVMLGAALLARNAVEKGLTSKPWVKTTIAPGSQVVNDYYDRSGLWPYLEKLGFYLVGYGCTTCIGNSGPLPEEISKAVNDNDLSVTAVLSGNRNFEGRINPDVKMNYLASPPLVIAYALAGTMDFDFQTQPLGQDKDGKNVFLRDIWPSQQDVSDTIAAAINQEMFTRNYADVFKGDDRWRNLPTPSGNTFEWDPNSTYVRKPPYFEGMTAKPEPVGNISGARVLALLGDSVTTDHISPAGAIKPGTPAARYLDEHGVDRKDYNSFGSRRGNHEVMIRGTFANIRLRNQLLDDVSGGYTRDFTQPGGPQAFIYDAAQNYAAQHIPLVVFGGKEYGSGSSRDWAAKGTLLLGVRAVIAESFERIHRSNLIGMGVIPLQFPEGKSASSLGLDGTEVFDITGIDVLNDGKTPKTVCVQATKGDGATIEFDAVVRIDTPGEADYYRNGGILQYVLRNILKSG
|
4.2.1.3; 4.2.1.99
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P09339}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P09339};
|
citrate metabolic process [GO:0006101]; propionate metabolic process, methylcitrate cycle [GO:0019679]; response to iron ion [GO:0010039]; tricarboxylic acid cycle [GO:0006099]
|
cytosol [GO:0005829]; extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
2-methylisocitrate dehydratase activity [GO:0047456]; 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; iron-responsive element binding [GO:0030350]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]
|
PF00330;PF00694;
|
6.10.190.10;3.30.499.10;3.20.19.10;
|
Aconitase/IPM isomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000269|PubMed:17384188}; CATALYTIC ACTIVITY: Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377, ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99; Evidence={ECO:0000250|UniProtKB:Q8ZP52};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.56 mM for isocitrate {ECO:0000269|PubMed:17384188}; Vmax=33.3 umol/min/mg enzyme with isocitrate as substrate {ECO:0000269|PubMed:17384188};
|
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. {ECO:0000305|PubMed:17384188}.; PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000305|PubMed:17384188}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. It retains a high specific activity over a broad pH range. {ECO:0000269|PubMed:17384188};
| null |
FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein which binds to selected IRE-like sequences present within the UTRs (untranslated regions) of 3' trxC and 5' IdeR mRNA (PubMed:17384188). Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate (By similarity). {ECO:0000250|UniProtKB:Q8ZP52, ECO:0000269|PubMed:17384188}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53168
|
RIPA_MYCTU
|
MRRNRRGSPARPAARFVRPAIPSALSVALLVCTPGLATADPQTDTIAALIADVAKANQRLQDLSDEVQAEQESVNKAMVDVETARDNAAAAEDDLEVSQRAVKDANAAIAAAQHRFDTFAAATYMNGPSVSYLSASSPDEIIATVTAAKTLSASSQAVMANLQRARTERVNTESAARLAKQKADKAAADAKASQDAAVAALTETRRKFDEQREEVQRLAAERDAAQARLQAARLVAWSSEGGQGAPPFRMWDPGSGPAGGRAWDGLWDPTLPMIPSANIPGDPIAVVNQVLGISATSAQVTANMGRKFLEQLGILQPTDTGITNAPAGSAQGRIPRVYGRQASEYVIRRGMSQIGVPYSWGGGNAAGPSKGIDSGAGTVGFDCSGLVLYSFAGVGIKLPHYSGSQYNLGRKIPSSQMRRGDVIFYGPNGSQHVTIYLGNGQMLEAPDVGLKVRVAPVRTAGMTPYVVRYIEY
|
3.4.-.-
| null |
cell wall organization [GO:0071555]; cell wall organization or biogenesis [GO:0071554]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]
|
cysteine-type peptidase activity [GO:0008234]; N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]
|
PF00877;
|
6.10.250.3150;3.90.1720.10;
|
Peptidase C40 family
|
PTM: Exported by the Tat system (PubMed:26933057). The position of the signal peptide cleavage has not been experimentally proven (PubMed:26933057). {ECO:0000269|PubMed:26933057}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17919286, ECO:0000269|PubMed:26933057}. Note=Secreted by the TAT secretion pathway (PubMed:26933057). Localizes to the septa upon expression in M.bovis or M.smegmatis. Remains associated with the cell. {ECO:0000269|PubMed:26933057}.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5 and 5.5.;
| null |
FUNCTION: Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages. {ECO:0000269|PubMed:16495549, ECO:0000269|PubMed:17919286, ECO:0000269|PubMed:18463693, ECO:0000269|PubMed:20826344, ECO:0000269|PubMed:21864539}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53177
|
RPFE_MYCTU
|
MKNARTTLIAAAIAGTLVTTSPAGIANADDAGLDPNAAAGPDAVGFDPNLPPAPDAAPVDTPPAPEDAGFDPNLPPPLAPDFLSPPAEEAPPVPVAYSVNWDAIAQCESGGNWSINTGNGYYGGLRFTAGTWRANGGSGSAANASREEQIRVAENVLRSQGIRAWPVCGRRG
|
3.-.-.-
| null |
negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; quorum sensing [GO:0009372]; regulation of cell population proliferation [GO:0042127]
|
extracellular region [GO:0005576]
|
hydrolase activity [GO:0016787]
|
PF06737;
|
1.10.530.10;
|
Transglycosylase family, Rpf subfamily
| null | null | null | null | null | null | null |
FUNCTION: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity. {ECO:0000269|PubMed:12410821}.; FUNCTION: Stimulates growth of stationary phase M.bovis (a slow-growing Mycobacterium), reduces the lag phase of diluted fast-growers M.smegmatis and Micrococcus luteus. Sequential gene disruption indicates RpfB and RpfE are higher than RpfD and RpfC in functional hierarchy. {ECO:0000269|PubMed:12410821}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53181
|
KORB_MYCTU
|
MTRSGDEAQLMTGVTGDLAGTELGLTPSLTKNAGVPTTDQPQKGKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRRENIVFISGIGCSSRFPYYLETYGFHSIHGRAPAIATGLALAREDLSVWVVTGDGDALSIGGNHLIHALRRNINVTILLFNNRIYGLTKGQYSPTSEVGKVTKSTPMGSLDHPFNPVSLALGAEATFVGRALDSDRNGLTEVLRAAAQHRGAALVEILQDCPIFNDGSFDALRKEGAEERVIKVRHGEPIVFGANGEYCVVKSGFGLEVAKTADVAIDEIIVHDAQVDDPAYAFALSRLSDQNLDHTVLGIFRHISRPTYDDAARSQVVAARNAAPSGTAALQSLLHGRDTWTVD
|
1.2.7.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19936047};
|
tricarboxylic acid cycle [GO:0006099]
|
cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]
|
2-oxoglutarate synthase activity [GO:0047553]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976]
|
PF02775;
|
3.40.50.970;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] + succinyl-CoA; Xref=Rhea:RHEA:17297, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=1.2.7.3; Evidence={ECO:0000269|PubMed:19936047};
| null |
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. {ECO:0000269|PubMed:19936047}.
| null | null |
FUNCTION: Component of KG oxidoreductase (KOR) that catalyzes the CoA-dependent oxidative decarboxylation of 2-oxoglutarate (alpha-ketoglutarate, KG) to succinyl-CoA. Methyl viologen can act as electron acceptor in vitro; the physiologic electron acceptor is unknown. Is involved in the alternative TCA pathway that functions concurrently with fatty acid beta-oxidation. Since a growing body of evidence indicates that lipids (for example cholesterol and fatty acids) are a predominant growth substrate for M.tuberculosis during infection, flux through KOR likely represents an important step in intermediary metabolism in vivo. KOR-dependent decarboxylation of KG also appears to be an important source of CO(2) in M.tuberculosis metabolism. {ECO:0000269|PubMed:19936047}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53223
|
LDT2_MYCTO
|
MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRTDVDWATQISYSGVFVHSAPWSVGAQGHTNTSHGCLNVSPSNAQWFYDHVKRGDIVEVVNTVGGTLPGIDGLGDWNIPWDQWRAGNAKA
|
2.3.2.-
| null |
cell wall organization [GO:0071555]; peptidoglycan metabolic process [GO:0000270]; peptidoglycan-based cell wall biogenesis [GO:0009273]; peptidoglycan-protein cross-linking [GO:0018104]; regulation of cell shape [GO:0008360]
|
extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
acyltransferase activity [GO:0016746]; metal ion binding [GO:0046872]; peptidoglycan L,D-transpeptidase activity [GO:0071972]
|
PF17964;PF03734;
|
2.60.40.3710;2.60.40.3780;2.40.440.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
| null | null |
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
| null | null |
FUNCTION: Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems. Is essential for virulence in a mouse model of acute infection. {ECO:0000269|PubMed:20305661}.
|
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
|
O53289
|
SERB2_MYCTU
|
MPAKVSVLITVTGMDQPGVTSALFEVLAQHGVELLNVEQVVIRGRLTLGVLVSCPLDVADGTALRDDVAAAIHGVGLDVAIERSDDLPIIRQPSTHTIFVLGRPITAGAFSAVARGVAALGVNIDFIRGISDYPVTGLELRVSVPPGCVGPLQIALTKVAAEEHVDVAVEDYGLAWRTKRLIVFDVDSTLVQGEVIEMLAARAGAQGQVAAITEAAMRGELDFAESLQRRVATLAGLPATVIDDVAEQLELMPGARTTIRTLRRLGFRCGVVSGGFRRIIEPLARELMLDFVASNELEIVDGILTGRVVGPIVDRPGKAKALRDFASQYGVPMEQTVAVGDGANDIDMLGAAGLGIAFNAKPALREVADASLSHPYLDTVLFLLGVTRGEIEAADAGDCGVRRVEIPAD
|
3.1.3.16; 3.1.3.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}; Note=Binds 1 Mg(2+) ion per subunit (By similarity). Can also use Mn(2+) (PubMed:25037224, PubMed:25521849). {ECO:0000250|UniProtKB:Q58989, ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849};
|
dephosphorylation [GO:0016311]; L-serine biosynthetic process [GO:0006564]; protein dephosphorylation [GO:0006470]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell cytosol [GO:0044164]
|
amino acid binding [GO:0016597]; L-phosphoserine phosphatase activity [GO:0036424]; magnesium ion binding [GO:0000287]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF13740;PF21086;PF12710;
|
3.30.70.260;3.40.50.1000;
|
HAD-like hydrolase superfamily, SerB family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26984196}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:26984196}. Note=Is secreted into the cytosol of infected macrophages and is found in bronchoalveolar lavage samples of tuberculosis patients. Co-localizes with host tubulin. {ECO:0000269|PubMed:26984196}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-serine = L-serine + phosphate; Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3; Evidence={ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-D-serine = D-serine + phosphate; Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247, ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3; Evidence={ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:26984196}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:26984196};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92.68 uM for O-phospho-L-serine {ECO:0000269|PubMed:25037224}; KM=135.9 uM for O-phospho-L-serine {ECO:0000269|PubMed:25521849}; Vmax=14250 nmol/min/mg enzyme {ECO:0000269|PubMed:25521849}; Note=kcat is 8.83 min(-1) (PubMed:25037224). kcat is 25400 sec(-1) (PubMed:25521849). {ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849};
|
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3. {ECO:0000305|PubMed:25037224}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 (PubMed:25037224, PubMed:25521849). Activity declines progressively before pH 7.5 and is almost abolished at 6.0 while at higher pH the enzyme remains active till pH 9.0 (PubMed:25521849). {ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Activity declines at higher temperatures and is completely abolished by 50 degrees Celsius. {ECO:0000269|PubMed:25521849};
|
FUNCTION: Catalyzes the dephosphorylation of O-phospho-L-serine into L-serine, a step in the L-serine biosynthetic pathway (PubMed:25037224, PubMed:25521849). Exhibits high specificity for L-phosphoserine compared to substrates like L-phosphothreonine (5% relative activity) and L-phosphotyrosine (1.7% relative activity) (PubMed:25521849). {ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}.; FUNCTION: In the host, induces significant cytoskeleton rearrangements through cofilin dephosphorylation and its subsequent activation, and affects the expression of genes that regulate actin dynamics. It specifically interacts with HSP90, HSP70 and HSP27 that block apoptotic pathways but not with other HSPs. Also interacts with GAPDH. It actively dephosphorylates MAP kinase p38 and NF-kappa B p65 (specifically at Ser-536) that play crucial roles in inflammatory and immune responses. This in turn leads to down-regulation of Interleukin 8, a chemotactic and inflammatory cytokine. Thus might help the pathogen to evade the host's immune response (PubMed:26984196). Exogenous addition of purified SerB2 protein to human THP-1 cells (that can be differentiated into macrophage-like cells) induces microtubule rearrangements; the phosphatase activity is co-related to the elicited rearrangements, while addition of the ACT-domains alone elicits no rearrangements (PubMed:25521849). {ECO:0000269|PubMed:25521849, ECO:0000269|PubMed:26984196}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53353
|
WHB2A_MYCTU
|
MVPEAPAPFEEPLPPEATDQWQDRALCAQTDPEAFFPEKGGSTREAKKICMGCEVRHECLEYALAHDERFGIWGGLSERERRRLKRGII
| null |
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250, ECO:0000305}; Note=Binds 1 [4Fe-4S] cluster per subunit. Contains 1 [2Fe-2S] cluster after reconstitution of overexpressed protein from E.coli. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit. {ECO:0000250, ECO:0000305};
|
cell redox homeostasis [GO:0045454]; negative regulation of DNA-templated transcription [GO:0045892]
|
cytoplasm [GO:0005737]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; dinitrosyl-iron complex binding [GO:0035731]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein-disulfide reductase (NAD(P)) activity [GO:0047134]
|
PF02467;
| null |
WhiB family
|
PTM: May be phosphorylated, possibly on Ser-42. {ECO:0000269|PubMed:22686939}.; PTM: The cluster is degraded quickly in the presence of air. Upon cluster removal intramolecular disulfide bonds are formed.; PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA (By similarity). {ECO:0000250}.; FUNCTION: The apo-form functions as a chaperone, preventing aggregation or helping in correct refolding of a number of substrates; this activity does not require ATP or the ability to bind a Fe-S cluster. Chaperone activity is insensitive to the redox state of its cysteine residues. The apo-form has no protein disulfide reductase activity. The apo-form binds to its own promoter. {ECO:0000269|PubMed:19016840, ECO:0000269|PubMed:22686939}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53361
|
SAPM_MYCTU
|
MLRGIQALSRPLTRVYRALAVIGVLAASLLASWVGAVPQVGLAASALPTFAHVVIVVEENRSQAAIIGNKSAPFINSLAANGAMMAQAFAETHPSEPNYLALFAGNTFGLTKNTCPVNGGALPNLGSELLSAGYTFMGFAEDLPAVGSTVCSAGKYARKHVPWVNFSNVPTTLSVPFSAFPKPQNYPGLPTVSFVIPNADNDMHDGSIAQGDAWLNRHLSAYANWAKTNNSLLVVTWDEDDGSSRNQIPTVFYGAHVRPGTYNETISHYNVLSTLEQIYGLPKTGYATNAPPITDIWGD
|
3.1.3.2; 3.1.3.64
|
COFACTOR: Name=a metal cation; Xref=ChEBI:CHEBI:25213; Evidence={ECO:0000305|PubMed:11073936};
|
NADP catabolic process [GO:0006742]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phospholipid catabolic process [GO:0009395]; symbiont-mediated suppression of host innate immune response [GO:0052170]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; peptidoglycan-based cell wall [GO:0009274]
|
acid phosphatase activity [GO:0003993]; phosphatase activity [GO:0016791]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphoenolpyruvate phosphatase activity [GO:0050189]; phosphoglycerate phosphatase activity [GO:0050192]; trehalose-phosphatase activity [GO:0004805]
|
PF04185;
|
3.40.720.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11073936, ECO:0000269|PubMed:15753315}. Host cytoplasmic vesicle, host phagosome {ECO:0000305|PubMed:15753315}. Note=It remains to be determined how SapM, once secreted into the phagosomal lumen, gains access to PI3P within the cytofacial membrane leaflet. It is possible that SapM is exported to the cytosolic side, or alternatively there may be a mechanism for PI3P presentation to SapM remaining on the luminal side. {ECO:0000305|PubMed:15753315}.
|
CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000269|PubMed:11073936}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000269|PubMed:15753315};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.43 mM for p-nitrophenyl phosphate {ECO:0000269|PubMed:11073936}; Vmax=2100000 nmol/h/mg enzyme with p-nitrophenyl phosphate as substrate {ECO:0000269|PubMed:11073936};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. Significant phosphatase activity is observed between pH 5.5 and 8.0. {ECO:0000269|PubMed:11073936};
| null |
FUNCTION: Virulence factor that plays an important role in blocking phagosome-lysosome fusion and thus participates in the intracellular survival of the pathogen (PubMed:15753315, PubMed:23923000). Acts as a phosphatase that dephosphorylates phosphatidylinositol 3-phosphate (PI3P), a membrane trafficking regulatory lipid essential for phagosomal acquisition of lysosomal constituents (PubMed:15753315). Therefore, SapM eliminates PI3P from the phagosomal membrane by catalyzing its hydrolysis, and thus contributes to inhibition of phagosome maturation (PubMed:15753315). Also interferes with autophagy: SapM blocks autophagosome-lysosome fusion in macrophages by binding to the small GTPase RAB7, which prevents RAB7 from being involved in this process and thus negatively regulates autophagy flux (PubMed:25896765). In vitro, displays phosphatase activity with broad specificity; can dephosphorylate a variety of phosphoester substrates, with the highest activity against phosphoenolpyruvate, glycerophosphate, GTP, NADPH, phosphotyrosine and trehalose-6-phosphate (PubMed:11073936). In contrast, the enzyme exhibits poor activity against glucose-6-phosphate, phosphothreonine, and a number of nucleotides (NADP, ATP, AMP, and GMP) (PubMed:11073936). {ECO:0000269|PubMed:11073936, ECO:0000269|PubMed:15753315, ECO:0000269|PubMed:23923000, ECO:0000269|PubMed:25896765}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53423
|
GDSLL_MYCTU
|
MPRRSTIALATAGALASTGTAYLGARNLLVGQATHARTVIPKSFDAPPRADGVYTRGGGPVQRWRREVPFDVHLMIFGDSTATGYGCASAEEVPGVLIARGLAEQTGKRIRLSTKAIVGATSKGVCGQVDAMFVVGPPPDAAVIMIGANDITALNGIGPSAQRLADCVRRLRTRGAVVVVGTCPDLGVITAIPQPLRALAHTRGVRLARAQTAAVKAAGGVPVPLGHLLAPKFRAMPELMFSADRYHPSAPAYALAADLLFLALRDALTEKLDIPIHETPSRPGTATLEPGHTRHSMMSRLRRPRPARAVPTGG
|
3.1.-.-; 3.1.1.6
| null | null |
peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
acetylesterase activity [GO:0008126]; lysophospholipase activity [GO:0004622]
|
PF13472;
|
3.40.50.1110;
|
'GDSL' lipolytic enzyme family
| null | null |
CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6; Evidence={ECO:0000269|PubMed:31001637}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:31001637}; CATALYTIC ACTIVITY: Reaction=H2O + triacetin = acetate + diacetylglycerol + H(+); Xref=Rhea:RHEA:48028, ChEBI:CHEBI:9661, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:88156; Evidence={ECO:0000269|PubMed:31001637}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:31001637};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=753 uM for pNP-acetate {ECO:0000269|PubMed:31001637};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (with pNP-acetate as substrate). {ECO:0000269|PubMed:31001637};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius (with pNP-acetate as substrate). {ECO:0000269|PubMed:31001637};
|
FUNCTION: Esterase that preferentially hydrolyzes short-chain fatty acids, particularly pNP-acetate (C2) and pNP-butyrate (C4). Has also weak activity with pNP-hexanoate (C6) and pNP-octanoate (C8). It can also hydrolyze short-chain tryglycerides such as triacetin and tributyrin (PubMed:31001637). Important for intracellular survival (PubMed:31001637). {ECO:0000269|PubMed:31001637}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53424
|
LIPU_MYCTU
|
MAVRPVLAVGSYLPHAPWPWGVIDQAARVLLPASTTVRAAVSLPNASAQLVRASGVLPADGTRRAVLYLHGGAFLTCGANSHGRLVELLSKFADSPVLVVDYRLIPKHSIGMALDDCHDGYRWLRLLGYEPEQIVLAGDSAGGYLALALAQRLQEVGEEPAALVAISPLLQLAKEHKQAHPNIKTDAMFPARAFDALDALVASAAARNQVDGEPEELYEPLEHITPGLPRTLIHVSGSEVLLHDAQLAAAKLAAAGVPAEVRVWPGQVHDFQVAASMLPEAIRSLRQIGEYIREATG
|
3.1.1.-
| null | null |
extracellular region [GO:0005576]
|
acetylesterase activity [GO:0008126]; triglyceride lipase activity [GO:0004806]
|
PF07859;
|
3.40.50.1820;
|
'GDXG' lipolytic enzyme family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28327423}. Note=Extracellular. {ECO:0000269|PubMed:28327423}.
|
CATALYTIC ACTIVITY: Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748; Evidence={ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; CATALYTIC ACTIVITY: Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658; Evidence={ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:26398213};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.73 uM for pNP-butyrate {ECO:0000269|PubMed:28164792}; KM=333 uM for pNP-butyrate {ECO:0000269|PubMed:28327423}; Note=kcat is 49.8 min(-1) with pNP-butyrate as substrate. {ECO:0000269|PubMed:28164792};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 (with pNP-butyrate as substrate). {ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius (with pNP-butyrate as substrate). {ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423};
|
FUNCTION: Esterase that shows preference for short chain fatty acids (PubMed:26398213, PubMed:28164792, PubMed:28327423). Contributes to the growth of M.tuberculosis during the nutritive stress (PubMed:28164792). Elicits strong humoral response in both extrapulmonary and relapsed cases of tuberculosis patients (PubMed:28327423). {ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53493
|
PPMNT_MYCTU
|
MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLTHRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRLLPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALVGCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPTVTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDIDPFVNPDAGQRISAAAEAIGAPILIGTLMDVPGRPRENPEWTNTAIVWNPGTGPADRHDKAIVQPFGEYLPMPWLFRHLSGYADRAGHFVPGNGTGVVRIAGVPVGVATCWEVIFDRAPRKSILGGAQLLTVPSNNATFNKTMSEQQLAFAKVRAVEHDRYVVVAGTTGISAVIAPDGGELIRTDFFQPAYLDSQVRLKTRLTPATRWGPILQWILVGAAAAVVLVAMRQNGWFPRPRRSEPKGENDDSDAPPGRSEASGPPALSESDDELIQPEQGGRHSSGFGRHRATSRSYMTTGQPAPPAPGNRPSQRVLVIIPTFNERENLPVIHRRLTQACPAVHVLVVDDSSPDGTGQLADELAQADPGRTHVMHRTAKNGLGAAYLAGFAWGLSREYSVLVEMDADGSHAPEQLQRLLDAVDAGADLAIGSRYVAGGTVRNWPWRRLVLSKTANTYSRLALGIGIHDITAGYRAYRREALEAIDLDGVDSKGYCFQIDLTWRTVSNGFVVTEVPITFTERELGVSKMSGSNIREALVKVARWGIEGRLSRSDHARARPDIARPGAGGSRVSRADVTE
|
2.3.1.269; 2.4.1.-; 2.4.1.83
| null |
glycolipid biosynthetic process [GO:0009247]; lipoprotein biosynthetic process [GO:0042158]; perturbation of host innate immune response [GO:0052167]
|
cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
dolichyl-phosphate beta-D-mannosyltransferase activity [GO:0004582]; hydrolase activity [GO:0016787]; N-acyltransferase activity [GO:0016410]
|
PF00795;PF00535;PF20154;
|
3.60.110.10;
|
CN hydrolase family, Apolipoprotein N-acyltransferase subfamily; Glycosyltransferase 2 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12427759}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]; Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684, ChEBI:CHEBI:15378, ChEBI:CHEBI:136912, ChEBI:CHEBI:140656, ChEBI:CHEBI:140657, ChEBI:CHEBI:140660; EC=2.3.1.269; Evidence={ECO:0000269|PubMed:19661058}; CATALYTIC ACTIVITY: Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683, ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83; Evidence={ECO:0000269|PubMed:11931640};
| null |
PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
| null | null |
FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. {ECO:0000269|PubMed:19661058}.; FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors (works best on C20-C95 lipid monophosphate substrates in which the lipid can be modified, tested with the C-terminal domain expressed in M.smegmatis) to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo-inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM). {ECO:0000269|PubMed:11931640}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53512
|
AROG_MYCTU
|
MNWTVDIPIDQLPSLPPLPTDLRTRLDAALAKPAAQQPTWPADQALAMRTVLESVPPVTVPSEIVRLQEQLAQVAKGEAFLLQGGDCAETFMDNTEPHIRGNVRALLQMAVVLTYGASMPVVKVARIAGQYAKPRSADIDALGLRSYRGDMINGFAPDAAAREHDPSRLVRAYANASAAMNLVRALTSSGLASLHLVHDWNREFVRTSPAGARYEALATEIDRGLRFMSACGVADRNLQTAEIYASHEALVLDYERAMLRLSDGDDGEPQLFDLSAHTVWIGERTRQIDGAHIAFAQVIANPVGVKLGPNMTPELAVEYVERLDPHNKPGRLTLVSRMGNHKVRDLLPPIVEKVQATGHQVIWQCDPMHGNTHESSTGFKTRHFDRIVDEVQGFFEVHRALGTHPGGIHVEITGENVTECLGGAQDISETDLAGRYETACDPRLNTQQSLELAFLVAEMLRD
|
2.5.1.54
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16288916}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16288916}; Name=Cd(2+); Xref=ChEBI:CHEBI:48775; Evidence={ECO:0000269|PubMed:16288916}; Note=Binds 1 divalent cation per subunit. The enzyme is active with manganese, cobalt or cadmium ions. {ECO:0000269|PubMed:16288916};
|
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; protein homooligomerization [GO:0051260]
|
cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; manganese ion binding [GO:0030145]
|
PF01474;
|
3.20.20.70;
|
Class-II DAHP synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000269|PubMed:16288916}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14718; Evidence={ECO:0000305|PubMed:16288916};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for D-erythrose 4-phosphate (E4P) {ECO:0000269|PubMed:16288916}; KM=37 uM for phosphoenolpyruvate (PEP) {ECO:0000269|PubMed:16288916}; Note=kcat is 3.1 sec(-1). {ECO:0000269|PubMed:16288916};
|
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000305|PubMed:16288916}.
| null | null |
FUNCTION: Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate. {ECO:0000269|PubMed:16288916}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53547
|
CHSB1_MYCTU
|
MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ
|
1.1.1.-
| null |
cholesterol catabolic process [GO:0006707]
| null |
oxidoreductase activity [GO:0016491]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null | null |
CATALYTIC ACTIVITY: Reaction=(22S)-hydroxy-3-oxo-chol-4-ene-24-oyl-CoA + NAD(+) = 3,22-dioxochol-4-en-24-oyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:72583, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:86014, ChEBI:CHEBI:192468; Evidence={ECO:0000269|PubMed:33826843}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72584; Evidence={ECO:0000269|PubMed:33826843}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72585; Evidence={ECO:0000269|PubMed:33826843};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.3 uM for (22S)-HOCO-CoA {ECO:0000269|PubMed:33826843}; KM=70 uM for NAD(+) with (22S)-HOCO-CoA {ECO:0000269|PubMed:33826843}; KM=169 uM for (3R)-hydroxyoctanoyl-CoA {ECO:0000269|PubMed:33826843}; KM=126 uM for NAD(+) with (3R)-hydroxyoctanoyl-CoA {ECO:0000269|PubMed:33826843}; KM=369 uM for 17-beta-hydroxyandrost-4-en-3-one {ECO:0000269|PubMed:33826843}; KM=99 uM for NAD(+) with 17-beta-hydroxyandrost-4-en-3-one {ECO:0000269|PubMed:33826843}; KM=25 uM for 3,22-dioxo-cholest-4-en-24-oyl-CoA {ECO:0000269|PubMed:33826843}; KM=40 uM for NADH {ECO:0000269|PubMed:33826843};
|
PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000269|PubMed:33826843}.
| null | null |
FUNCTION: A reversible dehydrogenase involved in cholesterol side-chain degradation. Catalyzes the oxidation of hydroxyl-cholesterol-CoA ester metabolic intermediate (22S)-HOCO-CoA (3-oxo-chol-4-ene-(22S)-hydroxy-24-oyl-CoA), the product of ChsH3, has no activity on (22R)-HOCO-CoA (the product of EchA19). Also acts on (3R)-hydroxyoctanoyl-CoA and 17-beta-hydroxyandrost-4-en-3-one, but not on 7-alpha-hydroxyandrost-4-en-3-one, uses NAD(+) but not NADP(+). {ECO:0000269|PubMed:33826843}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53551
|
FAC17_MYCTU
|
MTPTHPTVTELLLPLSEIDDRGVYFEDSFTSWRDHIRHGAAIAAALRERLDPARPPHVGVLLQNTPFFSATLVAGALSGIVPVGLNPVRRGAALAGDIAKADCQLVLTGSGSAEVPADVEHINVDSPEWTDEVAAHRDTEVRFRSADLADLFMLIFTSGTSGDPKAVKCSHRKVAIAGVTITQRFSLGRDDVCYVSMPLFHSNAVLVGWAVAAACQGSMALRRKFSASQFLADVRRYGATYANYVGKPLSYVLATPELPDDADNPLRAVYGNEGVPGDIDRFGRRFGCVVMDGFGSTEGGVAITRTLDTPAGALGPLPGGIQIVDPDTGEPCPTGVVGELVNTAGPGGFEGYYNDEAAEAERMAGGVYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLMRYPDATEVAVYPVPDPVVGDQVMAALVLAPGTKFDADKFRAFLTEQPDLGHKQWPSYVRVSAGLPRTMTFKVIKRQLSAEGVACADPVWPIRR
|
6.2.1.2; 6.2.1.3
| null |
Actinobacterium-type cell wall biogenesis [GO:0071766]; lipid biosynthetic process [GO:0008610]; long-chain fatty acid biosynthetic process [GO:0042759]; long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; triglyceride homeostasis [GO:0070328]; very long-chain fatty acid metabolic process [GO:0000038]
|
cytosol [GO:0005829]; lipid droplet [GO:0005811]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; fatty acid transmembrane transporter activity [GO:0015245]; long-chain fatty acid transporter activity [GO:0005324]; long-chain fatty acid-CoA ligase activity [GO:0004467]; medium-chain fatty acid-CoA ligase activity [GO:0031956]; very long-chain fatty acid-CoA ligase activity [GO:0031957]
|
PF00501;PF13193;
|
3.30.300.30;3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
| null | null |
CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2; Evidence={ECO:0000269|PubMed:19182784}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341; Evidence={ECO:0000269|PubMed:19182784}; CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000269|PubMed:19182784}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA; Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19182784}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741; Evidence={ECO:0000269|PubMed:19182784}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA; Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19182784}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624; Evidence={ECO:0000269|PubMed:19182784}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19182784}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000269|PubMed:19182784}; CATALYTIC ACTIVITY: Reaction=ATP + cholate + CoA = AMP + choloyl-CoA + diphosphate; Xref=Rhea:RHEA:23532, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:24244004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23533; Evidence={ECO:0000269|PubMed:24244004}; CATALYTIC ACTIVITY: Reaction=ATP + chenodeoxycholate + CoA = AMP + chenodeoxycholoyl-CoA + diphosphate; Xref=Rhea:RHEA:43764, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:24244004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43765; Evidence={ECO:0000269|PubMed:24244004};
| null |
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
| null | null |
FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension (PubMed:15042094, PubMed:19182784). Also involved in steroid side-chain degradation. Activates cholesterol metabolites with a C5 side chain, including cholate and chenodeoxycholate (PubMed:24244004). {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:24244004}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53561
|
ECH19_MYCTU
|
MATVESGPDALVERRGHTLIVTMNRPAARNALSTEMMRIMVQAWDRVDNDPDIRCCILTGAGGYFCAGMDLKAATQKPPGDSFKDGSYGPSRIDALLKGRRLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLYPMGGSAVRLVRQIPYTLACDLLLTGRHITAAEAKEMGLIGHVVPDGQALTKALELADAISANGPLAVQAILRSIRETECMPENEAFKIDTQIGIKVFLSDDAKEGPRAFAEKRAPNFQNR
|
4.2.1.-
| null |
cholesterol catabolic process [GO:0006707]; fatty acid beta-oxidation [GO:0006635]; response to host immune response [GO:0052572]
| null |
enoyl-CoA hydratase activity [GO:0004300]
|
PF00378;
|
1.10.12.10;
|
Enoyl-CoA hydratase/isomerase family
|
PTM: Succinylated in vitro at pH 8.1, succinylation reduces specific activity of the enzyme 5.5-fold; succinyl-CoA is a downstream by-product of cholesterol degradation. Can be de-succinylated in vitro by NAD-dependent protein deacylase (AC P9WGG3). Succinylation may be a negative feedback regulator of cholesterol metabolism. {ECO:0000269|PubMed:32649175}.
| null |
CATALYTIC ACTIVITY: Reaction=(22E)-3-oxochola-4,22-dien-24-oyl-CoA + H2O = (22R)-hydroxy-3-oxo-chol-4-ene-24-oyl-CoA; Xref=Rhea:RHEA:72575, ChEBI:CHEBI:15377, ChEBI:CHEBI:136759, ChEBI:CHEBI:192383; Evidence={ECO:0000269|PubMed:33826843};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 uM for octenoyl-CoA {ECO:0000269|PubMed:32649175}; KM=5.8 uM for 3-OCDO-CoA {ECO:0000269|PubMed:32649175}; KM=8 uM for 3-OCDO-CoA with succinylated enzyme {ECO:0000269|PubMed:32649175}; Note=kcat is 181.2 sec(-1) with 3-OCDO-CoA as substrate. kcat is 45.7 sec(-1) with 3-OCDO-CoA as substrate with succinylated EchA19. kcat is 1.2 sec(-1) with octenoyl-CoA as substrate. {ECO:0000269|PubMed:32649175};
|
PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000269|PubMed:32649175}.
| null | null |
FUNCTION: Degradation of the cholesterol side chain involves 3 multistep beta-oxidation cycles, this may be involved in the second cycle (Probable). Hydrates 3-OCDO-CoA ((22E)-3-oxo-chol-4,22-dien-24-oyl-CoA) to make (22R)-HOCO-CoA (3-oxo-chol-4-ene-(22R)-hydroxy-24-oyl-CoA). Also acts on octenoyl-CoA. Not active on (E)-3-OCDS-CoA ((E)-3-oxocholest-4,24-dien-26-oyl-CoA) or 3-OPDC-CoA (3-oxo-4,17-pregnadiene-20-carboxyl-CoA). Hydrates the same substrate as ChsH3, but the 2 enzymes make different stereoisomers of the product (PubMed:32649175, PubMed:33826843). {ECO:0000269|PubMed:32649175, ECO:0000269|PubMed:33826843, ECO:0000305|PubMed:32649175, ECO:0000305|PubMed:33826843}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53580
|
FAA32_MYCTU
|
MFVTGESGMAYHNPFIVNGKIRFPANTNLVRHVEKWAKVRGDKLAYRFLDFSTERDGVARDILWSDFSARNRAVGARLQQVTQPGDRVAILCPQNLDYLISFFGALYSGRIAVPLFDPAEPGHVGRLHAVLDDCAPSTILTTTDSAEGVRKFIRARSAKERPRVIAVDAVPTEVAATWQQPEANEETVAYLQYTSGSTRIPSGVQITHLNLPTNVVQVLNALEGQEGDRGVSWLPFFHDMGLITVLLASVLGHSFTFMTPAAFVRRPGRWIRELARKPGETGGTFSAAPNFAFEHAAVRGVPRDDEPPLDLSNVKGILNGSEPVSPASMRKFFEAFAPYGLKQTAVKPSYGLAEATLFVSTTPMDEVPTVIHVDRDELNNQRFVEVAADAPNAVAQVSAGKVGVSEWAVIVDADTASELPDGQIGEIWLHGNNLGTGYWGKEEESAQTFKNILKSRISESRAEGAPDDALWVRTGDYGTYFKDHLYIAGRIKDLVIIDGRNHYPQDLECTAQESTKALRVGYAAAFSVPANQLPQTVFDDSHAGLKFDPEDTSEQLVIVGERAAGTHKLDHQPIVDDIRAAIAVGHGVTVRDVLLVSAGTIPRTSSGKIGRRACRAAYLDGSLRSGVGSPTVFATSD
|
6.2.1.20
| null |
Actinobacterium-type cell wall biogenesis [GO:0071766]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610]; mycolate cell wall layer assembly [GO:0071769]
|
cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
adenylyltransferase activity [GO:0070566]; ATP binding [GO:0005524]; ligase activity [GO:0016874]; long-chain fatty acid [acyl-carrier-protein] ligase activity [GO:0008922]
|
PF00501;
|
3.30.300.30;3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
|
PTM: Phosphorylated on Thr-552 by PknA, PknB, PknD and PknF. Dephosphorylated by PstP. Phosphorylation regulates activity. {ECO:0000269|PubMed:27590338}.
| null |
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20; Evidence={ECO:0000269|PubMed:19436070}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45589; Evidence={ECO:0000269|PubMed:19436070}; CATALYTIC ACTIVITY: Reaction=ATP + dodecanoate + holo-[ACP] = AMP + diphosphate + dodecanoyl-[ACP]; Xref=Rhea:RHEA:63620, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19436070}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63621; Evidence={ECO:0000269|PubMed:19436070}; CATALYTIC ACTIVITY: Reaction=ATP + holo-[ACP] + tetradecanoate = AMP + diphosphate + tetradecanoyl-[ACP]; Xref=Rhea:RHEA:64888, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:30616, ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19477415}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64889; Evidence={ECO:0000269|PubMed:19477415}; CATALYTIC ACTIVITY: Reaction=ATP + hexadecanoate + holo-[ACP] = AMP + diphosphate + hexadecanoyl-[ACP]; Xref=Rhea:RHEA:63628, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19436070}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63629; Evidence={ECO:0000269|PubMed:19436070}; CATALYTIC ACTIVITY: Reaction=ATP + dodecanoate + H(+) = diphosphate + dodecanoyl-AMP; Xref=Rhea:RHEA:43712, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83623; Evidence={ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152, ECO:0000269|PubMed:27590338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43713; Evidence={ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152, ECO:0000269|PubMed:27590338}; CATALYTIC ACTIVITY: Reaction=ATP + H(+) + tetradecanoate = diphosphate + tetradecanoyl-AMP; Xref=Rhea:RHEA:43704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:83626; Evidence={ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:26900152}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43705; Evidence={ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:26900152}; CATALYTIC ACTIVITY: Reaction=ATP + H(+) + hexadecanoate = diphosphate + hexadecanoyl-AMP; Xref=Rhea:RHEA:43708, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83627; Evidence={ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:19477415}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43709; Evidence={ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:19477415};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2640 uM for dodecanoate {ECO:0000269|PubMed:19477415}; KM=72.09 uM for dodecanoate {ECO:0000269|PubMed:26900152}; KM=20.5 uM for tetradecanoate {ECO:0000269|PubMed:19477415}; KM=4.77 uM for tetradecanoate {ECO:0000269|PubMed:26900152}; KM=3.2 uM for hexadecanoate {ECO:0000269|PubMed:19477415}; KM=2020 uM for ATP {ECO:0000269|PubMed:19477415}; KM=248 uM for ATP {ECO:0000269|PubMed:26900152}; Note=kcat is 0.150 min(-1) with dodecanoate as substrate (PubMed:19477415). kcat is 2.04 min(-1) with dodecanoate as substrate (PubMed:26900152). kcat is 0.123 min(-1) with tetradecanoate as substrate (PubMed:19477415). kcat is 0.98 min(-1) with tetradecanoate as substrate (PubMed:26900152). kcat is 0.015 min(-1) with hexadecanoate as substrate (PubMed:19477415). {ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:26900152};
|
PATHWAY: Lipid metabolism; mycolic acid biosynthesis. {ECO:0000269|PubMed:19436070, ECO:0000269|PubMed:19477415}.
| null | null |
FUNCTION: Involved in the biosynthesis of mycolic acids (PubMed:19436070, PubMed:19477415). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (PubMed:15042094, PubMed:19436070, PubMed:19477415, PubMed:27547819, PubMed:27590338). Can use dodecanoate (C12), tetradecanoate (C14) and hexadecanoate (C16) (PubMed:19182784, PubMed:19436070, PubMed:19477415, PubMed:23364516, PubMed:26900152, PubMed:27590338). In vitro, displays a preference for long-chain over medium and short-chain fatty acid substrates (PubMed:19477415). {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:19436070, ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152, ECO:0000269|PubMed:27547819, ECO:0000269|PubMed:27590338}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53581
|
CULP6_MYCTU
|
MAKNSRRKRHRILAWIAAGAMASVVALVIVAVVIMLRGAESPPSAVPPGVLPPGPTPAHPHKPRPAFQDASCPDVQMISVPGTWESSPQQNPLNPVQFPKALLLKVTGPIAQQFAPARVQTYTVAYTAQFHNPLTTDNQMSYNDSRAEGTRAMVAAMTDMNNRCPLTSYVLIGFSQGAVIAGDVASDIGNGRGPVDEDLVLGVTLIADGRRQQGVGNQVPPSPRGEGAEITLHEVPVLSGLGLTMTGPRPGGFGALDGRTNEICAQGDLICAAPAQAFSPANLPTTLNTLAGGAGQPVHAMYATPEFWNSDGEPATEWTLNWAHQLIENAPHPKHR
|
3.1.1.-
| null |
lipid catabolic process [GO:0016042]
|
extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
carboxylesterase activity [GO:0106435]; fatty acyl-CoA hydrolase activity [GO:0047617]; lipase activity [GO:0016298]; phospholipase A1 activity [GO:0008970]
|
PF01083;
|
3.40.50.1820;
|
Cutinase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:19225166}.
|
CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:19225166}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47365; Evidence={ECO:0000269|PubMed:19225166}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:19225166}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47389; Evidence={ECO:0000269|PubMed:19225166}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:19225166}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393; Evidence={ECO:0000269|PubMed:19225166}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoate ester = an aliphatic alcohol + H(+) + octadecanoate; Xref=Rhea:RHEA:47396, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75925; Evidence={ECO:0000269|PubMed:19225166}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47397; Evidence={ECO:0000269|PubMed:19225166}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H(+); Xref=Rhea:RHEA:47328, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905; Evidence={ECO:0000269|PubMed:19169353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47329; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:19169353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-acyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40651, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:58168, ChEBI:CHEBI:75063; Evidence={ECO:0000269|PubMed:19169353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40652; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000269|PubMed:19169353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence={ECO:0000269|PubMed:19169353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:19169353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000269|PubMed:19169353};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.52 mM for nitrophenyl butyrate {ECO:0000269|PubMed:19169353}; KM=0.017 mM for palmitoyl-S-CoA {ECO:0000269|PubMed:19169353}; KM=2.28 mM for decanoyl-S-CoA {ECO:0000269|PubMed:19169353}; KM=4.52 mM for pNP-butyrate {ECO:0000269|PubMed:20656688}; KM=19.88 uM for 4-methylumbelliferyl heptanoate {ECO:0000269|PubMed:29247008}; Vmax=1.62 mol/min/mg enzyme with nitrophenyl butyrate as substrate {ECO:0000269|PubMed:19169353}; Vmax=1.35 mol/min/mg enzyme with palmitoyl-S-CoA as substrate {ECO:0000269|PubMed:19169353}; Vmax=1.11 mol/min/mg enzyme with decanoyl-S-CoA as substrate {ECO:0000269|PubMed:19169353}; Vmax=241 nmol/min/mg enzyme with pNP-butyrate as substrate {ECO:0000269|PubMed:20656688}; Note=kcat is 0.00881 sec(-1) with nitrophenyl butyrate as substrate. kcat is 0.0733 sec(-1) with palmitoyl-S-CoA as substrate. kcat is 0.0845 sec(-1) with decanoyl-S-CoA as substrate (PubMed:19169353). kcat is 0.143 sec(-1) with pNP-butyrate as substrate (PubMed:20656688). kcat is 10.05 min(-1) with 4-methylumbelliferyl heptanoate as substrate (PubMed:29247008). {ECO:0000269|PubMed:19169353, ECO:0000269|PubMed:20656688, ECO:0000269|PubMed:29247008};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is above 7.0 for lipase activity. {ECO:0000269|PubMed:19225166};
| null |
FUNCTION: Shows esterase and phospholipase A activities (PubMed:19169353, PubMed:19225166, PubMed:20656688, PubMed:29247008). May be involved in cell wall biosynthesis and/or maintenance (PubMed:19169353, PubMed:19225166, PubMed:20656688). Can hydrolyze various substrates, including the p-nitrophenol-linked aliphatic esters pNP-laurate (C12), pNP-myristate (C14), pNP-palmitate (C16), pNP-stearate (C18), pNP-butyrate (C4), phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, 4-methylumbelliferyl heptanoate and palmitic acid and arachidonic acid containing phospholipids (PubMed:19169353, PubMed:19225166, PubMed:20656688). Does not exhibit cutinase activity (PubMed:19225166). {ECO:0000269|PubMed:19169353, ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688, ECO:0000269|PubMed:29247008}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53585
|
GLFT2_MYCTU
|
MSELAASLLSRVILPRPGEPLDVRKLYLEESTTNARRAHAPTRTSLQIGAESEVSFATYFNAFPASYWRRWTTCKSVVLRVQVTGAGRVDVYRTKATGARIFVEGHDFTGTEDQPAAVETEVVLQPFEDGGWVWFDITTDTAVTLHSGGWYATSPAPGTANIAVGIPTFNRPADCVNALRELTADPLVDQVIGAVIVPDQGERKVRDHPDFPAAAARLGSRLSIHDQPNLGGSGGYSRVMYEALKNTDCQQILFMDDDIRLEPDSILRVLAMHRFAKAPMLVGGQMLNLQEPSHLHIMGEVVDRSIFMWTAAPHAEYDHDFAEYPLNDNNSRSKLLHRRIDVDYNGWWTCMIPRQVAEELGQPLPLFIKWDDADYGLRAAEHGYPTVTLPGAAIWHMAWSDKDDAIDWQAYFHLRNRLVVAAMHWDGPKAQVIGLVRSHLKATLKHLACLEYSTVAIQNKAIDDFLAGPEHIFSILESALPQVHRIRKSYPDAVVLPAASELPPPLHKNKAMKPPVNPLVIGYRLARGIMHNLTAANPQHHRRPEFNVPTQDARWFLLCTVDGATVTTADGCGVVYRQRDRAKMFALLWQSLRRQRQLLKRFEEMRRIYRDALPTLSSKQKWETALLPAANQEPEHG
|
2.4.1.288
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:22707726}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:22707726};
|
capsule polysaccharide biosynthetic process [GO:0045227]; cell wall macromolecule biosynthetic process [GO:0044038]; cell wall organization [GO:0071555]; cell wall polysaccharide biosynthetic process [GO:0070592]; lipopolysaccharide biosynthetic process [GO:0009103]; mycolate cell wall layer assembly [GO:0071769]; UDP-D-galactose metabolic process [GO:0052573]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
glycosyltransferase activity [GO:0016757]; lipopolysaccharide-1,5-galactosyltransferase activity [GO:0035496]; lipopolysaccharide-1,6-galactosyltransferase activity [GO:0008921]; metal ion binding [GO:0046872]; transferase activity [GO:0016740]; UDP-galactosyltransferase activity [GO:0035250]
|
PF19320;PF17994;PF13641;
|
3.90.550.60;
|
Glycosyltransferase 2 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11304545}.
|
CATALYTIC ACTIVITY: Reaction=beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol + 28 UDP-alpha-D-galactofuranose = [beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6)]14-beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol + 28 H(+) + 28 UDP; Xref=Rhea:RHEA:34391, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66915, ChEBI:CHEBI:67210, ChEBI:CHEBI:67212; EC=2.4.1.288; Evidence={ECO:0000269|PubMed:18055597, ECO:0000269|PubMed:19571009, ECO:0000305|PubMed:16704275};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.38 mM for UDP-Galf {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726}; KM=0.6 mM for beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726}; KM=1.7 mM for beta-D-Galf-(1->5)-beta-D-Galf-octyl {ECO:0000269|PubMed:16704275}; KM=0.635 mM for beta-D-Galf-(1->6)-beta-D-Galf-octyl {ECO:0000269|PubMed:16704275}; KM=0.208 mM for beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl {ECO:0000269|PubMed:16704275}; KM=0.204 mM for beta-D-Galf-(1->6)-beta-D-Galf-(1->5)-beta-D-Galf-octyl {ECO:0000269|PubMed:16704275}; Vmax=4.4 umol/min/mg enzyme for galtactose transfer on beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl {ECO:0000269|PubMed:16704275, ECO:0000269|PubMed:18423586}; Note=kcat is 430 min(-1) for galtactose transfer on beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl. {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726};
|
PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. {ECO:0000305|PubMed:11304545, ECO:0000305|PubMed:16704275}.
| null | null |
FUNCTION: Involved in the galactan polymerization of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacteria cell wall. Thus, successively transfers approximately 28 galactofuranosyl (Galf) residues from UDP-galactofuranose (UDP-Galf) onto the galactofuranosyl-galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-GlcNAc-PP-C50) acceptor produced by GlfT1, with alternating 1->5 and 1->6 links, forming a galactan domain with approximately 30 galactofuranosyl residues. {ECO:0000269|PubMed:18055597, ECO:0000269|PubMed:19571009, ECO:0000305|PubMed:10934214, ECO:0000305|PubMed:11304545, ECO:0000305|PubMed:16704275, ECO:0000305|PubMed:18423586}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53638
|
LDT1_MYCTU
|
MRRVVRYLSVVVAITLMLTAESVSIATAAVPPLQPIPGVASVSPANGAVVGVAHPVVVTFTTPVTDRRAVERSIRISTPHNTTGHFEWVASNVVRWVPHRYWPPHTRVSVGVQELTEGFETGDALIGVASISAHTFTVSRNGEVLRTMPASLGKPSRPTPIGSFHAMSKERTVVMDSRTIGIPLNSSDGYLLTAHYAVRVTWSGVYVHSAPWSVNSQGYANVSHGCINLSPDNAAWYFDAVTVGDPIEVVG
|
2.3.2.-
| null |
cell wall organization [GO:0071555]; peptidoglycan-protein cross-linking [GO:0018104]; regulation of cell shape [GO:0008360]
|
extracellular region [GO:0005576]; periplasmic space [GO:0042597]
|
acyltransferase activity [GO:0016746]; peptidoglycan L,D-transpeptidase activity [GO:0071972]
|
PF17964;PF03734;
|
2.60.40.3710;2.40.440.10;
| null | null |
SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
| null | null |
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
| null | null |
FUNCTION: Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems. Is thought to play a role in adaptation to the nonreplicative state of M.tuberculosis. {ECO:0000269|PubMed:18408028, ECO:0000269|PubMed:24041897}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53664
|
HTDX_MYCTU
|
MTQPSGLKNLLRAAAGALPVVPRTDQLPNRTVTVEELPIDPANVAAYAAVTGLRYGNQVPLTYPFALTFPSVMSLVTGFDFPFAAMGAIHTENHITQYRPIAVTDAVGVRVRAENLREHRRGLLVDLVTNVSVGNDVAWHQVTTFLHQQRTSLSGEPKPPPQKKPKLPPPAAVLRITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPDAVRYSVRFAKPVLLPATAGLYVAEGDGGWDLTLRNMAKGYPHLTATVRGL
|
4.2.1.-; 4.2.1.119; 4.2.1.55
| null |
fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]
|
fatty acid synthase complex [GO:0005835]; plasma membrane [GO:0005886]
|
(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; 3-hydroxyacyl-CoA dehydratase activity [GO:0018812]; fatty acid synthase activity [GO:0004312]
|
PF01575;
|
3.10.129.10;
|
Enoyl-CoA hydratase/isomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319, ChEBI:CHEBI:58856; EC=4.2.1.119; Evidence={ECO:0000269|PubMed:20511508}; CATALYTIC ACTIVITY: Reaction=(2E)-octenoyl-CoA + H2O = (3R)-hydroxyoctanoyl-CoA; Xref=Rhea:RHEA:40187, ChEBI:CHEBI:15377, ChEBI:CHEBI:62242, ChEBI:CHEBI:74279; Evidence={ECO:0000269|PubMed:20511508}; CATALYTIC ACTIVITY: Reaction=(3R)-3-hydroxydodecanoyl-CoA = (2E)-dodecenoyl-CoA + H2O; Xref=Rhea:RHEA:44024, ChEBI:CHEBI:15377, ChEBI:CHEBI:57330, ChEBI:CHEBI:74276; Evidence={ECO:0000269|PubMed:20511508}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O; Xref=Rhea:RHEA:39159, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526, ChEBI:CHEBI:74278; Evidence={ECO:0000269|PubMed:20511508}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyeicosanoyl-CoA = (2E)-eicosenoyl-CoA + H2O; Xref=Rhea:RHEA:39175, ChEBI:CHEBI:15377, ChEBI:CHEBI:74691, ChEBI:CHEBI:76373; Evidence={ECO:0000269|PubMed:20511508}; CATALYTIC ACTIVITY: Reaction=(3R)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O; Xref=Rhea:RHEA:17849, ChEBI:CHEBI:15377, ChEBI:CHEBI:57315, ChEBI:CHEBI:57332; EC=4.2.1.55; Evidence={ECO:0000269|PubMed:20511508};
| null | null | null | null |
FUNCTION: Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase activity (PubMed:19136596, PubMed:20511508). Displays a broad chain length specificity, with a predilection for the C8 to C12 substrates (PubMed:20511508). {ECO:0000269|PubMed:19136596, ECO:0000269|PubMed:20511508}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53666
|
FADE5_MYCTU
|
MSHYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPESFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVETGEPGERNGVFVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAVKVNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDKGVALAHVSGQIQEFVDSGAGNGRLKTERALLAKALTDVQGMAAALTGYLMAAQQDVTSLYKVGLGSVRFLMSVGDLIIGWLLQRQAAVAVAALDAGATGDERSFYEGKVAVASFFAKNFLPLLTSTREVIETLDNDIMELDEAAF
|
1.3.8.1; 1.3.8.7; 1.3.8.8
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305|PubMed:32601219};
|
fatty acid metabolic process [GO:0006631]; response to host immune response [GO:0052572]
|
extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
long-chain fatty acyl-CoA dehydrogenase activity [GO:0004466]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991]; short-chain fatty acyl-CoA dehydrogenase activity [GO:0016937]
|
PF00441;PF12806;PF02770;PF12418;
|
2.40.110.20;1.20.140.10;
|
Acyl-CoA dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721, ChEBI:CHEBI:83727; EC=1.3.8.8; Evidence={ECO:0000269|PubMed:32601219}; CATALYTIC ACTIVITY: Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723, ChEBI:CHEBI:83726; EC=1.3.8.7; Evidence={ECO:0000269|PubMed:32601219}; CATALYTIC ACTIVITY: Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87487, ChEBI:CHEBI:87488; EC=1.3.8.1; Evidence={ECO:0000269|PubMed:32601219}; CATALYTIC ACTIVITY: Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:71412; Evidence={ECO:0000269|PubMed:32601219}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61526; Evidence={ECO:0000269|PubMed:32601219}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; Evidence={ECO:0000269|PubMed:32601219}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:32601219}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; Evidence={ECO:0000269|PubMed:32601219}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; Evidence={ECO:0000269|PubMed:32601219};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=358.7 uM for butanoyl-CoA {ECO:0000269|PubMed:32601219}; KM=353 uM for hexanoyl-CoA {ECO:0000269|PubMed:32601219}; KM=162.5 uM for octadecanoyl-CoA {ECO:0000269|PubMed:32601219}; Note=kcat is 1.07 sec(-1) with butanoyl-CoA as substrate. kcat is 0.80 sec(-1) with hexanoyl-CoA as substrate. kcat is 0.61 sec(-1) with octadecanoyl-CoA as substrate. {ECO:0000269|PubMed:32601219};
|
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:32601219}.
| null | null |
FUNCTION: Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates. {ECO:0000269|PubMed:32601219}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53699
|
STF0_MYCTU
|
MSRAVRPYLVLATQRSGSTLLVESLRATGCAGEPQEFFQYLPSTGMAPQPREWFAGVDDDTILQLLDPLDPGTPDTATPVAWREHVRTSGRTPNGVWGGKLMWNQTALLQQRAAQLPDRSGDGLRAAIRDVIGNEPVFVHVHRPDVVSQAVSFWRAVQTQVWRGHPDPKRDSQAVYHAGAIAHIIRNLRDQENGWRAWFAEEGIDPIDIAYPVLWRNLTAIVASVLDAIGQDPKLAPAPMLERQANQRSDEWVDRYRAEAPRLGLPT
|
2.8.2.37
| null |
3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; sulfolipid biosynthetic process [GO:0046506]; trehalose metabolic process [GO:0005991]
|
peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
3'-phosphoadenosine 5'-phosphosulfate binding [GO:0050656]; protein homodimerization activity [GO:0042803]; sulfotransferase activity [GO:0008146]
|
PF09037;
|
3.40.50.300;
|
Stf0 sulfotransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha,alpha-trehalose = 2-O-sulfo-alpha,alpha-trehalose + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:41608, ChEBI:CHEBI:15378, ChEBI:CHEBI:16551, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:60091; EC=2.8.2.37; Evidence={ECO:0000269|PubMed:15258569};
| null |
PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:15258569}.
| null | null |
FUNCTION: Catalyzes the sulfuryl group transfer from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to trehalose-2-sulfate (T2S). The sulfation of trehalose is the first step in the biosynthesis of sulfolipid-1 (SL-1), a major cell wall glycolipid and the most abundant sulfated metabolite found in Mycobacterium tuberculosis, that is a potential virulence factor thought to mediate host-pathogen interactions. {ECO:0000269|PubMed:15258569}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53873
|
XPB_MYCTU
|
MTDGPLIVQSDKTVLLEVDHELAGAARAAIAPFAELERAPEHVHTYRITPLALWNARAAGHDAEQVVDALVSYSRYAVPQPLLVDIVDTMARYGRLQLVKNPAHGLTLVSLDRAVLEEVLRNKKIAPMLGARIDDDTVVVHPSERGRVKQLLLKIGWPAEDLAGYVDGEAHPISLHQEGWQLRDYQRLAADSFWAGGSGVVVLPCGAGKTLVGAAAMAKAGATTLILVTNIVAARQWKRELVARTSLTENEIGEFSGERKEIRPVTISTYQMITRRTKGEYRHLELFDSRDWGLIIYDEVHLLPAPVFRMTADLQSKRRLGLTATLIREDGREGDVFSLIGPKRYDAPWKDIEAQGWIAPAECVEVRVTMTDSERMMYATAEPEERYRICSTVHTKIAVVKSILAKHPDEQTLVIGAYLDQLDELGAELGAPVIQGSTRTSEREALFDAFRRGEVATLVVSKVANFSIDLPEAAVAVQVSGTFGSRQEEAQRLGRILRPKADGGGAIFYSVVARDSLDAEYAAHRQRFLAEQGYGYIIRDADDLLGPAI
|
5.6.2.4
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856}; Note=ATPase activity has a small preference for Mn(2+) over Mg(2+), Ca(2+) supports ATPase activity less well. Co(2+) and Zn(2+) are inactive (PubMed:19199647). Another study shows equal activity with Mg(2+) and Mn(2+), none with Ca(2+) (PubMed:22615856). {ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856};
|
transcription initiation at RNA polymerase II promoter [GO:0006367]
|
peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]; transcription preinitiation complex [GO:0097550]
|
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787]
|
PF16203;PF13625;PF04851;
|
3.40.50.300;
|
Helicase family, RAD25/XPB subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 nM for 21-mer ssDNA substrate {ECO:0000269|PubMed:19199647}; KM=22 uM for 10-mer ssDNA substrate {ECO:0000269|PubMed:19199647}; Note=kcat is 10 sec(-1) on a ssDNA 21-mer and about 50 sec(-1) on ssDNA 5kb template. {ECO:0000269|PubMed:19199647};
| null | null | null |
FUNCTION: ATP-dependent 3'-5' DNA helicase, unwinds 3'-overhangs, 3'- flaps, and splayed-arm DNA substrates but not 5'-overhangs, 5'-flap substrates, 3-way junctions or Holliday junctions. Not highly efficient in vitro (PubMed:19199647, PubMed:22615856). Requires ATP hydrolysis for helicase activity; the ATPase activity is DNA-dependent and requires a minimum of 4 single-stranded nucleotides (nt) with 6-10 nt providing all necessary interactions for full processive unwinding. The ATPase prefers ATP over CTP or GTP, is almost inactive with TTP (PubMed:19199647). DNA helicase activity requires ATP or dATP and only acts when the 3'-overhang is >20 nt. Capable of unwinding a DNA:RNA hybrid if the 3'-overhang is DNA. Also catalyzes ATP-independent annealing of complementary DNA strands; annealing requires Mg(2+) (PubMed:22615856). {ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53896
|
PEPD_MYCTU
|
MAKLARVVGLVQEEQPSDMTNHPRYSPPPQQPGTPGYAQGQQQTYSQQFDWRYPPSPPPQPTQYRQPYEALGGTRPGLIPGVIPTMTPPPGMVRQRPRAGMLAIGAVTIAVVSAGIGGAAASLVGFNRAPAGPSGGPVAASAAPSIPAANMPPGSVEQVAAKVVPSVVMLETDLGRQSEEGSGIILSAEGLILTNNHVIAAAAKPPLGSPPPKTTVTFSDGRTAPFTVVGADPTSDIAVVRVQGVSGLTPISLGSSSDLRVGQPVLAIGSPLGLEGTVTTGIVSALNRPVSTTGEAGNQNTVLDAIQTDAAINPGNSGGALVNMNAQLVGVNSAIATLGADSADAQSGSIGLGFAIPVDQAKRIADELISTGKASHASLGVQVTNDKDTLGAKIVEVVAGGAAANAGVPKGVVVTKVDDRPINSADALVAAVRSKAPGATVALTFQDPSGGSRTVQVTLGKAEQ
|
3.4.21.107
| null |
cellular response to antibiotic [GO:0071236]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF13180;PF13365;
|
2.30.42.10;2.40.10.10;
|
Peptidase S1C family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:21445360}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:21445360}. Secreted {ECO:0000269|PubMed:21445360}. Note=Traffics from the cytoplasm through the cell membrane to the cell wall where it is autoprocessed and eventually secreted into the culture filtrate protein. {ECO:0000269|PubMed:21445360}.
|
CATALYTIC ACTIVITY: Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107; Evidence={ECO:0000269|PubMed:18479146, ECO:0000269|PubMed:20061478};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7.0 and 8.5. {ECO:0000269|PubMed:20061478};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:20061478};
|
FUNCTION: Required for virulence (PubMed:18479146). Acts both as a protease, which degrades and/or refolds damaged substrate targets, and as a chaperone (PubMed:18479146, PubMed:20061478). Plays an important role in the stress response network mediated through the two-component regulatory system MprAB and SigE signaling networks (PubMed:20061478). May utilize its PDZ domain to recognize and process misfolded proteins at the cell membrane, leading to activation of the MprAB and SigE signaling pathways and subsequent establishment of a positive feedback loop that facilitates bacterial adaptation (PubMed:20061478). Interacts with and potentially cleaves several proteins, including the 35 kDa antigen PspA (PubMed:21445360). Proteolytic cleavage of PspA may help to maintain cell envelope homeostasis in Mycobacterium and regulate specific stress response pathways during periods of extracytoplasmic stress (PubMed:21445360). In vitro, exhibits proteolytic activity against the artificial substrate beta-casein (PubMed:18479146, PubMed:20061478). {ECO:0000269|PubMed:18479146, ECO:0000269|PubMed:20061478, ECO:0000269|PubMed:21445360}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O53901
|
PKS5_MYCTU
|
MGKERTKTVDRTRVTPVAVIGMGCRLPGGIDSPDRLWEALLRGDDLVTEIPADRWDIDEYYDPEPGVPGRTDCKWGAYLDNVGDFDPEFFGIGEKEAIAIDPQHRLLLETSWEAMEHGGLTPNQMASRTGVFVGLVHTDYILVHADNQTFEGPYGNTGTNACFASGRVAYAMGLQGPAITVDTACSSGLTAIHLACRSLHDGESDIALAGGVYVMLEPRRFASGSALGMLSATGRCHAFDVSADGFVSGEGCVMLALKRLPDALADGDRILAVIRGTAANQDGHTVNIATPSRSAQVAAYREALDVAGVDPATVGMVEAHGPGTPVGDPIEYASLAEVYGNDGPCALASVKTNFGHTQSAAGALGLMKAVLALQHGVVPQNLHFTALPDKLAAIETNLFVPQEITPWPGADQETPRRAAVSSYGMTGTNVHAIVEQAPVPAPESGAPGDTPATPGIDGALLFALSASSQDALRQTAARLADWVDAQGPELAPADLAYTLARRRGHRPVRTAVLAATTAELTEALREVATGEPPYPPAVGQDDRGPVWVFSGQGSQWAGMGADLLATEPVFAATIAAIEPLIAAESGFSVTEAMTAPEVVTGIDRVQPTLFAMQVALAATMKSYGVAPGAVIGHSLGESAAAVVAGALCLEDGVRVICRRSALMTRIAGAGAMASVELPAQQVLSELMARGVNDAVVAVVASPQSTVIGGATQTVRDLVAAWEQRDVLAREVAVDVASHSPQVDPILDELAEALAEISPLQPEIPYYSATSFDPREEPYCDAYYWVDNLRHTVRFAAAVQAALEDGYRVFTELTPHPLLTHAVDQTARSLDMSAAALAGMRREQPLPHGLRALAGDLYAAGAAVDFAVLYPTGRLINAPLPTWNHRRLLLDDTTRRIAHANTVAVHPLLGSHVRLPEEPERHVWQGEVGTVTQPWLADHQIHGAAALPGAAYCEMALAAARAVLGEASEVRDIRFEQMLLLDDETPIGVTATVEAPGVVPLTVETSHDGRYTRQLAAVLHVVREADDAPDQPPQKNIAELLASHPHKVDGAEVRQWLDKRGHRLGPAFAGLVDAYIAEGAGDTVLAEVNLPGPLRSQVKAYGVHPVLLDACFQSVAAHPAVQGMADGGLLLPLGVRRLRSYGSARHARYCCTTVTACGVGVEADLDVLDEHGAVVLAVRGLQLGTGASQASERARVLGERLLSIEWHERELPENSHAEPGAWLLISTCDATDLVAAQLTDALKVHDAQCTTMSWPQRADHAAQAARLRDQLGTGGFTGVFVLTAPQTGDPDAESPVRGGELVKHVVRIAREIPEITAQEPRLYVLTHNAQAVLSGDRPNLEQGGMRGLLRVIGAEHPHLKASYVDVDEQTGAESVARQLLAASGEDETAWRNDQWYTARLCPAPLRPEERQTTVVDHAEAGMRLQIRTPGDLQTLEFAAFDRVPPGPGEIEVAVTASSINFADVLVTFGRYQTLDGRQPQLGTDFAGVVSAVGPGVSELKVGDRVGGMSPNGCWATFVTCDARLATRLPEGLTDAQAAAVTTASATAWYGLQDLARIKAGDKVLIHSATGGVGQAAIAIARAAGAQIYATAGNEKRRDLLRDMGIEHVYDSRSVEFAEQIRRDTAGYGVDIVLNSVTGAAQLAGLKLLALGGRFIEIGKRDIYSNTRLELLPFRRNLAFYGLDLGLMSVSHPAAVRELLSTVYRLTVEGVLPMPQSTHYPLAEAATAIRVMGAAEHTGKLILDVPHAGRSSVVLPPEQARVFRSDGSYIITGGLGGLGLFLAEKMANAGAGRIVLSSRSQPSQKALETIELVRAIGSDVVVECGDIAQPDTADRLVTAATATGLPLRGVLHAAAVVEDATLANITDELIERDWAPKAYGAWQLHRATADQPLDWFCSFSSAAALVGSPGQGAYAAANSWLDTFTHWRRAQDLPATSIAWGAWGQIGRAIAFAEQTGDAIAPEEGAYAFETLLRHNRAYSGYAPVIGSPWLTAFAQHSPFAEKFQSLGQNRSGTSKFLAELVDLPREEWPDRLRRLLSKQVGLILRRTIDTDRLLSEYGLDSLSSQELRARVEAETGIRISATEINTTVRGLADLMCDKLAADRDAPAPA
|
2.3.1.-
| null |
DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]
|
PF00698;PF08240;PF00107;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765;
|
3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
| null | null |
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000250|UniProtKB:A0R1E8}.
| null | null |
FUNCTION: Polyketide synthase likely involved in the biosynthesis of a polymethyl-branched fatty acid (PMB-FA) that might only be produced during host infection. Is required for the full virulence of M.tuberculosis during host infection. {ECO:0000269|PubMed:12855735, ECO:0000305}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O54003
|
REP75_PYRAB
|
MVIYTSKFKNSLLDGLGVGHLSYDDQPILCNEVHPTLTLDTFISGGSSGSRPRPRWVYLDISTTNEGISEEFSSNTESKSPLLKVCGVSSKSSEGDGSSFIWFDKYRSVISRLEHSGFVEVERTVLKLRKISKELRSINKQLSRLFLDDRERAKLLSRKRKYLDFARALIGSISKSLTLYADRFFVEVPQDYAKLIQKLGFSSDTLLLHLFVNSGVLEVFLDDNSSHKFRIAYISKVHAGKYHPVKGISKGSQEAKRVLRDLLVLSELLEGSLVSYRSGGVETIHHLIPVRHFVLTAPKELSFSIWASLKKGDSSLFRAFKDAGAKAIKEFLSYLASKEHISGNLLFGFTINVHVTGDKNPFEPHFHIDAIVTFICYDKSSTKWFRLNPLLSESDLKKLRDIWKNVLLSYFGELLSEDTKSKDFDVWAGDNYYSLPLDVPQVFFELKYASRKLFVNFVNYFEQSNFDESSVSDWDFVRFVFEYSNRTERYGFLTNIKRYLSMSCSHLVEKRVQELEEFISRIEFDLSVNGNKMSDSLKRALLERLEYLKDELSELKERGFEYLFERALEKAEELLSNDNLTLERVIHILETLFTALGKSIVNYNFYVELEDVSFREFVDYLYDNHLSDVLVFSDRHRSITIIRLIPPPDGGVPV
|
2.7.7.31; 3.1.21.-; 6.5.1.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9570403}; Note=DNA nicking and nucleotidyltransferase are strictly dependent on Mn(2+); Mg(2+) is able to substitute in DNA nicking 5X less efficiently. {ECO:0000269|PubMed:9570403};
|
DNA replication [GO:0006260]; plasmid maintenance [GO:0006276]
| null |
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; DNA nucleotidylexotransferase activity [GO:0003912]; DNA topoisomerase activity [GO:0003916]; endonuclease activity [GO:0004519]
| null | null |
Gram-positive plasmids replication protein type 1 family
|
PTM: The N-terminus is blocked when overexpressed in E.coli.
| null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.31; CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1;
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 105 degrees Celsius for ssDNA nicking, 75 degrees Celsius for nucleotidyltransferase activity on a ssDNA substrate. Optimum temperature for ssDNA closing is substrate dependent, being 55 and 75 degrees Celsius for the 2 substrates tested. Topoisomerase activity is only seen between 55 and 75 degrees Celsius. {ECO:0000269|PubMed:10417644, ECO:0000269|PubMed:9570403};
|
FUNCTION: Required for rolling circle plasmid replication, has a site-specific endonuclease/ligase activity (nicking and closing). In vitro (no in vivo system yet exists) cleaves the double-stranded origin of replication (dso) site, on an ssDNA template, remaining covalently linked to the 5' end. Religates the appropriate substrates. Has nucleotidyltransferase activity, adding ATP or dATP to the 3' end of the nicked ssDNA site. Both activities require a G nucleotide at the 3' end of the nicking site. Also has topoisomerase activity, nicking and relaxing negatively supercoiled plasmids in a narrow concentration range (25-50 molar ratio of protein:DNA). Topoisomerase is not dependent on a dso sequence. Has no topoisomerase activity on slightly positively supercoiled plasmid. {ECO:0000269|PubMed:10417644, ECO:0000269|PubMed:10871346, ECO:0000269|PubMed:9570403}.
|
Pyrococcus abyssi (strain GE5 / Orsay)
|
O54259
|
SNOAB_STRNO
|
MPTRVNDGVDADEVTFVNRFTVHGGPAEFESVFARTAAFFARQPGFVRHTLLRERDKDNSYVNIAVWTDHDAFRRALAQPGFLPHATALRALSTSEHGLFTARQTLPEGGDTTGSGHR
|
1.13.12.22
| null |
antibiotic biosynthetic process [GO:0017000]
| null |
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases) [GO:0016703]
|
PF03992;
|
3.30.70.100;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=deoxynogalonate + O2 = H(+) + H2O + nogalonate; Xref=Rhea:RHEA:45056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:84897, ChEBI:CHEBI:84900; EC=1.13.12.22; Evidence={ECO:0000305|PubMed:19255477, ECO:0000305|PubMed:20052967};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=140 uM for dithranol {ECO:0000269|PubMed:20052967}; Vmax=6.3 umol/min/mg enzyme with dithranol as substrate {ECO:0000269|PubMed:20052967}; Note=kcat is 1.5 sec(-1) for monooxygenase activity with dithranol as substrate. {ECO:0000269|PubMed:20052967};
|
PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:8760909}.
| null | null |
FUNCTION: Involved in the biosynthesis of the anthracycline (aromatic polyketide) antibiotic nogalamycin (PubMed:8668120, PubMed:8760909). Catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to yield nogalonic acid (PubMed:19255477, PubMed:20052967). {ECO:0000269|PubMed:8668120, ECO:0000269|PubMed:8760909, ECO:0000305|PubMed:19255477, ECO:0000305|PubMed:20052967}.
|
Streptomyces nogalater
|
O54288
|
KDGA_SACSO
|
MPEIITPIITPFTKDNRIDKEKLKIHAENLIRKGIDKLFVNGTTGLGPSLSPEEKLENLKAVYDVTNKIIFQVGGLNLDDAIRLAKLSKDFDIVGIASYAPYYYPRMSEKHLVKYFKTLCEVSPHPVYLYNYPTATGKDIDAKVAKEIGCFTGVKDTIENIIHTLDYKRLNPNMLVYSGSDMLIATVASTGLDGNVAAGSNYLPEVTVTIKKLAMERKIDEALKLQFLHDEVIEASRIFGSLSSNYVLTKYFQGYDLGYPRPPIFPLDDEEERQLIKKVEGIRAKLVELKILKE
|
4.1.2.55
| null |
glyoxylate catabolic process [GO:0009436]
|
cytosol [GO:0005829]
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity [GO:0008674]; 2-dehydro-3-deoxy-phosphogluconate aldolase activity [GO:0008675]; 4-hydroxy-2-oxoglutarate aldolase activity [GO:0008700]; 4-hydroxy-tetrahydrodipicolinate synthase activity [GO:0008840]
|
PF00701;
|
3.20.20.70;
|
DapA family, KDPG aldolase subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-phosphate + pyruvate; Xref=Rhea:RHEA:17089, ChEBI:CHEBI:15361, ChEBI:CHEBI:57569, ChEBI:CHEBI:59776; EC=4.1.2.55; Evidence={ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170}; CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-6-phospho-D-galactonate = D-glyceraldehyde 3-phosphate + pyruvate; Xref=Rhea:RHEA:24464, ChEBI:CHEBI:15361, ChEBI:CHEBI:58298, ChEBI:CHEBI:59776; EC=4.1.2.55; Evidence={ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for KDPG (at 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; KM=0.17 mM for KDPGal (at 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; KM=3.9 mM for pyruvate (at 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; KM=3.9 mM for D-glyceraldehyde (at 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; KM=5.2 mM for D,L-glyceraldehyde (at 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; KM=7.1 mM for L-glyceraldehyde (at 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; KM=9.9 mM for KDGal (at 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; KM=25.7 mM for KDG (at 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; Vmax=12.3 umol/min/mg enzyme with KDGal as substrate (at 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; Vmax=15.7 umol/min/mg enzyme with pyruvate as substrate (at 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; Vmax=17.1 umol/min/mg enzyme with D,L-glyceraldehyde as substrate (at 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; Vmax=18 umol/min/mg enzyme with D-glyceraldehyde as substrate (at 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; Vmax=18 umol/min/mg enzyme with L-glyceraldehyde as substrate (at 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; Vmax=51.4 umol/min/mg enzyme with KDG as substrate (at 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; Note=kcat is 28.2 sec(-1) for KDG and 6.8 sec(-1) for KDGal.;
|
PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 2/2.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Extremely thermostable. {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030};
|
FUNCTION: Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal). It is equally active with both D- and L-glyceraldehyde. {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}.
|
Saccharolobus solfataricus (Sulfolobus solfataricus)
|
O54329
|
LANA_STRMG
|
MNKLNSNAVVSLNEVSDSELDTILGGNRWWQGVVPTVSYECRMNSWQHVFTCC
| null | null |
amino acid transport [GO:0006865]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; regulation of membrane potential [GO:0042391]
|
extracellular region [GO:0005576]
|
signaling receptor binding [GO:0005102]
|
PF04604;
| null |
Type A lantibiotic family
|
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor. {ECO:0000305}.; PTM: It is not established whether the 2,3-didehydrobutyrine is the E- or Z-isomer (PubMed:10821848, PubMed:16626493, PubMed:8021218, PubMed:8660519, PubMed:9647795).
| null | null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Stable from pH 2.0 to 4.0. Activity decreases gradually with increasing pH. {ECO:0000269|PubMed:16626493, ECO:0000269|PubMed:8021218};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:16626493, ECO:0000269|PubMed:8021218};
|
FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria including M.luteus, S.aureus, Streptococcus, P.micros, P.acidilactici, C.sporogenes, C.diphtheriae, A.viscosus, G.vaginalis, P.acnes, L.monocytogenes and M.smegmatis, and Gram-negative bacteria including C.jejuni, H.pylori and N.gonorrhoeae. Transiently and partially depolarizes the transmembrane electrical potential and pH gradient of susceptible cells, inhibits the uptake of amino acids and depletes the intracellular ATP pool. {ECO:0000269|PubMed:16626493, ECO:0000269|PubMed:8021218, ECO:0000269|PubMed:8592997}.
|
Streptococcus mutans
|
O54408
|
RELA_BACSU
|
MANEQVLTAEQVIDKARSYLSDEHIAFVEKAYLYAEDAHREQYRKSGEPYIIHPIQVAGILVDLEMDPSTIAGGFLHDVVEDTDVTLDDLKEAFSEEVAMLVDGVTKLGKIKYKSQEEQQAENHRKMFVAMAQDIRVILIKLADRLHNMRTLKHLPQEKQRRISNETLEIFAPLAHRLGISKIKWELEDTALRYLNPQQYYRIVNLMKKKRAERELYVDEVVNEVKKRVEEVNIKADFSGRPKHIYSIYRKMVLQNKQFNEIYDLLAVRILVNSIKDCYAVLGIIHTCWKPMPGRFKDYIAMPKPNMYQSLHTTVIGPKGDPLEVQIRTFEMHEIAEYGVAAHWAYKEGKAANEGATFEKKLSWFREILEFQNESTDAEEFMESLKIDLFSDMVYVFTPKGDVIELPSGSVPIDFSYRIHSEIGNKTIGAKVNGKMVTLDHKLRTGDIVEILTSKHSYGPSQDWVKLAQTSQAKHKIRQFFKKQRREENVEKGRELVEKEIKNLDFELKDVLTPENIQKVADKFNFSNEEDMYAAVGYNGITALQVANRLTEKERKQRDQEEQEKIVQEVTGEPKPYPQGRKREAGVRVKGIDNLLVRLSKCCNPVPGDDIVGFITKGRGVSVHREDCPNVKTNEAQERLIPVEWEHESQVQKRKEYNVEIEILGYDRRGLLNEVLQAVNETKTNISSVSGKSDRNKVATIHMAIFIQNINHLHKVVERIKQIRDIYSVRRVMN
|
2.7.6.5
| null |
guanosine tetraphosphate biosynthetic process [GO:0015970]; phosphorylation [GO:0016310]; response to starvation [GO:0042594]
|
plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; GTP binding [GO:0005525]; GTP diphosphokinase activity [GO:0008728]; guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity [GO:0008893]; kinase activity [GO:0016301]
|
PF13291;PF13328;PF19296;PF04607;PF02824;
|
3.10.20.30;3.30.70.260;3.30.460.10;1.10.3210.10;
|
RelA/SpoT family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate; Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
| null |
PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2.
| null | null |
FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp, it is probably the hydrolysis activity that is required for optimal growth (Probable). {ECO:0000250, ECO:0000305|PubMed:18067544}.
|
Bacillus subtilis (strain 168)
|
O54581
|
DSPE_ERWAM
|
MELKSLGTEHKAAVHTAAHNPVGHGVALQQGSSSSSPQNAAASLAAEGKNRGKMPRIHQPSTAADGISAAHQQKKSFSLRGCLGTKKFSRSAPQGQPGTTHSKGATLRDLLARDDGETQHEAAAPDAARLTRSGGVKRRNMDDMAGRPMVKGGSGEDKVPTQQKRHQLNNFGQMRQTMLSKMAHPASANAGDRLQHSPPHIPGSHHEIKEEPVGSTSKATTAHADRVEIAQEDDDSEFQQLHQQRLARERENPPQPPKLGVATPISARFQPKLTAVAESVLEGTDTTQSPLKPQSMLKGSGAGVTPLAVTLDKGKLQLAPDNPPALNTLLKQTLGKDTQHYLAHHASSDGSQHLLLDNKGHLFDIKSTATSYSVLHNSHPGEIKGKLAQAGTGSVSVDGKSGKISLGSGTQSHNKTMLSQPGEAHRSLLTGIWQHPAGAARPQGESIRLHDDKIHILHPELGVWQSADKDTHSQLSRQADGKLYALKDNRTLQNLSDNKSSEKLVDKIKSYSVDQRGQVAILTDTPGRHKMSIMPSLDASPESHISLSLHFADAHQGLLHGKSELEAQSVAISHGRLVVADSEGKLFSAAIPKQGDGNELKMKAMPQHALDEHFGHDHQISGFFHDDHGQLNALVKNNFRQQHACPLGNDHQFHPGWNLTDALVIDNQLGLHHTNPEPHEILDMGHLGSLALQEGKLHYFDQLTKGWTGAESDCKQLKKGLDGAAYLLKDGEVKRLNINQSTSSIKHGTENVFSLPHVRNKPEPGDALQGLNKDDKAQAMAVIGVNKYLALTEKGDIRSFQIKPGTQQLERPAQTLSREGISGELKDIHVDHKQNLYALTHEGEVFHQPREAWQNGAESSSWHKLALPQSESKLKSLDMSHEHKPIATFEDGSQHQLKAGGWHAYAAPERGPLAVGTSGSQTVFNRLMQGVKGKVIPGSGLTVKLSAQTGGMTGAEGRKVSSKFSERIRAYAFNPTMSTPRPIKNAAYATQHGWQGREGLKPLYEMQGALIKQLDAHNVRHNAPQPDLQSKLETLDLGEHGAELLNDMKRFRDELEQSATRSVTVLGQHQGVLKSNGEINSEFKPSPGKALVQSFNVNRSGQDLSKSLQQAVHATPPSAESKLQSMLGHFVSAGVDMSHQKGEIPLGRQRDPNDKTALTKSRLILDTVTIGELHELADKAKLVSDHKPDADQIKQLRQQFDTLREKRYESNPVKHYTDMGFTHNKALEANYDAVKAFINAFKKEHHGVNLTTRTVLESQGSAELAKKLKNTLLSLDSGESMSFSRSYGGGVSTVFVPTLSKKVPVPVIPGAGITLDRAYNLSFSRTSGGLNVSFGRDGGVSGNIMVATGHDVMPYMTGKKTSAGNASDWLSAKHKISPDLRIGAAVSGTLQGTLQNSLKFKLTEDELPGFIHGLTHGTLTPAELLQKGIEHQMKQGSKLTFSVDTSANLDLRAGINLNEDGSKPNGVTARVSAGLSASANLAAGSRERSTTSGQFGSTTSASNNRPTFLNGVGAGANLTAALGVAHSSTHEGKPVGIFPAFTSTNVSAALALDNRTSQSISLELKRAEPVTSNDISELTSTLGKHFKDSATTKMLAALKELDDAKPAEQLHILQQHFSAKDVVGDERYEAVRNLKKLVIRQQAADSHSMELGSASHSTTYNNLSRINNDGIVELLHKHFDAALPASSAKRLGEMMNNDPALKDIIKQLQSTPFSSASVSMELKDGLREQTEKAILDGKVGREEVGVLFQDRNNLRVKSVSVSQSVSKSEGFNTPALLLGTSNSAAMSMERNIGTINFKYGQDQNTPRRFTLEGGIAQANPQVASALTDLKKEGLEMKS
| null | null | null |
extracellular region [GO:0005576]; host cell [GO:0043657]
| null |
PF11725;
| null |
AvrE family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18705858, ECO:0000269|PubMed:19737101, ECO:0000269|PubMed:20110301, ECO:0000269|PubMed:9426142, ECO:0000269|PubMed:9555912}. Host cell {ECO:0000269|PubMed:18705858, ECO:0000269|PubMed:19737101, ECO:0000269|PubMed:20110301}. Note=Secreted via the Hrp type III secretion system (T3SS) (PubMed:18705858, PubMed:19737101, PubMed:20110301, PubMed:9426142, PubMed:9555912). Translocated into the plant cells (PubMed:18705858, PubMed:19737101, PubMed:20110301). Gaudriault et al. observed that the chaperone DspF is required for secretion, but a more recent study by Oh et al. showed that short lengths of the N-terminal portion of DspE could be secreted in the absence of DspF (PubMed:20110301, PubMed:9426142). Translocation of DspE into plant cells is strongly enhanced in the presence of DspF (PubMed:20110301). HrpJ and HrpN are required for efficient translocation, but not for expression and secretion of DspE (PubMed:18705858). {ECO:0000269|PubMed:18705858, ECO:0000269|PubMed:19737101, ECO:0000269|PubMed:20110301, ECO:0000269|PubMed:9426142, ECO:0000269|PubMed:9555912}.
| null | null | null | null | null |
FUNCTION: Major virulence factor that may function as a water- and solute-permeable channel dedicated to creating osmotic/water potential perturbation and a water- and nutrient-rich apoplast in which bacteria multiply within the infected plant tissues (PubMed:37704725). Expression in Xenopus oocytes results in inward and outward currents, permeability to water and osmolarity-dependent oocyte swelling and bursting (PubMed:37704725). {ECO:0000269|PubMed:37704725}.; FUNCTION: Acts as a major cell-death inducer during fire blight, a necrotic disease affecting plants of the rosaceous family, and during hypersensitive response (HR) on non-host plants (PubMed:16404949). Essential for pathogenicity on host plants (PubMed:16404949, PubMed:19737101, PubMed:9426142, PubMed:9448330). Contributes quantitatively and in a strain-dependent fashion to HR elicitation in non-host plants such as tobacco (PubMed:9448330). Induces cell death in leaves of apple, a host plant, and tobacco, a non-host plant (PubMed:16404949). Also triggers necrosis in the widely used model, non-host, N.benthamiana and in yeast (PubMed:20507497). Required for the transient multiplication and survival of E.amylovora in non-host A.thaliana leaves (PubMed:23634775). In A.thaliana, triggers electrolyte leakage, activation of defense pathways, reactive oxygen species (ROS) accumulation and cell death (PubMed:18616404, PubMed:23634775). The toxicity of DspE in A.thaliana is associated with an early repression of de novo protein synthesis (PubMed:23634775). {ECO:0000269|PubMed:16404949, ECO:0000269|PubMed:18616404, ECO:0000269|PubMed:19737101, ECO:0000269|PubMed:20507497, ECO:0000269|PubMed:23634775, ECO:0000269|PubMed:9426142, ECO:0000269|PubMed:9448330}.
|
Erwinia amylovora (Fire blight bacteria)
|
O54689
|
CCR6_MOUSE
|
MNSTESYFGTDDYDNTEYYSIPPDHGPCSLEEVRNFTKVFVPIAYSLICVFGLLGNIMVVMTFAFYKKARSMTDVYLLNMAITDILFVLTLPFWAVTHATNTWVFSDALCKLMKGTYAVNFNCGMLLLACISMDRYIAIVQATKSFRVRSRTLTHSKVICVAVWFISIIISSPTFIFNKKYELQDRDVCEPRYRSVSEPITWKLLGMGLELFFGFFTPLLFMVFCYLFIIKTLVQAQNSKRHRAIRVVIAVVLVFLACQIPHNMVLLVTAVNTGKVGRSCSTEKVLAYTRNVAEVLAFLHCCLNPVLYAFIGQKFRNYFMKIMKDVWCMRRKNKMPGFLCARVYSESYISRQTSETVENDNASSFTM
| null | null |
calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; chemotaxis [GO:0006935]; DN2 thymocyte differentiation [GO:1904155]; DN3 thymocyte differentiation [GO:1904156]; immune response [GO:0006955]; isotype switching to IgA isotypes [GO:0048290]; leukocyte migration involved in inflammatory response [GO:0002523]; lymphocyte migration [GO:0072676]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of dendritic cell chemotaxis [GO:2000510]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of flagellated sperm motility involved in capacitation [GO:0060474]; regulation of T cell migration [GO:2000404]; T cell migration [GO:0072678]; thymocyte migration [GO:0072679]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; sperm flagellum [GO:0036126]; sperm midpiece [GO:0097225]; sperm plasma membrane [GO:0097524]; sperm principal piece [GO:0097228]
|
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23765988}; Multi-pass membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P51684}.
| null | null | null | null | null |
FUNCTION: Receptor for the C-C type chemokine CCL20. Binds to CCL20 and subsequently transduces a signal by increasing the intracellular calcium ion levels (PubMed:20068036). Although CCL20 is its major ligand it can also act as a receptor for non-chemokine ligands such as beta-defensins (PubMed:25122636). Binds to defensin DEFB1 leading to increase in intracellular calcium ions and cAMP levels. Its binding to DEFB1 is essential for the function of DEFB1 in regulating sperm motility and bactericidal activity (By similarity). Binds to defensins DEFB4 and DEFB4A/B and mediates their chemotactic effects (PubMed:20068036). The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases. CCR6-mediated signals are essential for immune responses to microbes in the intestinal mucosa and in the modulation of inflammatory responses initiated by tissue insult and trauma (PubMed:21376174). CCR6 is essential for the recruitment of both the pro-inflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation (PubMed:19050256). Required for the normal migration of Th17 cells in Peyers patches and other related tissue sites of the intestine and plays a role in regulating effector T-cell balance and distribution in inflamed intestine (PubMed:19129757). Plays an important role in the coordination of early thymocyte precursor migration events important for normal subsequent thymocyte precursor development, but is not required for the formation of normal thymic natural regulatory T-cells (nTregs). Required for optimal differentiation of DN2 and DN3 thymocyte precursors (PubMed:24638065). Essential for B-cell localization in the subepithelial dome of Peyers-patches and for efficient B-cell isotype switching to IgA in the Peyers-patches (PubMed:27174992). Essential for appropriate anatomical distribution of memory B-cells in the spleen and for the secondary recall response of memory B-cells (PubMed:25505290). Positively regulates sperm motility and chemotaxis via its binding to CCL20 (PubMed:23765988). {ECO:0000250|UniProtKB:P51684, ECO:0000269|PubMed:19050256, ECO:0000269|PubMed:19129757, ECO:0000269|PubMed:20068036, ECO:0000269|PubMed:23765988, ECO:0000269|PubMed:24638065, ECO:0000269|PubMed:25122636, ECO:0000269|PubMed:25505290, ECO:0000269|PubMed:27174992, ECO:0000303|PubMed:21376174}.
|
Mus musculus (Mouse)
|
O54692
|
ZW10_MOUSE
|
MASFVTEVLAHSGSLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPTMQSAQALVTQVDTLSNDIDQLKSRIETEVCRDLHISTVEFTNLKQQLERDSVVLTLLKQLQEFSSAIEEYNSALAEKKYIPAARHLEEAQECLKLLKSRKCFDLKMLKSLSMELTVQKQNILYHLGEDWQKLVVWKFPPAKDTSSLESCLQTELHLCTEQPEKEDMTPLPSISSVLLAFSILGELPTKLKSFGQMLLKYILKPLVTCPSLHAVIERQPSSVSICFESLTTDLEHPSPPEAFAKIRLVLEVLQKQLLDLPLDADLEIGKVPGIVLAEMLGEGIWEDLSECLIRNCLVYSIPTNSSKLQEYEEIIQSTEEFEKFLKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARNLMTSEIHNTVKIGPDCKEALPDLPSPDADHKLQVQTVCKAQFTDAGNLEPETSLDPQSFSLPTCRISEAVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLRKLPQLAAIHHNNCMYIAHHLLTLGHQFRLRLAPILCDGTTTFVDLVPGFRRLGTECFLAQMQAQKGELLERLSSARSFANMDDEENYSAASKAVRQVLHQLRRLGIVWQDVLPVNIYCKAMGTLLNTAIAEMMSRITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSDENKNKKYQEEVPVYVSKWMPFKELMIMLQASLQEIGDRWADGKGPLATAFPSSEVKALIRALFQNTERRAAALAKIK
| null | null |
cell division [GO:0051301]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; establishment of mitotic spindle orientation [GO:0000132]; Golgi organization [GO:0007030]; mitotic metaphase chromosome alignment [GO:0007080]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; protein localization to kinetochore [GO:0034501]; protein transport [GO:0015031]; protein-containing complex assembly [GO:0065003]; regulation of exit from mitosis [GO:0007096]
|
cytosol [GO:0005829]; Dsl1/NZR complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; lipid droplet [GO:0005811]; nucleus [GO:0005634]; RZZ complex [GO:1990423]; spindle pole [GO:0000922]
| null |
PF20666;PF20665;PF06248;
|
1.10.357.150;
|
ZW10 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43264}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43264}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43264}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O43264}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43264}. Lipid droplet {ECO:0000250|UniProtKB:O43264}. Note=Dynamic pattern of localization during the cell cycle. In most cells at interphase, present diffusely in the cytoplasm. In prometaphase, associated with the kinetochore. At metaphase, detected both at the kinetochores and, most prominently, at the spindle, particularly at the spindle poles. In very early anaphase, detected on segregating kinetochores. In late anaphase and telophase, accumulates at the spindle midzone. {ECO:0000250|UniProtKB:O43264}.
| null | null | null | null | null |
FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (By similarity). {ECO:0000250|UniProtKB:O43264}.
|
Mus musculus (Mouse)
|
O54693
|
EDA_MOUSE
|
MGYPEVERREPLPAAAPRERGSQGCGCRGAPARAGEGNSCRLFLGFFGLSLALHLLTLCCYLELRSELRRERGTESRLGGPGAPGTSGTLSSPGSLDPVGPITRHLGQPSFQQQPLEPGEDPLPPDSQDRHQMALLNFFFPDEKAYSEEESRRVRRNKRSKSGEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKTGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKIAVKMVHADISINMSKHTTFFGAIRLGEAPAS
| null | null |
animal organ development [GO:0048513]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; cell-matrix adhesion [GO:0007160]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; hair follicle development [GO:0001942]; hair follicle placode formation [GO:0060789]; immune response [GO:0006955]; odontogenesis of dentin-containing tooth [GO:0042475]; pigmentation [GO:0043473]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of gene expression [GO:0010628]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; regulation of non-canonical NF-kappaB signal transduction [GO:1901222]; salivary gland cavitation [GO:0060662]; skin development [GO:0043588]; trachea gland development [GO:0061153]
|
apical part of cell [GO:0045177]; collagen trimer [GO:0005581]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886]
|
death receptor agonist activity [GO:0038177]; death receptor binding [GO:0005123]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:10534613}.; PTM: Processing by furin produces a secreted form. {ECO:0000250|UniProtKB:Q92838}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10534613}; Single-pass type II membrane protein {ECO:0000269|PubMed:10534613}.; SUBCELLULAR LOCATION: [Ectodysplasin-A, secreted form]: Secreted {ECO:0000250|UniProtKB:Q92838}.
| null | null | null | null | null |
FUNCTION: Cytokine which is involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Functions as a ligand activating the DEATH-domain containing receptors EDAR and EDA2R. Isoform TAA binds only to the receptor EDAR, while isoform TA-A2 binds exclusively to the receptor EDA2R (By similarity). May also play a role in cell adhesion (PubMed:10534613). {ECO:0000250|UniProtKB:Q92838, ECO:0000269|PubMed:10534613}.; FUNCTION: Isoform TAA binds only to the receptor EDAR, while isoform TA-A2 binds exclusively to the receptor EDA2R. {ECO:0000250|UniProtKB:Q92838}.; FUNCTION: Isoform TA-A2 binds exclusively to the receptor EDA2R. {ECO:0000250|UniProtKB:Q92838}.
|
Mus musculus (Mouse)
|
O54695
|
SPTC1_CRIGR
|
MAMAAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSKNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKAAALASLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMRTEEAIIYSYGFSTIASAIPAYSKRGDIVFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTVCPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKKKCQHIHKSLQGISGLKVVGESLSPALHLQLEESTGSREKDVQLLQEMVIHCMNEGIALTQARYLDKEEKCLPPPSIRVVVTVEQTEEELERAASTIREAAQAVLL
|
2.3.1.50
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250};
|
ceramide biosynthetic process [GO:0046513]; positive regulation of lipophagy [GO:1904504]; regulation of fat cell apoptotic process [GO:1904649]; sphinganine biosynthetic process [GO:0046511]; sphingomyelin biosynthetic process [GO:0006686]; sphingosine biosynthetic process [GO:0046512]
|
endoplasmic reticulum membrane [GO:0005789]; serine C-palmitoyltransferase complex [GO:0017059]; SPOTS complex [GO:0035339]
|
pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-II pyridoxal-phosphate-dependent aminotransferase family
|
PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell survival. {ECO:0000250|UniProtKB:O15269}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12464627}; Single-pass membrane protein {ECO:0000269|PubMed:12464627}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762; Evidence={ECO:0000250|UniProtKB:O15269}; CATALYTIC ACTIVITY: Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine + CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:65073; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684; Evidence={ECO:0000250|UniProtKB:O15269}; CATALYTIC ACTIVITY: Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-oxohexadecasphinganine + CO2 + CoA; Xref=Rhea:RHEA:35675, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:71007; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676; Evidence={ECO:0000250|UniProtKB:O15269}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-oxotetradecasphinganine + CO2 + CoA; Xref=Rhea:RHEA:35679, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:71008; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680; Evidence={ECO:0000250|UniProtKB:O15269};
| null |
PATHWAY: Lipid metabolism; sphingolipid metabolism.
| null | null |
FUNCTION: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is also composed of SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer with SPTLC2 or SPTLC3 forms the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (By similarity). Required for adipocyte cell viability and metabolic homeostasis (By similarity). {ECO:0000250|UniProtKB:O15269, ECO:0000250|UniProtKB:O35704}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O54697
|
NALDL_RAT
|
MHWAKILGVGIGAAALLGLGIILGHFAIPKATEPLASSVSDSQDLDLAILDSVMGQLDASRIRENLRELSKEPHVATSARDEALVQLLLGRWKDSASGLDTAKTYEYTVLLSFPSTEQPNSVEVVGPNGTVFHSFQPFEKNLTGEQAEPNVLQPYAAYAPPGTPKGPLVYANRGSEDDFKKLEAEGINLKGTIALTRYGSVGRGAKAINAARHGVVGVLVYTDPGDINDGKSLPNETFPNSWGLPPSGVERGSYYEYFGDPLTPYLPAHPVSFRLDPHNISGFPPIPTQPIGFEDAKNLLCNLNGTSAPDSWQGALGCEYKLGPGFEPNGNFPAGSEVKVSVYNRLELRNSSNVLGIIQGAVEPDRYVIYGNHRDSWVHGAVDPSSGTAVLLEISRVLGTLLKKGTWRPRRSIIFASWGAEEFGLIGSTEFTEEFLSKLQERTVTYINVDISVFSNATLRAQGTPPVQSVIFSATKEISAPGSSGLSIYDNWIRYTNRSSPVYGLVPSMGTLGAGSDYASFIHFLGITSMDLAYTYDRSKTSARIYPTYHTAFDTFDYVEKFLDPGFSSHQAVARTAGSVLLRLSDSLFLPLNVSDYSETLQSFLQAAQENLGALLESHNISLGPLVTAVEKFKAAAAALNQHILTLQKSSPDPLQVRMVNDQLMLLERAFLNPRAFPEERYYSHVLWAPNTASVATFPGLANAYARAQEINSGAEAWAEVERQLSIAVMALEGAAATLQPVTDL
|
3.4.11.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9UQQ1}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UQQ1};
|
peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]
|
apical plasma membrane [GO:0016324]; membrane [GO:0016020]
|
aminopeptidase activity [GO:0004177]; calcium ion binding [GO:0005509]; carboxypeptidase activity [GO:0004180]; metallopeptidase activity [GO:0008237]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]
|
PF02225;PF04389;PF04253;
|
3.50.30.30;1.20.930.40;3.40.630.10;
|
Peptidase M28 family, M28B subfamily
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9388249}.
|
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9388249}; Single-pass type II membrane protein {ECO:0000305|PubMed:9388249}. Note=Ileal brush border membrane. {ECO:0000269|PubMed:9388249}.
| null | null | null | null | null |
FUNCTION: Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity. {ECO:0000250|UniProtKB:Q9UQQ1}.
|
Rattus norvegicus (Rat)
|
O54698
|
S29A1_RAT
|
MTTSHQPQDRYKAVWLIFFVLGLGTLLPWNFFITATQYFTSRLNTSQNISLVTNQSCESTEALADPSVSLPARSSLSAIFNNVMTLCAMLPLLIFTCLNSFLHQKVSQSLRILGSLLAILLVFLVTATLVKVQMDALSFFIITMIKIVLINSFGAILQASLFGLAGVLPANYTAPIMSGQGLAGFFTSVAMICAVASGSKLSESAFGYFITACAVVILAILCYLALPWMEFYRHYLQLNLAGPAEQETKLDLISEGEEPRGGREESGVPGPNSLPANRNQSIKAILKSIWVLALSVCFIFTVTIGLFPAVTAEVESSIAGTSPWKNCYFIPVACFLNFNVFDWLGRSLTAICMWPGQDSRWLPVLVACRVVFIPLLMLCNVKQHHYLPSLFKHDVWFITFMAAFAFSNGYLASLCMCFGPKKVKPAEAETAGNIMSFFLCLGLALGAVLSFLLRALV
| null | null |
adenine transport [GO:0015853]; adenosine transport [GO:0032238]; cellular response to glucose stimulus [GO:0071333]; cellular response to hypoxia [GO:0071456]; cytidine transport [GO:0015861]; excitatory postsynaptic potential [GO:0060079]; guanine transmembrane transport [GO:1903716]; hypoxanthine transport [GO:0035344]; inosine transport [GO:0035340]; lactation [GO:0007595]; neurotransmitter transport [GO:0006836]; neurotransmitter uptake [GO:0001504]; nucleobase transport [GO:0015851]; nucleoside transmembrane transport [GO:1901642]; nucleoside transport [GO:0015858]; purine nucleobase transmembrane transport [GO:1904823]; purine nucleoside transmembrane transport [GO:0015860]; pyrimidine nucleobase transmembrane transport [GO:1904082]; pyrimidine-containing compound transmembrane transport [GO:0072531]; thymine transport [GO:0035364]; uracil transmembrane transport [GO:1903791]; uridine transport [GO:0015862]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793]
|
adenine transmembrane transporter activity [GO:0015207]; cytidine transmembrane transporter activity [GO:0015212]; guanine transmembrane transporter activity [GO:0015208]; neurotransmitter transmembrane transporter activity [GO:0005326]; nucleoside transmembrane transporter activity [GO:0005337]; purine nucleoside transmembrane transporter activity [GO:0015211]; pyrimidine- and adenosine-specific:sodium symporter activity [GO:0015389]; uracil transmembrane transporter activity [GO:0015210]; uridine transmembrane transporter activity [GO:0015213]
|
PF01733;
| null |
SLC29A/ENT transporter (TC 2.A.57) family
| null |
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:23639800}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:Q99808}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11584005}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the basolateral membrane of Sertoli cells. {ECO:0000269|PubMed:23639800}.
|
CATALYTIC ACTIVITY: Reaction=adenosine(in) = adenosine(out); Xref=Rhea:RHEA:75343, ChEBI:CHEBI:16335; Evidence={ECO:0000269|PubMed:17379602}; CATALYTIC ACTIVITY: Reaction=guanosine(in) = guanosine(out); Xref=Rhea:RHEA:75371, ChEBI:CHEBI:16750; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=inosine(in) = inosine(out); Xref=Rhea:RHEA:75375, ChEBI:CHEBI:17596; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=uridine(out) = uridine(in); Xref=Rhea:RHEA:71519, ChEBI:CHEBI:16704; Evidence={ECO:0000269|PubMed:23639800}; CATALYTIC ACTIVITY: Reaction=thymidine(in) = thymidine(out); Xref=Rhea:RHEA:75363, ChEBI:CHEBI:17748; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=cytidine(in) = cytidine(out); Xref=Rhea:RHEA:75367, ChEBI:CHEBI:17562; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=adenine(out) = adenine(in); Xref=Rhea:RHEA:71523, ChEBI:CHEBI:16708; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=guanine(out) = guanine(in); Xref=Rhea:RHEA:71531, ChEBI:CHEBI:16235; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=thymine(out) = thymine(in); Xref=Rhea:RHEA:71527, ChEBI:CHEBI:17821; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=uracil(in) = uracil(out); Xref=Rhea:RHEA:69404, ChEBI:CHEBI:17568; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=hypoxanthine(out) = hypoxanthine(in); Xref=Rhea:RHEA:71515, ChEBI:CHEBI:17368; Evidence={ECO:0000250|UniProtKB:Q99808};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.4 uM for adenosine {ECO:0000269|PubMed:17379602}; Vmax=530 pmol/min/mg enzyme {ECO:0000269|PubMed:17379602};
| null | null | null |
FUNCTION: Uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis (PubMed:9353301). Functions as a Na(+)-independent transporter (By similarity). Involved in the transport of nucleosides such as adenosine, thymidine and uridine (PubMed:23639800, PubMed:9353301). Also transports purine nucleobases (hypoxanthine, adenine, guanine) and pyrimidine nucleobases (thymine, uracil) (By similarity). Mediates basolateral nucleoside uptake into Sertoli cells, thereby regulating the transport of nucleosides in testis across the blood-testis barrier (PubMed:23639800). Regulates inosine levels in brown adipocytes tissues (BAT) and extracellular inosine levels, which controls BAT-dependent energy expenditure (By similarity). {ECO:0000250|UniProtKB:Q99808, ECO:0000269|PubMed:23639800, ECO:0000269|PubMed:9353301}.
|
Rattus norvegicus (Rat)
|
O54699
|
S29A2_RAT
|
MAHGNAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQGRLAGTNSSAETPSTNHTSPTDTFNFNNWVTLLSQLPLLLFTLLNSFLYQCIPESVRILGSLLAILLLFALTAALVKVDLSPGLFFSITMASVWFINSFCAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLTSLASGVDPQTSALGYFITPCVGILLSIICYLSLPHLKFARYYLTKKPQAPVQELETKAELLGADEKNGIPVSPQQAGPTLDLDPEKELELGLEEPQKPGKPSVFVVFRKIWLTALCLVLVFTVTLSVFPAITAMVTTSSNSPGKWSQFFNPICCFLLFNVMDWLGRSLTSYFLWPDEDSQLLPLLVCLRFLFVPLFMLCHVPQRARLPIIFWQDAYFITFMLLFAISNGYFVSLTMCLAPRQVLPHEREVAGALMTFFLALGLSCGASLSFLFKALL
| null | null |
adenine transport [GO:0015853]; adenosine transport [GO:0032238]; cellular response to insulin stimulus [GO:0032869]; cytidine transport [GO:0015861]; guanine transmembrane transport [GO:1903716]; guanine transport [GO:0015854]; hypoxanthine transport [GO:0035344]; inosine transport [GO:0035340]; lactation [GO:0007595]; neurotransmitter transport [GO:0006836]; neurotransmitter uptake [GO:0001504]; nucleobase transport [GO:0015851]; nucleoside transmembrane transport [GO:1901642]; nucleoside transport [GO:0015858]; purine nucleobase transmembrane transport [GO:1904823]; purine nucleoside transmembrane transport [GO:0015860]; pyrimidine-containing compound transmembrane transport [GO:0072531]; thymine transport [GO:0035364]; uracil transmembrane transport [GO:1903791]; uridine transport [GO:0015862]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]
|
adenine transmembrane transporter activity [GO:0015207]; cytidine transmembrane transporter activity [GO:0015212]; guanine transmembrane transporter activity [GO:0015208]; neurotransmitter transmembrane transporter activity [GO:0005326]; nucleobase transmembrane transporter activity [GO:0015205]; nucleoside transmembrane transporter activity [GO:0005337]; purine nucleoside transmembrane transporter activity [GO:0015211]; uracil transmembrane transporter activity [GO:0015210]; uridine transmembrane transporter activity [GO:0015213]
|
PF01733;
| null |
SLC29A/ENT transporter (TC 2.A.57) family
| null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:23639800}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q14542}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the apical membrane of Sertoli cells. {ECO:0000269|PubMed:23639800}.
|
CATALYTIC ACTIVITY: Reaction=uridine(out) = uridine(in); Xref=Rhea:RHEA:71519, ChEBI:CHEBI:16704; Evidence={ECO:0000269|PubMed:9353301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71520; Evidence={ECO:0000305|PubMed:9353301}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71521; Evidence={ECO:0000305|PubMed:9353301}; CATALYTIC ACTIVITY: Reaction=inosine(in) = inosine(out); Xref=Rhea:RHEA:75375, ChEBI:CHEBI:17596; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75376; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75377; Evidence={ECO:0000250|UniProtKB:Q14542}; CATALYTIC ACTIVITY: Reaction=adenosine(in) = adenosine(out); Xref=Rhea:RHEA:75343, ChEBI:CHEBI:16335; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75344; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75345; Evidence={ECO:0000250|UniProtKB:Q14542}; CATALYTIC ACTIVITY: Reaction=thymidine(in) = thymidine(out); Xref=Rhea:RHEA:75363, ChEBI:CHEBI:17748; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75364; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75365; Evidence={ECO:0000250|UniProtKB:Q14542}; CATALYTIC ACTIVITY: Reaction=hypoxanthine(out) = hypoxanthine(in); Xref=Rhea:RHEA:71515, ChEBI:CHEBI:17368; Evidence={ECO:0000269|PubMed:18048066}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71516; Evidence={ECO:0000269|PubMed:18048066}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71517; Evidence={ECO:0000269|PubMed:18048066}; CATALYTIC ACTIVITY: Reaction=adenine(out) = adenine(in); Xref=Rhea:RHEA:71523, ChEBI:CHEBI:16708; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71524; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71525; Evidence={ECO:0000250|UniProtKB:Q14542}; CATALYTIC ACTIVITY: Reaction=cytidine(in) = cytidine(out); Xref=Rhea:RHEA:75367, ChEBI:CHEBI:17562; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75368; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75369; Evidence={ECO:0000250|UniProtKB:Q14542}; CATALYTIC ACTIVITY: Reaction=thymine(out) = thymine(in); Xref=Rhea:RHEA:71527, ChEBI:CHEBI:17821; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71528; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71529; Evidence={ECO:0000250|UniProtKB:Q14542}; CATALYTIC ACTIVITY: Reaction=uracil(in) = uracil(out); Xref=Rhea:RHEA:69404, ChEBI:CHEBI:17568; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69405; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69406; Evidence={ECO:0000250|UniProtKB:Q14542}; CATALYTIC ACTIVITY: Reaction=guanine(out) = guanine(in); Xref=Rhea:RHEA:71531, ChEBI:CHEBI:16235; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71532; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71533; Evidence={ECO:0000250|UniProtKB:Q14542}; CATALYTIC ACTIVITY: Reaction=guanosine(in) = guanosine(out); Xref=Rhea:RHEA:75371, ChEBI:CHEBI:16750; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75372; Evidence={ECO:0000250|UniProtKB:Q14542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75373; Evidence={ECO:0000250|UniProtKB:Q14542};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for hypoxanthine (for influx kinetics) {ECO:0000269|PubMed:18048066}; KM=189 uM for hypoxanthine (for efflux kinetics) {ECO:0000269|PubMed:18048066};
| null | null | null |
FUNCTION: Bidirectional uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis (PubMed:18048066, PubMed:9353301). Functions as a Na(+)-independent, passive transporter (By similarity). Involved in the transport of nucleosides such as inosine, adenosine, uridine, thymidine, cytidine and guanosine (PubMed:9353301). Also able to transport purine nucleobases (hypoxanthine, adenine, guanine) and pyrimidine nucleobases (thymine, uracil) (PubMed:18048066). Involved in nucleoside transport at basolateral membrane of kidney cells, allowing liver absorption of nucleoside metabolites (By similarity). Mediates apical nucleoside uptake into Sertoli cells, thereby regulating the transport of nucleosides in testis across the blood-testis-barrier (PubMed:23639800). Mediates both the influx and efflux of hypoxanthine in skeletal muscle microvascular endothelial cells to control the amount of intracellular hypoxanthine available for xanthine oxidase-mediated ROS production (PubMed:18048066). {ECO:0000250|UniProtKB:Q14542, ECO:0000269|PubMed:18048066, ECO:0000269|PubMed:23639800, ECO:0000269|PubMed:9353301}.
|
Rattus norvegicus (Rat)
|
O54701
|
NCKX2_RAT
|
MDLHQSATVRLLQEWCSHESPSGCRRHYNTRKKLKLIRVIGLVMGLVAVSTVPFSISAFTETYSQNNRGEASDVTGPRAAPGHRQRTLLDLNDKIRDYTPQPPASQEDRSENGTDHAQGDYPKDVFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLIMLIIFFLDNVIMWWESLLLLTAYFAYVVFMKFNVQVERWVKQMINRNKVVKVTVSEAQAKASTAGDKEEPTLPNKPRLQRGGSSASLHNSLMRNSIFQLMIHTLDPLAEELGSYGKLKYYDTMTEEGRFREKASILHKIAKKKCQVDENERQNGAANHVDYAAEKIELPNSTSTEVEMTPSSEASEPVQNGNLSHSIEAADAPQATETAEEDDDQPLSLSWPSNTRKQITFLIVLPIVFPLWITLPDVRKPASKKFFPITFFGSITWIAVFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWLLYTIIHRFKPVTVSSNGLFCAIVLLFIMLIFVILSIALCKWRMNKILGFIMFGLYFAFLVVSVLLEDKVLECPVSI
| null | null |
calcium ion import [GO:0070509]; calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; establishment of localization in cell [GO:0051649]; intracellular calcium ion homeostasis [GO:0006874]; learning [GO:0007612]; long-term synaptic depression [GO:0060292]; long-term synaptic potentiation [GO:0060291]; memory [GO:0007613]; monoatomic ion transmembrane transport [GO:0034220]; neuron cellular homeostasis [GO:0070050]; potassium ion transmembrane transport [GO:0071805]; protein-containing complex assembly [GO:0065003]; sodium ion transmembrane transport [GO:0035725]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
calcium channel activity [GO:0005262]; calcium, potassium:sodium antiporter activity [GO:0008273]; symporter activity [GO:0015293]
|
PF01699;
|
1.20.1420.30;
|
Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family, SLC24A subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9461611}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in) + 4 Na(+)(out); Xref=Rhea:RHEA:69967, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:9461611};
| null | null | null | null |
FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) (PubMed:9461611). Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:Q8BUN9, ECO:0000269|PubMed:9461611}.
|
Rattus norvegicus (Rat)
|
O54702
|
CHSTA_RAT
|
MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDGYSAKQEFVFLTAMPEAEKLRGEKHFSEVMKPTGKMLSESHPDQPPVYLERLELIRNACKEEALRNLSHTEVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSKIGIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRKNRTETRGIQFEDFVRYLGDPNRRWLDLQFGDHIIHWVTYVKLCAPCEIKYSVIGHHETLEADAPYILKEAGIDHLVSYPTIPPGITMYNRTKVEQYFLGISKRDIRRLYARFEGDFKLFGYQKPDFLLN
|
2.8.2.-
| null |
androgen metabolic process [GO:0008209]; carbohydrate biosynthetic process [GO:0016051]; estrogen metabolic process [GO:0008210]; learning [GO:0007612]; long-term memory [GO:0007616]; proteoglycan biosynthetic process [GO:0030166]
|
Golgi membrane [GO:0000139]
|
HNK-1 sulfotransferase activity [GO:0016232]; sulfotransferase activity [GO:0008146]
|
PF03567;
| null |
Sulfotransferase 2 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23723439}; Single-pass type II membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] = 3-O-{O-3-S-beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68304, Rhea:RHEA-COMP:17486, Rhea:RHEA-COMP:17487, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:177355, ChEBI:CHEBI:177363; Evidence={ECO:0000269|PubMed:23723439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68305; Evidence={ECO:0000305|PubMed:23723439}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 3-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 17beta-estradiol 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68696, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136641, ChEBI:CHEBI:178093; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68697; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 3-O-(beta-D-glucuronate) 17-sulfate + 3'-phosphoadenylyl sulfate = 17beta-estradiol 3-O-(3-sulfo-beta-D-glucuronate) 17-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68660, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178094, ChEBI:CHEBI:178095; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68661; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 17beta-estradiol 17-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68664, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:82961, ChEBI:CHEBI:178096; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68665; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=16alpha,17beta-estriol 3-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 16alpha,17beta-estriol 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68668, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136649, ChEBI:CHEBI:178097; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68669; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=16alpha,17beta-estriol 16-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 16alpha,17beta-estriol 16-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68672, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136650, ChEBI:CHEBI:178098; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68673; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=16alpha,17beta-estriol 17-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 16alpha,17beta-estriol 17-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68700, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178099, ChEBI:CHEBI:178100; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68701; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + estrone 3-O-(beta-D-glucuronate) = adenosine 3',5'-bisphosphate + estrone 3-O-(3-sulfo-beta-D-glucuronate) + H(+); Xref=Rhea:RHEA:68676, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136634, ChEBI:CHEBI:178101; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68677; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3alpha,20alpha-dihydroxy-5beta-pregnane 3-O-(beta-D-glucuronate) = 3alpha,20alpha-dihydroxy-5beta-pregnane 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68680, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178102, ChEBI:CHEBI:178103; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68681; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + testosterone 17-O-(beta-D-glucuronate) = adenosine 3',5'-bisphosphate + H(+) + testosterone 17-O-(3-sulfo-beta-D-glucuronate); Xref=Rhea:RHEA:68684, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136639, ChEBI:CHEBI:178104; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68685; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3beta-androst-5-en-17-one 3-O-(beta-D-glucuronate) = 3beta-androst-5-en-17-one 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68688, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178105, ChEBI:CHEBI:178106; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68689; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3alpha,17alpha-dihydroxy-5beta-androstane-11-one-17beta-carboxylate 3-O-(beta-D-glucuronate) = 3alpha,17alpha-dihydroxy-5beta-androstane-11-one-17beta-carboxylate 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68692, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178107, ChEBI:CHEBI:178108; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68693; Evidence={ECO:0000250|UniProtKB:O43529}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3alpha-hydroxyetiocholan-17-one 3-O-(beta-D-glucuronate) = 3alpha-hydroxyetiocholan-17-one 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68704, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178197, ChEBI:CHEBI:178198; Evidence={ECO:0000250|UniProtKB:O43529}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68705; Evidence={ECO:0000250|UniProtKB:O43529};
| null |
PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:O43529}.; PATHWAY: Protein modification; carbohydrate sulfation. {ECO:0000250|UniProtKB:O43529}.
| null | null |
FUNCTION: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis (PubMed:9368071). Sulfates terminal glucuronyl residue of the laminin globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and prevents further polymerization by LARGE1 glycosyltransferase. Likely defines the chain length of LG epitope, conferring binding specificity to extracellular matrix components (PubMed:23723439). Plays a role in down-regulating the steroid hormones. Sulfates glucuronidated estrogens and androgens with an impact in hormone cycle and fertility. Has a preference for glucuronyl moiety at the 3-hydroxyl group of a sterol ring rather than the 17-hydroxyl group, showing high catalytic efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones (By similarity). {ECO:0000250|UniProtKB:O43529, ECO:0000269|PubMed:23723439, ECO:0000269|PubMed:9368071}.
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Rattus norvegicus (Rat)
|
O54705
|
NOS2_CAVPO
|
MACPWNFLWKLKSSRYDLTEEKDINNNVGKASHLYSPEIQDDPKYCSPGKHQNGSSQSLTGTAKKVPESQSKPHKPSPTCSQHMKIKNWGNGMILQDTLHTKAKTNFTCKPKSCLGSVMNPRSMTRGPRDTPIPPDELLPQAIEFVNQYYDSFKEAKIEEYLARVETVTKEIETTGTYQLTGDELIFATKLAWRNAPRCIGRIQWSNLQVFDARSCHTAQEMFEHICRHVRYSTNNGNIRSAITVFPQRTDGKHDFRVWNAQLIRYAGYQMPDGTIQGDPANLEFTQLCIDLGWKPRYGRFDVLPLILQADGRDPELFEIPPDLVLEVPMEHPKYEWFQDLGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDAQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHSAAESFMKHMQNEYRARGGCPADWIWLVPPISGSITPVFHQEMLNYILSPFYYYQVEAWKTHVWQDETRRPKRREIPFRVLAKATLFASLLMRKMMASRVRATILFATETGKSEALAQDLGALFSCAFNPKVLCMDQYQLSSLEEEKLLLVVTSTFGNGDCPGNGETLKKSLFVLKKLTNTFRYAVFGLGSSMYPRFCAFAHDIDIKLSQLGASQLTPVGEGDELSGQEDAFCTWAVQTFQAACAAFDVRGRHHITIPKRYTSSVTWEPYHYRLVQDSQPLDLNKALSRMHATDVFTMRLKSQKNLQSPKSSRTTLLMELSCDDSRSLAYLPGEHLGVFPCNQPALVQGILECVVDNPGPHHTVCLEVLDDSGSYWAKDKRLPPCSLSQALTYFLDITTPPTQLQLQKLARLATEQAERLRLESLSQPSEYNKWKFTNSPTFLEVLEEFPSLRVPAAFLLSQLPILKPRYYSISSSLDHTPAEVHLTVAVVTYRTRDGRGPLHHGVCSTWFSGLKPQDPVPCLVRSVNSFQLPKDPSQPCILIGPGTGIAPFRSFWQQRLHNLKHTGLQGGRMTLLFGCRHPEEDHIYKEEMQEMVQKGVLHEVHTAYSRLPGKPKAYVQDILRQQLAREVLRVLHEEPGHLYVCGNVLMAQDVACTLKQLLAAKLNLNEEQVEDYFFQLKSQKRYHEDIFGAVFPHGVKKDRAERPPGDDKL
|
1.14.13.39
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P35228}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P29476}; Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P35228}; Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P35228}; COFACTOR: Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:P35228}; Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme. {ECO:0000250|UniProtKB:P35228};
|
defense response to bacterium [GO:0042742]; nitric oxide biosynthetic process [GO:0006809]; peptidyl-cysteine S-nitrosylation [GO:0018119]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; prostaglandin secretion [GO:0032310]; regulation of cytokine production involved in inflammatory response [GO:1900015]; superoxide metabolic process [GO:0006801]
|
cytosol [GO:0005829]
|
calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517]
|
PF00667;PF00258;PF00175;PF02898;
|
3.40.50.360;6.10.250.410;3.90.440.10;3.40.50.80;2.40.30.10;
|
NOS family
|
PTM: Polyubiquitinated; mediated by SPSB1, SPSB2 and SPSB4, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P35228}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35228}. Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. {ECO:0000250|UniProtKB:P35228}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={ECO:0000250|UniProtKB:P35228}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898; Evidence={ECO:0000250|UniProtKB:P35228};
| null | null | null | null |
FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8. {ECO:0000250|UniProtKB:P35228, ECO:0000250|UniProtKB:P79290}.
|
Cavia porcellus (Guinea pig)
|
O54709
|
NKG2D_MOUSE
|
MALIRDRKSHHSEMSKCHNYDLKPAKWDTSQEQQKQRLALTTSQPGENGIIRGRYPIEKLKISPMFVVRVLAIALAIRFTLNTLMWLAIFKETFQPVLCNKEVPVSSREGYCGPCPNNWICHRNNCYQFFNEEKTWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQIPANGSWQWEDGSSLSYNQLTLVEIPKGSCAVYGSSFKAYTEDCANLNTYICMKRAV
| null | null |
adaptive immune response [GO:0002250]; cell differentiation [GO:0030154]; cellular response to lipopolysaccharide [GO:0071222]; defense response to Gram-positive bacterium [GO:0050830]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of natural killer cell chemotaxis [GO:2000502]; nitric oxide biosynthetic process [GO:0006809]; positive regulation of apoptotic process [GO:0043065]; positive regulation of myeloid dendritic cell activation [GO:0030887]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target [GO:0002860]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of type II interferon production [GO:0032729]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; MHC class I protein binding [GO:0042288]; MHC class Ib receptor activity [GO:0032394]; signaling receptor activity [GO:0038023]
|
PF00059;
|
3.10.100.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}; Single-pass type II membrane protein {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}. Note=Colocalized with HCST and TYROBP on the cell surface.
| null | null | null | null | null |
FUNCTION: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1. {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:11248803, ECO:0000269|PubMed:11557981, ECO:0000269|PubMed:11567106, ECO:0000269|PubMed:12150888, ECO:0000269|PubMed:12370332, ECO:0000269|PubMed:12426564, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15189740, ECO:0000269|PubMed:16086018, ECO:0000269|PubMed:18394936, ECO:0000269|PubMed:19631564, ECO:0000269|PubMed:21898152, ECO:0000269|PubMed:23298206}.
|
Mus musculus (Mouse)
|
O54714
|
PIAS3_MOUSE
|
MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPGPLAPIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILNSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSAVQEGIQPESKKRVEVIDLTIESSSDEEDLPPTKKHCPVTSAAIPALPGSKGALTSGHQPSSVLRSPAMGTLGSDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYGPSVITSLDEQDTLGHFFQYRGTPSHFLGPLAPTLGSSHRSSTPAPPPGRVSSIVAPGSSLREGHGGPLPSGPSLTGCRSDVISLD
|
2.3.2.-
| null |
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of protein sumoylation [GO:0033234]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of gene expression [GO:0010628]; positive regulation of membrane potential [GO:0045838]; positive regulation of protein sumoylation [GO:0033235]; protein sumoylation [GO:0016925]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
ionotropic glutamate receptor binding [GO:0035255]; potassium channel regulator activity [GO:0015459]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription coregulator activity [GO:0003712]; transmembrane transporter binding [GO:0044325]; zinc ion binding [GO:0008270]
|
PF14324;PF02891;
|
2.60.120.780;1.10.720.30;3.30.40.10;
|
PIAS family
|
PTM: Sumoylated. {ECO:0000269|PubMed:12387893}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556}. Nucleus {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:14596924}. Nucleus speckle {ECO:0000269|PubMed:12077349}. Note=Colocalizes with MITF in the nucleus (PubMed:11709556). Colocalizes with GFI1 in nuclear dots (PubMed:11060035). Colocalizes with SUMO1 in nuclear granules (PubMed:12077349). {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:12077349}.
| null | null |
PATHWAY: Protein modification; protein sumoylation.
| null | null |
FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. Repressor of STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing cell growth. Repressor of MITF transcriptional activity. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1 (By similarity). Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9Y6X2, ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:14596924}.
|
Mus musculus (Mouse)
|
O54715
|
VAS1_RAT
|
MMAATVVSRIRTGTRWAPVLWLLLSLVAVAAAVAAEQQVPLVLWSSDRDLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLATLKELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLESEDVPYTAALTAVRPSRVARDVAMVAGGLGRQLLQTQVASPAIHPPVSYNDTAPRILFWAQNFSVAYKDEWKDLTSLTFGVENLNLTGSFWNDSFAMLSLTYEPLFGATVTFKFILASRFYPVSARYWFTMERLEIHSNGSVAHFNVSQVTGPSIYSFHCEYVSSLSKKGSLLVTNVPSLWQMTLHNFQIQAFNVTGEQFSYASDCAGFFSPGIWMGLLTTLFMLFIFTYGLHMILSLKTMDRFDDRKGPTITLTQIV
| null | null |
cellular response to increased oxygen levels [GO:0036295]; endosome to plasma membrane protein transport [GO:0099638]; intracellular iron ion homeostasis [GO:0006879]; osteoclast development [GO:0036035]; regulation of cellular pH [GO:0030641]; synaptic vesicle lumen acidification [GO:0097401]
|
clathrin-coated vesicle membrane [GO:0030665]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endosome membrane [GO:0010008]; membrane [GO:0016020]; proton-transporting V-type ATPase complex [GO:0033176]; synaptic vesicle membrane [GO:0030672]
|
ATPase activator activity [GO:0001671]; small GTPase binding [GO:0031267]; transporter activator activity [GO:0141109]
|
PF20520;PF05827;
|
2.40.160.110;
|
Vacuolar ATPase subunit S1 family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q15904}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15904}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q15904}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q15904}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Single-pass type I membrane protein {ECO:0000305}. Note=Not detected in trans-Golgi network. {ECO:0000250|UniProtKB:Q15904}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles (PubMed:32165585). Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca(2+)-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules (By similarity). {ECO:0000250|UniProtKB:Q15904, ECO:0000250|UniProtKB:Q9R1Q9, ECO:0000269|PubMed:32165585}.
|
Rattus norvegicus (Rat)
|
O54724
|
CAVN1_MOUSE
|
MEDVTLHIVERPYSGFPDASSEGPEPTQGEARATEEPSGTGSDELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSVSKSLKESEALPEKEGDELGEGERPEDDTAAIELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPVERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKVPPFTFHVKKIREGEVEVLKATEMVEVGPEDDEVGAERGEATDLLRGSSPDVHTLLEITEESDAVLVDKSDSD
| null | null |
positive regulation of cell motility [GO:2000147]; protein secretion [GO:0009306]; rRNA transcription [GO:0009303]; termination of RNA polymerase I transcription [GO:0006363]; transcription initiation at RNA polymerase I promoter [GO:0006361]
|
caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
identical protein binding [GO:0042802]; rRNA primary transcript binding [GO:0042134]
|
PF15237;
| null |
CAVIN family
|
PTM: Phosphorylated. Present in active and inactive forms. Changes in phosphorylation pattern may alter activity. Phosphorylation at Tyr-158 is essential for its function in the regulation of the ribosomal transcriptional activity. {ECO:0000269|PubMed:11139612, ECO:0000269|PubMed:27528195}.; PTM: Monoubiquitinated. {ECO:0000269|PubMed:27528195}.
|
SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25514038}. Cell membrane {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225}. Microsome {ECO:0000250|UniProtKB:Q6NZI2}. Endoplasmic reticulum {ECO:0000269|PubMed:30188967}. Cytoplasm, cytosol {ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242}. Mitochondrion {ECO:0000250|UniProtKB:Q6NZI2}. Nucleus {ECO:0000269|PubMed:25514038, ECO:0000269|PubMed:27528195}. Note=Translocates to the cytoplasm from caveolae upon insulin stimulation (By similarity). Colocalizes with CAV1 in lipid rafts in adipocytes (PubMed:18056712). Localizes in the caveolae in a caveolin-dependent manner (PubMed:19546242). {ECO:0000250|UniProtKB:Q6NZI2, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:19546242}.
| null | null | null | null | null |
FUNCTION: Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:18840361, PubMed:30188967). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1) (PubMed:19546242). Essential for normal oligomerization of CAV1 (PubMed:23652019). Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop (PubMed:27528195). Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (PubMed:10589839, PubMed:11139612, PubMed:9582279). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (PubMed:30188967). {ECO:0000269|PubMed:10589839, ECO:0000269|PubMed:11139612, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:18840361, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23652019, ECO:0000269|PubMed:27528195, ECO:0000269|PubMed:30188967, ECO:0000269|PubMed:9582279}.
|
Mus musculus (Mouse)
|
O54728
|
PLB1_RAT
|
MESWPGVSLVGLLLLLLLGQGPSQIHGSSGENTSQPQQVFRTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPVGRKDGTLNEAERKTMKCPSQESPYLFTYRNSNYQARQLKPIGKFQMKEGTKFTCPDKDPSDSIPTTVHRLRPADIKVIGAMGDSLTAGNGAGSSPGNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKENTPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKVSCPRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKLIESGRYDTRDDFTVVLQPMFENVVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVGRKTRHQNFEIKVPIMCPNQTSPFLSTTKNSNLGHGTSMSCEEKAPSASPPTSVHTLRPADIQVVAALGDSVTAGNGISSQEGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDVNSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDILHKEVPRALVNLVDFMNPSIIRQVFLKNPDKCPVNQTSVLCNCVLTPGEDSHELARLEAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLFNIRLPILENGNPDTSFFAPDCILLSQKFHTQLARALWANMLEPLGKKMDTLDPKELIALACPTKDKPFLRTFRNSNYTYPIKPAIENWGSDFLCTEQSPSSKVPTSVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENTAGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYEELPRVFINVVEVMELSGLLHDQGGKCAMPLAVQKNCSCLKRSQNLMAMQELKKVNGNLQSALSELSYWHRYMQREDFAVTVQPFFRNTFVPLDERGGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVGKKTTSNNFTYNRTKLKCPSPENPFLYTVRNSQILLDKAKENSNTLYWAVPVAAVGGLVVGILGMMLWRTVRLVQ
|
3.1.1.3; 3.1.1.4; 3.1.1.5
| null |
diacylglycerol catabolic process [GO:0046340]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylethanolamine catabolic process [GO:0046338]; phosphatidylglycerol catabolic process [GO:0034478]; phospholipid metabolic process [GO:0006644]; positive regulation of acrosome reaction [GO:2000344]; retinol metabolic process [GO:0042572]; triglyceride catabolic process [GO:0019433]
|
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]
|
calcium-independent phospholipase A2 activity [GO:0047499]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A2 activity [GO:0004623]; retinyl-palmitate esterase activity [GO:0050253]; triglyceride lipase activity [GO:0004806]
|
PF00657;
|
3.40.50.1110;
|
'GDSL' lipolytic enzyme family, Phospholipase B1 subfamily
|
PTM: Undergoes proteolytic cleavage in the ileum. {ECO:0000269|PubMed:9442065}.
|
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064, ECO:0000305|PubMed:9442065}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064, ECO:0000305|PubMed:9442065}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064, ECO:0000305|PubMed:9442065}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064, ECO:0000305|PubMed:9442065}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73002, ChEBI:CHEBI:76084; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2 H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112, ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064, ECO:0000305|PubMed:9442065}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064, ECO:0000305|PubMed:9442065}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466, ChEBI:CHEBI:77623; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-octadecenoate + 1,3-dihexadecanoylglycerol + H(+); Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623, ChEBI:CHEBI:77624; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558, ChEBI:CHEBI:77623; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:41219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75757; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41220; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938; Evidence={ECO:0000269|PubMed:9442064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605; Evidence={ECO:0000305|PubMed:9442064}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342, ChEBI:CHEBI:75735; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000250|UniProtKB:Q05017};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:9442064};
| null |
FUNCTION: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (By similarity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids (PubMed:11401559, PubMed:9442064, PubMed:9442065). Preferentially cleaves sn-2 ester bonds over sn-1 bonds (PubMed:9442064). Acts as a lipase toward glycerolipid substrates (PubMed:11401559, PubMed:9442064, PubMed:9442065). Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity (PubMed:11401559, PubMed:9442064, PubMed:9442065). May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (Probable). {ECO:0000250|UniProtKB:Q05017, ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065, ECO:0000305|PubMed:9442064}.
|
Rattus norvegicus (Rat)
|
O54732
|
MMP15_MOUSE
|
MGSDRSALGRPGCTGSCLSSRASLLPLLLVLLDCLGHGTASKDAEVYAAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQSFYGIPVTGVLDEETKTWMKRPRCGVPDQFGVHVKANLRRRRKRYTLTGKAWNNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVSYDDIRLRRRAEADIMVLFASGFHGDSSPFDGVGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTDNFQLPEDDLRGIQQLYGSPDGKPQPTRPLPTVRPRRPGRPDHQPPRPPQPPHPGGKPERPPKPGPPPQPRATERPDQYGPNICDGNFDTVAVLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGNISAAYERQDGHFVFFKGNRYWLFREANLEPGYPQPLSSYGTDIPYDRIDTAIWWEPTGHTFFFQADRYWRFNEETQHGDPGYPKPISVWQGIPTSPKGAFLSNDAAYTYFYKGTKYWKFNNERLRMEPGHPKSILRDFMGCQEHVEPRSRWPDVARPPFNPNGGAEPEADGDSKEENAGDKDEGSRVVVQMEEVVRTVNVVMVLVPLLLLLCILGLAFALVQMQRKGAPRMLLYCKRSLQEWV
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
|
collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; response to estradiol [GO:0032355]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; membrane [GO:0016020]
|
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF11857;PF00045;PF00413;PF01471;
|
3.40.390.10;2.110.10.10;
|
Peptidase M10A family
|
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
|
Mus musculus (Mouse)
|
O54735
|
PDE5A_RAT
|
MLPFGDKTRDMVNAWFSERVHNIPVCKEGIRAHTESCSCSLPQSPHADNTTPGAPARKISASEFDRPLRPIVVKDSEGTVSFLSDSGKKEQMPLTSPRFDSDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSKDKFLVSRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAAFGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCPDSFSRVFQMEWEEVGKSSEPLTREHDANKINYMYAQYVKNTMEPLNIPDVTKDNRFPWTNENMGHINTHCIRSLLCTPIKNGKKNKVIGVCQLVNKMEEKTGKIKAFNQNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQALAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLETLALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSTMEHHHFDQCLMVLNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNEFSFEDPLQKELFLAMLMTACDLSAITKPWPIQQRIAELVAAEFFDQGDRERKELNMEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCLPLLDGCRKNRQKWQALADQQEKTLLNGESGQAKRD
|
3.1.4.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O76074}; Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc. {ECO:0000250|UniProtKB:O76074}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O76074}; Note=Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc. {ECO:0000250|UniProtKB:O76074};
|
cAMP-mediated signaling [GO:0019933]; cGMP catabolic process [GO:0046069]; cGMP metabolic process [GO:0046068]; negative regulation of cardiac muscle contraction [GO:0055118]; negative regulation of T cell proliferation [GO:0042130]; nervous system development [GO:0007399]; oocyte development [GO:0048599]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of chronic inflammatory response [GO:0002678]; positive regulation of oocyte development [GO:0060282]; positive regulation of vasoconstriction [GO:0045907]; regulation of nitric oxide mediated signal transduction [GO:0010749]; regulation of the force of heart contraction [GO:0002026]; relaxation of cardiac muscle [GO:0055119]; response to hypoxia [GO:0001666]; response to lipopolysaccharide [GO:0032496]; response to testosterone [GO:0033574]; short-term memory [GO:0007614]; T cell proliferation [GO:0042098]; vasodilation [GO:0042311]
| null |
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; 3',5'-cyclic-nucleotide phosphodiesterase activity [GO:0004114]; cGMP binding [GO:0030553]; cyclic-nucleotide phosphodiesterase activity [GO:0004112]; metal ion binding [GO:0046872]
|
PF01590;PF00233;
|
3.30.450.40;1.10.1300.10;
|
Cyclic nucleotide phosphodiesterase family
|
PTM: Phosphorylation is regulated by binding of cGMP to the two allosteric sites. Phosphorylation by PRKG1 leads to its activation. {ECO:0000250}.
| null |
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000250|UniProtKB:O76074}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000250|UniProtKB:O76074};
| null |
PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
| null | null |
FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP. {ECO:0000250|UniProtKB:O76074}.
|
Rattus norvegicus (Rat)
|
O54743
|
FOXF2_MOUSE
|
MSTEGGPPPPPPRPPPAPLRRACSPAPGALQAALMSPPPAATLESTSSSSSSSSASCASSSSNSVSASAGACKSAASSGGAGAGSGGTKKATSGLRRPEKPPYSYIALIVMAIQSSPSKRLTLSEIYQFLQARFPFFRGAYQGWKNSVRHNLSLNECFIKLPKGLGRPGKGHYWTIDPASEFMFEEGSFRRRPRGFRRKCQALKPMYHRVVSGLGFGASLLPQGFDFQAPPSAPLGCHGQGGYGGLDMMPAGYDTGAGAPGHAHPHHLHHHHVPHMSPNPGSTYMASCPVPAGPAGVGAAAGGGGGGGDYGPDSSSSPVPSSPAMASAIECHSPYTSPAAHWSSPGASPYLKQPPALTPSSNPAASAGLHPSMSSYSLEQSYLHQNAREDLSVGLPRYQHHSTPVCDRKDFVLNFNGISSFHPSASGSYYHHHHQSVCQDIKPCVM
| null | null |
animal organ morphogenesis [GO:0009887]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic digestive tract development [GO:0048566]; establishment of planar polarity of embryonic epithelium [GO:0042249]; extracellular matrix organization [GO:0030198]; genitalia development [GO:0048806]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulation of protein polyubiquitination [GO:1902914]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0060021]
|
nuclear body [GO:0016604]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; TFIIB-class transcription factor binding [GO:0001093]
|
PF00250;
|
1.10.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12947}.
| null | null | null | null | null |
FUNCTION: Probable transcription activator for a number of lung-specific genes (PubMed:9676429). Mediates up-regulation of the E3 ligase IRF2BPL and drives ubiquitination and degradation of CTNNB1 (By similarity). {ECO:0000250|UniProtKB:Q12947, ECO:0000269|PubMed:9676429}.
|
Mus musculus (Mouse)
|
O54747
|
DPOD1_RAT
|
MDGKRRQAPSSGVPPKRACKGLWDEDEPSQFEENLALLEEIEAENRLQEAEEELQLPPEGIVGGQFSTADIDPRWLRPTPLALDPSTEPLIFQQLEIDHYVGTSPPLPEGPPASRNSVPILRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGAEHLSELQRELNAAISRDQRGGKELSGPAVLAIELCSRESMFGYHGHGPSPFLRITLALPRLMAPARRLLEQGIRVPGLGTPSFAPYEANVDFEIRFMVDADIVGCNWLELPAGKYVRRAEKKATLCQLEVDVLWSDVISHPPEGQWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEREEDLLQAWATFILAMDPDVITGYNIQNFDLPYLISRAQTLKVDRFPFLGRVTGLRSNIRDSSFQSRQVGRRDSKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNEQTRRRLAVYCLKDAFLPLRLLERLMVLVNNVEMARVTGVPLGYLLSRGQQVKVVSQLLRQAMREGLLMPVVKTEGGEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGAAQKLGLKPDEFIKTPTGDEFVKASVRKGLLPQILENLLSARKRAKAELAQETDPLRRQVLDGRQLALKVSPNSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEKTKQLVETKYTLENGYDANAKVVYGDTDSVMCRFGVSSVAEAMSLGREAANWVSSHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRSDAHDRMDCKGLEAVRRDNCPLVANLVTSSLRRILVDRDPDGAVAHAKDVISDLLCNRIDISQLVITKELTRAAADYAGKQAHVELAERMRKRDPGSAPNLGDRVPYVIIGAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQQLAKPLLRIFEPILGEGRAESVLLRGDHTRCKTVLTSKVGGLLAFTKRRNSCIGCRSVIDHQGAVCKFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQERLLQRFGPPGPEAW
|
2.7.7.7; 3.1.11.-
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
|
base-excision repair, gap-filling [GO:0006287]; cellular response to UV [GO:0034644]; DNA biosynthetic process [GO:0071897]; DNA replication [GO:0006260]; DNA replication proofreading [GO:0045004]; DNA synthesis involved in DNA repair [GO:0000731]; DNA-templated DNA replication [GO:0006261]; error-free translesion synthesis [GO:0070987]; fatty acid homeostasis [GO:0055089]; nucleotide-excision repair, DNA gap filling [GO:0006297]
|
delta DNA polymerase complex [GO:0043625]; nucleotide-excision repair complex [GO:0000109]; nucleus [GO:0005634]
|
3'-5' exonuclease activity [GO:0008408]; 3'-5'-DNA exonuclease activity [GO:0008296]; 4 iron, 4 sulfur cluster binding [GO:0051539]; chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; enzyme binding [GO:0019899]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]
|
PF00136;PF03104;PF14260;
|
6.10.140.1540;1.10.132.60;3.30.342.10;1.10.287.690;3.90.1600.10;3.30.420.10;
|
DNA polymerase type-B family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28340}. Note=Colocalizes with PCNA and POLD3 at S phase replication sites. After UV irradiation, recruited to DNA damage sites within 2 hours, independently on the cell cycle phase, nor on PCNA ubiquitination. This recruitment requires POLD3, PCNA and RFC1-replication factor C complex. {ECO:0000250|UniProtKB:P28340}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P28340};
| null | null | null | null |
FUNCTION: As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine, 8oxoG or abasic sites. {ECO:0000250|UniProtKB:P28340}.
|
Rattus norvegicus (Rat)
|
O54748
|
STK3_RAT
|
MEQPPAPKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDVQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKSPEQRATATQLLQHPFIKNAKPVSILRELITEGMEIKAKRHEEQQRELEDEEENSDEDELDSHTMVKTSSEGVGTMRATSTMSEGAQTMIEHNSTMLESDLGTMVINSEDEEEEDGTMKRNATSPQVQRPSFMDYFDKQDFKNKSHENCDQSMREPCPMSNNVFPDNWRVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELHQRYSAKRQPILDAMDAKKRRQQNF
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13188};
|
apoptotic process [GO:0006915]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation involved in embryonic placenta development [GO:0060706]; cell population proliferation [GO:0008283]; central nervous system development [GO:0007417]; endocardium development [GO:0003157]; epithelial cell proliferation [GO:0050673]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; hepatocyte apoptotic process [GO:0097284]; hippo signaling [GO:0035329]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of organ growth [GO:0046621]; neural tube formation [GO:0001841]; organ growth [GO:0035265]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of JNK cascade [GO:0046330]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; primitive hemopoiesis [GO:0060215]; protein import into nucleus [GO:0006606]; protein localization to centrosome [GO:0071539]; protein stabilization [GO:0050821]; protein tetramerization [GO:0051262]; regulation of cell differentiation involved in embryonic placenta development [GO:0060800]; regulation of MAPK cascade [GO:0043408]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF11629;PF00069;
|
1.10.287.4270;4.10.170.10;1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Autophosphorylated on two residues Thr-174 and Thr-180, leading to activation. Phosphorylation at Thr-117 and Thr-384 by PKB/AKT1, leads to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation, and increase in its binding to RAF1. Phosphorylated at Ser-15 by PLK1, leading to activation. {ECO:0000250|UniProtKB:Q13188}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N) (By similarity). {ECO:0000250|UniProtKB:Q13188}.; PTM: Ubiquitinated by TRIM69; leading to its redistribution to the perinuclear cytoskeleton. {ECO:0000250|UniProtKB:Q13188}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13188}. Nucleus {ECO:0000250|UniProtKB:Q13188}. Note=The caspase-cleaved form cycles between nucleus and cytoplasm (By similarity). Phosphorylation at Thr-117 leads to inhibition of nuclear translocation (By similarity). {ECO:0000250|UniProtKB:Q13188}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13188}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13188}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13188}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13188};
| null | null | null | null |
FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates NKX2-1. Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38 (By similarity). {ECO:0000250|UniProtKB:Q13188, ECO:0000250|UniProtKB:Q9JI10, ECO:0000269|PubMed:9430685}.
|
Rattus norvegicus (Rat)
|
O54750
|
CP2J6_MOUSE
|
MLAATGSLLATIWAALHPRTLLVAAVTFLLLADYFKNRRPKNYPPGPWGLPFVGNIFQLDFGQPHLSIQPLVKKYGNIFSLNLGDITSVVITGLPLIKEALTQMEQNIMNRPLSVMQERISNKNGLIFSSGQIWKEQRRFALMTLRNFGLGKKSLEERMQEEASHLVEAIREEEGKPFNPHFSINNAVSNIICSVTFGERFDYHDSRFQEMLRLLDEVMYLETTMISQLYNIFPWIMKYIPGSHQKVFRNWEKLKLFVSCMIDDHRKDWNPDEPRDFIDAFLKEMTKYPEKTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEVQEKVQAEIDRVIGQKRAARLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAMDTNLNGFHLPKGTMVLTNLTALHRDPKEWATPDVFNPEHFLENGQFKKRESFLPFSMGKRACLGEQLARSELFIFFTSLMQKFTFNPPINEKLSPKFRNGLTLSPVSHRICAVPRQ
|
1.14.14.1
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
arachidonic acid metabolic process [GO:0019369]; negative regulation of collagen biosynthetic process [GO:0032966]; negative regulation of peroxisome proliferator activated receptor signaling pathway [GO:0035359]; organic acid metabolic process [GO:0006082]; positive regulation of extracellular matrix organization [GO:1903055]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of tumor necrosis factor production [GO:0032760]; retinoid metabolic process [GO:0001523]; xenobiotic metabolic process [GO:0006805]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
|
arachidonic acid epoxygenase activity [GO:0008392]; arachidonic acid monooxygenase activity [GO:0008391]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1;
| null | null | null | null | null |
Mus musculus (Mouse)
|
O54751
|
CRX_MOUSE
|
MMAYMNPGPHYSVNALALSGPNVDLMHQAVPYSSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGAQTKARPAKRKAGTSPRPSTDVCTDPLGISDSYSPSLPGPSGSPTTAVATVSIWSPASEAPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYASPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYSTYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL
| null | null |
cell differentiation [GO:0030154]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to stimulus [GO:0050896]; retina development in camera-type eye [GO:0060041]; visual perception [GO:0007601]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor binding [GO:0016922]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
|
PF00046;PF03529;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:16574740}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors. {ECO:0000269|PubMed:16574740}.
|
Mus musculus (Mouse)
|
O54753
|
H17B6_RAT
|
MWFYLVTLVGLYYLLRWYRERQVVSHLHDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELKSKTSDRLETVILDVTNTDSISAATQWVKEHVGDKGLWGLVNNAGVFQAFAYIEWCRPEDCMSIFQVNLIGLAQVTLSMLFLVKKARGRIVNVSSVLGRVALFGGFYSCSKYGVEAFSDVLRREIRDFGVKVSIIEPGSFKTRMTDAELIIEKTKKTWEATPEHIRESYGQQFFDDFCNTTRRELKKCSTNLSLVTDCMEHALTSKYPRTRYSAGWDARLFFIPLSYLPTSLVDCLLAISRRKPAQAV
|
1.1.1.105; 1.1.1.209; 1.1.1.239; 1.1.1.53; 1.1.1.62
| null |
androgen metabolic process [GO:0008209]; brexanolone catabolic process [GO:0062175]; retinol metabolic process [GO:0042572]; steroid metabolic process [GO:0008202]
|
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
|
5alpha-androstane-3beta,17beta-diol dehydrogenase activity [GO:0047024]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; androsterone dehydrogenase activity [GO:0047023]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; NAD-retinol dehydrogenase activity [GO:0004745]; testosterone 17-beta-dehydrogenase (NADP+) activity [GO:0047045]; testosterone dehydrogenase (NAD+) activity [GO:0047035]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:O14756}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14756}; Lumenal side {ECO:0000250|UniProtKB:O14756}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14756}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14756}; Lumenal side {ECO:0000250|UniProtKB:O14756}.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH; Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228; EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:O14756}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH; Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:O14756}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285; Evidence={ECO:0000250|UniProtKB:O14756}; CATALYTIC ACTIVITY: Reaction=androsterone + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:20381, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.209; Evidence={ECO:0000269|PubMed:9188497}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20382; Evidence={ECO:0000305|PubMed:9188497}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20383; Evidence={ECO:0000305|PubMed:9188497}; CATALYTIC ACTIVITY: Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.239; Evidence={ECO:0000269|PubMed:9188497}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence={ECO:0000269|PubMed:9188497}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006; Evidence={ECO:0000305|PubMed:9188497}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence={ECO:0000269|PubMed:9188497}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62; Evidence={ECO:0000269|PubMed:9188497}; CATALYTIC ACTIVITY: Reaction=3alpha-hydroxy-5alpha-pregnan-20-one + NAD(+) = 5alpha-pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41980, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:50169, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:O14756}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41981; Evidence={ECO:0000250|UniProtKB:O14756}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3beta,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42184, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:O14756}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42186; Evidence={ECO:0000250|UniProtKB:O14756}; CATALYTIC ACTIVITY: Reaction=3beta-hydroxy-5alpha-androstan-17-one + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:42188, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:541975; Evidence={ECO:0000250|UniProtKB:O14756}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42190; Evidence={ECO:0000250|UniProtKB:O14756};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 uM for 5-alpha-androstan-3-alpha,17-beta-diol {ECO:0000269|PubMed:9188497}; KM=0.2 uM for androsterone {ECO:0000269|PubMed:9188497}; KM=0.5 uM for dihydrotestosterone {ECO:0000269|PubMed:9188497}; KM=1.1 uM for testosterone {ECO:0000269|PubMed:9188497}; KM=0.8 uM for estradiol {ECO:0000269|PubMed:9188497}; KM=3 uM for NAD {ECO:0000269|PubMed:9188497}; KM=1 mM for NADP {ECO:0000269|PubMed:9188497}; Vmax=2.5 nmol/min/mg enzyme for 5-alpha-androstan-3-alpha,17-beta-diol {ECO:0000269|PubMed:9188497}; Vmax=0.1 nmol/min/mg enzyme for androsterone {ECO:0000269|PubMed:9188497}; Vmax=0.5 nmol/min/mg enzyme for dihydrotestosterone {ECO:0000269|PubMed:9188497}; Vmax=1.1 nmol/min/mg enzyme for testosterone {ECO:0000269|PubMed:9188497}; Vmax=2.1 nmol/min/mg enzyme for estradiol {ECO:0000269|PubMed:9188497}; Note=Vmax was measured using transfected cell lysates.;
| null | null | null |
FUNCTION: NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro) (By similarity). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). {ECO:0000250|UniProtKB:O14756, ECO:0000269|PubMed:9188497}.
|
Rattus norvegicus (Rat)
|
O54754
|
AOXA_MOUSE
|
MDPIQLLFYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTAVTTVEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKASACCQSKENGVCCLDQEINGLAESQEEDKTSPELFSEEEFLPLDPTQELIFPPELMRIAEKQPPKTRVFYGERVTWISPVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIVQKLPEEKTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLSEEFLRKCPEADLKPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFREGGGVIEELSILYGGVGSTIISAKNSCQRLIGRPWNEGMLDTRCRLVLDEVTLAASAPGGKVEFKRTLIISFLFKFYLEVSQGLKREDPGHSPSLAGNHESALDDLHSKHPWRTLTHQNVDPAQLPQDPIGRPIMHLSGIKHATGEAIYCDDMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLQEANTFGTETFLATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLAPLILTIEEAIQHKSFFKSERKLECGNVDEAFKIVDQILEGEIHIGGQEHFYMETQSMLVVPKGEDGEIDIYVSTQFPKYIQDIVAATLKLSANKVMCHVRRVGGAFGGKVGKTSILAAITAFAASKHGRAVRCILERGEDMLITGGRHPYLGKYKAGFMNEGRILALDVEHYCNGGCSLDESLWVIEMGLLKLDNAYKFPNLRCRGWACRTNLPSNTALRGFGFPQAGLVTEACITEVAIKCGLSPEQVRTINMYKHVDTTHYKQEFSAKALSECWRECMAKCSYFERKAAIGKFNAENSWKKRGMAVIPLKFPVGIGSVAMGQAAALVHIYLDGSALVSHGGIEMGQGVHTKMIQVVSRELRMPMSSVHLRGTSTETVPNTNASGGSVVADLNGLAVKDACQTLLKRLEPIISKNPQGTWKDWAQTAFDQSISLSAVGYFRGYESNIDWEKGEGHPFEYFVFGAACSEVEINCLTGDHKNIRTNIVMDVGHSINPALDIGQVEGAFIQGMGLYTIEELSYSPQGTLYSRGPNQYKIPAICDIPTEMHISFLPPSEHSNTLYSSKGLGESGVFLGCSVFFAIHDAVKAARQERGISGPWKLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPCNIPV
|
1.17.3.-; 1.2.3.1
|
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:19401776}; Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000269|PubMed:19401776}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19401776}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19401776}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000269|PubMed:19401776}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000269|PubMed:19401776};
|
lipid metabolic process [GO:0006629]; xenobiotic metabolic process [GO:0006805]
|
cytosol [GO:0005829]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; aldehyde oxidase activity [GO:0004031]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; iron ion binding [GO:0005506]; molybdopterin cofactor binding [GO:0043546]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803]
|
PF01315;PF03450;PF00941;PF00111;PF01799;PF02738;PF20256;
|
3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10;
|
Xanthine dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10377246}.
|
CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2; Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067; EC=1.2.3.1; Evidence={ECO:0000269|PubMed:10190983, ECO:0000269|PubMed:19401776}; CATALYTIC ACTIVITY: Reaction=H2O + O2 + retinal = H(+) + H2O2 + retinoate; Xref=Rhea:RHEA:56736, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; Evidence={ECO:0000269|PubMed:10190983, ECO:0000269|PubMed:19401776};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.8 uM for retinal (at 37 degrees Celsius and pH 7.8) {ECO:0000269|PubMed:10190983}; KM=97.7 uM for benzaldehyde (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19401776}; KM=11.4 uM for phthalazine (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19401776}; KM=55.8 uM for retinal (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19401776}; KM=17.5 mM for acetaldehyde (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19401776}; Vmax=807 nmol/min/mg enzyme with retinal as substrate (at 37 degrees Celsius and pH 7.8) {ECO:0000269|PubMed:10190983}; Note=kcat is 317.6 min(-1) for benzaldehyde oxidation, 128.1 min(-1) for phthalazine oxidation, 49.5 min(-1) for retinal oxidation, and 519.9 min(-1) for acetaldehyde oxidation (at 30 degrees Celsius and pH 7.5) (PubMed:19401776). However in this article, the measures are done with the recombinant protein, which is only 20% active, due to an incomplete saturation of the molybdenum cofactor with the sulfido ligand (PubMed:19401776). {ECO:0000269|PubMed:19401776};
| null | null | null |
FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imidacloprid (IMI) via its nitroreduction to nitrosoguanidine (IMI-NNO) and aminoguanidine (IMI-NNH(2)). Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. Cannot use xanthine and hypoxanthine as substrate. {ECO:0000269|PubMed:10190983, ECO:0000269|PubMed:18671973, ECO:0000269|PubMed:19401776, ECO:0000269|PubMed:23462233}.
|
Mus musculus (Mouse)
|
O54766
|
ZP1_RAT
|
MAWGCFVVLLLLVAAPLRLGQHLHLKPGFQYSYDCGVQGMQLLVFPRPNQTIQFKVLDEFGNRFEVNNCSICYHWVISEAQKPAVFSADYKGCHVLEKQDGRFHLRVFIQAVLPNGRVDTAQDVTLICPKPDHILTPESYLAPPTTPQPFIPHTFALHPISGHTLAGSGHTGLTTLYPETHPTPAPPSSEPGPVGPTVPQSQWGTLGSWELTELDSIGTHLLQERCQVASGHIPCMVKGSSEEACQQAGCCYDNTKEMPCYYGNTVTLQCFRSGYFTLVMSQETALTHGVMLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGKQLVYENQLVSNIEVQTGPQGSITRDGVFRLHVRCIFNASDFLPIRASIFSPQPPAPVTRSGPLRLELRIATDKTFSSYYQGSDYPLVRLLQEPVYIEVRLLQRTDPGLALMLHQCWATPSASPFEQPQWPILSDGCPFKGDNYRTQMVAADRATLPFWSHYQRFTIATFTLLDSSSQNALRGQVYFFCSASACHPVGSETCSTTCDSEIARHRRSSGHHNSTIRALDIVSSPGAVGFEDAPKLEPSGSTRNSGSRPLLWVLQLLALTLVLGDGVLVGLSWAWAWA
| null | null |
binding of sperm to zona pellucida [GO:0007339]; prevention of polyspermy [GO:0060468]
|
collagen-containing extracellular matrix [GO:0062023]; egg coat [GO:0035805]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
acrosin binding [GO:0032190]; structural constituent of egg coat [GO:0035804]
|
PF00088;PF00100;
|
2.60.40.4100;2.60.40.3210;
|
ZP domain family, ZPB subfamily
|
PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.; PTM: O-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 1]: Zona pellucida {ECO:0000250|UniProtKB:P60852}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48829}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida.
|
Rattus norvegicus (Rat)
|
O54767
|
ZP2_RAT
|
MARWQRVYWLRSLFFALVTSVNSLSLPQSENPAFPGTLICDKDEVRVEFSSRFDMEKWNPSLVDTFGNEISNCTYALDLEKFILKFPYETCTIKVIGGYQVNIRVQDTNADVSYKDDVHHFFCPAIQAEIHEVSEIVVCMEDLISFSFPQLFSRLADENQNVSEMGWIIKIGNGTRVHTLPLKDAIVQGFNLLIDSQKITLHVPANATGVAHYVQESSYLYTVQLKLLFSSPGQKITFSSQAICAPDLSVACNVTHMSLTIPEFPGKLKSVGFGQRNIPEDQWHANGIDKEATNGLRLHFRKSLLKTKPSEKCPFYQFYFSSLELTFNFQGDMLSTVIDPECHCESPVSIDELCTRDGFMDFEVYSHQTKPALNLESLLVGNSSCQPIFKVQSLGLARFHIPLNGCGTRQKFEGDKVIYENEIHALWENPPSNIIFRNSEFRMTVRCHYIRDSMLLRAHIKSHSSPVASVKPGPLALVLQTYPDISYQRPYRKNEYPLVRYLRQPIYMEVTVLNRNDPNIKLVLDDCWATTFEDPASVPQWQIIMDGCEYELDNYRTTFHAANSSAAHSGHYQRFDVKTFAFVSESRGLSSLIYFHCSALICNQASPLCSVTCPAPLRNKREASKEGTMTVSLPGPIILLSDDSSSKGVMNPDSYEITKDIASKTLGAVAALVGSAVIIGFICYLHKKRIVRFNS
| null | null |
binding of sperm to zona pellucida [GO:0007339]; prevention of polyspermy [GO:0060468]
|
collagen-containing extracellular matrix [GO:0062023]; egg coat [GO:0035805]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]
|
acrosin binding [GO:0032190]; identical protein binding [GO:0042802]; structural constituent of egg coat [GO:0035804]
|
PF00100;
|
2.60.40.4100;2.60.40.3210;
|
ZP domain family, ZPA subfamily
|
PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida. {ECO:0000250|UniProtKB:P20239}.; PTM: Proteolytically cleaved in the N-terminal part by the metalloendopeptidase ASTL exocytosed from cortical granules after fertilization, yielding a N-terminal peptide of about 30 kDa which remains covalently attached to the C-terminal peptide via disulfide bond(s). This cleavage may play an important role in the post-fertilization block to polyspermy. Additional proteolytically cleavage of the N-terminal peptide of 30 kDa occurs in one-cell and two-cell embryos. {ECO:0000250|UniProtKB:P20239}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20239}.; PTM: O-glycosylated; contains sulfate-substituted glycans. {ECO:0000250|UniProtKB:P20239}.
|
SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 2]: Zona pellucida {ECO:0000250|UniProtKB:P20239}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20239}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor. {ECO:0000250|UniProtKB:P20239}.
|
Rattus norvegicus (Rat)
|
O54774
|
AP3D1_MOUSE
|
MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVCKLTYLQMLGYDISWAAFNIIEVMSASKFTFKRVGYLAASQCFHEGTDVIMLTTNQIRKDLSSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPESLRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAVLISLSSGMPNHSASIQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQSHKDLILQCLDDKDESIRLRALDLLYGMVSKKNLMEIVKKLMTHVDKAEGTTYRDELLTKIIDICSQSNYQHITNFEWYISILVELTRLEGTRHGHLIAAQMLDVAIRVKAIRKFAVSQMSSLLDSAHLVASSTQRNGICEVLYAAAWICGEFSEHLQGPQQTLEAMLRPKVTTLPGHIQAVYVQNVVKLYASILQQKEQAADTEAAQEVTQLLVERLPQFVQSADLEVQERASCILQLVKHVQKLQAKGVPVAEEVSALFAGELNPVAPKAQKKVPVPEGLDLDAWINEPPSDSESEDEKPKAIFHEEEPRHTRRRQPEEDEEELARRREARKQEQANNPFYIKSSPSPQKRYQDAPGVEHIPVVQIDLSVPLKVPGMPMSDQYVKLEEQRRHRQRLEKDKKRKKKEKGKRRHSSLPTESDEDIAPAQRVDIITEEMPENALPSDEDDKDPNDPYRALDIDLDKPLADSEKLPVQKHRNAEAVKSPEKEGVLGVEKKSKKPKKKEKKTKEREREKKDKKGEDLDFWLSTTPPPAAAPIPAPSTEELAASTITSPKDECEVLKGEEEDHVDHDQERKSSRHKKKKHRKEKEKEERPRDKKKAKKKQVAPLENGAAAEEEEEPIPPMSSYCLLAESPYIKVTYDIQASLQKDSQVTVSIILENQSSSFLKNMELNVLDSLNTKMTRPEGSSVHDGVPVPFQLPPGVSNEAQFVFTIQSIVMAQKLKGTLSFIAKDDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMNSIKVDGISMSFQNLLAKICFYHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGESSVSVDGKCSDATLLSSLLEEMKTTLAQC
| null | null |
anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; antigen processing and presentation [GO:0019882]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; clathrin-coated vesicle cargo loading, AP-3-mediated [GO:0035654]; endosome to melanosome transport [GO:0035646]; Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; intracellular transport [GO:0046907]; melanosome assembly [GO:1903232]; neurotransmitter receptor transport, postsynaptic endosome to lysosome [GO:0098943]; platelet dense granule organization [GO:0060155]; positive regulation of NK T cell differentiation [GO:0051138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to membrane [GO:0072657]; protein localization to organelle [GO:0033365]; protein targeting [GO:0006605]; protein targeting to vacuole [GO:0006623]; synaptic vesicle budding from endosome [GO:0016182]; synaptic vesicle coating [GO:0016183]; synaptic vesicle membrane organization [GO:0048499]; synaptic vesicle recycling [GO:0036465]; vesicle-mediated transport [GO:0016192]; vesicle-mediated transport in synapse [GO:0099003]; zinc ion import into lysosome [GO:0140916]
|
AP-3 adaptor complex [GO:0030123]; axon [GO:0030424]; axon cytoplasm [GO:1904115]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; postsynapse [GO:0098794]; presynapse [GO:0098793]; presynaptic endosome [GO:0098830]; terminal bouton [GO:0043195]; trans-Golgi network [GO:0005802]
| null |
PF01602;PF06375;
|
1.25.10.10;3.30.450.50;
|
Adaptor complexes large subunit family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes (By similarity). Involved in process of CD8+ T-cell and NK cell degranulation (By similarity). In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals (PubMed:21998198). {ECO:0000250|UniProtKB:O14617, ECO:0000269|PubMed:21998198}.
|
Mus musculus (Mouse)
|
O54775
|
CCN4_MOUSE
|
MRWLLPWTLAAVAVLRVGNILATALSPTPTTMTFTPAPLEETTTRPEFCKWPCECPQSPPRCPLGVSLITDGCECCKICAQQLGDNCTEAAICDPHRGLYCDYSGDRPRYAIGVCAQVVGVGCVLDGVRYTNGESFQPNCRYNCTCIDGTVGCTPLCLSPRPPRLWCRQPRHVRVPGQCCEQWVCDDDARRPRQTALLDTRAFAASGAVEQRYENCIAYTSPWSPCSTTCGLGISTRISNVNARCWPEQESRLCNLRPCDVDIQLHIKAGKKCLAVYQPEEATNFTLAGCVSTRTYRPKYCGVCTDNRCCIPYKSKTISVDFQCPEGPGFSRQVLWINACFCNLSCRNPNDIFADLESYPDFEEIAN
| null | null |
bone development [GO:0060348]; cell adhesion [GO:0007155]; glucose homeostasis [GO:0042593]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of fat cell differentiation [GO:0045599]; osteoblast differentiation [GO:0001649]; osteoclast differentiation [GO:0030316]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of inflammatory response [GO:0050729]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of Wnt signaling pathway [GO:0030177]; positive regulation of wound healing [GO:0090303]; regulation of cytokine production [GO:0001817]; signal transduction [GO:0007165]; Wnt signaling pathway [GO:0016055]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
heparin binding [GO:0008201]; integrin binding [GO:0005178]
|
PF00007;PF00219;PF19035;PF00093;
|
2.10.70.10;2.20.100.10;
|
CCN family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Downstream regulator in the Wnt/Frizzled-signaling pathway (By similarity). Associated with cell survival. Adheres to skin and melanoma fibroblasts (By similarity). In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan (By similarity). Suppresses tumor growth in vivo. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O54781
|
SRPK2_MOUSE
|
MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPEVTLKAADLEDTTEEETAKDNGEVEDQEEKEDAEKENAEKDEDDVEQELANLDPTWVESPKANGHIENGPFSLEQQLEDEEDDEDDCANPEEYNLDEPNAESDYTYSSSYEQFNGELPNGQHKTSEFPTPLFSGPLEPVACGSVISEGSPLTEQEESSPSHDRSRTVSASSTGDLPKTKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9446799};
|
angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; intracellular signal transduction [GO:0035556]; negative regulation of viral genome replication [GO:0045071]; nuclear speck organization [GO:0035063]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of viral genome replication [GO:0045070]; protein phosphorylation [GO:0006468]; R-loop processing [GO:0062176]; regulation of mRNA processing [GO:0050684]; RNA splicing [GO:0008380]; spliceosomal complex assembly [GO:0000245]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family
|
PTM: Phosphorylation at Thr-485 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic cleavage (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved at Asp-137 and Asp-401 by caspase-3 during apoptotic cell death. Cleavage at Asp-137 which is the major site of cleavage, produces a small N-terminal fragment that translocates into nucleus and promotes VP16-induced apoptosis (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9446799}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9446799}. Nucleus speckle {ECO:0000250|UniProtKB:P78362}. Chromosome {ECO:0000250|UniProtKB:P78362}. Note=Shuttles between the nucleus and the cytoplasm (By similarity). KAT5/TIP60 inhibits its nuclear translocation (By similarity). Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation (By similarity). Preferentially localizes across the entire gene coding region (By similarity). During transcription, accumulates at chromatin loci where unscheduled R-loops form and colocalizes with paused 'Ser-5'-phosphorlyated POLR2A/RNA polymerase II and helicase DDX23 (By similarity). {ECO:0000250|UniProtKB:P78362}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9446799}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9446799};
| null | null | null | null |
FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing (PubMed:9446799). Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression (PubMed:19592491). This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (By similarity). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (By similarity). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (By similarity). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity). {ECO:0000250|UniProtKB:P78362, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:9446799}.
|
Mus musculus (Mouse)
|
O54784
|
DAPK3_MOUSE
|
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRAAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9488481};
|
apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to type II interferon [GO:0071346]; chromatin organization [GO:0006325]; intracellular signal transduction [GO:0035556]; negative regulation of translation [GO:0017148]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cell shape [GO:0008360]; regulation of focal adhesion assembly [GO:0051893]; regulation of mitotic cell cycle [GO:0007346]; regulation of myosin II filament organization [GO:0043519]
|
actin filament [GO:0005884]; centrosome [GO:0005813]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nucleus [GO:0005634]; PML body [GO:0016605]
|
ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; kinase activity [GO:0016301]; leucine zipper domain binding [GO:0043522]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily
|
PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase does not lead to proteasomal degradation, but influences promyelocytic leukemia protein nuclear bodies (PML-NBs) formation in the nucleus. {ECO:0000269|PubMed:18515077}.; PTM: The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm and nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. {ECO:0000250|UniProtKB:O43293}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9488481}. Nucleus, PML body {ECO:0000269|PubMed:12917339}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O88764}. Chromosome, centromere {ECO:0000250|UniProtKB:O88764}. Cytoplasm {ECO:0000250|UniProtKB:O88764}. Note=Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments. Associated with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis (By similarity). {ECO:0000250|UniProtKB:O88764}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481};
| null | null | null | null |
FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation; in vitro phosphorylates PAWR (By similarity). Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates STAT3 and enhances its transcriptional activity. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis (By similarity). Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. {ECO:0000250|UniProtKB:O88764, ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481}.
|
Mus musculus (Mouse)
|
O54785
|
LIMK2_MOUSE
|
MAALAGDEAWRCRGCGTYVPLSQRLYRTANEAWHGSCFRCSECQESLTNWYYEKDGKLYCHKDYWAKFGEFCHGCSLLMTGPAMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQDQLPYSVTLISMPATTECRRGFSVTVESASSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAIKQTSQTLQLLIEHDPVPQRLDQLRLDARLPPHMQSTGHTLMLSTLDTKENQEGTLRRRSLRRSNSISKSPGPSSPKEPLLLSRDISRSESLRCSSSYSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSVDPFPWQQKVRFAKGISSGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRPPVEKATTKKRTLRKSDRKKRYTVVGNPYWMAPEMLNGKSYDETVDVFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCKLEPESRPAFSKLEDSFEALSLFLGELAIPLPAELEDLDHTVSMEYGLTRDSPP
|
2.7.11.1
| null |
actin cytoskeleton organization [GO:0030036]; astral microtubule organization [GO:0030953]; cornea development in camera-type eye [GO:0061303]; establishment of vesicle localization [GO:0051650]; head development [GO:0060322]; negative regulation of cilium assembly [GO:1902018]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein phosphorylation [GO:0001934]; protein phosphorylation [GO:0006468]; spermatogenesis [GO:0007283]
|
centrosome [GO:0005813]; cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00412;PF00595;PF07714;
|
2.30.42.10;2.10.110.10;1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family
|
PTM: Phosphorylated on serine and/or threonine residues by ROCK1. {ECO:0000250|UniProtKB:P53671}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53671}.; SUBCELLULAR LOCATION: [Isoform LIMK2a]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}.; SUBCELLULAR LOCATION: [Isoform LIMK2b]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53671}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:P53671}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53671}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:P53671};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP. Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). {ECO:0000250|UniProtKB:P53671}.
|
Mus musculus (Mouse)
|
O54786
|
DFFA_MOUSE
|
MELSRGASAPDPDDVRPLKPCLLRRNHSRDQHGVAASSLEELRSKACELLAIDKSLTPITLVLAEDGTIVDDDDYFLCLPSNTKFVALACNEKWIYNDSDGGTAWVSQESFEADEPDSRAGVKWKNVARQLKEDLSSIILLSEEDLQALIDIPCAELAQELCQSCATVQGLQSTLQQVLDQREEARQSKQLLELYLQALEKEGNILSNQKESKAALSEELDAVDTGVGREMASEVLLRSQILTTLKEKPAPELSLSSQDLESVSKEDPKALAVALSWDIRKAETVQQACTTELALRLQQVQSLHSLRNLSARRSPLPGEPQRPKRAKRDSS
| null | null |
apoptotic DNA fragmentation [GO:0006309]; chaperone-mediated protein folding [GO:0061077]; negative regulation of apoptotic DNA fragmentation [GO:1902511]; negative regulation of execution phase of apoptosis [GO:1900118]; positive regulation of apoptotic process [GO:0043065]; thymocyte apoptotic process [GO:0070242]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
deoxyribonuclease inhibitor activity [GO:0060703]; protein domain specific binding [GO:0019904]; protein folding chaperone [GO:0044183]
|
PF02017;PF09033;
|
3.10.20.10;1.10.1490.10;
| null |
PTM: Caspase-3 cleaves DFF45 at 2 sites to generate an active factor. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Inhibitor of the caspase-activated DNase (DFF40).
|
Mus musculus (Mouse)
|
O54788
|
DFFB_MOUSE
|
MCAVLRQPKCVKLRALHSACKFGVAARSCQELLRKGCVRFQLPMPGSRLCLYEDGTEVTDDCFPGLPNDAELLLLTAGETWHGYVSDITRFLSVFNEPHAGVIQAARQLLSDEQAPLRQKLLADLLHHVSQNITAETREQDPSWFEGLESRFRNKSGYLRYSCESRIRGYLREVSAYTSMVDEAAQEEYLRVLGSMCQKLKSVQYNGSYFDRGAEASSRLCTPEGWFSCQGPFDLESCLSKHSINPYGNRESRILFSTWNLDHIIEKKRTVVPTLAEAIQDGREVNWEYFYSLLFTAENLKLVHIACHKKTTHKLECDRSRIYRPQTGSRRKQPARKKRPARKR
|
3.-.-.-
| null |
apoptotic chromosome condensation [GO:0030263]; apoptotic DNA fragmentation [GO:0006309]; negative regulation of apoptotic DNA fragmentation [GO:1902511]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
disordered domain specific binding [GO:0097718]; DNA binding [GO:0003677]; DNA endonuclease activity [GO:0004520]; DNA nuclease activity [GO:0004536]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; nuclease activity [GO:0004518]
|
PF02017;PF09230;
|
3.10.20.10;6.10.140.170;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
| null | null | null | null | null |
FUNCTION: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
|
Mus musculus (Mouse)
|
O54790
|
MAFG_MOUSE
|
MTTPNKGNKALKVKREPGENGTSLTDEELVTMSVRELNQHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFARTVARSPVAPARGPLAAGLGPLVPGKVAATSVITIVKSKTDARS
| null | null |
adult behavior [GO:0030534]; in utero embryonic development [GO:0001701]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]; regulation of cellular pH [GO:0030641]; regulation of epidermal cell differentiation [GO:0045604]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF03131;
|
1.20.5.170;
|
BZIP family, Maf subfamily
|
PTM: Sumoylation at Lys-14 is required for active transcriptional repression. {ECO:0000269|PubMed:16738329}.; PTM: Acetylated in erythroid cells by CREB-binding protein (CBP). Acetylation augments the DNA-binding activity of NFE2, but has no effect on binding NFE2. {ECO:0000250|UniProtKB:O15525}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15525, ECO:0000255|PROSITE-ProRule:PRU00978}.
| null | null | null | null | null |
FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:16738329, PubMed:9679061). However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and recruiting them to specific DNA-binding sites (PubMed:16738329, PubMed:9679061). Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NFE2L2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NFE2L2. Activates globin gene expression when associated with NFE2L2 (By similarity). May be involved in signal transduction of extracellular H(+) (By similarity). {ECO:0000250|UniProtKB:O15525, ECO:0000250|UniProtKB:Q76MX4}.
|
Mus musculus (Mouse)
|
O54794
|
AQP7_MOUSE
|
MAPRSVLETIQSVLQKNMVREFLAEFLSTYVMMVFGLGSVAHMVLGENSGSYLGVNLGFGFGVTMGVHVAGGISGAHMNAAVTFTNCALGRMTWKKFPVYVLGQFLGSFSAAATTYLIFYGAINHFAGGDLLVTGSKATANIFATYLPEYMTLWRGFLDEAFVTGMLQLCLFAITDKKNSPALQGTEPLVIGILVTVLGVSLGMNSGYAINPSRDLPPRLFTFIAGWGKQVFRAGNNWWWVPVVAPLLGAYLGGIVYLGLIHPSIPQDPQRLENFTARDQKVTASYKNAASANISGSVPLEHF
| null | null |
glycerol transmembrane transport [GO:0015793]; renal water absorption [GO:0070295]; urea transport [GO:0015840]; water transport [GO:0006833]
|
basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cell cortex [GO:0005938]; cytoplasmic vesicle membrane [GO:0030659]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904]
|
glycerol channel activity [GO:0015254]; urea channel activity [GO:0015265]; urea transmembrane transporter activity [GO:0015204]; water channel activity [GO:0015250]
|
PF00230;
|
1.20.1080.10;
|
MIP/aquaporin (TC 1.A.8) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15746100, ECO:0000269|PubMed:17077387, ECO:0000269|PubMed:25643985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Cytoplasm, cell cortex {ECO:0000269|PubMed:25643985}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25643985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Lipid droplet {ECO:0000269|PubMed:25643985}. Note=Internalized from the cell membrane in response to catecholamine-induced activation of PKA; detected on intracellular membranes and colocalizes with lipid droplets (PubMed:25643985). Colocalizes with PLIN1 in adipocytes, probably on lipid droplets (By similarity). {ECO:0000250|UniProtKB:O14520, ECO:0000269|PubMed:25643985}.
| null | null | null | null | null |
FUNCTION: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH (PubMed:15591341, PubMed:15746100, PubMed:16009937). The channel is also permeable to urea (By similarity). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids (PubMed:15591341, PubMed:16009937). Mediates glycerol export from adipocytes (PubMed:15591341, PubMed:15746100, PubMed:16009937). After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia (PubMed:15591341). Required for normal glycerol reabsorption in the kidney (PubMed:15998844, PubMed:17077387). {ECO:0000250|UniProtKB:O14520, ECO:0000269|PubMed:15591341, ECO:0000269|PubMed:15746100, ECO:0000269|PubMed:15998844, ECO:0000269|PubMed:16009937, ECO:0000269|PubMed:17077387}.
|
Mus musculus (Mouse)
|
O54799
|
NMBR_MOUSE
|
MPPRSLSNLSFPTEANESELVPEVWEKDFLPDSDGTTAELVIRCVIPSLYLIIISVGLLGNIMLVKIFLTNSAMRNVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWVFGKLGCKLIPAIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGVLLWTSLKAVGIWVVSVLLAVPEAVFSEVARIGSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLVIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFVFCWFPNHVLYLYRSFNYKEIDPSLGHMIVTLVARVLSFSNSCVNPFALYLLSESFRKHFNSQLCCGRKSYPERSTSYLLSSSAVRMTSLKSNTKNVVTNSVLLNGHSTKQEIAL
| null | null |
antiviral innate immune response [GO:0140374]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of interleukin-6 production [GO:0032715]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of osteoclast proliferation [GO:0090290]; positive regulation of respiratory gaseous exchange [GO:1903942]; sneeze reflex [GO:0160023]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
bombesin receptor activity [GO:0004946]; neuropeptide receptor activity [GO:0008188]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Receptor for neuromedin-B (By similarity). Contributes to the maintenance of basal sigh rate through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (PubMed:26855425). Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR-expressing neurons in the sneeze-evoking region of the brainstem (PubMed:34133943). These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response (PubMed:34133943). Contributes to induction of acute itch, possibly through its activation on dorsal root ganglion neurons by the NMB peptide (PubMed:30734045). Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6 (PubMed:31601264). Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to the positive regulation of the expression of the CSF1 receptor CSF1R (PubMed:28780306). {ECO:0000250|UniProtKB:P24053, ECO:0000269|PubMed:26855425, ECO:0000269|PubMed:28780306, ECO:0000269|PubMed:30734045, ECO:0000269|PubMed:31601264, ECO:0000269|PubMed:34133943}.
|
Mus musculus (Mouse)
|
O54800
|
CADH8_RAT
|
MPERLAETLLDLWTPLIILWITLPSFVYMAPMNQAHVLTTGSPLELSRQSEEMRILNRSKRGWVWNQMFVLEEFSGPEPILVGRLHTDLDPGSKKIKYILSGDGAGTIFQINDITGDIHAIKRLDREEKAEYTLTAQAVDWETNKPLEPPSEFIIKVQDINDNAPEFLNGPYHATVPEMSILGTSVTNVTATDADDPVYGNSAKLVYSILEGQPYFSIEPETAIIKTALPNMDREAKEEYLVVIQAKDMGGHSGGLSGTTTLTVTLTDVNDNPPKFAQSLYHFSVPEDVVLGTAIGRVKANDQDIGENAQSSYDIIDGDGTALFEITSDAQAQDGVIRLRKPLDFETKKSYTLKVEAANIHIDPRFSGRGPFKDTATVKIVVEDADEPPVFSSPTYLLEVHENAALNSVIGQVTARDPDITSSPIRFSIDRHTDLERQFNINADDGKITLATPLDRELSVWHNISIIATEIRNHSQISRVPVAIKVLDVNDNAPEFASEYEAFLCENGKPGQVIQTVSAMDKDDPKNGHFFLYSLLPEMVNNPNFTIKKNEDNSLSILAKHNGFNRQKQEVYLLPIVISDSGNPPLSSTSTLTIRVCGCSNDGVVQSCNVEPYVLPIGLSMGALIAILACIILLLVIVVLFVTLRRHKNEPLIIKDDEDVRENIIRYDDEGGGEEDTEAFDIATLQNPDGINGFLPRKDIKPDLQFMPRQGLAPVPNGVDVDEFINVRLHEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESTTSDSDQNFDYLSDWGPRFKRLGELYSVGESDKET
| null | null |
adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; chemical synaptic transmission [GO:0007268]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; regulation of synapse organization [GO:0050807]; response to cold [GO:0009409]; spermatogenesis [GO:0007283]; synaptic transmission, glutamatergic [GO:0035249]
|
adherens junction [GO:0005912]; axon terminus [GO:0043679]; catenin complex [GO:0016342]; glutamatergic synapse [GO:0098978]; synaptic cleft [GO:0043083]; synaptic membrane [GO:0097060]
|
cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]
|
PF01049;PF00028;
|
2.60.40.60;4.10.900.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
|
Rattus norvegicus (Rat)
|
O54803
|
P2RX6_MOUSE
|
MQLQPAGTGNMASAAAAALVSWGFLDYKTEKYVLTRNCRVGVSQRLLQLAVVVYVIGWALLAKKGYQERDLAPQTSVITKLKGVSVTQVKELENRLWDVADFVKPSQGENVFFLVTNFLVTPAQVQGRCPEHPSVPLANCWADEDCPEGETGTYSHGIKTGQCVVFNGTHRTCEIWSWCPVESGAVPRKPLLAQAKNFTLFIKNTVTFSKFNFSRSNALLTWDNTYFKHCLYDPLSSPYCPVFRIGDLVAMAGGDFEDLALLGGAVGISIHWDCNLDTKGSDCCPQYSFQLQQKGYNFRTANHWWAASGVETRSLLKLYGIRFDILVTGQAGKFALIPTAITVGTGAAWLGMVTFLCDLLLLYVDREAGFYWRTKYEEARAPKTTTNSS
| null | null |
calcium ion transmembrane transport [GO:0070588]; response to ATP [GO:0033198]
|
cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; extracellularly ATP-gated monoatomic cation channel activity [GO:0004931]; protein-containing complex binding [GO:0044877]; purinergic nucleotide receptor activity [GO:0001614]
|
PF00864;
|
1.10.287.940;2.60.490.10;
|
P2X receptor family
|
PTM: N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O54804
|
CHKA_MOUSE
|
MKTKFCTGGEAEPSPLGLLLSCGGNAAPTPGVGQQRDAAGELESKQLGGRTQPLALPPPPPPPLPLPPPPSPPLADEQPEPRTRRRAYLWCKEFLPGAWRGLREDQFHISVIRGGLSNMLFQCSLPDSIASVGDEPRKVLLRLYGAILKMRSCNKEGSEQAQNENEFQGAEAMVLESVMFAILAERSLGPKLFGIFPQGRLEQFIPSRRLDTEELRLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLNQVLRLKFSREARVQQLHKILSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEGQENSERRKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPSRKQQLHFISSYLTTFQNDFESLSSEEQFATKEDMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMEYAQARFEAYFDQKRKLGV
|
2.7.1.32; 2.7.1.82
| null |
CDP-choline pathway [GO:0006657]; cellular response to glucose starvation [GO:0042149]; choline metabolic process [GO:0019695]; ethanolamine metabolic process [GO:0006580]; lipid droplet disassembly [GO:1905691]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811]
|
ATP binding [GO:0005524]; choline binding [GO:0033265]; choline kinase activity [GO:0004103]; cholinesterase activity [GO:0004104]; ethanolamine kinase activity [GO:0004305]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase activity [GO:0004713]
|
PF01633;
|
3.90.1200.10;
|
Choline/ethanolamine kinase family
|
PTM: [Isoform 1]: Phosphorylated at Ser-275 by AMPK in response to glucose deprivation, leading to localization to lipid droplets. {ECO:0000250|UniProtKB:P35790}.; PTM: [Isoform 1]: Acetylated by KAT5 at Lys-243 following phosphorylation by AMPK, leading to monomerization and conversion into a tyrosine-protein kinase. {ECO:0000250|UniProtKB:P35790}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35790}.; SUBCELLULAR LOCATION: [Isoform 1]: Lipid droplet {ECO:0000250|UniProtKB:P35790}. Note=Isoform 1 localizes to lipid droplets following phosphorylation by AMPK. {ECO:0000250|UniProtKB:P35790}.
|
CATALYTIC ACTIVITY: Reaction=ATP + choline = ADP + H(+) + phosphocholine; Xref=Rhea:RHEA:12837, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:295975, ChEBI:CHEBI:456216; EC=2.7.1.32; Evidence={ECO:0000250|UniProtKB:P35790}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838; Evidence={ECO:0000250|UniProtKB:P35790}; CATALYTIC ACTIVITY: Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine; Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216; EC=2.7.1.82; Evidence={ECO:0000250|UniProtKB:P35790}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070; Evidence={ECO:0000250|UniProtKB:P35790}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P35790}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597; Evidence={ECO:0000250|UniProtKB:P35790};
| null |
PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1. {ECO:0000250|UniProtKB:P35790}.; PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. {ECO:0000250|UniProtKB:P35790}.
| null | null |
FUNCTION: Plays a key role in phospholipid biosynthesis by catalyzing the phosphorylation of free choline to phosphocholine, the first step in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine, thereby contributing to phosphatidylethanolamine biosynthesis. Has higher activity with choline. May contribute to tumor cell growth. {ECO:0000250|UniProtKB:P35790}.; FUNCTION: [Isoform 1]: This isoform plays a key role in lipolysis of lipid droplets following glucose deprivation (By similarity). In response to glucose deprivation, phosphorylated by AMPK, promoting localization to lipid droplets (By similarity). Phosphorylation is followed by acetylation by KAT5, leading to dissociation of the homodimer into a monomer (By similarity). Monomeric CHKA isoform 1 is converted into a tyrosine-protein kinase, which phosphorylates lipid droplet structural proteins PLIN2 and PLIN3, leading to lipolysis of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P35790}.
|
Mus musculus (Mouse)
|
O54814
|
CCR3_RAT
|
MASNEEELKTVVETFETTPYEYEWAPPCEKVSIRELGSWLLPPLYSLVFIVGLLGNMMVVLILIKYRKLQIMTNIYLLNLAISDLLFLFTVPFWIHYVLWNEWGFGHCMCKMLSGLYYLALYSEIFFIILLTIDRYLAIVHAVLALRARTVTFATITSIITWGFAVLAALPEFIFHESQDNFGDLSCSPRYPEGEEDSWKRFHALRMNIFGLALPLLIMVICYSGIIKTLLRCPNKKKHKAIQLIFVVMIVFFIFWTPYNLVLLLSAFHSTFLETSCQQSIHLDLAMQVTEVITHTHCCINPIIYAFVGERFRKHLRLFFHRNVAIYLRKYISFLPGEKLERTSSVSPSTGEQEISVVF
| null | null |
angioblast cell migration [GO:0035476]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; chemotaxis [GO:0006935]; eosinophil chemotaxis [GO:0048245]; ERK1 and ERK2 cascade [GO:0070371]; immune response [GO:0006955]; inflammatory response [GO:0006954]; mast cell chemotaxis [GO:0002551]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of endothelial cell proliferation [GO:0001938]
|
cytoplasm [GO:0005737]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]
|
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; chemokine receptor activity [GO:0004950]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Receptor for C-C type chemokine. Binds and responds to a variety of chemokines, including CCL11, CCL26, CCL7, CCL13, RANTES(CCL5) and CCL15. Subsequently transduces a signal by increasing the intracellular calcium ions level. In addition acts as a possible functional receptor for NARS1. {ECO:0000250|UniProtKB:P51677}.
|
Rattus norvegicus (Rat)
|
O54824
|
IL16_MOUSE
|
MEPHGHSGKSRKSTKFRSISRSLILCNAKTSDDGSSPDEKYPDPFETSLCQGKEGFFHSSMQLADTFEAGLSNIPDLALASDSAQLAAAGSDRGKHCRKMFFMKESSSTSSKEKSGKPEAQSSSFLFPKACHQRTRSNSTSVNPYSAGEIDFPMTKKSAAPTDRQPYSLCSNRKSLSQQLDYPILGTARPTRSLSTAQLGQLSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKSIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTTPPSLCSHLSPPLCRSLSSSTCGAQDSSPFSLESPASPASTAKPNYRIMVEVSLKKEAGVGLGIGLCSIPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEINDSPVHCLTLNEVYTILSHCDPGPVPIIVSRHPDPQVSEQQLKEAVAQAVEGVKFGKDRHQWSLEGVKRLESSWHGRPTLEKEREKHSAPPHRRAQKIMVRSSSDSSYMSGSPGGSPCSAGAEPQPSEREGSTHSPSLSPGEEQEPCPGVPSRPQQESPPLPESLERESHPPLRLKKSFEILVRKPTSSKPKPPPRKYFKNDSEPQKKLEEKEKVTDPSGHTLPTCSQETRELLPLLLQEDTAGRAPCTAACCPGPAASTQTSSSTEGESRRSASPETPASPGKHPLLKRQARMDYSFDITAEDPWVRISDCIKNLFSPIMSENHSHTPLQPNTSLGEEDGTQGCPEGGLSKMDAANGAPRVYKSADGSTVKKGPPVAPKPAWFRQSLKGLRNRAPDPRRPPEVASAIQPTPVSRDPPGPQPQASSSIRQRISSFENFGSSQLPDRGVQRLSLQPSSGETTKFPGKQDGGRFSGLLGQGATVTAKHRQTEVESMSTTFPNSSEVRDPGLPESPPPGQRPSTKALSPDPLLRLLTTQSEDTQGPGLKMPSQRARSFPLTRTQSCETKLLDEKASKLYSISSQLSSAVMKSLLCLPSSVSCGQITCIPKERVSPKSPCNNSSAAEGFGEAMASDTGFSLNLSELREYSEGLTEPGETEDRNHCSSQAGQSVISLLSAEELEKLIEEVRVLDEATLKQLDSIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGATHNDALAILRQARDPRQAVIVTRRTTVEATHDLNSSTDSAASASAASDISVESKEATVCTVTLEKTSAGLGFSLEGGKGSLHGDKPLTINRIFKGTEQGEMVQPGDEILQLAGTAVQGLTRFEAWNVIKALPDGPVTIVIRRTSLQCKQTTASADS
| null | null |
induction of positive chemotaxis [GO:0050930]; leukocyte chemotaxis [GO:0030595]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 alpha production [GO:0032730]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; regulation of calcium ion transport [GO:0051924]
|
collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular space [GO:0005615]; Flemming body [GO:0090543]; focal adhesion [GO:0005925]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]
|
CD4 receptor binding [GO:0042609]; cytokine activity [GO:0005125]
|
PF00595;
|
2.30.42.10;
| null |
PTM: Synthesized as a chemo-attractant inactive precursor which is proteolytically cleaved by caspase-3 to yield IL-16. {ECO:0000269|PubMed:10479680}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:10479680}. Note=Colocalizes with GRIN2C in neuronal cell bodies and neurites.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; FUNCTION: Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane.; FUNCTION: Isoform 2 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
|
Mus musculus (Mouse)
|
O54825
|
BYST_MOUSE
|
MPKFKVTRGASNREKHAPLAEQILAGNAVRAGTREKRRGREVEEEEEYVGPRLSRRILQQARQQQEELETDHGAGDRSAPPRERATRLGPGLPQDGSDEEDEEWPTLEKAAKMAGVDHQAEVIVDPEDERAIEMFMNKNPPVRRTLADIIMEKLTEKQTEVETVMSEVSGFPMPQLDPRVLEVYRGVREVLCKYRSGKLPKAFKVIPALSNWEQILYVTEPEAWTAAAMYQATRIFASNLKERMAQRFYNLVLLPRVRDDIAEYKRLNFHLYMALKKALFKPGAWFKGILIPLCESGTCTLREAIIVGSIITKCSIPVLHSSAAMLKIAEMEYSGANSIFLRLLLDKKYALPYRVLDALVFHFLAFRTEKRQLPVLWHQCLLTLAQRYKADLATEQKEALLELLRLQPHPQLSPEIRRELQSAVPRDVEDGGVTME
| null | null |
blastocyst formation [GO:0001825]; in utero embryonic development [GO:0001701]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; rRNA processing [GO:0006364]; stem cell proliferation [GO:0072089]; trophectodermal cell differentiation [GO:0001829]
|
apical part of cell [GO:0045177]; cell projection [GO:0042995]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; preribosome, small subunit precursor [GO:0030688]
|
snoRNA binding [GO:0030515]
|
PF05291;
| null |
Bystin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17242206}. Nucleus, nucleolus {ECO:0000269|PubMed:17242206}. Note=Associated with 40S ribosomal subunits.
| null | null | null | null | null |
FUNCTION: Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. {ECO:0000269|PubMed:17055491, ECO:0000269|PubMed:17242206}.
|
Mus musculus (Mouse)
|
O54827
|
AT10A_MOUSE
|
MERELPAAEESASSGWRRPRRRRWEGRTRTVRSNLLPPLGTEDSTIGAPKGERLLMRGCIQHLADNRLKTTKYTLLSFLPKNLFEQFHRLANVYFVFIALLNFVPAVNAFQPGLALAPVLFILAVTAIKDLWEDYSRHRSDHEINHLGCLVFSREEKKYVNRYWKEIRVGDFVRLCCNEIIPADILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDLSRFRGYIMHSNGEKAGLHKENLLLRGCTIRNTEAVAGIVIYAGHETKALLNNSGPRYKRSQLERQMNCDVLWCVLLLVCISLFSAVGHGLWVRRYQEKKALFDVPESDGSSLSPATAAVYSFFTMIIVLQVLIPISLYVSIEIVKVCQVYFINQDIELYDEETDSQLQCRALNITEDLGQIKYIFSDKTGTLTENKMVFRRCTVSGIEYSHDANAQRLARYQEADSEEEEVVSKVGTISHRGSTGSHQSIWMTHKTQSIKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEKVSECDRFLAIARHQEHPLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRQKVRVRFELKSPVKTIEDFLRRFTPSRLASGCSSIGNLSTSKSSHKSGSAFLPSLSQDSMLLGLEEKLGQTAPSIASNGYASQAGQEESWASECTTDQKCPGEQREQQEGELRYEAESPDEAALVYAARAYNCALVDRLHDQVSVELPHLGRLTFELLHTLGFDSIRKRMSVVIRHPLTDEINVYTKGADSVVMDLLLPCSSDDARGRHQKKIRSKTQNYLNLYAVEGLRTLCIAKRVLSKEEYACWLQSHIEAEASVESREELLFQSAVRLETNLHLLGATGIEDRLQEGVPETIAKLRQAGLQIWVLTGDKQETAINIAYACKLLDHGEEVITLNADSQEACAALLDQCLSYVQSRNPRSTLQNSESNLSVGFSFNPVSTSTDASPSPSLVIDGRSLAYALEKSLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRSKLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPRFRYLERLLIVHGHWCYSRLANMVLYFFYKNTMFVGLLFWFQFYCGFSASAMIDQWYLIFFNLLFSSLPQLVTGVLDKDVPADMLLREPQLYKSGQNMEEYRPRAFWLNMVDAAFQSLVCFFIPYLAYYDSDVDVFTWGTPVTAIALFTFLLHLGIETKTWTWLNWLACGFSTFLFFSVALIYNTSCATCYPPSNPYWTMQTLLGDPLFYLTCLIAPIAALLPRLFFKALQGSLFPTQLQLGRQLAKKPLNKFSDPKETFAQGQPPGHSETELSERKTMGPFETLPRDCASQASQFTQQLTCSPEASGEPSAVDTNMPLRENTLLEGLGSQASGSSMPRGAISEVCPGDSKRQSTSASQTARLSSLFHLPSFGSLNWISSLSLASGLGSVLQLSGSSLQMDKQDGEFLSNPPQPEQDLHSFQGQVTGYL
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
|
phospholipid translocation [GO:0045332]; positive regulation of membrane tubulation [GO:1903527]
|
endoplasmic reticulum membrane [GO:0005789]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; glycosylceramide flippase activity [GO:0140351]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine floppase activity [GO:0090554]
|
PF13246;PF16212;PF16209;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
|
PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase signature sequence. {ECO:0000250|UniProtKB:O94823}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60312}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60312}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60312}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not that of TMEM30B. {ECO:0000250|UniProtKB:O60312}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:O60312}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60312}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584; Evidence={ECO:0000250|UniProtKB:O60312}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60312}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037; Evidence={ECO:0000250|UniProtKB:O60312};
| null | null | null | null |
FUNCTION: Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. Initiates inward plasma membrane bending and recruitment of Bin/amphiphysin/Rvs (BAR) domain-containing proteins involved in membrane tubulation and cell trafficking. Facilitates ITGB1/beta1 integrin endocytosis, delaying cell adhesion and cell spreading on extracellular matrix. Has low flippase activity toward glucosylceramide (GlcCer). {ECO:0000250|UniProtKB:O60312}.
|
Mus musculus (Mouse)
|
O54828
|
RGS9_MOUSE
|
MTIRHQGQQYRPRMAFLQKIEALVKDMQNPETGVRMHNQRVLVTSVPHAMTGGDVLQWITQRLWISNLEAQNLGNFIVKYGYIYPLQDPKNLILKPDSSLYRFQTPYFWPTQQWPAEDTDYAIYLAKRNIKKKGILEEYEKENYDFLNKKINYKWDFVIMQAKEQYRTGKERNKADRYALDCQEKAYWLVHRSPPGMNNVLDYGLDRVTNPNEVKKQTVTAVRKEIMYYQQALMRSTVKSSVSLGGIVKYSEQFSSNDAIMSGCLPSNPWITDDTQFWDLNAKLVEIPTKMRVERWAFNFSELIRDPKGRQSFQYFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDITVKGLRHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKEMLAKAIEPQETTKRSSTLPFMRRHLRSSPSPVILRQLEEEEKAREAANTVDITQPGQHLAPSPHLAVYTGTCVPPSPSSPFSPSCRSPRKPFASPSRFIRRPSIAICPSPSRVALEGSSGLEPKGEASWSGANSGPSVTENREPSADHSRPQPRAPPKARAALSLGRFLRRGCLASPVFARLSPKCPSVSHGKVQPLGDMGQQLPRLKPKKVANFFQIKMEMPTDSGTCLMDSDDPRAGESGDQTTEKEVICPWESLAEGKAG
| null | null |
dark adaptation [GO:1990603]; dopamine receptor signaling pathway [GO:0007212]; G protein-coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; light adaption [GO:0036367]; negative regulation of signal transduction [GO:0009968]; nervous system development [GO:0007399]; regulation of calcium ion export across plasma membrane [GO:1905912]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; response to amphetamine [GO:0001975]; response to estradiol [GO:0032355]; visual perception [GO:0007601]
|
cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]
|
GTPase activator activity [GO:0005096]
|
PF00610;PF00631;PF00615;PF18148;
|
1.10.1240.60;1.10.167.10;4.10.260.10;1.10.10.10;
| null |
PTM: Retinal isoform 1 is light-dependent phosphorylated at 'Ser-475'. Phosphorylation is decreased by light exposition. Interaction with RGS9BP is decreased when isoform 1 is phosphorylated at 'Ser-475'. {ECO:0000269|PubMed:11292825}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Peripheral membrane protein. Note=Isoform 1 is targeted to the membrane via its interaction with RGS9BP.
| null | null | null | null | null |
FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction; key element in the recovery phase of visual transduction.
|
Mus musculus (Mouse)
|
O54829
|
RGS7_MOUSE
|
MAQGNNYGQTSNGVADESPNMLVYRKMEDVIARMQDEKNGIPIRTVKSFLSKIPSVFSGSDIVQWLIKNLTIEDPVEALHLGTLMAAHGYFFPISDHVLTLKDDGTFYRFQTPYFWPSNCWEPENTDYAVYLCKRTMQNKARLELADYEAESLARLQRAFARKWEFIFMQAEAQAKVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDIKKSSRMRNPHKTRKSVYGLQNDIRSHSPTHTPTPETKPPTEDELHQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYVEYDPFLVPPDPSNPWLSDDTTFWELEASKEPSQQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKRRPIREVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQELLQAKRKGKTLTSKRLTSLVQSY
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; positive regulation of potassium ion transmembrane transport [GO:1901381]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of postsynaptic membrane potential [GO:0060078]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite terminus [GO:0044292]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynapse [GO:0098793]; protein-containing complex [GO:0032991]
|
G-protein alpha-subunit binding [GO:0001965]; G-protein beta-subunit binding [GO:0031681]; GTPase activator activity [GO:0005096]
|
PF00610;PF00631;PF00615;PF18148;
|
1.10.1240.60;1.10.167.10;4.10.260.10;1.10.10.10;
| null |
PTM: Palmitoylated. {ECO:0000250|UniProtKB:O46470}.; PTM: Ubiquitinated, leading to rapid proteasomal degradation. {ECO:0000250|UniProtKB:P49802}.; PTM: Phosphorylation and subsequent interaction with 14-3-3 proteins inhibits GAP activity. {ECO:0000250|UniProtKB:P49802}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49802}. Cytoplasm {ECO:0000250|UniProtKB:P49802}. Cell membrane {ECO:0000269|PubMed:22689652, ECO:0000269|PubMed:25792749, ECO:0000269|PubMed:30546127}. Membrane {ECO:0000250|UniProtKB:P49802}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49802}; Cytoplasmic side {ECO:0000250|UniProtKB:P49802}. Note=Interaction with PKD1 promotes location at the cell membrane. Interaction with RGS7BP promotes location at the cell membrane. {ECO:0000250|UniProtKB:P49802}.
| null | null | null | null | null |
FUNCTION: GTPase activator component of the RGS7-GNB5 complex that regulates G protein-coupled receptor signaling cascades (PubMed:25792749). The RGS7-GNB5 complex acts as an inhibitor signal transduction by promoting the GTPase activity of G protein alpha subunits, such as GNAO1, thereby driving them into their inactive GDP-bound form (By similarity). May play a role in synaptic vesicle exocytosis (By similarity). Glycine-dependent regulation of the RGS7-GNB5 complex by GPR158 affects mood and cognition via its ability to regulate neuronal excitability in L2/L3 pyramidal neurons of the prefrontal cortex (PubMed:30546127, PubMed:31311860). Modulates the activity of potassium channels that are activated by GNAO1 in response to muscarinic acetylcholine receptor M2/CHRM2 signaling (By similarity). {ECO:0000250|UniProtKB:P49802, ECO:0000269|PubMed:25792749, ECO:0000269|PubMed:30546127, ECO:0000269|PubMed:31311860}.
|
Mus musculus (Mouse)
|
O54833
|
CSK22_MOUSE
|
MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGQDNYDQLVRIAKVLGTDELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCAENTVLSSGLTAAR
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; cell cycle [GO:0007049]; double-strand break repair [GO:0006302]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of chromosome separation [GO:1905818]; spermatogenesis [GO:0007283]; Wnt signaling pathway [GO:0016055]
|
acrosomal vesicle [GO:0001669]; chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; protein kinase CK2 complex [GO:0005956]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28355567}. Cytoplasm {ECO:0000269|PubMed:28355567}. Note=Interaction with SIRT6 prevents translocation into the nucleus. {ECO:0000269|PubMed:28355567}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Phosphorylates a number of DNA repair proteins in response to DNA damage, such as MDC1, RAD9A, RAD51 and HTATSF1, promoting their recruitment to DNA damage sites. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. {ECO:0000250|UniProtKB:P19784}.
|
Mus musculus (Mouse)
|
O54834
|
RHG06_MOUSE
|
MSAQSLLHSVFSCSSPASGGTASAKGFSKRKLRQTRSLDPALIGGCGSEMGAEGGLRGSTVSRLHSPQLLAEGLGSRLASSPRSQHLRATRFQTPRPLCSSFSTPSTPQEKSPSGSFHFDYEVPLSRSGLKKSMAWDLPSVLAGSGSASSRSPASILSSSGGGPNGIFSSPRRWLQQRKFQPPPNSRSHPYVVWRSEGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLGCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQREEQKDASSDFVSSLLPFGNKKQNKELSSSNSSLSSTSETPNESTSPNTPEPAPRARRRGAMSVDSITDLDDNQSRLLEALQLSLPAEAQSKKEKARDKKLSLNPIYRQVPRLVDSCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGVDVCLEEEHSVHDVAALLKEFLRDMPDPLLTRELYTAFINTLLLEPEEQLGTLQLLIYLLPPCNCDTLHRLLQFLSIVARHADDNVSKDGQEVTGNKMTSLNLATIFGPNLLHKQKSSDKEYSVQSSARAEESTAIIAVVQKMIENYEALFMVPPDLQNEVLISLLETDPDVVDYLLRRKASQSSSPDILQTEVSFSMGGRHSSTDSNKASSGDISPYDNNSPVLSERSLLAMQEDRARGGSEKLYKVPEQYTLVGHLSSPKSKSRESSPGPRLGKEMSEEPFNIWGTWHSTLKSGSKDPGMTGSYGDIFESSSLRPRPCSLSQGNLSLNWPRCQGSPTGLDSGTQVIRRTQTAATVEQCSVHLPVSRVCSTPHIQDGSRGTRRPAASSDPFLSLNSTEDLAEGKEDVAWLQSQARPVYQRPQESGKDDRRPPPPYPGSGKPATTSAQLPLEPPLWRLQRHEEGSETAVEGGQQASGEHQTRPKKLSSAYSLSASEQDKQNLGEASWLDWQRERWQIWELLSTDNPDALPETLV
| null | null |
actin filament organization [GO:0007015]; focal adhesion assembly [GO:0048041]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of stress fiber assembly [GO:0051497]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165]
|
actin cytoskeleton [GO:0015629]; cytosol [GO:0005829]
|
GTPase activator activity [GO:0005096]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; SH3 domain binding [GO:0017124]
|
PF00620;
|
1.10.555.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O54835
|
SMAD9_RAT
|
MHPSTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQSLGPAPPSSPGHVFPQSPCPTSYPQSPGSPSESDSPYQHSDFRPVCYEEPLHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKVFNNQLFAQLLAQLLAQSVHHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
| null | null |
anatomical structure morphogenesis [GO:0009653]; BMP signaling pathway [GO:0030509]; bone development [GO:0060348]; cartilage development [GO:0051216]; cell differentiation [GO:0030154]; cellular response to organic cyclic compound [GO:0071407]; hindbrain development [GO:0030902]; midbrain development [GO:0030901]; Mullerian duct regression [GO:0001880]; positive regulation of cell differentiation [GO:0045597]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; response to hypoxia [GO:0001666]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]
|
cytoplasm [GO:0005737]; heteromeric SMAD protein complex [GO:0071144]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF03165;PF03166;
|
2.60.200.10;3.90.520.10;
|
Dwarfin/SMAD family
|
PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase (By similarity). Phosphorylated by activin type I receptor-like kinase-2 (ALK-2). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD) (By similarity). Has been shown to be activated by activin type I receptor-like kinase-2 (ALK-2) which stimulates heteromerization between SMAD9 and SMAD4. ALK-2 binds TGF-beta, activin and BMP. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O54838
|
DUS5_RAT
|
MKVTSLDGRRLRKMLRKEAEARCVVLDCRPYLAFAASSVRGSLNVNLNSVVLRRARGGAVSARYVLADEAARARLLQEGGGGVAAVVVLDQGSRHWQKLREESAARVVLTSLLACLSAGPRVYFLKGGYETFYSQYPECCVDAKPISQEKLEGERGLLSQCGKPILSVAYRPAYDQGGPVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRTSEACTTHLHYKWIPVEDSHTADISSHFQEAIDFIDCVREEGGKVLVHCEAGVSRSPTICMAYLMKTKQFRLKEAFEYIKQRRSVVSPNFGFMGQLLQYESEILPSTPTPQPPSCQGEAASSTFIGHLQTLSPDMQGAYCTFPTSVLAPVPTHATVAELHRSPVATATSC
|
3.1.3.16; 3.1.3.48
| null |
dephosphorylation [GO:0016311]; endoderm formation [GO:0001706]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of vasoconstriction [GO:0045906]; peptidyl-threonine dephosphorylation [GO:0035970]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of cerebral blood circulation [GO:0120277]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
MAP kinase tyrosine phosphatase activity [GO:0033550]; MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine/threonine phosphatase activity [GO:0008330]
|
PF00782;PF00581;
|
3.90.190.10;3.40.250.10;
|
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q16690, ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:Q16690}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:Q16690};
| null | null | null | null |
FUNCTION: Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues. The highest relative activity is toward ERK1. {ECO:0000250|UniProtKB:Q16690}.
|
Rattus norvegicus (Rat)
|
O54839
|
EOMES_MOUSE
|
MQLGEQLLVSSVNLPGAHFYSLESARGGGGGGGGGGGGGGGSVSLLPGAAPSPQRLDLDKASKKFPGSLPCQAGSAEPAGAGAGAPAAMLSDADAGDTFGSTSAVAKPGPPDGRKGSPCAEEELPSAATAAATARYSMDSLSSERYYLPSPGPQGSELAAPCSLFQYPAAAGAAHGPVYPASNGARYPYGSMLPPGGFPAAVCPPARAQFGPAAGSGSGAGSSGGGAGGPGAYPYGQGSPLYGPYAGTSAAGSCGGLGGLGVPGSGFRAHVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNINGLNPTAHYNVFVEVVLADPNHWRFQGGKWVTCGKADNNMQGNKMYVHPESPNTGSHWMRQEISFGKLKLTNNKGANNNNTQMIVLQSLHKYQPRLHIVEVTEDGVEDLNEPSKTQTFTFSETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDSMYTASENDRLTPSPTDSPRSHQIVPGGRYGVQNFFPEPFVNTLPQARYYNGERTVPQTNGLLSPQQSEEVANPPQRWLVTPVQQPVTNKLDIGSYESEYTSSTLLPYGIKSLPLQTSHALGYYPDPTFPAMAGWGGRGAYQRKMAAGLPWTSRMSPPVFPEDQLAKEKVKEEISSSWIETPPSIKSLDSSDSGVYNSACKRKRLSPSTPSNGNSPPIKCEDINTEEYSKDTSKGMGAYYAFYTSP
| null | null |
adaptive immune response [GO:0002250]; anatomical structure morphogenesis [GO:0009653]; astrocyte differentiation [GO:0048708]; blastocyst development [GO:0001824]; cardioblast differentiation [GO:0010002]; CD8-positive, alpha-beta T cell differentiation involved in immune response [GO:0002302]; cell differentiation [GO:0030154]; cell differentiation involved in embryonic placenta development [GO:0060706]; cerebral cortex development [GO:0021987]; cerebral cortex neuron differentiation [GO:0021895]; cerebral cortex regionalization [GO:0021796]; chromatin remodeling [GO:0006338]; DNA demethylation [GO:0080111]; endoderm development [GO:0007492]; endoderm formation [GO:0001706]; endodermal cell fate specification [GO:0001714]; gene expression [GO:0010467]; mesendoderm development [GO:0048382]; mesoderm formation [GO:0001707]; mesodermal to mesenchymal transition involved in gastrulation [GO:0060809]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neurogenesis [GO:0022008]; neuron differentiation [GO:0030182]; neuron migration [GO:0001764]; olfactory bulb development [GO:0021772]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle cell differentiation [GO:0035914]; stem cell population maintenance [GO:0019827]; trophectodermal cell differentiation [GO:0001829]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]
|
PF00907;PF16176;
|
2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation of the intermediate progenitor cells and their progeny in the cerebral cortex. Also involved in the differentiation of CD8+ T-cells during immune response regulating the expression of lytic effector genes. {ECO:0000269|PubMed:10716450, ECO:0000269|PubMed:14605368, ECO:0000269|PubMed:18171685, ECO:0000269|PubMed:18940588}.
|
Mus musculus (Mouse)
|
O54842
|
NUPR1_RAT
|
MATLPPTAHTSQQPVNIEDEDGILDEYDQYSLAQSYVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR
| null | null |
acute inflammatory response [GO:0002526]; fibroblast apoptotic process [GO:0044346]; fibroblast proliferation [GO:0048144]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; male gonad development [GO:0008584]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagosome assembly [GO:1902902]; negative regulation of autophagy [GO:0010507]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of glycolytic process [GO:0045820]; negative regulation of programmed necrotic cell death [GO:0062099]; negative regulation of type B pancreatic cell proliferation [GO:1904691]; positive regulation of cell cycle [GO:0045787]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of neuroinflammatory response [GO:0150078]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of oxidative phosphorylation [GO:1903862]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of protein modification process [GO:0031401]; protein-containing complex assembly [GO:0065003]; regulation of autophagy [GO:0010506]; regulation of female gonad development [GO:2000194]; regulation of response to endoplasmic reticulum stress [GO:1905897]; response to toxic substance [GO:0009636]; skeletal muscle cell differentiation [GO:0035914]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-DNA complex [GO:0032993]
|
acetyltransferase activator activity [GO:0010698]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713]
|
PF10195;
| null |
NUPR family
|
PTM: Phosphorylated. Phosphorylation promotes DNA-binding activity. {ECO:0000250|UniProtKB:O60356}.; PTM: Acetylated. {ECO:0000250|UniProtKB:O60356}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60356}. Cytoplasm {ECO:0000250|UniProtKB:O60356}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O60356}.
| null | null | null | null | null |
FUNCTION: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses (PubMed:20181828, PubMed:27031958, PubMed:28694771). Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (By similarity). Negatively regulates apoptosis through interaction with PTMA (By similarity). Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter (PubMed:20181828). Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (PubMed:27031958, PubMed:28694771). Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (By similarity). Coactivator of PAX2 transcription factor activity, both by recruiting the EP300 cofactor to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (By similarity). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (By similarity). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (By similarity). Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity). {ECO:0000250|UniProtKB:O60356, ECO:0000250|UniProtKB:Q9WTK0, ECO:0000269|PubMed:20181828, ECO:0000269|PubMed:27031958, ECO:0000269|PubMed:28694771}.
|
Rattus norvegicus (Rat)
|
O54851
|
CXD2_MOUSE
|
MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVAIVGETVYDDEQTMFVCNTLQPGCNQACYDRAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSAKQRERRYSTVFLALDRDPAESIGGPGGTGGGGSGGSKREDKKLQNAIVNGVLQNTETTSKETEPDCLEVKELTPHPSGLRTAARSKLRRQEGISRFYIIQVVFRNALEIGFLVGQYFLYGFSVPGLYECNRYPCIKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKLAVRGAQAKRKSVYEIRNKDLPRVSVPNFGRTQSSDSAYV
| null | null |
cell-cell signaling [GO:0007267]; chemical synaptic transmission [GO:0007268]; neuronal action potential [GO:0019228]; visual perception [GO:0007601]
|
connexin complex [GO:0005922]; gap junction [GO:0005921]; synapse [GO:0045202]
|
gap junction channel activity [GO:0005243]
|
PF00029;
|
1.20.1440.80;
|
Connexin family, Delta-type subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
| null | null | null | null | null |
FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
|
Mus musculus (Mouse)
|
O54852
|
KCNH7_RAT
|
MPVRRGHVAPQNTFLGTIIRKFEGQNKKFIIANARVQNCAIIYCNDGFCEMTGFSRPDVMQKPCTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEGVAMMFIINFEYVTDEDNAASPERVNPILPVKSVNRKLFGFKFPGLRVLTYRKQSLPQEDPDVVVIDSSKHSDDSVAMKHFKSPTKESCSPSEADDTKALIQPSQCSPLVNISGPLDHSSPKRQWDRLYPDMLQSSSQLTHSRSRESLCSIRRASSVHDIEGFNVHPKNIFRDRHASEDNGRNVKGPFNHIKSSLLGSTSDSNLNKYSTINKIPQLTLNFSDVKTEKKNTSPPSSDKTIIAPKVKERTHNVTEKVTQVLSLGADVLPEYKLQTPRINKFTILHYSPFKAVWDWLILLLVIYTAIFTPYSAAFLLNDREEQKRRECGYSCSPLNVVDLIVDIMFIIDILINFRTTYVNQNEEVVSDPAKIAVHYFKGWFLIDMVAAIPFDLLIFGSGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLMLLMCIFALIAHWLACIWYAIGNVERPYLTDKIGWLDSLGTQIGKRYNDSDSSSGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHMQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWTYTNGIDMNMVLKGFPECLQADICLHLNQTLLQNCKAFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKDDIVVAILGKNDIFGEMVHLYAKPGKSNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFLTNLELTFNLRHESAKSQSINDSEGDTCKLRRRRLSFESEGDKDFSKENSANDADDSTDTIRRYQSSKKHFEEKKSRSSSFISSIDDEQKPLFLGTVDSTPRMVKASRHHGEEAAPPSGRIHTDKRSHSCKDITDTHSWEREHARAQPEECSPSGLQRAAWGISETESDLTYGEVEQRLDLLQEQLNRLESQMTTDIQAILQLLQKQTTVVPPAYSMVTAGAEYQRPILRLLRTSHPRASIKTDRSFSPSSQCPEFLDLEKSKLKSKESLSSGKRLNTASEDNLTSLLKQDSDASSELDPRQRKSYLHPIRHPSLPDSSLSTVGILGLHRHVSDPGLPGK
| null | null |
circadian rhythm [GO:0007623]; membrane repolarization during action potential [GO:0086011]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of membrane potential [GO:0042391]
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monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]
|
inward rectifier potassium channel activity [GO:0005242]; potassium channel activity [GO:0005267]; protein-containing complex binding [GO:0044877]; voltage-gated potassium channel activity [GO:0005249]
|
PF00027;PF00520;PF13426;
|
1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20;
|
Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.3/KCNH7 sub-subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly. {ECO:0000269|PubMed:11212207}.
|
Rattus norvegicus (Rat)
|
O54853
|
KCNH6_RAT
|
MPVRRGHVAPQNTYLDTIIRKFEGQSRKFLIANAQMENCAIIYCNDGFCELFGYSRVEVMQRPCTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDGAVIMFILNFEDLAQLLAKSSSRSLTQRLLSHSFLGSEGSHSRPSGQGPGPGRGKYRTVSQIPQFTLNFVEFNLEKHRSGSTTEIEIIAPHKVVERTQNVTEKVTQVLSLGADVLPEYKLQAPRIHRGTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLSDQDESQRGTCGYTCSPLTVVDLIVDIMFVVDIVINFRTTYVNTNDEVVSHPRRIAVHYFKGWFLIDMVAAIPFDLLIFRTGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNVERPYLEPKIGWLDSLGAQLGKQYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLHRALLQHCPAFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDDVVVAILGKNDIFGEPASLHARPGKSSADVRALTYCDLHKIHRADLLEVLDMYPAFADTFWNKLEVTFNLRDADGGLQSTPRQAPGHQDPQGFFLNDSQSGAAPSLSISDTSALWPELLQQMPPSPPNPRQDLDCWHRELGFKLEQLQAQMNRLESRVSSDLSRILQLLQHPQGRPSYILGASASSDLASFPETSVTRSSESTLLVGHVPSAQTLSYGDLDDHIQTPRNFSPRTPHVAMAMDKTLVPSSEQEQPGGLLSPLASPLRPLEVPGLGGSRFPSLPEHLSSVPKQLEFQRHGSDPGFTRS
| null | null |
membrane repolarization during cardiac muscle cell action potential [GO:0086013]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]
|
monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]
|
inward rectifier potassium channel activity [GO:0005242]; potassium channel activity [GO:0005267]; protein-containing complex binding [GO:0044877]; voltage-gated potassium channel activity [GO:0005249]
|
PF00027;PF00520;PF13426;
|
1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20;
|
Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.2/KCNH6 sub-subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
|
Rattus norvegicus (Rat)
|
O54857
|
PTEN_RAT
|
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKLMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHSQITKV
|
3.1.3.-; 3.1.3.16; 3.1.3.48; 3.1.3.67
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O08586};
|
adult behavior [GO:0030534]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; B cell proliferation [GO:0042100]; brain morphogenesis [GO:0048854]; canonical Wnt signaling pathway [GO:0060070]; cardiac muscle tissue development [GO:0048738]; cell migration [GO:0016477]; cell motility [GO:0048870]; cell population proliferation [GO:0008283]; cellular response to decreased oxygen levels [GO:0036294]; cellular response to electrical stimulus [GO:0071257]; cellular response to ethanol [GO:0071361]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cellular response to leptin stimulus [GO:0044320]; cellular response to nerve growth factor stimulus [GO:1990090]; central nervous system development [GO:0007417]; central nervous system myelin maintenance [GO:0032286]; central nervous system neuron axonogenesis [GO:0021955]; dendritic spine morphogenesis [GO:0060997]; dentate gyrus development [GO:0021542]; endothelial cell migration [GO:0043542]; forebrain morphogenesis [GO:0048853]; gene expression [GO:0010467]; heart development [GO:0007507]; inositol phosphate catabolic process [GO:0071545]; learning or memory [GO:0007611]; locomotor rhythm [GO:0045475]; locomotory behavior [GO:0007626]; long-term synaptic depression [GO:0060292]; long-term synaptic potentiation [GO:0060291]; male mating behavior [GO:0060179]; maternal behavior [GO:0042711]; memory [GO:0007613]; multicellular organismal response to stress [GO:0033555]; myelination [GO:0042552]; negative regulation of apoptotic process [GO:0043066]; negative regulation of axon regeneration [GO:0048681]; negative regulation of axonogenesis [GO:0050771]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell cycle G1/S phase transition [GO:1902807]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell size [GO:0045792]; negative regulation of cellular senescence [GO:2000773]; negative regulation of defense response to bacterium [GO:1900425]; negative regulation of dendrite extension [GO:1903860]; negative regulation of dendritic spine morphogenesis [GO:0061002]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of excitatory postsynaptic potential [GO:0090394]; negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis [GO:1905450]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of keratinocyte migration [GO:0051548]; negative regulation of myelination [GO:0031642]; negative regulation of neuron projection development [GO:0010977]; negative regulation of organ growth [GO:0046621]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of ribosome biogenesis [GO:0090071]; negative regulation of synaptic vesicle clustering [GO:2000808]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; negative regulation of wound healing, spreading of epidermal cells [GO:1903690]; neuron projection development [GO:0031175]; neuron-neuron synaptic transmission [GO:0007270]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol dephosphorylation [GO:0046856]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; postsynaptic density assembly [GO:0097107]; prepulse inhibition [GO:0060134]; presynaptic membrane assembly [GO:0097105]; prostate gland growth [GO:0060736]; protein stabilization [GO:0050821]; regulation of axon regeneration [GO:0048679]; regulation of B cell apoptotic process [GO:0002902]; regulation of cell cycle [GO:0051726]; regulation of cellular component size [GO:0032535]; regulation of cellular localization [GO:0060341]; regulation of macrophage apoptotic process [GO:2000109]; regulation of neuron projection development [GO:0010975]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; regulation of protein stability [GO:0031647]; regulation of synaptic transmission, GABAergic [GO:0032228]; response to activity [GO:0014823]; response to arsenic-containing substance [GO:0046685]; response to ATP [GO:0033198]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to glucose [GO:0009749]; response to inorganic substance [GO:0010035]; response to nutrient [GO:0007584]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to xenobiotic stimulus [GO:0009410]; response to zinc ion [GO:0010043]; rhythmic synaptic transmission [GO:0060024]; social behavior [GO:0035176]; spindle assembly involved in female meiosis [GO:0007056]; synapse assembly [GO:0007416]; synapse maturation [GO:0060074]; T cell proliferation [GO:0042098]
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apical plasma membrane [GO:0016324]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; myelin sheath adaxonal region [GO:0035749]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; postsynaptic cytosol [GO:0099524]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; Schmidt-Lanterman incisure [GO:0043220]
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anaphase-promoting complex binding [GO:0010997]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity [GO:0030351]; inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity [GO:0051717]; ionotropic glutamate receptor binding [GO:0035255]; myosin phosphatase activity [GO:0017018]; PDZ domain binding [GO:0030165]; phosphatidylinositol phosphate phosphatase activity [GO:0052866]; phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity [GO:0016314]; phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity [GO:0051800]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphoprotein phosphatase activity [GO:0004721]; platelet-derived growth factor receptor binding [GO:0005161]; protein kinase binding [GO:0019901]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine kinase binding [GO:1990782]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; ubiquitin-specific protease binding [GO:1990381]
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PF10409;PF00102;
|
2.60.40.1110;3.90.190.10;
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PTEN phosphatase protein family
|
PTM: Constitutively phosphorylated by CK2 under normal conditions. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding to NEDD4 (By similarity). Phosphorylation by PLK3 promotes its stability and prevents its degradation by the proteasome. Phosphorylation by ROCK1 is essential for its stability and activity (By similarity). Phosphorylated on Thr-319 and Thr-321 in the C2-type tensin domain following EGF stimulation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 (By similarity). {ECO:0000250|UniProtKB:O08586, ECO:0000250|UniProtKB:P60484}.; PTM: Monoubiquitinated; monoubiquitination is increased in presence of retinoic acid. Deubiquitinated by USP7; leading to its nuclear exclusion. Monoubiquitination of one of either Lys-13 and Lys-289 amino acid is sufficient to modulate PTEN compartmentalization (By similarity). Ubiquitinated by XIAP/BIRC4 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O08586}.; PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation. {ECO:0000250|UniProtKB:P60484}.; PTM: ISGylated. ISGylation promotes PTEN degradation. {ECO:0000250|UniProtKB:P60484}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O08586}. Nucleus {ECO:0000250|UniProtKB:O08586}. Nucleus, PML body {ECO:0000250|UniProtKB:P60484}. Synapse, synaptosome {ECO:0000250|UniProtKB:O08586}. Cell projection, dendritic spine {ECO:0000269|PubMed:20628354}. Postsynaptic density {ECO:0000269|PubMed:20628354}. Note=Monoubiquitinated form is nuclear (By similarity). Nonubiquitinated form is cytoplasmic (By similarity). Colocalized with PML and USP7 in PML nuclear bodies (By similarity). XIAP/BIRC4 promotes its nuclear localization (By similarity). Associares with the postsynaptic density in response to NMDAR activation (PubMed:20628354). {ECO:0000250|UniProtKB:O08586, ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:20628354}.
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CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456; EC=3.1.3.67; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25018; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43552, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416, ChEBI:CHEBI:83419; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43553; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43560, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420, ChEBI:CHEBI:83423; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43561; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77143, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627, ChEBI:CHEBI:57733; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77144; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphate; Xref=Rhea:RHEA:77155, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895, ChEBI:CHEBI:203600; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77156; Evidence={ECO:0000250|UniProtKB:P60484};
| null | null | null | null |
FUNCTION: Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for PtdIns(3,4,5)P3. Furthermore, this enzyme can also act as a cytosolic inositol 3-phosphatase acting on Ins(1,3,4,5,6)P5/inositol 1,3,4,5,6 pentakisphosphate and possibly Ins(1,3,4,5)P4/1D-myo-inositol 1,3,4,5-tetrakisphosphate. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement (By similarity). Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Required for growth factor-induced epithelial cell migration; growth factor stimulation induces PTEN phosphorylation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 and results in translocation of the PTEN-DLC1 complex to the posterior of migrating cells to promote RHOA activation (By similarity). Meanwhile, TNS3 switches binding preference from DLC1 to p85 and the TNS3-p85 complex translocates to the leading edge of migrating cells to activate RAC1 activation (By similarity). Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Involved in the regulation of synaptic function in excitatory hippocampal synapses. Recruited to the postsynaptic membrane upon NMDA receptor activation, is required for the modulation of synaptic activity during plasticity. Enhancement of lipid phosphatase activity is able to drive depression of AMPA receptor-mediated synaptic responses, activity required for NMDA receptor-dependent long-term depression (LTD) (Ref.7). May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability (By similarity). {ECO:0000250|UniProtKB:O08586, ECO:0000250|UniProtKB:P60484, ECO:0000269|Ref.7}.
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Rattus norvegicus (Rat)
|
O54861
|
SORT_RAT
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MERPRGAADGLLRWPLGLLLLLQLLPPAAVGQDRLDAPPPPAPPLLRWAGPVGVSWGLRAAAPGGPVPRAGRWRRGAPAEDQDCGRLPDFIAKLTNNTHQHVFDDLSGSVSLSWVGDSTGVILVLTTFQVPLVIVSFGQSKLYRSEDYGKNFKDITNLINNTFIRTEFGMAIGPENSGKVILTAEVSGGSRGGRVFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGEKWEEIHKAVCLAKWGPNNIIFFTTHVNGSCKADLGALELWRTSDLGKTFKTIGVKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSTLSEDNSIQSMITFDQGGRWEHLQKPENSKCDATAKNKNECSLHIHASYSISQKLNVPMAPLSEPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWAKMLEGPHYYTILDSGGIIVAIEHSNRPINVIKFSTDEGQCWQSYVFSQEPVYFTGLASEPGARSMNISIWGFTESFLTRQWVSYTIDFKDILERNCEENDYTTWLAHSTDPGDYKDGCILGYKEQFLRLRKSSVCQNGRDYVVAKQPSICPCSLEDFLCDFGYFRPENASECVEQPELKGHELEFCLYGKEEHLTTNGYRKIPGDRCQGGMNPAREVKDLKKKCTSNFLNPKKQNSKSSSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAEADGVEALDTASHAKSGYHDDSDEDLLE
| null | null |
endocytosis [GO:0006897]; endosome to lysosome transport [GO:0008333]; endosome transport via multivesicular body sorting pathway [GO:0032509]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose import [GO:0046323]; Golgi to endosome transport [GO:0006895]; Golgi to lysosome transport [GO:0090160]; intracellular protein transport [GO:0006886]; maintenance of synapse structure [GO:0099558]; myotube differentiation [GO:0014902]; negative regulation of fat cell differentiation [GO:0045599]; neuropeptide signaling pathway [GO:0007218]; neurotrophin TRK receptor signaling pathway [GO:0048011]; ossification [GO:0001503]; plasma membrane to endosome transport [GO:0048227]; positive regulation of epithelial cell apoptotic process [GO:1904037]; protein targeting to lysosome [GO:0006622]; regulation of gene expression [GO:0010468]; response to insulin [GO:0032868]; vesicle organization [GO:0016050]
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cell surface [GO:0009986]; cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network transport vesicle [GO:0030140]
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enzyme binding [GO:0019899]; G protein-coupled neurotensin receptor activity [GO:0016492]; nerve growth factor binding [GO:0048406]; nerve growth factor receptor activity [GO:0010465]; neurotensin receptor activity, non-G protein-coupled [GO:0030379]; retromer complex binding [GO:1905394]
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PF15902;PF15901;
|
2.10.70.80;3.30.60.270;2.130.10.10;
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VPS10-related sortilin family, SORT1 subfamily
|
PTM: The N-terminal propeptide is cleaved by furin and possibly other homologous proteases. {ECO:0000250|UniProtKB:Q99523}.; PTM: Phosphorylation at Ser-819 facilitates the interaction with GGA1. {ECO:0000250|UniProtKB:Q99523}.; PTM: Palmitoylated. Undergoes cysteine S-palmitoylation which promotes the partitioning of the receptor into an endosomal membrane subdomain where it can interact with the retromer cargo-selective complex which mediates its retrograde trafficking to the Golgi apparatus. {ECO:0000250|UniProtKB:Q99523}.
|
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Nucleus membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Cell membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}; Extracellular side {ECO:0000250|UniProtKB:Q99523}. Lysosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Note=Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin. {ECO:0000250|UniProtKB:Q99523}.
| null | null | null | null | null |
FUNCTION: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin (By similarity). May also mediate transport from the endoplasmic reticulum to the Golgi (PubMed:12771154). {ECO:0000250|UniProtKB:Q99523, ECO:0000269|PubMed:12771154}.
|
Rattus norvegicus (Rat)
|
O54862
|
MBTP2_CRIGR
|
MIPVSLVVVVVGGWTAVYLADLVLKSSVYFKHSYEDWLEKNGLSISPFHIRWQTSVFNRAFYSWGRRKARMLYQWFNFGMVFGVIAMFSSFFLLGKTLMQTLAQMMADSPSSSSSSSSSSSSSSSSSIHNEQVLQVVVPGINLPVNQLTYFFAAVLISGVVHEIGHGIAAIREQVRFNGFGIFLFIIYPGAFVDLFTTHLQLISPVQQLRIFCAGIWHNFVLALLGILALVLLPVILLPFYYTGVGVLITEVAEDSPAIGPRGLFVGDLVTHLQDCPVTNVQDWNECLDTIAYEPQIGYCISASTLQQLSFPVRAYKRLDGSTECCNNHSLTDVCFSYRNNFNKRLHTCLPARKAVEATQVCRTNKDCKTSSSSSFCIVPSLETHTRLIKVKHPPQIDMLYVGHPLHLHYTVSITSFIPRFNFLSIDLPVIVETFVKYLISLSGALAIVNAVPCFALDGQWILNSFLDATLTSVIGDNDVKDLIGFFILLGGSVLLAANVTLGLWMVTAR
|
3.4.24.85
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O43462}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O43462};
|
bone maturation [GO:0070977]; cholesterol metabolic process [GO:0008203]; membrane protein intracellular domain proteolysis [GO:0031293]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein maturation [GO:0051604]; regulation of response to endoplasmic reticulum stress [GO:1905897]; response to endoplasmic reticulum stress [GO:0034976]
|
cytoplasm [GO:0005737]; Golgi membrane [GO:0000139]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription regulator activator activity [GO:0140537]
|
PF02163;
|
2.30.42.10;
|
Peptidase M50A family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O43462}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O43462}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O43462}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.; EC=3.4.24.85; Evidence={ECO:0000250|UniProtKB:O43462};
| null | null | null | null |
FUNCTION: Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2. Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription. Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B). Involved in intramembrane proteolysis during bone formation. In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression. {ECO:0000250|UniProtKB:O43462}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O54863
|
TSSK2_MOUSE
|
MDDAAVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHRSIIKTYEIFETSDGRIYIVMELGVQGDLLEFIKCRGALHEDVARKMFRQLSSAVKYCHDLDVVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDGSGRIVLSKTFCGSAAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIKKMLRIQKEHRVDFPRSKNLTGECKDLIYRILQPDVNRRLHIDEILSHSWLQPPKPKAMSSASFKREGEGKYRADCKLDTRPGSRPEHRPDHKLATKPQQRMLVTPENEDRMEDRLAETSRAKDHHISGAEVEKAST
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23599433}; Note=Mg(2+) and Mn(2+) were both present in the kinase buffer but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305|PubMed:23599433};
|
intracellular signal transduction [GO:0035556]; peptidyl-serine phosphorylation [GO:0018105]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; spermatid development [GO:0007286]
|
acrosomal vesicle [GO:0001669]; centriole [GO:0005814]; cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
|
PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q96PF2}.; PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:23599433}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Present in the cytoplasm of elongating spermatids. In spermatozoa, localizes in the equatorial segment, neck, the midpiece and in a specific sperm head compartment. In spermatids, concentrates in centrioles during flagellogenesis. Localizes in the tail and acrosomal regions of epididymal sperm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23599433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23599433};
| null | null | null | null |
FUNCTION: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-281' of TSKS and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body. {ECO:0000269|PubMed:18367677, ECO:0000269|PubMed:18533145, ECO:0000269|PubMed:20053632, ECO:0000269|PubMed:9412477}.
|
Mus musculus (Mouse)
|
O54864
|
SUV91_MOUSE
|
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF
|
2.1.1.355
| null |
blastocyst hatching [GO:0001835]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to glucose starvation [GO:0042149]; cellular response to hypoxia [GO:0071456]; chromosome organization [GO:0051276]; circadian rhythm [GO:0007623]; determination of adult lifespan [GO:0008340]; DNA damage response [GO:0006974]; energy homeostasis [GO:0097009]; heterochromatin formation [GO:0031507]; methylation [GO:0032259]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription by RNA polymerase II [GO:0000122]; rDNA heterochromatin formation [GO:0000183]; regulation of bone mineralization [GO:0030500]; regulation of cellular senescence [GO:2000772]; regulation of DNA repair [GO:0006282]; regulation of multicellular organism growth [GO:0040014]; regulation of transcription by glucose [GO:0046015]; rRNA processing [GO:0006364]
|
chromatin silencing complex [GO:0005677]; chromosome, centromeric region [GO:0000775]; eNoSc complex [GO:0061773]; heterochromatin [GO:0000792]; nuclear lamina [GO:0005652]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 trimethyltransferase activity [GO:0140949]; histone H3K9me2 methyltransferase activity [GO:0140947]; protein methyltransferase activity [GO:0008276]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF00385;PF05033;PF00856;
|
2.40.50.40;2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar3-9 subfamily
|
PTM: Phosphorylated on serine residues, and to a lesser degree, on threonine residues. {ECO:0000250}.; PTM: Acetylated at Lys-266, leading to inhibition of enzyme activity. SIRT1-mediated deacetylation relieves this inhibition (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation. {ECO:0000269|PubMed:30111536}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43463}. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355; Evidence={ECO:0000255|PROSITE-ProRule:PRU00912, ECO:0000269|PubMed:10949293};
| null | null | null | null |
FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:11701123, ECO:0000269|PubMed:12867029, ECO:0000269|PubMed:14690609, ECO:0000269|PubMed:14690610, ECO:0000269|PubMed:14702045, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:24413057, ECO:0000269|PubMed:30111536}.
|
Mus musculus (Mouse)
|
O54865
|
GCYB1_MOUSE
|
MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRNLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGAEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNVTILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPLFHLEHRGPVSMKGKKEPMQVWFLSRKNTGTEETNEEDEN
|
4.6.1.2
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P16068}; Note=Binds 1 or 2 heme groups per heterodimer. Heme is required for responding to nitric oxide, but not for catalytic activity. {ECO:0000250|UniProtKB:P16068};
|
cellular response to nitric oxide [GO:0071732]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; response to oxygen levels [GO:0070482]; trans-synaptic signaling by nitric oxide, modulating synaptic transmission [GO:0099555]
|
cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; guanylate cyclase complex, soluble [GO:0008074]; presynaptic active zone [GO:0048786]; presynaptic active zone cytoplasmic component [GO:0098831]; protein-containing complex [GO:0032991]
|
adenylate cyclase activity [GO:0004016]; cytidylate cyclase activity [GO:0047805]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; heme binding [GO:0020037]; Hsp90 protein binding [GO:0051879]; ion binding [GO:0043167]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]
|
PF00211;PF07700;PF07701;
|
6.10.250.780;3.90.1520.10;3.30.450.260;3.30.70.1230;
|
Adenylyl cyclase class-4/guanylyl cyclase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16068}.
|
CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q02153};
| null | null | null | null |
FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP. {ECO:0000250|UniProtKB:P16068}.
|
Mus musculus (Mouse)
|
O54874
|
MRCKA_RAT
|
MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWAKPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEEMARFYLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKKHPFFSGIDWDNIRNCEAPYIPEVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTAGPTSLDLDVNVQRTLDNNLATEAYERRIKRLEQEKLELTRKLQESTQTVQALQYSTVDGPLTASKDLEIKSLKEEIEKLRKQVAEVNHLEQQLEEANSVRRELDDAFRQIKAFEKQIKTLQQEREELNKELVQASERLKNQSKELKDAHCQRKLAMQEFMEINERLTELHTQKQKLARHVRDKEEEVDLVMQKAESLRQELRRAERAKKELEVHTEALIAEASKDRKLREQSRHYSKQLENELEGLKQKQISYSPGICSIEHQQEITKLKTDLEKKSIFYEEEISKREGIHASEIKNLKKELHDSEGQQLALNKEIMVLKDKLEKTRRESQSEREEFENEFKQQYEREKVLLTEENKKLTSELDKLTSLYESLSLRNQHLEEEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQALASKMTEELEALRNSSLGTRATDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEELNKVKASNIITECKLKDSEKKNLELLSEIEQLIKDTEELRSEKGVEHRDSQHSFLAFLNTPTDALDQFERSPSCTPAGKGRRIADSAPLPVHTPTLRKKGCPASAGFPPKRKTHQFFVKSFTAPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITCVNKAPTTCPVPPEQTKGPLGIDPQKGVGTAYEGHVRIPKPAGVKKGWQRALAVVCDFKLFLYDIAEGKASQPSSVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSAPSDKCSILMLADSETERSKWVGVLSELHKVLKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAAIIDHERVALGNEEGLFVVHVTKDEIIRVGDNKKIHQIELIPSDQLVAVISGRNRHVRLFPMSALDGRETDFYKLAETKGCQTIAAGKVRHGALSCLCVAMKRQVLCYELFQSKTRHRKFKEIQVPCNVQWMAIFSEHLCVGFQSGFLRYPLNGEGSPCNMLHSNDHTLAFITHQPMDAICAVEISNKEYLLCFSSIGIYTDCQGRRSRQQELMWPANPSSCCYNAPYLSIYSENAVDIFDVNSMEWIQTLPLKKVRPLNTEGSLNLLGLETIRLIYFKNKMAEGDELVVPETSDNSRKQMVRNINNKRRYSFRVPEEERMQQRREMLRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKDLPMNPRPQESRTVFSGSVSIPSITKSRPEPGRSMSASSGLSARSSAQNGSALKREFSGGSYNTKRQPMPSPSEGSLSSGGVDQGSDAPVRDYDGEDSDSPRHSTASNSSNLSSPPSPVSPRKTKSLSLESTDRGSWDP
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9418861};
|
actin cytoskeleton organization [GO:0030036]; actomyosin structure organization [GO:0031032]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; microtubule cytoskeleton organization [GO:0000226]; nuclear migration [GO:0007097]; protein phosphorylation [GO:0006468]; regulation of small GTPase mediated signal transduction [GO:0051056]
|
actomyosin [GO:0042641]; cell leading edge [GO:0031252]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; lamellipodium [GO:0030027]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00130;PF00780;PF08826;PF15796;PF00069;PF00433;
|
1.10.287.1490;1.20.5.340;3.30.60.20;2.30.29.30;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, DMPK subfamily
|
PTM: Proteolytically cleaved by caspases upon apoptosis induction. The cleavage at Asp-478 by CASP3 increases its kinase activity (in vitro). {ECO:0000250|UniProtKB:Q5VT25}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9418861}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q3UU96}. Note=Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (PubMed:9418861). Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q3UU96, ECO:0000269|PubMed:9418861}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9418861}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9418861};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration (PubMed:9418861). Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12A and MYL9/MLC2 (PubMed:21457715). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates: PPP1R12C, LIMK1 and LIMK2. May play a role in TFRC-mediated iron uptake. In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). Triggers the formation of an extrusion apical actin ring required for epithelial extrusion of apoptotic cells (By similarity). {ECO:0000250|UniProtKB:Q3UU96, ECO:0000250|UniProtKB:Q5VT25, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:9418861}.
|
Rattus norvegicus (Rat)
|
O54879
|
HMGB3_MOUSE
|
MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSSKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSTNPGISIGDVAKKLGEMWNNLSDNEKQPYVTKAAKLKEKYEKDVADYKSKGKFDGAKGPAKVARKKVEEEEEEEEEEEEEEEEEEDE
| null | null |
DNA geometric change [GO:0032392]; innate immune response [GO:0045087]; negative regulation of B cell differentiation [GO:0045578]; negative regulation of myeloid cell differentiation [GO:0045638]; regulation of transcription by RNA polymerase II [GO:0006357]
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chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
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DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; RNA binding [GO:0003723]
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PF00505;PF09011;
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1.10.30.10;
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HMGB family
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PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-104 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB3 (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so). {ECO:0000250|UniProtKB:P09429}.
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SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40618, ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19890330}.
| null | null | null | null | null |
FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference for non-canonical DNA structures such as single-stranded DNA. Can bend DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor (PubMed:19890330). Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (PubMed:12714519, PubMed:15358624, PubMed:16945912). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P40618, ECO:0000269|PubMed:12714519, ECO:0000269|PubMed:15358624, ECO:0000269|PubMed:16945912, ECO:0000269|PubMed:19890330}.
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Mus musculus (Mouse)
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