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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O35425
|
BOK_MOUSE
|
MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQIRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER
| null | null |
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; male gonad development [GO:0008584]; negative regulation of mitochondrial depolarization [GO:0051902]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; negative regulation of necroptotic process [GO:0060546]; negative regulation of neuron apoptotic process [GO:0043524]; neuron apoptotic process [GO:0051402]; oligodendrocyte differentiation [GO:0048709]; positive regulation of apoptotic process [GO:0043065]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of execution phase of apoptosis [GO:1900119]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of PERK-mediated unfolded protein response [GO:1903899]; protein complex oligomerization [GO:0051259]; regulation of autophagy [GO:0010506]; regulation of chorionic trophoblast cell proliferation [GO:1901382]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of granulosa cell apoptotic process [GO:1904708]; release of cytochrome c from mitochondria [GO:0001836]
|
cis-Golgi network membrane [GO:0033106]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; nuclear outer membrane [GO:0005640]; nucleus [GO:0005634]; recycling endosome membrane [GO:0055038]; trans-Golgi network membrane [GO:0032588]
|
BH domain binding [GO:0051400]; protein dimerization activity [GO:0046983]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; ubiquitin protein ligase binding [GO:0031625]
|
PF00452;
|
1.10.437.10;
|
Bcl-2 family
|
PTM: Ubiquitinated by AMFR/gp78 E3 ubiquitin ligase complex; mediates degradation by ubiquitin-proteasome pathway in a VCP/p97-dependent manner; prevents from proapoptotic activity; promotes degradation of newly synthesized proteins that are not ITPR1 associated. {ECO:0000269|PubMed:23884412, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27053113}.
|
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UMX3}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMX3}. Nucleus {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion {ECO:0000250|UniProtKB:Q9UMX3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9UMX3}. Early endosome membrane {ECO:0000269|PubMed:23429263}. Recycling endosome membrane {ECO:0000269|PubMed:23429263}. Nucleus outer membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23429263}. Membrane {ECO:0000250|UniProtKB:Q9UMX3}. Note=Nuclear and cytoplasmic compartments in the early stages of apoptosis and during apoptosis associates with mitochondria. In healthy cells, associates loosely with the membrane in a hit-and-run mode. The insertion and accumulation on membranes is enhanced through the activity of death signals, resulting in the integration of the membrane-bound protein into the membrane (By similarity). The transmembrane domain controls subcellular localization; constitutes a tail-anchor (PubMed:23429263, PubMed:26949185). Localizes in early and late endosome upon blocking of apoptosis (PubMed:23429263). Must localize to the mitochondria to induce mitochondrial outer membrane permeabilization and apoptosis (PubMed:26949185). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}.
| null | null | null | null | null |
FUNCTION: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:23429263, PubMed:26015568, PubMed:26949185, PubMed:27098698, PubMed:9535847). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (PubMed:23429263, PubMed:26015568, PubMed:26949185). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (PubMed:26015568). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release (PubMed:26949185, PubMed:9535847). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (PubMed:27098698). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression.May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26015568, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27098698, ECO:0000269|PubMed:9535847}.
|
Mus musculus (Mouse)
|
O35426
|
XBP1_MOUSE
|
MVVVAAAPSAATAAPKVLLLSGQPASGGRALPLMVPGPRAAGSEASGTPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENHKLQLENQLLREKTHGLVVENQELRTRLGMDTLDPDEVPEVEAKGSGVRLVAGSAESAALRLCAPLQQVQAQLSPPQNIFPWTLTLLPLQILSLISFWAFWTSWTLSCFSNVLPQSLLVWRNSQRSTQKDLVPYQPPFLCQWGPHQPSWKPLMNSFVLTMYTPSL
| null | null |
adipose tissue development [GO:0060612]; angiogenesis [GO:0001525]; autophagy [GO:0006914]; cellular response to amino acid stimulus [GO:0071230]; cellular response to fluid shear stress [GO:0071498]; cellular response to fructose stimulus [GO:0071332]; cellular response to glucose starvation [GO:0042149]; cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; cellular response to interleukin-4 [GO:0071353]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to nutrient [GO:0031670]; cellular response to oxidative stress [GO:0034599]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; cholesterol homeostasis [GO:0042632]; endoplasmic reticulum unfolded protein response [GO:0030968]; endothelial cell proliferation [GO:0001935]; epithelial cell maturation involved in salivary gland development [GO:0060691]; exocrine pancreas development [GO:0031017]; fatty acid homeostasis [GO:0055089]; glandular epithelial cell maturation [GO:0002071]; intracellular triglyceride homeostasis [GO:0035356]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; lipid metabolic process [GO:0006629]; liver development [GO:0001889]; muscle organ development [GO:0007517]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of endoplasmic reticulum unfolded protein response [GO:1900102]; negative regulation of myotube differentiation [GO:0010832]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron development [GO:0048666]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of autophagy [GO:0010508]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of hepatocyte proliferation [GO:2000347]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of lactation [GO:1903489]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of plasma cell differentiation [GO:1900100]; positive regulation of protein acetylation [GO:1901985]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of TOR signaling [GO:0032008]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein destabilization [GO:0031648]; protein transport [GO:0015031]; regulation of autophagy [GO:0010506]; regulation of cell growth [GO:0001558]; regulation of protein stability [GO:0031647]; regulation of transcription by RNA polymerase II [GO:0006357]; response to electrical stimulus [GO:0051602]; response to endoplasmic reticulum stress [GO:0034976]; response to insulin-like growth factor stimulus [GO:1990418]; response to xenobiotic stimulus [GO:0009410]; serotonin secretion, neurotransmission [GO:0060096]; sterol homeostasis [GO:0055092]; transcription by RNA polymerase II [GO:0006366]; ubiquitin-dependent protein catabolic process [GO:0006511]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; presynapse [GO:0098793]
|
chromatin DNA binding [GO:0031490]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone deacetylase binding [GO:0042826]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]; ubiquitin-like protein ligase binding [GO:0044389]
|
PF00170;
|
1.20.5.170;
|
BZIP family
|
PTM: [Isoform 2]: Acetylated by EP300; acetylation positively regulates the transcriptional activity of XBP1 isoform 2 (PubMed:20955178). Isoform 2 is deacetylated by SIRT1; deacetylation negatively regulates the transcriptional activity of XBP1 isoform 2 (PubMed:20955178). {ECO:0000269|PubMed:20955178, ECO:0000305|PubMed:20955178}.; PTM: [Isoform 1]: Ubiquitinated, leading to proteasomal degradation in response to ER stress (PubMed:11780124, PubMed:12902539, PubMed:16332684). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:11780124, ECO:0000269|PubMed:12902539, ECO:0000269|PubMed:16332684}.; PTM: X-box-binding protein 1, cytoplasmic form and luminal form are produced by intramembrane proteolytic cleavage of ER membrane-anchored isoform 1 triggered by HM13/SPP in a DERL1-RNF139-dependent and VCP/p97-independent manner. X-box-binding protein 1, luminal form is ubiquitinated leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P17861}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P17861}. Note=Colocalizes with ERN1 and KDR in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (By similarity). {ECO:0000250|UniProtKB:P17861}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:16332684}. Cytoplasm {ECO:0000269|PubMed:16332684}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17861}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P17861}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17861}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17861}. Membrane {ECO:0000250|UniProtKB:P17861}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17861}. Note=Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Localizes predominantly at the endoplasmic reticulum membrane as a membrane-spanning protein; whereas may be only marginally localized on the cytosolic side of the ER membrane as a peripheral membrane (By similarity). Shows no preferential localization to either the nucleus or the cytoplasm (PubMed:16332684). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:16332684}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:16332684, ECO:0000269|PubMed:18556558, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:20955178}. Cytoplasm {ECO:0000269|PubMed:16332684}. Note=Localizes predominantly in the nucleus (PubMed:16332684). Colocalizes in the nucleus with SIRT1 (PubMed:20955178). Translocates into the nucleus in a PIK3R-, ER stress-induced- and/or insulin-dependent manner (PubMed:20348926). {ECO:0000269|PubMed:16332684, ECO:0000269|PubMed:18556558, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:20955178}.; SUBCELLULAR LOCATION: [X-box-binding protein 1, cytoplasmic form]: Cytoplasm {ECO:0000250|UniProtKB:P17861}. Nucleus {ECO:0000250|UniProtKB:P17861}. Note=Localizes in the cytoplasm and nucleus after HM13/SPP-mediated intramembranaire proteolytic cleavage of isoform 1 (By similarity). {ECO:0000250|UniProtKB:P17861}.
| null | null | null | null | null |
FUNCTION: Functions as a transcription factor during endoplasmic reticulum stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development and the development of secretory tissues such as exocrine pancreas and salivary gland (PubMed:10425189, PubMed:10652269, PubMed:16362047, PubMed:17612490). Involved in differentiation of B lymphocytes to plasma cells and production of immunoglobulins. Modulates the cellular response to ER stress in a PIK3R-dependent manner. Binds to the cis-acting X box present in the promoter regions of major histocompatibility complex class II genes (By similarity). Involved in VEGF-induced endothelial cell (EC) proliferation and retinal blood vessel formation during embryonic development but also for angiogenesis in adult tissues under ischemic conditions (PubMed:23529610). Functions also as a major regulator of the UPR in obesity-induced insulin resistance and type 2 diabetes for the management of obesity and diabetes prevention (PubMed:15486293). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:10425189, ECO:0000269|PubMed:10652269, ECO:0000269|PubMed:15486293, ECO:0000269|PubMed:16362047, ECO:0000269|PubMed:17612490, ECO:0000269|PubMed:23529610}.; FUNCTION: [Isoform 1]: Plays a role in the unconventional cytoplasmic splicing processing of its own mRNA triggered by the endoplasmic reticulum (ER) transmembrane endoribonuclease ERN1: upon ER stress, the emerging XBP1 polypeptide chain, as part of a mRNA-ribosome-nascent chain (R-RNC) complex, cotranslationally recruits its own unprocessed mRNA through transient docking to the ER membrane and translational pausing, therefore facilitating efficient IRE1-mediated XBP1 mRNA isoform 2 production. In endothelial cells (EC), associated with KDR, promotes IRE1-mediated XBP1 mRNA isoform 2 production in a vascular endothelial growth factor (VEGF)-dependent manner, leading to EC proliferation and angiogenesis (By similarity). Functions as a negative feed-back regulator of the potent transcription factor XBP1 isoform 2 protein levels through proteasome-mediated degradation, thus preventing the constitutive activation of the ER stress response signaling pathway (PubMed:16332684). Inhibits the transactivation activity of XBP1 isoform 2 in myeloma cells (PubMed:12902539). Acts as a weak transcriptional factor. Together with HDAC3, contributes to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to EC survival under disturbed flow/oxidative stress. Binds to the ER stress response element (ERSE) upon ER stress. Binds to the consensus 5'-GATGACGTG[TG]N(3)[AT]T-3' sequence related to cAMP responsive element (CRE)-like sequences. Binds the Tax-responsive element (TRE) present in the long terminal repeat (LTR) of T-cell leukemia virus type 1 (HTLV-I) and to the TPA response elements (TRE). Associates preferentially to the HDAC3 gene promoter region in a static flow-dependent manner. Binds to the CDH5/VE-cadherin gene promoter region (By similarity). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:12902539, ECO:0000269|PubMed:16332684}.; FUNCTION: [Isoform 2]: Functions as a stress-inducible potent transcriptional activator during endoplasmic reticulum (ER) stress by inducing unfolded protein response (UPR) target genes via binding to the UPR element (UPRE). Up-regulates target genes encoding ER chaperones and ER-associated degradation (ERAD) components to enhance the capacity of productive folding and degradation mechanism, respectively, in order to maintain the homeostasis of the ER under ER stress (PubMed:11850408, PubMed:14559994). Plays a role in the production of immunoglobulins and interleukin-6 in the presence of stimuli required for plasma cell differentiation, and promotes as well membrane phospholipid biosynthesis necessary for ER expansion (PubMed:12612580, PubMed:17213183). Contributes to the VEGF-induced endothelial cell (EC) growth and proliferation in a Akt/GSK-dependent and/or -independent signaling pathway, respectively, leading to beta-catenin nuclear translocation and E2F2 gene expression. Promotes umbilical vein EC apoptosis and atherosclerotisis development in a caspase-dependent signaling pathway, and contributes to VEGF-induced EC proliferation and angiogenesis in adult tissues under ischemic conditions. Involved in the regulation of endostatin-induced autophagy in EC through BECN1 transcriptional activation. Plays a role as an oncogene by promoting tumor progression: stimulates zinc finger protein SNAI1 transcription to induce epithelial-to-mesenchymal (EMT) transition, cell migration and invasion of breast cancer cells (By similarity). Involved in adipocyte differentiation by regulating lipogenic gene expression during lactation (PubMed:23623498, PubMed:25223794). Plays a role in the survival of both dopaminergic neurons of the substantia nigra pars compacta (SNpc), by maintaining protein homeostasis and of myeloma cells (PubMed:12902539, PubMed:24753614). Increases insulin sensitivity in the liver as a response to a high carbohydrate diet, resulting in improved glucose tolerance (PubMed:20348926). Improves also glucose homeostasis in an ER stress- and/or insulin-independent manner through both binding and proteasome-induced degradation of the transcription factor FOXO1, hence resulting in suppression of gluconeogenic genes expression and in a reduction of blood glucose levels (PubMed:21317886). Controls the induction of de novo fatty acid synthesis in hepatocytes by regulating the expression of a subset of lipogenic genes in an ER stress- and UPR-independent manner (PubMed:18556558). Binds to the 5'-CCACG-3' motif in the PPARG promoter (PubMed:25223794). Associates preferentially to the HDAC3 gene promoter region in a disturbed flow-dependent manner. Binds to the BECN1 gene promoter region. Binds to the CDH5/VE-cadherin gene promoter region. Binds to the ER stress response element (ERSE) upon ER stress (By similarity). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:11850408, ECO:0000269|PubMed:12612580, ECO:0000269|PubMed:12902539, ECO:0000269|PubMed:14559994, ECO:0000269|PubMed:17213183, ECO:0000269|PubMed:18556558, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:21317886, ECO:0000269|PubMed:23623498, ECO:0000269|PubMed:24753614, ECO:0000269|PubMed:25223794}.
|
Mus musculus (Mouse)
|
O35427
|
RPC9_MOUSE
|
MEVKDANAALLSNYEVFQLLTDLKEQRKESGKNKHSAGQQNLNAITYETLKYISKTPCRNQSPAIVQEFLTAMKSHKLTKAEKLQLLNHRPMTAVEIQLMVEESEERLTEEQIEALLHTVTSILPAGPEDEQSKSTSNDVAMEEEEPA
| null | null |
defense response to virus [GO:0051607]; innate immune response [GO:0045087]; neuropeptide signaling pathway [GO:0007218]; transcription by RNA polymerase III [GO:0006383]; transcription initiation at RNA polymerase III promoter [GO:0006384]
|
acrosomal vesicle [GO:0001669]; axon [GO:0030424]; dendrite [GO:0030425]; DNA polymerase III complex [GO:0009360]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; RNA polymerase III complex [GO:0005666]
|
calcitonin gene-related peptide receptor activity [GO:0001635]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; nucleotide binding [GO:0000166]
|
PF03874;
|
1.20.1250.40;
|
Eukaryotic RPC9 RNA polymerase subunit family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75575}. Cell membrane {ECO:0000269|PubMed:10903324}; Peripheral membrane protein {ECO:0000269|PubMed:10903324}; Cytoplasmic side {ECO:0000269|PubMed:10903324}.
| null | null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity). Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci. With POLR3H/RPC8 forms a mobile stalk that protrudes from Pol III core and functions primarily in transcription initiation (By similarity). Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through the RIG-I pathway (By similarity). {ECO:0000250|UniProtKB:O75575, ECO:0000250|UniProtKB:Q9C0Z9}.; FUNCTION: Accessory protein for the calcitonin gene-related peptide (CGRP) receptor. It modulates CGRP responsiveness in a variety of tissues. {ECO:0000269|PubMed:10903324}.
|
Mus musculus (Mouse)
|
O35430
|
APBA1_RAT
|
MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVEEEQQPSPPPPAGHAPEDHRAHPAPPPPPPPQEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHAEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSITPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDAKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
| null | null |
chemical synaptic transmission [GO:0007268]; establishment of localization in cell [GO:0051649]; gamma-aminobutyric acid secretion [GO:0014051]; glutamate secretion [GO:0014047]; in utero embryonic development [GO:0001701]; intracellular protein transport [GO:0006886]; locomotory behavior [GO:0007626]; multicellular organism growth [GO:0035264]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of gene expression [GO:0010468]; synaptic vesicle exocytosis [GO:0016079]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; presynaptic active zone membrane [GO:0048787]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685]
|
amyloid-beta binding [GO:0001540]; PDZ domain binding [GO:0030165]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]
|
PF00595;PF00640;
|
2.30.42.10;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20531236}. Note=Only a small proportion of the protein is nuclear.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta.
|
Rattus norvegicus (Rat)
|
O35431
|
APBA2_RAT
|
MAHRKRQSTASSMLDHRARPGPIPHDQEPENEDTELPLESYVPTGLELGTLRPDSPTPEEQECHNHSPDGDSSSDYVNNTSEEEDYDEGLPEEEEGVTYYIRYCPEDDSYLEGMDCNGEEYLAHGAHPVDTDECQEAVEDWTDSVGPHTHSHGAENSQEYPDSHLPIPEDDPTVLEVHDQEEDGHYCPSKESYQDYYPPETNGNTGGASPYRMRRGDGDLEEQEEDIDQIVAEIKMSLSMTSITSASEASPEHMPELDPGDSTEACSPSDTGRGPSRQEARPKSLNLPPEVKHSGDPQRGLKTKTRTPEERPKWPQEQVCNGLEQPRKQQRSDLNGPTDNNNIPETKKVASFPSFVAVPGPCEPEDLIDGIIFAANYLGSTQLLSERNPSKNIRMMQAQEAVSRVKRMQKAAKIKKKANSEGDAQTLTEVDLFISTQRIKVLNADTQETMMDHALRTISYIADIGNIVVLMARRRMPRSASQDCIETTPGAQEGKKQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDIINTQEMYNDDLIHFSNSENCKELQLEKHKGEILGVVVVESGWGSILPTVILANMMNGGPAARSGKLSIGDQIMSINGTSLVGLPLATCQGIIKGLKNQTQVKLNIVSCPPVTTVLIKRPDLKYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATAHEKIVQALSNSVGEIHMKTMPAAMFRLLTGQETPLYI
| null | null |
chemical synaptic transmission [GO:0007268]; in utero embryonic development [GO:0001701]; locomotory behavior [GO:0007626]; multicellular organism growth [GO:0035264]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; protein transport [GO:0015031]; regulation of gene expression [GO:0010468]; synaptic vesicle exocytosis [GO:0016079]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; Schaffer collateral - CA1 synapse [GO:0098685]
|
amyloid-beta binding [GO:0001540]; identical protein binding [GO:0042802]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF00595;PF00640;
|
2.30.42.10;2.30.29.30;
| null | null | null | null | null | null | null | null |
FUNCTION: Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta.
|
Rattus norvegicus (Rat)
|
O35433
|
TRPV1_RAT
|
MEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSEEASPLDCPYEEGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSLPMESTPHKCRGSACKPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRDRHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPGEK
| null | null |
behavioral response to pain [GO:0048266]; calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cellular response to acidic pH [GO:0071468]; cellular response to alkaloid [GO:0071312]; cellular response to ATP [GO:0071318]; cellular response to cytokine stimulus [GO:0071345]; cellular response to growth factor stimulus [GO:0071363]; cellular response to heat [GO:0034605]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to temperature stimulus [GO:0071502]; cellular response to tumor necrosis factor [GO:0071356]; detection of chemical stimulus involved in sensory perception of pain [GO:0050968]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; detection of temperature stimulus involved in thermoception [GO:0050960]; diet induced thermogenesis [GO:0002024]; fever generation [GO:0001660]; glutamate secretion [GO:0014047]; lipid metabolic process [GO:0006629]; microglial cell activation [GO:0001774]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of establishment of blood-brain barrier [GO:0090212]; negative regulation of heart rate [GO:0010459]; negative regulation of mitochondrial membrane potential [GO:0010917]; negative regulation of systemic arterial blood pressure [GO:0003085]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptide secretion [GO:0002790]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; protein homotetramerization [GO:0051289]; response to capsazepine [GO:1901594]; response to heat [GO:0009408]; response to organonitrogen compound [GO:0010243]; response to pain [GO:0048265]; response to peptide hormone [GO:0043434]; response to pH [GO:0009268]; sensory perception of mechanical stimulus [GO:0050954]; sensory perception of pain [GO:0019233]; smooth muscle contraction involved in micturition [GO:0060083]; temperature homeostasis [GO:0001659]; thermoception [GO:0050955]; urinary bladder smooth muscle contraction [GO:0014832]
|
dendrite [GO:0030425]; dendritic spine membrane [GO:0032591]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]
|
ATP binding [GO:0005524]; calcium channel activity [GO:0005262]; calmodulin binding [GO:0005516]; chloride channel regulator activity [GO:0017081]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; identical protein binding [GO:0042802]; intracellularly gated calcium channel activity [GO:0015278]; ligand-gated monoatomic ion channel activity [GO:0015276]; metal ion binding [GO:0046872]; monoatomic cation channel activity [GO:0005261]; monoatomic cation transmembrane transporter activity [GO:0008324]; phosphatidylinositol binding [GO:0035091]; phosphoprotein binding [GO:0051219]; temperature-gated ion channel activity [GO:0097603]; transmembrane signaling receptor activity [GO:0004888]
|
PF00023;PF12796;PF00520;
|
1.10.287.70;1.25.40.20;
|
Transient receptor (TC 1.A.4) family, TrpV subfamily, TRPV1 sub-subfamily
|
PTM: Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-116 as a major phosphorylation site. Phosphorylation by CAMKII seems to regulate binding to vanilloids. Phosphorylated and modulated by PRKCE, PRKCM and probably PRKCZ. Dephosphorylation by calcineurin seems to lead to receptor desensitization and phosphorylation by CAMKII recovers activity. {ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912, ECO:0000269|PubMed:15471852}.
|
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:15857679}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:15857679}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11578842, ECO:0000269|PubMed:15857679, ECO:0000269|PubMed:9349813}; Multi-pass membrane protein {ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:24305161, ECO:0000269|PubMed:27281200}. Note=Mostly, but not exclusively expressed in postsynaptic dendritic spines. {ECO:0000269|PubMed:15857679}.
| null | null | null | null | null |
FUNCTION: Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis. {ECO:0000269|PubMed:11140687, ECO:0000269|PubMed:11418861, ECO:0000269|PubMed:11578842, ECO:0000269|PubMed:12095983, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:12764195, ECO:0000269|PubMed:12808128, ECO:0000269|PubMed:14523239, ECO:0000269|PubMed:14630912, ECO:0000269|PubMed:15173182, ECO:0000269|PubMed:17582331, ECO:0000269|PubMed:20510930, ECO:0000269|PubMed:21076423, ECO:0000269|PubMed:23109716, ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:9349813}.; FUNCTION: [Isoform 3]: Does not display channel activity in response to noxious chemical compounds, such as capsaicin and the vanilloid resiniferatoxin. Channel activity is not elicited by mildly acidic extracellular pH, and only slight channel activity is observed in response to noxiuos heat stimuli. {ECO:0000269|PubMed:10644739}.
|
Rattus norvegicus (Rat)
|
O35435
|
PYRD_MOUSE
|
MAWRQLRKRALDAAIILGGGGLLFTSYLTATGDDHFYAEYLMPALQRLLDPESAHRLAVRVISLGLLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKQTQLTTDGLPLGINLGKNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQKPAVLVKIAPDLTAQDKEDIASVARELGIDGLIITNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIGVDHRR
|
1.3.5.2
|
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q02127}; Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q02127};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; positive regulation of apoptotic process [GO:0043065]; pyrimidine ribonucleotide biosynthetic process [GO:0009220]; regulation of mitochondrial fission [GO:0090140]; UDP biosynthetic process [GO:0006225]
|
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
dihydroorotase activity [GO:0004151]; dihydroorotate dehydrogenase (quinone) activity [GO:0106430]; dihydroorotate dehydrogenase activity [GO:0004152]; FMN binding [GO:0010181]; quinone binding [GO:0048038]; ubiquinone binding [GO:0048039]
|
PF01180;
|
3.20.20.70;
|
Dihydroorotate dehydrogenase family, Type 2 subfamily
|
PTM: The uncleaved transit peptide is required for mitochondrial targeting and proper membrane integration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q02127}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q02127}.
|
CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000250|UniProtKB:Q02127};
| null |
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
| null | null |
FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Required for UMP biosynthesis via de novo pathway. {ECO:0000250|UniProtKB:Q02127}.
|
Mus musculus (Mouse)
|
O35437
|
TCF21_MOUSE
|
MSTGSLSDVEDLQEVEMLDCDSLKVDSNKEFGTSNESTEEGSNCENGSPQKGRGGLGKRRKAPTKKSPLSGVSQEGKQVQRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLASSYIAHLRQILANDKYENGYIHPVNLTWPFMVAGKPENDLKEVVTANRLCGTTAS
| null | null |
animal organ morphogenesis [GO:0009887]; branching involved in ureteric bud morphogenesis [GO:0001658]; branchiomeric skeletal muscle development [GO:0014707]; bronchiole development [GO:0060435]; developmental process [GO:0032502]; diaphragm development [GO:0060539]; embryonic digestive tract morphogenesis [GO:0048557]; epithelial cell differentiation [GO:0030855]; gland development [GO:0048732]; glomerulus development [GO:0032835]; kidney development [GO:0001822]; lung alveolus development [GO:0048286]; lung morphogenesis [GO:0060425]; lung vasculature development [GO:0060426]; metanephric glomerular capillary formation [GO:0072277]; metanephric mesenchymal cell differentiation [GO:0072162]; morphogenesis of a branching structure [GO:0001763]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; reproductive structure development [GO:0048608]; respiratory system development [GO:0060541]; roof of mouth development [GO:0060021]; Sertoli cell differentiation [GO:0060008]; sex determination [GO:0007530]; sex differentiation [GO:0007548]; spleen development [GO:0048536]; ureteric bud development [GO:0001657]; vasculature development [GO:0001944]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
bHLH transcription factor binding [GO:0043425]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; histone deacetylase binding [GO:0042826]; nuclear androgen receptor binding [GO:0050681]; protein dimerization activity [GO:0046983]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
| null | null | null | null | null |
FUNCTION: Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis. May be involved in the organogenesis of the spleen and heart and in cardiac and coronary artery development. May function in the development and sex differentiation of gonad via transcriptional regulation of AD4BP/SF-1. {ECO:0000269|PubMed:10944221}.
|
Mus musculus (Mouse)
|
O35445
|
RNF5_MOUSE
|
MAAAEEEDGGPEGPNRERGGASATFECNICLETAREAVVSVCGHLYCWPCLHQWLETRPDRQECPVCKAGISREKVVPLYGRGSQKPQDPRLKTPPRPQGQRPAPESRGGFQPFGDAGGFHFSFGVGAFPFGFFTTVFNAHEPFRRGAGVDLGQGHPASSWQDSLFLFLAIFFFFWLLSI
|
2.3.2.27
| null |
ERAD pathway [GO:0036503]; negative regulation of autophagy [GO:0010507]; protein destabilization [GO:0031648]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; regulation of autophagosome assembly [GO:2000785]; response to bacterium [GO:0009617]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-like protein conjugating enzyme binding [GO:0044390]; ubiquitin-protein transferase activity [GO:0004842]
|
PF13920;
|
3.30.40.10;
|
RNF5 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12861019}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q99942}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99942}; Multi-pass membrane protein {ECO:0000255}. Note=Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles. {ECO:0000250|UniProtKB:Q99942}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q99942};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23093945}.
| null | null |
FUNCTION: Membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination of target proteins (PubMed:23093945). May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4 (By similarity). Mediates ubiquitination of PXN/paxillin,thereby regulating cell motility and localization of PXN/paxillin (By similarity). Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N (By similarity). Mediates the 'Lys-48'-linked polyubiquitination of STING1 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurs in mitochondria after viral transfection and regulates antiviral responses (By similarity). Catalyzes ubiquitination and subsequent degradation of ATG4B, thereby inhibiting autophagy (PubMed:23093945). {ECO:0000250|UniProtKB:Q99942, ECO:0000269|PubMed:23093945}.
|
Mus musculus (Mouse)
|
O35449
|
PRRT1_MOUSE
|
MSSEKSGLPDSVPHTSPPPYNAPQPPAEPPIPPPQTAPSSHHHHHHHYHQSGTATLPRLGAGGLASAAASAQRGPSSSATLPRPPHHAPPGPAAGAPPPGCATLPRMPPDPYLQETRFEGPLPPPPPAAAAPPPPAPAPTAQAPGFVVPTHAGAVGTLPLGGYVAPGYPLQLQPCTAYVPVYPVGTPYAGGTPGGPGVTSTLPPPPQGPGLALLEPRRPPHDYMPIAVLTTICCFWPTGIIAIFKAVQVRTALARGDLVSAEIASREARNFSFISLAVGIAAMVLCTILTVVIIIAAQHHENYWDP
| null | null |
learning or memory [GO:0007611]; long-term synaptic depression [GO:0060292]; long-term synaptic potentiation [GO:0060291]; protein localization [GO:0008104]; protein localization to cell surface [GO:0034394]; protein phosphorylation [GO:0006468]; regulation of AMPA receptor activity [GO:2000311]; synapse organization [GO:0050808]
|
glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; synaptic vesicle membrane [GO:0030672]
|
signaling receptor regulator activity [GO:0030545]
|
PF04505;
| null |
CD225/Dispanin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22632720}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6MG82}. Synapse {ECO:0000305|PubMed:22632720}.
| null | null | null | null | null |
FUNCTION: Required to maintain a pool of extrasynaptic AMPA-regulated glutamate receptors (AMPAR) which is necessary for synapse development and function (PubMed:29490264). Regulates AMPAR function and synaptic transmission during development but is dispensable at mature hippocampal synapses (PubMed:29490264, PubMed:31216424). Plays a role in regulating basal phosphorylation levels of glutamate receptor GRIA1 and promotes GRIA1 and GRIA2 cell surface expression (PubMed:31216424). {ECO:0000269|PubMed:29490264, ECO:0000269|PubMed:31216424}.
|
Mus musculus (Mouse)
|
O35451
|
ATF6B_MOUSE
|
MAELMLLSEIADPTRFFTDNLLSPEDWDSTLYSGLDEVAEEQAQLFRCVEQDVPFDSSSLDVGMDVSPPEPPWDPLPIFPDLQVKSEPSSPCSSSSLSSESSHLSTEPPSQVPGVGEVLHVKMESLAPPLCLLGDDPASPFETVQITVGSASDDLSDIQTKLEPASPSSSVHSEASLLSADSPSQPFIGEEVLEVKTESPSPPGCLLWDVPASSLGAVQISMGPSPDSSSGKAPATRKPPLQPKPVVLTTVPVPPRAGPTSAAVLLQPLVQQPAVSPVVLIQGAIRVQPEGPAPAAPRPERKSIVPAPMPGNSCPPEVDAKLLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSGLKLGSGNRKVVCIMVFLLFIAFNFGPVSISEPPPAPMSPRMSREEPRPQRHLLGFSEPGPAHGMEPLREAAQSPGEQQPSSAGRPSFRNLTAFPGGAKELLLRDLDQLFLSSDCRHFNRTESLRLADELSGWVQRHQRGRRKIPHRAQERQKSQLRKKSPPVKPVPTQPPGPPERDPVGQLQLYRHPGRSQPEFLDAIDRREDTFYVVSFRRDHLLLPAISHNKTSRPKMSLVMPAMAPNETVSGRGPPGDYEEMMQIECEVMDTRVIHIKTSTVPPSLRKQPSPSPGNTTGGPLPGSAASPAHQASQPLYLNHP
| null | null |
endoplasmic reticulum unfolded protein response [GO:0030968]; mitotic chromosome condensation [GO:0007076]; negative regulation of ATF6-mediated unfolded protein response [GO:1903892]; negative regulation of gene expression [GO:0010629]; regulation of transcription by RNA polymerase II [GO:0006357]
|
condensed nuclear chromosome [GO:0000794]; early endosome [GO:0005769]; endomembrane system [GO:0012505]; endoplasmic reticulum membrane [GO:0005789]; microtubule organizing center [GO:0005815]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00170;
|
1.20.5.170;
|
BZIP family, ATF subfamily
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q99941}.; PTM: During unfolded protein response, a fragment of approximately 60 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage is probably performed sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases. {ECO:0000250|UniProtKB:Q99941}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99941}; Single-pass type II membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 beta]: Nucleus {ECO:0000250|UniProtKB:Q99941}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. {ECO:0000250|UniProtKB:Q99941}.
| null | null | null | null | null |
FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 beta]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 beta), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR). {ECO:0000250|UniProtKB:Q99941}.; FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6 beta]: Transcription factor that acts in the unfolded protein response (UPR) pathway by activating UPR target genes induced during ER stress. Binds DNA on the 5'-CCAC[GA]-3' half of the ER stress response element (ERSE) (5'-CCAATN(9)CCAC[GA]-3') when NF-Y is bound to ERSE. {ECO:0000250|UniProtKB:Q99941}.
|
Mus musculus (Mouse)
|
O35453
|
HEPS_MOUSE
|
MAKEDEEPGAHRGGSTCSRPQPGKGGRTAACCSRPKVAALIVGTLLFLTGIGAASWAIVTILLQSDQEPLYQVQLSPGDSRLAVFDKTEGTWRLLCSSRSNARVAGLGCEEMGFLRALAHSELDVRTAGANGTSGFFCVDEGGLPLAQRLLDVISVCDCPRGRFLTATCQDCGRRKLPVDRIVGGQDSSLGRWPWQVSLRYDGTHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVARTSPHAVQLGVQAVIYHGGYLPFRDPTIDENSNDIALVHLSSSLPLTEYIQPVCLPAAGQALVDGKVCTVTGWGNTQFYGQQAMVLQEARVPIISNEVCNSPDFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISGTSRWRLCGIVSWGTGCALARKPGVYTKVTDFREWIFKAIKTHSEASGMVTQP
|
3.4.21.106
| null |
basement membrane disassembly [GO:0034769]; cholesterol homeostasis [GO:0042632]; cochlea morphogenesis [GO:0090103]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; epithelium development [GO:0060429]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; pilomotor reflex [GO:0097195]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of cell growth [GO:0030307]; positive regulation of gene expression [GO:0010628]; positive regulation of hepatocyte proliferation [GO:2000347]; positive regulation of plasminogen activation [GO:0010756]; positive regulation of thyroid hormone generation [GO:2000611]; potassium ion transmembrane transport [GO:0071805]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to thyroid hormone [GO:0097066]; sensory perception of sound [GO:0007605]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
serine-type endopeptidase activity [GO:0004252]; serine-type exopeptidase activity [GO:0070008]; serine-type peptidase activity [GO:0008236]
|
PF09272;PF00089;
|
3.10.250.10;2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P05981}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P05981}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:9395459}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.; EC=3.4.21.106; Evidence={ECO:0000305|PubMed:26673890, ECO:0000305|PubMed:9395459};
| null | null | null | null |
FUNCTION: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2 (By similarity). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization (PubMed:26673890). {ECO:0000250|UniProtKB:P05981, ECO:0000269|PubMed:26673890}.
|
Mus musculus (Mouse)
|
O35454
|
CLCN6_MOUSE
|
MAGCRGSVCCCCRWCCCCGERESRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFSVRLFTQLKFGVVQTSVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEIKCYLNGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLLVSLVTTVVVFVASMVLGECRQMSSTSQTGNGSFQLQVTSEDVNSTIKAFFCPNDTYNDMATLFFNSQESAILQLFHQDGTFSPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDLFNKGIYDVHIGLRGVPLLEWETDVEMDKLRASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNEKEFMKGNQLISNNIKFKKSSILTRAGEQRKRGQSMKSYPSSELRNVCDEHVASEEPAEKEDLLQQMLERRYTPYPNLYPDQSPSEDWTMEERFRPLTFHGLVLRSQLVTLLVRGVCYSESQSSASQPRLSYAEMAEDYPRYPDIHDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQARLRQHYQTL
| null | null |
chloride transport [GO:0006821]; response to mechanical stimulus [GO:0009612]
|
intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]
|
antiporter activity [GO:0015297]; ATP binding [GO:0005524]; chloride transmembrane transporter activity [GO:0015108]; voltage-gated chloride channel activity [GO:0005247]
|
PF00571;PF00654;
|
3.10.580.10;1.10.3080.10;
|
Chloride channel (TC 2.A.49) family, ClC-6/CLCN6 subfamily
|
PTM: N-glycosylated on several asparagine residues. {ECO:0000250|UniProtKB:P51797}.
|
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:16950870}; Multi-pass membrane protein {ECO:0000269|PubMed:16950870}.
|
CATALYTIC ACTIVITY: Reaction=2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in); Xref=Rhea:RHEA:29567, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P51797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29568; Evidence={ECO:0000250|UniProtKB:P51797};
| null | null | null | null |
FUNCTION: Voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the late endosome lumen. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters. {ECO:0000269|PubMed:16950870}.
|
Mus musculus (Mouse)
|
O35457
|
CCRL2_MOUSE
|
MDNYTVAPDDEYDVLILDDYLDNSGPDQVPAPEFLSPQQVLQFCCAVFAVGLLDNVLAVFILVKYKGLKNLGNIYFLNLALSNLCFLLPLPFWAHTAAHGESPGNGTCKVLVGLHSSGLYSEVFSNILLLVQGYRVFSQGRLASIFTTVSCGIVACILAWAMATALSLPESVFYEPRMERQKHKCAFGKPHFLPIEAPLWKYVLTSKMIILVLAFPLLVFIICCRQLRRRQSFRERQYDLHKPALVITGVFLLMWAPYNTVLFLSAFQEHLSLQDEKSSYHLDASVQVTQLVATTHCCVNPLLYLLLDRKAFMRYLRSLFPRCNDIPYQSSGGYQQAPPREGHGRPIELYSNLHQRQDII
| null | null |
calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]
|
cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
|
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; chemokine receptor binding [GO:0042379]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Receptor for CCL19 and chemerin/RARRES2. Does not appear to be a signaling receptor, but may have a role in modulating chemokine-triggered immune responses by capturing and internalizing CCL19 or by presenting RARRES2 ligand to CMKLR1, a functional signaling receptor. Plays a critical role for the development of Th2 responses (By similarity). {ECO:0000250, ECO:0000269|PubMed:12885941, ECO:0000269|PubMed:18794339, ECO:0000269|PubMed:20606167}.
|
Mus musculus (Mouse)
|
O35458
|
VIAAT_RAT
|
MATLLRSKLTNVATSVSNKSQAKVSGMFARMGFQAATDEEAVGFAHCDDLDFEHRQGLQMDILKSEGEPCGDEGAEPPVEGDIHYQRGGAPLPPSGSKDQAVGAGGEFGGHDKPKITAWEAGWNVTNAIQGMFVLGLPYAILHGGYLGLFLIIFAAVVCCYTGKILIACLYEENEDGEVVRVRDSYVAIANACCAPRFPTLGGRVVNVAQIIELVMTCILYVVVSGNLMYNSFPGLPVSQKSWSIIATAVLLPCAFLKNLKAVSKFSLLCTLAHFVINILVIAYCLSRARDWAWEKVKFYIDVKKFPISIGIIVFSYTSQIFLPSLEGNMQQPSEFHCMMNWTHIAACVLKGLFALVAYLTWADETKEVITDNLPGSIRAVVNIFLVAKALLSYPLPFFAAVEVLEKSLFQEGSRAFFPACYGGDGRLKSWGLTLRCALVVFTLLMAIYVPHFALLMGLTGSLTGAGLCFLLPSLFHLRLLWRKLLWHQVFFDVAIFVIGGICSVSGFVHSLEGLIEAYRTNAED
| null | null |
beta-alanine transport [GO:0001762]; gamma-aminobutyric acid import [GO:0051939]; gamma-aminobutyric acid transport [GO:0015812]; glycine transport [GO:0015816]; hippocampus development [GO:0021766]; neurotransmitter loading into synaptic vesicle [GO:0098700]; neurotransmitter transport [GO:0006836]
|
cell surface [GO:0009986]; cell tip [GO:0051286]; cone cell pedicle [GO:0044316]; dendrite [GO:0030425]; dendrite terminus [GO:0044292]; GABA-ergic synapse [GO:0098982]; inhibitory synapse [GO:0060077]; neuron projection [GO:0043005]; neuron projection terminus [GO:0044306]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; vacuolar membrane [GO:0005774]
|
gamma-aminobutyric acid transmembrane transporter activity [GO:0015185]; gamma-aminobutyric acid:proton antiporter activity [GO:0140800]; glycine transmembrane transporter activity [GO:0015187]; glycine:proton antiporter activity [GO:0140799]
|
PF01490;
| null |
Amino acid/polyamine transporter 2 family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:10036231, ECO:0000269|PubMed:9822734}; Multi-pass membrane protein {ECO:0000255}. Presynapse {ECO:0000269|PubMed:10036231}. Note=Presents in glycine-, GABA- or GABA- and glycine-containing boutons. {ECO:0000269|PubMed:10036231}.
|
CATALYTIC ACTIVITY: Reaction=beta-alanine(out) + n H(+)(in) = beta-alanine(in) + n H(+)(out); Xref=Rhea:RHEA:70987, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966; Evidence={ECO:0000305|PubMed:23919636}; CATALYTIC ACTIVITY: Reaction=4-aminobutanoate(out) + n H(+)(in) = 4-aminobutanoate(in) + n H(+)(out); Xref=Rhea:RHEA:70979, ChEBI:CHEBI:15378, ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:9349821}; CATALYTIC ACTIVITY: Reaction=glycine(out) + n H(+)(in) = glycine(in) + n H(+)(out); Xref=Rhea:RHEA:70983, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305; Evidence={ECO:0000250|UniProtKB:O35633};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 mM for 4-aminobutanoate {ECO:0000269|PubMed:9349821}; KM=3.5 mM for beta-alanine {ECO:0000269|PubMed:23919636}; KM=0.8 mM for 4-aminobutanoate {ECO:0000269|PubMed:19843525}; KM=2.1 mM for chloride {ECO:0000269|PubMed:19843525}; KM=2.3 mM for chloride (for 4-aminobutanoate uptake) {ECO:0000269|PubMed:19843525}; Vmax=38 nmol/min/mg enzyme toward beta-alanine {ECO:0000269|PubMed:23919636}; Vmax=41 nmol/min/mg enzyme toward 4-aminobutanoate {ECO:0000269|PubMed:19843525}; Vmax=90.6 nmol/min/mg enzyme toward chloride {ECO:0000269|PubMed:19843525}; Vmax=7.4 nmol/min/mg enzyme toward chloride (for 4-aminobutanoate uptake) {ECO:0000269|PubMed:19843525};
| null | null | null |
FUNCTION: Antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals (By similarity) (PubMed:9349821). The transport is equally dependent on the chemical and electrical components of the proton gradient (PubMed:9349821). May also transport beta-alanine (PubMed:23919636). Acidification of GABAergic synaptic vesicles is a prerequisite for 4-aminobutanoate uptake (By similarity). {ECO:0000250|UniProtKB:O35633, ECO:0000269|PubMed:23919636, ECO:0000269|PubMed:9349821}.
|
Rattus norvegicus (Rat)
|
O35460
|
ANGP1_RAT
|
MTVFLSFAFFAAILTHIGCSNQRRSPENGGRRYNRIQHGQCAYTFILPEHDGNCRESATEQYNTNALQRDAPHVETDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYELEKQLLQQTNEILKIQEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVTRQTFIIQELEKQLSRATSNNSVLQKQQLELMDTVHNLVSLCTKEVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNEGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNQKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
| null | null |
angiogenesis [GO:0001525]; animal organ regeneration [GO:0031100]; cell-substrate adhesion [GO:0031589]; glomerulus vasculature development [GO:0072012]; hemopoiesis [GO:0030097]; heparin biosynthetic process [GO:0030210]; in utero embryonic development [GO:0001701]; liver regeneration [GO:0097421]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of vascular permeability [GO:0043116]; neuron apoptotic process [GO:0051402]; ovarian follicle development [GO:0001541]; positive chemotaxis [GO:0050918]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of blood-brain barrier permeability [GO:1905605]; positive regulation of cell adhesion [GO:0045785]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of receptor internalization [GO:0002092]; protein localization to cell surface [GO:0034394]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of macrophage migration inhibitory factor signaling pathway [GO:2000446]; regulation of skeletal muscle satellite cell proliferation [GO:0014842]; regulation of tumor necrosis factor production [GO:0032680]; response to estrogen [GO:0043627]; response to hypoxia [GO:0001666]; response to vitamin B3 [GO:0033552]; sprouting angiogenesis [GO:0002040]; Tie signaling pathway [GO:0048014]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; microvillus [GO:0005902]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor binding [GO:0005102]
|
PF00147;
|
3.90.215.10;4.10.530.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08538}.
| null | null | null | null | null |
FUNCTION: Binds and activates TIE2 receptor by inducing its tyrosine phosphorylation. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. Mediates blood vessel maturation/stability. It may play an important role in the heart early development.
|
Rattus norvegicus (Rat)
|
O35462
|
ANGP2_RAT
|
MWQIVFLTFGCDLVLASAYNNFRKSVDSTGRRQYQVQNGPCSYTFLLPETDSCRSSSSPYMSNAVQRDAPLDYDDSVQRLQVLENILENNTQWLMKLENYIQDNMKKEMVEIQQNVVQNQTAVMIEIGTSLLNQTAAQTRKLTDVEAQVLNQTTRLELQLLQHSISTNKLEKQILDQTSEINKLQDKNSFLEKKVLDMEDKHSVQLQSMKEQKDQLQVLVSKQSSVIDELEKKLVTATVNNSVLQKQQHDLMETVNSLLTMMSSPDYKSSVAVPKEEKTTFRDCAEIFKSGLTTSGIYTLTFPNSTEEVKAYCDMDMGGGGWTVIQHREDGSVDFQRTWKEYKEGFGSPLGEYWLGNEFVSQLTSGHRYVLKIQLKDWEGSEAHSLYEHFYLSGEESNYRIHLTGLTGTAGKISSISQPGSDFSTKDSDNDKCICKCSQMLTGGWWFDACGPSNLNGQYYPQKQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF
| null | null |
angiogenesis [GO:0001525]; animal organ regeneration [GO:0031100]; blood vessel morphogenesis [GO:0048514]; cellular response to growth factor stimulus [GO:0071363]; gene expression [GO:0010467]; germ cell development [GO:0007281]; glomerulus vasculature development [GO:0072012]; maternal process involved in female pregnancy [GO:0060135]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of positive chemotaxis [GO:0050928]; positive regulation of angiogenesis [GO:0045766]; response to activity [GO:0014823]; response to glucose [GO:0009749]; response to hypoxia [GO:0001666]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; Tie signaling pathway [GO:0048014]
|
cell projection [GO:0042995]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; receptor tyrosine kinase binding [GO:0030971]
|
PF00147;
|
3.90.215.10;4.10.530.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O15123}.
| null | null | null | null | null |
FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (By similarity). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression (By similarity). In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (By similarity). Involved in the regulation of lymphangiogenesis (By similarity). {ECO:0000250|UniProtKB:O15123}.
|
Rattus norvegicus (Rat)
|
O35464
|
SEM6A_MOUSE
|
MRPAALLLCLTLLHCAGAGFPEDSEPISISHGNYTKQYPVFVGHKPGRNTTQRHRLDIQMIMIMNRTLYVAARDHIYTVDIDTSHTEEIYCSKKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLKKNDDTLFVCGTNAFNPSCRNYRVDTLETFGDEFSGMARCPYDAKHANIALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAVDYGDYIYFFFREIAVEYNTMGKVVFPRVAQVCKNDMGGSQRVLEKQWTSFLKARLNCSVPGDSHFYFNILQAVTDVIRINGRDVVLATFSTPYNSIPGSAVCAYDMLDIANVFTGRFKEQKSPDSTWTPVPDERVPKPRPGCCAGSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYRLTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLARIGSSGFLNGSLFLEEMNVYNPEKCSYDGVEDKRIMGMQLDRASGSLYVAFSTCVIKVPLGRCERHGKCKKTCIASRDPYCGWVRESGSCAHLSPLSRLTFEQDIERGNTDGLGDCHNSFVALNGHASSLYPSTTTSDSASRDGYESRGGMLDWNDLLEAPGSTDPLGAVSSHNHQDKKGVIRESYLKSNDQLVPVTLLAIAVILAFVMGAVFSGIIVYCVCDHRRKDVAVVQRKEKELTHSRRGSMSSVTKLSGLFGDTQSKDPKPEAILTPLMHNGKLATPSNTAKMLIKADQHHLDLTALPTPESTPTLQQKRKPNRGSREWERNQNIINACTKDMPPMGSPVIPTDLPLRASPSHIPSVVVLPITQQGYQHEYVDQPKMSEVVAQMALEDQAATLEYKTIKEHLSSKSPNHGVNLVENLDSLPPKVPQREASLGPPGTSLSQTGLSKRLEMQHSSSYGLEYKRSYPTNSLTRSHQTTTLKRNNTNSSNSSHLSRNQSFGRGDNPPPAPQRVDSIQVHSSQPSGQAVTVSRQPSLNAYNSLTRSGLKRTPSLKPDVPPKPSFAPLSTSMKPNDACT
| null | null |
apoptotic process [GO:0006915]; axon guidance [GO:0007411]; cell surface receptor signaling pathway [GO:0007166]; centrosome localization [GO:0051642]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; neural crest cell migration [GO:0001755]; neuron migration [GO:0001764]; positive regulation of neuron migration [GO:2001224]; semaphorin-plexin signaling pathway [GO:0071526]
|
axon [GO:0030424]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
chemorepellent activity [GO:0045499]; identical protein binding [GO:0042802]; semaphorin receptor binding [GO:0030215]; transmembrane signaling receptor activity [GO:0004888]
|
PF01437;PF01403;
|
3.30.1680.10;2.130.10.10;
|
Semaphorin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20881961}; Single-pass type I membrane protein {ECO:0000269|PubMed:20881961}.
| null | null | null | null | null |
FUNCTION: Cell surface receptor for PLXNA2 that plays an important role in cell-cell signaling. Required for normal granule cell migration in the developing cerebellum. Promotes reorganization of the actin cytoskeleton and plays an important role in axon guidance in the developing central nervous system. Can act as repulsive axon guidance cue. Has repulsive action towards migrating granular neurons. May play a role in channeling sympathetic axons into the sympathetic chains and controlling the temporal sequence of sympathetic target innervation. {ECO:0000269|PubMed:16205717, ECO:0000269|PubMed:19063725, ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}.
|
Mus musculus (Mouse)
|
O35465
|
FKBP8_MOUSE
|
MASWAEPSEPAALRLPGAPLLEGFEVLDGVDDAEEEDDLSGLPPLEDMGQPTVEEAEQPGALAREFLAATEPEPAPAPAPEEWLDILGNGLLRMKTLVPGPKGSSRPLKGQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAEDGPDLEMLSGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSNTKVDMTCEEEEELLQLKVKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKRAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN
|
5.2.1.8
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
|
apoptotic process [GO:0006915]; BMP signaling pathway [GO:0030509]; camera-type eye development [GO:0043010]; cell fate specification [GO:0001708]; dorsal/ventral neural tube patterning [GO:0021904]; dorsal/ventral pattern formation [GO:0009953]; multicellular organism growth [GO:0035264]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein phosphorylation [GO:0001933]; neural tube development [GO:0021915]; neuron fate specification [GO:0048665]; positive regulation of BMP signaling pathway [GO:0030513]; protein folding [GO:0006457]; protein localization to mitochondrion [GO:0070585]; regulation of BMP signaling pathway [GO:0030510]; regulation of gene expression [GO:0010468]; regulation of mitophagy [GO:1901524]; smoothened signaling pathway [GO:0007224]
|
cytosol [GO:0005829]; endomembrane system [GO:0012505]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial envelope [GO:0005740]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]
|
calmodulin binding [GO:0005516]; disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; protein folding chaperone [GO:0044183]
|
PF00254;PF13432;
|
3.10.50.40;1.25.40.10;
| null |
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q14318}.
|
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:15105374}; Single-pass membrane protein {ECO:0000269|PubMed:15105374}; Cytoplasmic side {ECO:0000269|PubMed:15105374}.
|
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
| null | null | null | null |
FUNCTION: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (By similarity). Required for normal embryonic development. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35468
|
WNT9B_MOUSE
|
MRPAPALALAALCLLVLPAAAAAAAYFGLTGREVLTPFPGLGTAAAPAQAGAHLKQCDLLKLSRRQKQLCRREPGLAETLRDAAHLGLLECQFQFRQERWNCSLEGRTGLLQRGFKETAFLYAVSAAALTHALARACSAGRMERCTCDDSPGLESRQAWQWGVCGDNLKYSTKFLSNFLGPKRGSKDLRARADAHNTHVGIKAVKSGLRTTCKCHGVSGSCAVRTCWKQLSPFRETGQVLKLRYDTAVKVSSATNEALGRLELWAPAKPGGPAKGLAPRPGDLVYMEDSPSFCRPSKYSPGTAGRVCSRDSSCSSLCCGRGYDTQSRMVVFSCHCQVQWCCYVECQQCAQQELVYTCKR
| null | null |
animal organ morphogenesis [GO:0009887]; branching involved in ureteric bud morphogenesis [GO:0001658]; branching morphogenesis of an epithelial tube [GO:0048754]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cell-cell signaling [GO:0007267]; cellular response to starvation [GO:0009267]; collecting duct development [GO:0072044]; embryonic cranial skeleton morphogenesis [GO:0048701]; establishment of planar polarity involved in nephron morphogenesis [GO:0072046]; in utero embryonic development [GO:0001701]; kidney development [GO:0001822]; kidney morphogenesis [GO:0060993]; kidney rudiment formation [GO:0072003]; male genitalia development [GO:0030539]; mesenchymal stem cell maintenance involved in nephron morphogenesis [GO:0072038]; mesonephric duct formation [GO:0072181]; mesonephric tubule development [GO:0072164]; metanephric tubule development [GO:0072170]; metanephric tubule formation [GO:0072174]; midbrain dopaminergic neuron differentiation [GO:1904948]; negative regulation of stem cell population maintenance [GO:1902455]; nephron tubule morphogenesis [GO:0072078]; neuron differentiation [GO:0030182]; regulation of asymmetric cell division [GO:0009786]; regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis [GO:0003339]; regulation of protein phosphorylation [GO:0001932]; regulation of tube size [GO:0035150]; roof of mouth development [GO:0060021]; signal transduction [GO:0007165]; uterus morphogenesis [GO:0061038]; Wnt signaling pathway [GO:0016055]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; Wnt-Frizzled-LRP5/6 complex [GO:1990851]
|
co-receptor binding [GO:0039706]; cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; signaling receptor binding [GO:0005102]
|
PF00110;
|
3.30.2460.20;
|
Wnt family
|
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:O14905}. Secreted {ECO:0000250|UniProtKB:O14905}.
| null | null | null | null | null |
FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:16054034, PubMed:17537789, PubMed:22461561). Required for normal embryonic kidney development, and for normal development of the urogenital tract, including uterus and part of the oviduct and the upper vagina in females, and epididymis and vas deferens in males (PubMed:16054034). Activates a signaling cascade in the metanephric mesenchyme that induces tubulogenesis (PubMed:16054034, PubMed:17537789). Acts upstream of WNT4 in the signaling pathways that mediate development of kidney tubules and the Muellerian ducts (PubMed:16054034). Plays a role in cranofacial development and is required for normal fusion of the palate during embryonic development (PubMed:16054034, PubMed:22461561, PubMed:25257647). {ECO:0000269|PubMed:16054034, ECO:0000269|PubMed:17537789, ECO:0000269|PubMed:22461561, ECO:0000269|PubMed:25257647, ECO:0000305}.
|
Mus musculus (Mouse)
|
O35469
|
3BHS6_MOUSE
|
MPGWSCLVTGAGGFLGQRIVQLLMQEKDLEEIRVLDKFFRPETREQFFNLDTNIKVTVLEGDILDTQYLRKACQGISVVIHTAAVIDVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKEIILNGNEEEHHESIWSDPYPYSKKMAEKAVLAANGSMLKIGGTLHTCALRPMYIYGERSPFISNTIITALKNKNILGCTGKFSTANPVYVGNVAWAHILAARGLRDPKKSPNIQGEFYYISDDTPHQSYDDLNYTLSKEWGFCPDSSWSLPVPLLYWLAFMLETVSFLLSPIYRFIPPFNRHLVTLTGSTFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWIGTLVEQHRETLDTKSQ
|
1.1.1.-; 1.1.1.145; 5.3.3.1
| null |
androgen biosynthetic process [GO:0006702]; C21-steroid hormone biosynthetic process [GO:0006700]; C21-steroid hormone metabolic process [GO:0008207]; hippocampus development [GO:0021766]; negative regulation of iron ion transport [GO:0034757]; response to corticosterone [GO:0051412]; steroid biosynthetic process [GO:0006694]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial membrane [GO:0031966]
|
3-beta-hydroxy-delta5-steroid dehydrogenase activity [GO:0003854]; cholesterol dehydrogenase activity [GO:0102294]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; steroid delta-isomerase activity [GO:0004769]
|
PF01073;
|
3.40.50.720;
|
3-beta-HSD family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-steroid + H(+) + NADH; Xref=Rhea:RHEA:24076, ChEBI:CHEBI:1722, ChEBI:CHEBI:15378, ChEBI:CHEBI:47907, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.145; CATALYTIC ACTIVITY: Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid; Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909; EC=5.3.3.1;
| null |
PATHWAY: Lipid metabolism; steroid biosynthesis.
| null | null |
FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. May be involved in local production of progesterone.
|
Mus musculus (Mouse)
|
O35473
|
C1D_MOUSE
|
MAGEEMNEDYPVEIHESLTALESSLGAVDDMLKTMMAVSRNELLQKLDPLEQAKVDLVSAYTLNSMFWVYLATQGVNPKEHPVKQELERIRVYMNRVKEITDKKKAAKLDRGAASRFVKNALWEPKAKSTPKVANKGKSKH
| null | null |
apoptotic process [GO:0006915]; maturation of 5.8S rRNA [GO:0000460]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of gene expression [GO:0010468]
|
cytoplasm [GO:0005737]; exosome (RNase complex) [GO:0000178]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; transcription repressor complex [GO:0017053]
|
DNA binding [GO:0003677]; nuclear receptor binding [GO:0016922]; RNA binding [GO:0003723]; transcription corepressor activity [GO:0003714]
|
PF04000;
| null |
C1D family
|
PTM: Phosphorylated by PRKDC. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9405624}. Cytoplasm {ECO:0000250|UniProtKB:Q13901}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13901}. Note=EXOSC10 is required for nucleolar localization. Colocalizes with TSNAX in the nucleus. {ECO:0000250|UniProtKB:Q13901}.
| null | null | null | null | null |
FUNCTION: Plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this function may include MPHOSPH6. Can activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. Can induce apoptosis in a p53/TP53 dependent manner. May regulate the TRAX/TSN complex formation. Potentiates transcriptional repression by NR1D1 and THRB (By similarity). {ECO:0000250, ECO:0000269|PubMed:10362552, ECO:0000269|PubMed:9405624}.
|
Mus musculus (Mouse)
|
O35476
|
OPSG_RAT
|
MAQQLTGEQTLDHYEDSTQASIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSTWMILVVIASVFTNGLVLAATMRFKKLRHPLNWILVNLAVADLAETIIASTISVVNQIYGYFVLGHPLCVIEGYIVSLCGITGLWSLAIISWERWLVVCKPFGNVRFDAKLATVGIVFSWVWAAVWTAPPIFGWSRYWPYGLKTSCGPDVFSGTSYPGVQSYMMVLMVTCCIFPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVFAYCLCWGPYTFFACFATAHPGYAFHPLVASLPSYFAKSATIYNPIIYVFMNRQFRNCILQLFGKKVDDSSELSSTSKTEVSSVSSVSPA
| null | null |
cellular response to light stimulus [GO:0071482]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; positive regulation of cytokinesis [GO:0032467]; visual perception [GO:0007601]
|
photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
|
G protein-coupled photoreceptor activity [GO:0008020]; identical protein binding [GO:0042802]; photoreceptor activity [GO:0009881]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: O-glycosylated. {ECO:0000250|UniProtKB:O35599}.; PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light.
|
Rattus norvegicus (Rat)
|
O35484
|
AZIN1_MOUSE
|
MKGFIDDANYSVGLLDEGTNLGNVIDNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQTVVAQIKPFYTVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIFTSPCKQVSQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQLEEVNHVISPLLDIYFPEGSGIQIISEPGSYYVSSAFTLAVNIIAKKVVENDKFSSGVEKNGSDEPAFVYYMNDGVYGSFASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYFMMSFSDWYEMQDAGITSDAMMKNFFFAPSCIQLSQEDSFSTEA
| null | null |
negative regulation of protein catabolic process [GO:0042177]; polyamine metabolic process [GO:0006595]; positive regulation of centrosome duplication [GO:0010825]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of polyamine transmembrane transport [GO:1902269]; putrescine biosynthetic process from ornithine [GO:0033387]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ornithine decarboxylase activator activity [GO:0042978]; ornithine decarboxylase activity [GO:0004586]
|
PF02784;PF00278;
|
3.20.20.10;
|
Orn/Lys/Arg decarboxylase class-II family, ODC antizyme inhibitor subfamily
|
PTM: Ubiquitinated, leading to its proteasomal degradation; a process that is reduced in presence of antizyme OAZ1. {ECO:0000269|PubMed:18062773}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19449338}.
| null | null | null | null | null |
FUNCTION: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:16916800, PubMed:18062773, PubMed:18508777). Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:10698696, PubMed:18062773, PubMed:18369191). {ECO:0000269|PubMed:10698696, ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18369191, ECO:0000269|PubMed:18508777}.
|
Mus musculus (Mouse)
|
O35485
|
VEGFB_RAT
|
MSPLLRRLLLVALLQLACTQAPVSQFDGPSHQKKVVSWIDVYARATCQPREVVVPLSMELMGNVVKQLVPSCVTVQRCGGCCPDDGLECVPIGQHQVRMQILMIQYPSSQLGEMSLEEHSQCECRPKRKESAVKPDRVAIPHHRPQPRSVLSWDSAPGASSPADIIHPTPAPGPSAHAAPSAVSALIPGPAVAAADAAASSIAKGGA
| null | null |
angiogenesis [GO:0001525]; cardiac muscle contraction [GO:0060048]; coronary vasculature development [GO:0060976]; heart development [GO:0007507]; induction of positive chemotaxis [GO:0050930]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell division [GO:0051781]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of mast cell chemotaxis [GO:0060754]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of vascular wound healing [GO:0035470]; protein O-linked glycosylation [GO:0006493]; response to hypoxia [GO:0001666]; response to xenobiotic stimulus [GO:0009410]; sprouting angiogenesis [GO:0002040]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vascular endothelial growth factor signaling pathway [GO:0038084]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]
|
chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; vascular endothelial growth factor receptor 1 binding [GO:0043183]; vascular endothelial growth factor receptor 2 binding [GO:0043184]
|
PF00341;
|
2.10.90.10;
|
PDGF/VEGF growth factor family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted but remains associated to cells or to the extracellular matrix unless released by heparin. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O35488
|
S27A2_MOUSE
|
MLPVLYTGLAGLLLLPLLLTCCCPYLLQDVRYFLRLANMARRVRSYRQRRPVRTILRAFLEQARKTPHKPFLLFRDETLTYAQVDRRSNQVARALHDQLGLRQGDCVALFMGNEPAYVWIWLGLLKLGCPMACLNYNIRAKSLLHCFQCCGAKVLLASPDLQEAVEEVLPTLKKDAVSVFYVSRTSNTNGVDTILDKVDGVSAEPTPESWRSEVTFTTPAVYIYTSGTTGLPKAATINHHRLWYGTGLAMSSGITAQDVIYTTMPLYHSAALMIGLHGCIVVGATLALRSKFSASQFWDDCRKYNVTVIQYIGELLRYLCNTPQKPNDRDHKVKKALGNGLRGDVWREFIKRFGDIHVYEFYASTEGNIGFVNYPRKIGAVGRANYLQRKVARYELIKYDVEKDEPVRDANGYCIKVPKGEVGLLVCKITQLTPFIGYAGGKTQTEKKKLRDVFKKGDIYFNSGDLLMIDRENFVYFHDRVGDTFRWKGENVATTEVADIVGLVDFVEEVNVYGVPVPGHEGRIGMASLKIKENYEFNGKKLFQHIAEYLPSYARPRFLRIQDTIEITGTFKHRKVTLMEEGFNPTVIKDTLYFMDDAEKTFVPMTENIYNAIIDKTLKL
|
6.2.1.-; 6.2.1.15; 6.2.1.24; 6.2.1.3; 6.2.1.7
| null |
bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; fatty acid alpha-oxidation [GO:0001561]; fatty acid beta-oxidation [GO:0006635]; fatty acid transport [GO:0015908]; long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; methyl-branched fatty acid metabolic process [GO:0097089]; very long-chain fatty acid catabolic process [GO:0042760]; very long-chain fatty acid metabolic process [GO:0000038]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]
|
arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; cholate-CoA ligase activity [GO:0047747]; enzyme binding [GO:0019899]; fatty acid transmembrane transporter activity [GO:0015245]; long-chain fatty acid transporter activity [GO:0005324]; long-chain fatty acid-CoA ligase activity [GO:0004467]; oleate transmembrane transporter activity [GO:1901480]; phytanate-CoA ligase activity [GO:0050197]; pristanate-CoA ligase activity [GO:0070251]; 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 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14975}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:20530735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P97524}. Cell membrane {ECO:0000269|PubMed:20530735}; Multi-pass membrane protein {ECO:0000255}. Microsome {ECO:0000250|UniProtKB:P97524}.
|
CATALYTIC ACTIVITY: Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879, ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:20530735, ECO:0000269|PubMed:9671728}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in); Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823; Evidence={ECO:0000250|UniProtKB:O14975}; 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:15699031, ECO:0000305|PubMed:20530735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000305|PubMed:15699031, ECO:0000305|PubMed:20530735}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000305|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000305|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936, ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O14975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937; Evidence={ECO:0000250|UniProtKB:O14975}; 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:0000305|PubMed:20530735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000305|PubMed:20530735}; CATALYTIC ACTIVITY: Reaction=2,6,10,14-tetramethylpentadecanoate + ATP + CoA = AMP + diphosphate + pristanoyl-CoA; Xref=Rhea:RHEA:47264, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:77250, ChEBI:CHEBI:77268, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O14975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47265; Evidence={ECO:0000250|UniProtKB:O14975}; CATALYTIC ACTIVITY: Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526, ChEBI:CHEBI:72745, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O14975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140; Evidence={ECO:0000250|UniProtKB:O14975}; CATALYTIC ACTIVITY: Reaction=3,7,11,15-tetramethylhexadecanoate + ATP + CoA = AMP + diphosphate + phytanoyl-CoA; Xref=Rhea:RHEA:21380, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37257, ChEBI:CHEBI:57287, ChEBI:CHEBI:57391, ChEBI:CHEBI:456215; EC=6.2.1.24; Evidence={ECO:0000250|UniProtKB:O14975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21381; Evidence={ECO:0000250|UniProtKB:O14975}; CATALYTIC ACTIVITY: Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15699031, ECO:0000305|PubMed:20530735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537; Evidence={ECO:0000305|PubMed:15699031, ECO:0000305|PubMed:20530735}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate + tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15699031, ECO:0000305|PubMed:20530735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640; Evidence={ECO:0000305|PubMed:15699031, ECO:0000305|PubMed:20530735}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + ATP + CoA = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44932, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:77016, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O14975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44933; Evidence={ECO:0000250|UniProtKB:O14975}; CATALYTIC ACTIVITY: Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + ATP + CoA = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:22976, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58677, ChEBI:CHEBI:58734, ChEBI:CHEBI:456215; EC=6.2.1.7; Evidence={ECO:0000250|UniProtKB:O14975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22977; Evidence={ECO:0000250|UniProtKB:O14975};
| null | null | null | null |
FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes, playing an important role in hepatic fatty acid uptake (PubMed:15699031, PubMed:20530735, PubMed:9671728). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake (PubMed:15699031, PubMed:20530735). Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis (PubMed:15699031, PubMed:20530735). Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid (By similarity). May contribute to the synthesis of sphingosine-1-phosphate (By similarity). Does not activate C24 bile acids, cholate and chenodeoxycholate (By similarity). In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. However, it is not critical for THCA activation and bile synthesis in vivo (By similarity). {ECO:0000250|UniProtKB:O14975, ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:20530735, ECO:0000269|PubMed:9671728}.
|
Mus musculus (Mouse)
|
O35491
|
CLK2_MOUSE
|
MPHPRRYHSSERGSRGSYHEHYQSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDHSSDRRLYDRRYCGSYRRNDYSRDRGEAYYDTDFRQSYEYHRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGTQVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPVPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEDHHQLFDLIENMLEYEPAKRLTLGEALQHPFFACLRTEPPNTKLWDSSRDISR
|
2.7.12.1
| null |
negative regulation of gluconeogenesis [GO:0045721]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of RNA splicing [GO:0043484]; response to ionizing radiation [GO:0010212]; response to organic substance [GO:0010033]; response to retinoic acid [GO:0032526]
|
nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, Lammer subfamily
|
PTM: Autophosphorylates on all three types of residues. Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin. Phosphorylation plays a critical role in cell proliferation following low dose radiation and prevents cell death following high dose radiation. Phosphorylation at Thr-343 by PKB/AKT2 induces its kinase activity which is required for its stability. The phosphorylation status at Ser-141 influences its subnuclear localization; inhibition of phosphorylation at Ser-141 results in accumulation in the nuclear speckle. {ECO:0000269|PubMed:20074525, ECO:0000269|PubMed:9852100}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9307018, ECO:0000269|PubMed:9852100}. Nucleus speckle {ECO:0000269|PubMed:9852100}. Note=Inhibition of phosphorylation at Ser-141 results in accumulation in the nuclear speckle. {ECO:0000269|PubMed:9852100}.
|
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=2.7.12.1; 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=2.7.12.1; CATALYTIC ACTIVITY: 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; EC=2.7.12.1;
| null | null | null | null |
FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Phosphorylates PAGE4 at several serine and threonine residues and this phosphorylation attenuates the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (By similarity). {ECO:0000250|UniProtKB:P49760, ECO:0000269|PubMed:20074525, ECO:0000269|PubMed:21329884, ECO:0000269|PubMed:9307018}.
|
Mus musculus (Mouse)
|
O35492
|
CLK3_MOUSE
|
MPVLSARRKRLASTAGPRRGSGPSLAVRWVPPLGPEPSSDRGRAPMRPRGPTCSTTRRGAGRGPRLLPGPPGRDLHRCRPDPGGAGQSPRVCEFGARAVRPLGRVEPGPPTAASREGAVLPRAEARAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRIPYQRRYREHRDSDTYRCEERSPSFGEDCYGSSRSRHRRRSRERAPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHSSRNPSR
|
2.7.12.1
| null |
protein phosphorylation [GO:0006468]; regulation of RNA splicing [GO:0043484]
|
acrosomal vesicle [GO:0001669]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, Lammer subfamily
|
PTM: Autophosphorylates on all three types of residues. {ECO:0000269|PubMed:9307018}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic vesicle, secretory vesicle, acrosome.
|
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=2.7.12.1; Evidence={ECO:0000269|PubMed:10585269}; 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=2.7.12.1; Evidence={ECO:0000269|PubMed:10585269}; CATALYTIC ACTIVITY: 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; EC=2.7.12.1;
| null | null | null | null |
FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:9307018}.
|
Mus musculus (Mouse)
|
O35493
|
CLK4_MOUSE
|
MRHSKRTHCPDWDSRESWGHESYSGSHKRKRRSHSSTQENRHCKPHHQFKDSDCHYLEARCLNERDYRDRRYIDEYRNDYCEGYVPRHYHRDVESTYRIHCSKSSVRSRRSSPKRKRNRPCASHQSHSKSHRRKRSRSIEDDEEGHLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHGMDGLHVAVKIVKNVGRYREAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKSDYVVKYNSKMKRDERTLKNTDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPIPAHMIQKTRKRKYFHHNQLDWDEHSSAGRYVRRRCKPLKEFMLCHDEEHEKLFDLVRRMLEYDPARRITLDEALQHPFFDLLKRK
|
2.7.12.1
| null |
phosphorylation [GO:0016310]; regulation of RNA splicing [GO:0043484]
|
nucleus [GO:0005634]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, Lammer subfamily
|
PTM: Autophosphorylates on all three types of residues. {ECO:0000269|PubMed:9307018}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9307018}.
|
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=2.7.12.1; 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=2.7.12.1; CATALYTIC ACTIVITY: 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; EC=2.7.12.1;
| null | null | null | null |
FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:11461155, ECO:0000269|PubMed:9307018}.
|
Mus musculus (Mouse)
|
O35495
|
CDK14_MOUSE
|
MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKEDTTFDEICVTKMSTRNCQGTDSVIKHLDTIPEDKKVRVQRTQSTFDPFEKPANQVKRVHSENNACINFKSSSAGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTVYSSKSLRQAWNKLSYVNHAEDLASKLLQCSPKNRLSAQAALSHEYFSDLPPRLWELTDMSSIFTVPNVRLQPEAGESMRAFGKNNSYGKSLSNSKH
|
2.7.11.22
| null |
cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; phosphorylation [GO:0016310]; regulation of canonical Wnt signaling pathway [GO:0060828]; Wnt signaling pathway [GO:0016055]
|
cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytoplasmic cyclin-dependent protein kinase holoenzyme complex [GO:0000308]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; 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, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm. Nucleus. Note=Recruited to the cell membrane by CCNY. {ECO:0000250}.
|
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=2.7.11.22; 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=2.7.11.22;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport (By similarity). {ECO:0000250, ECO:0000269|PubMed:9547506}.
|
Mus musculus (Mouse)
|
O35505
|
CAC1C_CAVPO
|
MVPLVQPTTPAYRPLPSHLSADTEVRGRGTLVHEAQLNCFYISPGGSNYGSPRPAHANINANAAAGLAPEHIPTPGAALSWQAAIDAGRQAKLMGSAGNTTISTVSSTQRKRQQYGKPKKQSGTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHTALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGITDVPAEEDPSPCALESGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGVDEEKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPHWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRLDCFIVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMRTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQEVVEKPAVEETKEEKIELKSITADGESPPTTKINMDDLQPNENEDKSPYPNPDAAGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSPNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDQPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSMNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESDPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVVMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTAMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFGRAGGLFGNHVSYYQSDSRSTFPQTFTTQRPLHINKAGNNQGDTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRFPHPAGYPSTVSTVEGHRPPSSPATWAQEATRKLGAMRCHSRESQIAVVCQEEPSQDKTYDVELNKDAEYCSEPSLLSTEMLSYKDDENRQLTPPEEDKGDTRPSPKKGFLRSASLGRRASFHLECLKRQKNHGGDISQKTVLPLHLVHHQALAVAGLSPLLQRSHSPTAIPRPCATPPATPGSRGWPPKPIPTLRLEGAESCEKLNSSFPSIHCSSWSEEPSPCGGGSSAARRARPVSLMVPSQAGAPGRQFHGSASSLAEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIGEMENAADNILSGGAPQSPNGTLLPFVNCRDPGQDRAGGDEDEGCACALGRGWSEEELADSRVHVRSL
| null | null |
calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transmembrane transport via high voltage-gated calcium channel [GO:0061577]; calcium ion transport into cytosol [GO:0060402]; cardiac conduction [GO:0061337]; positive regulation of adenylate cyclase activity [GO:0045762]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]
|
dendrite [GO:0030425]; L-type voltage-gated calcium channel complex [GO:1990454]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]
|
calmodulin binding [GO:0005516]; high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]; voltage-gated calcium channel activity [GO:0005245]
|
PF08763;PF16885;PF16905;PF00520;
|
1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1C subfamily
|
PTM: Phosphorylation by PKA at Ser-1927 activates the channel. Elevated levels of blood glucose lead to increased phosphorylation by PKA. {ECO:0000250|UniProtKB:Q01815}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15381}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P15381}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15381}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P15381}. Perikaryon {ECO:0000250|UniProtKB:P22002}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q01815}. Note=Colocalizes with ryanodine receptors in distinct clusters at the junctional membrane, where the sarcolemma and the sarcoplasmic reticulum are in close contact. The interaction between RRAD and CACNB2 promotes the expression of CACNA1C at the cell membrane. {ECO:0000250|UniProtKB:P15381}.
| null | null | null | null | null |
FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:10101289). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart (By similarity). Required for normal heart development and normal regulation of heart rhythm (By similarity). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine (By similarity). Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (By similarity). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (By similarity). {ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q01815, ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:10101289}.
|
Cavia porcellus (Guinea pig)
|
O35507
|
PPARA_CAVPO
|
MVDMESPLCPLSPLEAEDLESPLSEYFLQEMGTIQDISRSLGEDSSGSFGFPEYQYLGSGPGSDGSVITDTLSPASSPSSVSYPEVPCGVDEPPSSALNIECRICGDKASGYHYGVHACEGCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSEKAKLKAEVLTCDRDSEGAETADLKSLAKRIYEAYLKNFHMNKVKARIILAGKTSSHPLFVIHDMETLCTAEKTLMAKVVSDGIRDKEAEVRIFHCCQCVSVETVTNLTEFAKAIPGFASLDLNDQVTLLKYGVYEAIFTMLSSTMNKDGMLVAYGHGFITREFLKNLRKPFCDMMEPKFNFAMKFNALELDDSDISLFVAAIICCGDRPGLLNIDHIEKMQEAIVHVLKLHLQSNHPDDTFLFPKLLQKLADLRQLVTEHAQLVQVIKTESDAALHPLLQEIYRDMY
| null | null |
cell differentiation [GO:0030154]; cellular response to starvation [GO:0009267]; circadian regulation of gene expression [GO:0032922]; enamel mineralization [GO:0070166]; epidermis development [GO:0008544]; fatty acid metabolic process [GO:0006631]; gluconeogenesis [GO:0006094]; negative regulation of appetite [GO:0032099]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of glycolytic process [GO:0045820]; negative regulation of hepatocyte apoptotic process [GO:1903944]; negative regulation of inflammatory response [GO:0050728]; negative regulation of leukocyte cell-cell adhesion [GO:1903038]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; negative regulation of sequestering of triglyceride [GO:0010891]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of ATP biosynthetic process [GO:2001171]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fatty acid oxidation [GO:0046321]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of transformation of host cell by virus [GO:1904189]; regulation of circadian rhythm [GO:0042752]; wound healing [GO:0042060]
|
nucleoplasm [GO:0005654]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; lipid binding [GO:0008289]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; ubiquitin conjugating enzyme binding [GO:0031624]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as a transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2 (By similarity). {ECO:0000250}.
|
Cavia porcellus (Guinea pig)
|
O35509
|
RB11B_RAT
|
MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL
|
3.6.5.2
| null |
amyloid-beta clearance by transcytosis [GO:0150093]; cellular response to acidic pH [GO:0071468]; constitutive secretory pathway [GO:0045054]; endocytic recycling [GO:0032456]; establishment of protein localization to membrane [GO:0090150]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; melanosome transport [GO:0032402]; receptor recycling [GO:0001881]; regulated exocytosis [GO:0045055]; regulation of endocytic recycling [GO:2001135]; regulation of monoatomic anion transport [GO:0044070]; regulation of protein localization to cell surface [GO:2000008]; transferrin transport [GO:0033572]
|
cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; Golgi apparatus [GO:0005794]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; myosin V binding [GO:0031489]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
|
PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P46638}.
|
SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250|UniProtKB:P46638}; Lipid-anchor {ECO:0000250|UniProtKB:P46638}; Cytoplasmic side {ECO:0000250|UniProtKB:P46638}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:14627637}; Lipid-anchor {ECO:0000305|PubMed:14627637}; Cytoplasmic side {ECO:0000305|PubMed:14627637}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q15907}; Lipid-anchor {ECO:0000250|UniProtKB:Q15907}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15907}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:Q15907}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:Q15907};
| null | null | null | null |
FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The small Rab GTPase RAB11B plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis. Promotes Rabin8/RAB3IP preciliary vesicular trafficking to mother centriole by forming a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating ciliogenesis initiation. On the contrary, upon LPAR1 receptor signaling pathway activation, interaction with phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (By similarity). {ECO:0000250|UniProtKB:Q15907, ECO:0000269|PubMed:14627637}.
|
Rattus norvegicus (Rat)
|
O35516
|
NOTC2_MOUSE
|
MPALRPAALRALLWLWLCGAGPAHALQCRGGQEPCVNEGTCVTYHNGTGFCRCPEGFLGEYCQHRDPCEKNRCQNGGTCVPQGMLGKATCRCAPGFTGEDCQYSTSHPCFVSRPCQNGGTCHMLSRDTYECTCQVGFTGKQCQWTDACLSHPCENGSTCTSVASQFSCKCPAGLTGQKCEADINECDIPGRCQHGGTCLNLPGSYRCQCPQGFTGQHCDSPYVPCAPSPCVNGGTCRQTGDFTFECNCLPGFEGSTCERNIDDCPNHKCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCTNRNGGYGCVCVNGWSGDDCSENIDDCAYASCTPGSTCIDRVASFSCLCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQGYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEVNECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGILCDENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGLNCEINFDDCASNPCMHGVCVDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKGATCINDVNGFRCICPEGPHHPSCYSQVNECLSNPCIHGNCTGGLSGYKCLCDAGWVGVNCEVDKNECLSNPCQNGGTCNNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCFDDVSGYTCHCMLPYTGKNCQTVLAPCSPNPCENAAVCKEAPNFESFSCLCAPGWQGKRCTVDVDECISKPCMNNGVCHNTQGSYVCECPPGFSGMDCEEDINDCLANPCQNGGSCVDHVNTFSCQCHPGFIGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCTCPAGFHGVHCENNIDECTESSCFNGGTCVDGINSFSCLCPVGFTGPFCLHDINECSSNPCLNAGTCVDGLGTYRCICPLGYTGKNCQTLVNLCSRSPCKNKGTCVQEKARPHCLCPPGWDGAYCDVLNVSCKAAALQKGVPVEHLCQHSGICINAGNTHHCQCPLGYTGSYCEEQLDECASNPCQHGATCNDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDECAGGPHCLNGGQCVDRIGGYTCRCLPGFAGERCEGDINECLSNPCSSEGSLDCVQLKNNYNCICRSAFTGRHCETFLDVCPQKPCLNGGTCAVASNMPDGFICRCPPGFSGARCQSSCGQVKCRRGEQCIHTDSGPRCFCLNPKDCESGCASNPCQHGGTCYPQRQPPHYSCRCPPSFGGSHCELYTAPTSTPPATCQSQYCADKARDGICDEACNSHACQWDGGDCSLTMEDPWANCTSTLRCWEYINNQCDEQCNTAECLFDNFECQRNSKTCKYDKYCADHFKDNHCDQGCNSEECGWDGLDCASDQPENLAEGTLIIVVLLPPEQLLQDSRSFLRALGTLLHTNLRIKQDSQGALMVYPYFGEKSAAMKKQKMTRRSLPEEQEQEQEVIGSKIFLEIDNRQCVQDSDQCFKNTDAAAALLASHAIQGTLSYPLVSVFSELESPRNAQLLYLLAVAVVIILFFILLGVIMAKRKRKHGFLWLPEGFTLRRDSSNHKRREPVGQDAVGLKNLSVQVSEANLIGSGTSEHWVDDEGPQPKKAKAEDEALLSEDDPIDRRPWTQQHLEAADIRHTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVLCGPNRSFLSLKHTPMGKKARRPNTKSTMPTSLPNLAKEAKDAKGSRRKKCLNEKVQLSESSVTLSPVDSLESPHTYVSDATSSPMITSPGILQASPTPLLAAAAPAAPVHTQHALSFSNLHDMQPLAPGASTVLPSVSQLLSHHHIAPPGSSSAGSLGRLHPVPVPADWMNRVEMNETQYSEMFGMVLAPAEGAHPGIAAPQSRPPEGKHMSTQREPLPPIVTFQLIPKGSIAQAAGAPQTQSSCPPAVAGPLPSMYQIPEMPRLPSVAFPPTMMPQQEGQVAQTIVPTYHPFPASVGKYPTPPSQHSYASSNAAERTPSHGGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGGGGGQRGPGTHMSEPPHSNMQVYA
| null | null |
animal organ morphogenesis [GO:0009887]; apoptotic process [GO:0006915]; atrial septum morphogenesis [GO:0060413]; BMP signaling pathway [GO:0030509]; bone remodeling [GO:0046849]; cell fate determination [GO:0001709]; cell population proliferation [GO:0008283]; cellular response to tumor cell [GO:0071228]; cholangiocyte proliferation [GO:1990705]; ciliary body morphogenesis [GO:0061073]; defense response to bacterium [GO:0042742]; determination of left/right symmetry [GO:0007368]; embryonic limb morphogenesis [GO:0030326]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; glial cell differentiation [GO:0010001]; glomerular capillary formation [GO:0072104]; heart looping [GO:0001947]; hepatocyte proliferation [GO:0072574]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; humoral immune response [GO:0006959]; in utero embryonic development [GO:0001701]; inflammatory response to antigenic stimulus [GO:0002437]; intracellular signal transduction [GO:0035556]; intrahepatic bile duct development [GO:0035622]; left/right axis specification [GO:0070986]; liver development [GO:0001889]; liver morphogenesis [GO:0072576]; marginal zone B cell differentiation [GO:0002315]; morphogenesis of an epithelial sheet [GO:0002011]; multicellular organism growth [GO:0035264]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of gene expression [GO:0010629]; negative regulation of transcription by RNA polymerase II [GO:0000122]; Notch signaling pathway [GO:0007219]; placenta blood vessel development [GO:0060674]; placenta development [GO:0001890]; podocyte development [GO:0072015]; positive regulation of apoptotic process [GO:0043065]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of keratinocyte proliferation [GO:0010838]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of smooth muscle cell differentiation [GO:0051152]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proximal tubule development [GO:0072014]; pulmonary valve morphogenesis [GO:0003184]; regulation of osteoclast development [GO:2001204]; regulation of transcription by RNA polymerase II [GO:0006357]; wound healing [GO:0042060]
|
cell surface [GO:0009986]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
calcium ion binding [GO:0005509]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; enzyme binding [GO:0019899]; NF-kappaB binding [GO:0051059]; transmembrane signaling receptor activity [GO:0004888]
|
PF00023;PF12796;PF00008;PF07645;PF12661;PF06816;PF07684;PF00066;
|
3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10;
|
NOTCH family
|
PTM: Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form (PubMed:11459941, PubMed:11518718). Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC) (PubMed:11459941, PubMed:11518718). Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT) (By similarity). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane (PubMed:11459941, PubMed:11518718). {ECO:0000250|UniProtKB:Q01705, ECO:0000269|PubMed:11459941, ECO:0000269|PubMed:11518718}.; PTM: Hydroxylated by HIF1AN. {ECO:0000269|PubMed:18299578}.; PTM: Can be either O-glucosylated or O-xylosylated at Ser-613 by POGLUT1. {ECO:0000269|PubMed:21949356}.; PTM: Phosphorylated by GSK3. GSK3-mediated phosphorylation is necessary for NOTCH2 recognition by FBXW7, ubiquitination and degradation via the ubiquitin proteasome pathway. {ECO:0000250|UniProtKB:Q04721}.
|
SUBCELLULAR LOCATION: [Notch 2 extracellular truncation]: Cell membrane {ECO:0000250|UniProtKB:Q04721}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q04721}.; SUBCELLULAR LOCATION: [Notch 2 intracellular domain]: Nucleus {ECO:0000250|UniProtKB:Q04721}. Cytoplasm {ECO:0000250|UniProtKB:Q04721}. Note=Following proteolytical processing NICD is translocated to the nucleus. Retained at the cytoplasm by TCIM. {ECO:0000250|UniProtKB:Q04721}.
| null | null | null | null | null |
FUNCTION: Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination (PubMed:10393120). Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus (PubMed:10393120, PubMed:18710934). Affects the implementation of differentiation, proliferation and apoptotic programs (PubMed:10393120, PubMed:18710934). May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation (By similarity). In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation (PubMed:18710934). Positively regulates self-renewal of liver cancer cells (By similarity). {ECO:0000250|UniProtKB:Q04721, ECO:0000269|PubMed:10393120, ECO:0000269|PubMed:18710934}.
|
Mus musculus (Mouse)
|
O35521
|
PSB9_MUSTR
|
MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGAAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPKFYGE
|
3.4.25.1
| null |
immune system process [GO:0002376]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, beta-subunit complex [GO:0019774]; spermatoproteasome complex [GO:1990111]
|
endopeptidase activity [GO:0004175]; threonine-type endopeptidase activity [GO:0004298]
|
PF00227;
|
3.60.20.10;
|
Peptidase T1B family
|
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250|UniProtKB:O35955}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;
| null | null | null | null |
FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
|
Mus terricolor (Earth-colored mouse) (Mus dunni)
|
O35522
|
PSB9_MUSMB
|
MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTISGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPKFYDE
|
3.4.25.1
| null |
immune system process [GO:0002376]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, beta-subunit complex [GO:0019774]; spermatoproteasome complex [GO:1990111]
|
endopeptidase activity [GO:0004175]; threonine-type endopeptidase activity [GO:0004298]
|
PF00227;
|
3.60.20.10;
|
Peptidase T1B family
|
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250|UniProtKB:O35955}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;
| null | null | null | null |
FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
|
Mus musculus bactrianus (Southwestern Asian house mouse)
|
O35523
|
PSB9_MUSPL
|
MLRAGAPTAGSFRTKEVHTGTTIMAVEFDGGVVVGSDSRVSAGEAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTSEECRRFTTNAITLAMNRDGSSGGVIYLVTITVAGVDHRVILGDELPKFYDE
|
3.4.25.1
| null |
immune system process [GO:0002376]; proteolysis involved in protein catabolic process [GO:0051603]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, beta-subunit complex [GO:0019774]; spermatoproteasome complex [GO:1990111]
|
threonine-type endopeptidase activity [GO:0004298]
|
PF00227;
|
3.60.20.10;
|
Peptidase T1B family
|
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250|UniProtKB:O35955}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;
| null | null | null | null |
FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
|
Mus platythrix (Flat-haired mouse) (Pyromys platythrix)
|
O35524
|
PSB9_MUSSI
|
MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPRFYDE
|
3.4.25.1
| null |
immune system process [GO:0002376]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome core complex, beta-subunit complex [GO:0019774]; spermatoproteasome complex [GO:1990111]
|
endopeptidase activity [GO:0004175]; threonine-type endopeptidase activity [GO:0004298]
|
PF00227;
|
3.60.20.10;
|
Peptidase T1B family
|
PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250|UniProtKB:O35955}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;
| null | null | null | null |
FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
|
Mus spicilegus (Steppe mouse)
|
O35526
|
STX1A_MOUSE
|
MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLETSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG
| null | null |
calcium-ion regulated exocytosis [GO:0017156]; exocytosis [GO:0006887]; hormone secretion [GO:0046879]; insulin secretion [GO:0030073]; intracellular protein transport [GO:0006886]; modulation of excitatory postsynaptic potential [GO:0098815]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; positive regulation of catecholamine secretion [GO:0033605]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of exocytosis [GO:0045921]; positive regulation of neurotransmitter secretion [GO:0001956]; positive regulation of norepinephrine secretion [GO:0010701]; protein localization to membrane [GO:0072657]; protein sumoylation [GO:0016925]; regulated exocytosis [GO:0045055]; regulation of exocytosis [GO:0017157]; regulation of synaptic vesicle priming [GO:0010807]; response to gravity [GO:0009629]; SNARE complex assembly [GO:0035493]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle exocytosis [GO:0016079]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; vesicle docking [GO:0048278]
|
acrosomal vesicle [GO:0001669]; actomyosin [GO:0042641]; axon [GO:0030424]; endomembrane system [GO:0012505]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuron projection [GO:0043005]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; presynaptic active zone membrane [GO:0048787]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685]; secretory granule [GO:0030141]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; synaptobrevin 2-SNAP-25-syntaxin-1a complex [GO:0070044]; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex [GO:0070032]; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex [GO:0070033]; voltage-gated potassium channel complex [GO:0008076]
|
ATP-dependent protein binding [GO:0043008]; calcium channel inhibitor activity [GO:0019855]; calcium-dependent protein binding [GO:0048306]; chloride channel inhibitor activity [GO:0019869]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; myosin binding [GO:0017022]; myosin head/neck binding [GO:0032028]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; transmembrane transporter binding [GO:0044325]
|
PF05739;PF00804;
|
1.20.5.110;1.20.58.70;
|
Syntaxin family
|
PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1 (By similarity). {ECO:0000250}.; PTM: Phosphorylated by CK2 (By similarity). Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16623}.; PTM: Sumoylated, sumoylation is required for regulation of synaptic vesicle endocytosis. {ECO:0000250|UniProtKB:Q16623}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:18760330}; Single-pass type IV membrane protein {ECO:0000269|PubMed:18760330}. Synapse, synaptosome {ECO:0000269|PubMed:18760330}. Cell membrane {ECO:0000250|UniProtKB:P32851}. Note=Colocalizes with KCNB1 at the cell membrane. {ECO:0000250|UniProtKB:P32851}.
| null | null | null | null | null |
FUNCTION: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis (PubMed:17502420, PubMed:28031464, PubMed:28596237). Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion. Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm (PubMed:12101244). Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (PubMed:17502420, PubMed:28031464, PubMed:28596237). {ECO:0000269|PubMed:12101244, ECO:0000269|PubMed:17502420, ECO:0000269|PubMed:28031464, ECO:0000269|PubMed:28596237}.
|
Mus musculus (Mouse)
|
O35532
|
MSMO1_RAT
|
MAMNKSVGLFSSASLAVDYVDSLLPENPLQEPFKNAWVYMLDNYTKFQIATWGSLIVHETIYFLFSLPGFLFQFIPFMRKYKIQKDKPETFEGQWKCLKGILFNHFFIQLPLICGTYYFTEFFNIPYDWERMPRWYFTLARCLGCAVIEDTWHYFLHRLLHHKRIYKYIHKVHHEFQAPFGIEAEYAHPLETLILGTGFFIGIVLLCDHVILLWAWVTMRLLETIDVHSGYDIPLNPLNYIPFYTGARHHDFHHMNFIGNYASTFTWWDRIFGTDVQYHAYTEKMKKLGKKSE
|
1.14.18.9
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:Q15800};
|
cholesterol biosynthetic process via lathosterol [GO:0033490]; ergosterol biosynthetic process [GO:0006696]; sphingolipid biosynthetic process [GO:0030148]; sterol biosynthetic process [GO:0016126]
|
endoplasmic reticulum membrane [GO:0005789]
|
C-4 methylsterol oxidase activity [GO:0000254]; C-5 sterol desaturase activity [GO:0000248]; iron ion binding [GO:0005506]; sphingolipid delta-4 desaturase activity [GO:0042284]; sphingosine hydroxylase activity [GO:0000170]
|
PF04116;
| null |
Sterol desaturase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-4beta-methyl-5alpha-cholest-7-ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:55220, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16455, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58387; EC=1.14.18.9; Evidence={ECO:0000305|PubMed:7228857}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55221; Evidence={ECO:0000305|PubMed:7228857}; CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4beta-methylzymosterol-4alpha-carboxylate + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:55244, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18364, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:64925; Evidence={ECO:0000250|UniProtKB:Q15800}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55245; Evidence={ECO:0000250|UniProtKB:Q15800}; CATALYTIC ACTIVITY: Reaction=4alpha-methylzymosterol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxyzymosterol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:47056, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:1949, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:143575; Evidence={ECO:0000250|UniProtKB:Q15800}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47057; Evidence={ECO:0000250|UniProtKB:Q15800}; CATALYTIC ACTIVITY: Reaction=4alpha-methyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-5alpha-cholest-7-en-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:62768, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145943; Evidence={ECO:0000305|PubMed:7228857}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62769; Evidence={ECO:0000305|PubMed:7228857}; CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholest-8-en-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-4beta-methyl-5alpha-cholest-8-en-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:62776, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:87044, ChEBI:CHEBI:87047; Evidence={ECO:0000250|UniProtKB:Q15800}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62777; Evidence={ECO:0000250|UniProtKB:Q15800}; CATALYTIC ACTIVITY: Reaction=4alpha-methyl-5alpha-cholest-8-en-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-5alpha-cholest-8-ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:62780, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:87051, ChEBI:CHEBI:87055; Evidence={ECO:0000250|UniProtKB:Q15800}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62781; Evidence={ECO:0000250|UniProtKB:Q15800};
| null |
PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 3/6. {ECO:0000305}.; PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000305|PubMed:4394229, ECO:0000305|PubMed:7228857}.
| null | null |
FUNCTION: Catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, which can be subsequently metabolized to cholesterol. {ECO:0000305|PubMed:4394229, ECO:0000305|PubMed:7228857}.
|
Rattus norvegicus (Rat)
|
O35543
|
HPGDS_RAT
|
MPNYKLLYFNMRGRAEIIRYIFAYLDIKYEDHRIEQADWPKIKPTLPFGKIPVLEVEGLTLHQSLAIARYLTKNTDLAGKTELEQCQVDAVVDTLDDFMSLFPWAEENQDLKERTFNDLLTRQAPHLLKDLDTYLGDKEWFIGNYVTWADFYWDICSTTLLVLKPDLLGIYPRLVSLRNKVQAIPAISAWILKRPQTKL
|
2.5.1.18; 5.3.99.2
|
COFACTOR: Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; Note=Glutathione is required for the prostaglandin D synthase activity. {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424};
|
glutathione metabolic process [GO:0006749]; negative regulation of male germ cell proliferation [GO:2000255]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin metabolic process [GO:0006693]
|
cytoplasm [GO:0005737]
|
calcium ion binding [GO:0005509]; glutathione transferase activity [GO:0004364]; magnesium ion binding [GO:0000287]; prostaglandin-D synthase activity [GO:0004667]; protein homodimerization activity [GO:0042803]
|
PF14497;PF02798;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily, Sigma family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:9323136}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10601; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:9323136}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin D2; Xref=Rhea:RHEA:51232, ChEBI:CHEBI:85166, ChEBI:CHEBI:133979; Evidence={ECO:0000250|UniProtKB:O60760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51233; Evidence={ECO:0000250|UniProtKB:O60760};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for glutathione for the prostaglandin D synthase activity {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; KM=500 uM for glutathione for the glutathione-conjugating activity {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; KM=500 uM for PGH2 for the prostaglandin D synthase activity {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; KM=3 mM for 1-chloro-2,4-dinitrobenzene {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; Vmax=17.6 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; Vmax=9.2 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; Vmax=48.3 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; Vmax=17.9 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; Vmax=0.35 umol/min/mg enzyme with cumene hydroperoxide as substrate {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; Vmax=10.2 umol/min/mg enzyme with allyl isothiocyanate as substrate {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424}; Vmax=11.3 umol/min/mg enzyme with benzyl isothiocyanate as substrate {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424};
| null | null | null |
FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide. {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:9323136}.
|
Rattus norvegicus (Rat)
|
O35544
|
EAA4_MOUSE
|
MSSHGNSLFLRESGAGGGCLQGLQDSLQQRALRTRLRLQTMTREHVRRFLRRNAFILLTVSAVIIGVSLAFALRPYQLSYRQIKYFSFPGELLMRMLQMLVLPLIVSSLVTGMASLDNKATGRMGMRAAVYYMVTTVIAVFIGILMVTIIHPGKGSKEGLHREGRIETVPTADAFMDLVRNMFPPNLVEACFKQFKTQYSTRVVTRTIVRTDNGSELGASMSPTSSVENETSILENVTRALGTLQEVISFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIAGKILEMEDMAVLGGQLGMYTLTVIVGLFLHAGGVLPLIYFLVTHRNPFPFIGGMLQALITAMGTSSSSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQEKGASRGRGGNESVM
| null | null |
establishment of localization in cell [GO:0051649]; L-aspartate import across plasma membrane [GO:0140009]; L-glutamate import across plasma membrane [GO:0098712]; L-glutamate transmembrane transport [GO:0015813]; neurotransmitter uptake [GO:0001504]; regulation of membrane potential [GO:0042391]
|
glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; intermediate filament cytoskeleton [GO:0045111]; membrane [GO:0016020]; membrane protein complex [GO:0098796]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]
|
glutamate:sodium symporter activity [GO:0015501]; high-affinity L-glutamate transmembrane transporter activity [GO:0005314]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamate transmembrane transporter activity [GO:0005313]; metal ion binding [GO:0046872]; monoatomic anion transmembrane transporter activity [GO:0008509]; neutral L-amino acid transmembrane transporter activity [GO:0015175]
|
PF00375;
|
1.10.3860.10;
|
Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family, SLC1A6 subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9379843}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) = H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:P48664}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) + L-aspartate(out) + 3 Na(+)(out) = H(+)(in) + K(+)(out) + L-aspartate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70851, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29991; Evidence={ECO:0000250|UniProtKB:P48664}; CATALYTIC ACTIVITY: Reaction=D-aspartate(out) + H(+)(out) + K(+)(in) + 3 Na(+)(out) = D-aspartate(in) + H(+)(in) + K(+)(out) + 3 Na(+)(in); Xref=Rhea:RHEA:71379, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29990; Evidence={ECO:0000250|UniProtKB:P48664};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for L-glutamate {ECO:0000269|PubMed:9379843};
| null | null | null |
FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:9379843). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable). {ECO:0000250|UniProtKB:O35921, ECO:0000269|PubMed:9379843, ECO:0000305}.
|
Mus musculus (Mouse)
|
O35547
|
ACSL4_RAT
|
MKLKLNVLTIVLLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVAKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKAALLDINCVKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMYGGK
|
6.2.1.15; 6.2.1.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
dendritic spine development [GO:0060996]; embryonic process involved in female pregnancy [GO:0060136]; fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; lipid metabolic process [GO:0006629]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; long-chain fatty-acyl-CoA metabolic process [GO:0035336]; neuron differentiation [GO:0030182]; positive regulation of insulin secretion [GO:0032024]; response to interleukin-15 [GO:0070672]; response to nutrient [GO:0007584]; triglyceride biosynthetic process [GO:0019432]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lipid droplet [GO:0005811]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]
|
arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; very long-chain fatty acid-CoA ligase activity [GO:0031957]
|
PF00501;
|
3.30.300.30;3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60488}; Single-pass type III membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:O60488}.
|
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:23766516, ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:9096315}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000269|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000269|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109; Evidence={ECO:0000305|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=5,6-epoxy-(8Z,11Z,14Z)-eicosatrienoate + ATP + CoA = 5,6-epoxy-(8Z,11Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52088, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:131992, ChEBI:CHEBI:136351, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23766516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52089; Evidence={ECO:0000305|PubMed:23766516}; CATALYTIC ACTIVITY: Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52016, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84024, ChEBI:CHEBI:136117, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017; Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52012, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:76625, ChEBI:CHEBI:136115, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013; Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804}; CATALYTIC ACTIVITY: Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + ATP + CoA = 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52008, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84025, ChEBI:CHEBI:136107, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52009; Evidence={ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804}; 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:0000250|UniProtKB:O60488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000250|UniProtKB:O60488}; CATALYTIC ACTIVITY: Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526, ChEBI:CHEBI:72745, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O60488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140; Evidence={ECO:0000250|UniProtKB:O60488};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34 uM for ATP {ECO:0000269|PubMed:15683247}; KM=4.1 uM for CoA {ECO:0000269|PubMed:15683247}; KM=5.4 uM for palmitate {ECO:0000269|PubMed:15683247}; KM=19.5 uM for oleate {ECO:0000269|PubMed:15683247}; KM=10 uM for arachidonate {ECO:0000269|PubMed:15683247}; KM=4.5 uM for palmitate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=2.9 uM for stearate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=16.7 uM for oleate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=4 uM for linoleate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=11.4 uM for arachidonate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=24.8 uM for palmitate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; KM=12.5 uM for stearate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; KM=3.6 uM for oleate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; KM=13.3 uM for linoleate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; KM=7.5 uM for arachidonate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; Vmax=2800 nmol/min/mg enzyme with palmitate as substrate {ECO:0000269|PubMed:15683247}; Vmax=673 nmol/min/mg enzyme with oleate as substrate {ECO:0000269|PubMed:15683247}; Vmax=4200 nmol/min/mg enzyme with arachidonate as substrate {ECO:0000269|PubMed:15683247}; Vmax=4451 nmol/min/mg enzyme with palmitate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=2737 nmol/min/mg enzyme with stearate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=2366 nmol/min/mg enzyme with oleate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=1231 nmol/min/mg enzyme with linoleate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=7180 nmol/min/mg enzyme with arachidonate as substrate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; Vmax=1990 nmol/min/mg enzyme with palmitate as substrate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; Vmax=1240 nmol/min/mg enzyme with stearate as substrate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; Vmax=466 nmol/min/mg enzyme with oleate as substrate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; Vmax=1011 nmol/min/mg enzyme with linoleate as substrate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804}; Vmax=4339 nmol/min/mg enzyme with arachidonate as substrate (when expressed in mammalian cell) {ECO:0000269|PubMed:28209804};
| null | null | null |
FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:23766516, PubMed:28209804, PubMed:9096315). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:9096315). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET (PubMed:23766516). Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (PubMed:23766516). Modulates prostaglandin E2 secretion (By similarity). {ECO:0000250|UniProtKB:O60488, ECO:0000269|PubMed:23766516, ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:9096315}.
|
Rattus norvegicus (Rat)
|
O35548
|
MMP16_RAT
|
MILLAFSSGRRLDFVHRSGVFFFQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFNIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRRAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDRSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSVPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGNGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITIWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRDKEGLSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 zinc ions per subunit. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
|
bone development [GO:0060348]; chondrocyte proliferation [GO:0035988]; collagen catabolic process [GO:0030574]; craniofacial suture morphogenesis [GO:0097094]; embryonic cranial skeleton morphogenesis [GO:0048701]; endochondral ossification [GO:0001958]; extracellular matrix organization [GO:0030198]; ossification [GO:0001503]; protein processing [GO:0016485]; proteolysis [GO:0006508]; response to odorant [GO:1990834]; skeletal system development [GO:0001501]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
metalloaminopeptidase activity [GO:0070006]; 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: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. Note=Localized at the cell surface of melanoma cells. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Short]: Secreted, extracellular space, extracellular matrix.
| null | null | null | null | null |
FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. The short isoform efficiently converts progelatinase A to the intermediate form but not to the mature one. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.
|
Rattus norvegicus (Rat)
|
O35550
|
RABE1_RAT
|
MAQPGPAPQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEEDEQQRINKGKDNKKIDTEEEVKIPVVCALTQEESSTPLSNEEEHLDSTHGSVHSLDADLLLPSGDPFSKSDNDMFKEGLRRAQSTDSLGTSSSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTVSLGSLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSETEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKEKQELEDFLRQSAEDSSHQISALVLRAQASEVLLEELQQSFSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQLAEDFILPDTVQVLRELVLKYRENIVHVRTAADHMEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKVNLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQLPET
| null | null |
apoptotic process [GO:0006915]; endocytosis [GO:0006897]; Golgi to plasma membrane transport [GO:0006893]; protein localization to ciliary membrane [GO:1903441]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]
|
early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; presynaptic cytosol [GO:0099523]; protein-containing complex [GO:0032991]; recycling endosome [GO:0055037]
|
growth factor activity [GO:0008083]; GTPase activator activity [GO:0005096]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]
|
PF09311;PF03528;
|
1.20.5.340;1.20.5.730;
|
Rabaptin family
|
PTM: Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex from the endoplasmic reticulum through the Golgi to the cilium. {ECO:0000250|UniProtKB:O35551, ECO:0000250|UniProtKB:Q15276}.
|
Rattus norvegicus (Rat)
|
O35551
|
RABE1_MOUSE
|
MAQPGPAPQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAIMKETVRDYEHQFHLRLEQERAQWAQYRESAEREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEEDEQQRVNKRKDNKKTDTEEEVKIPVVCALTQEESSTPLSNEEEHLDSTHGSVHSLDADLMLPSGDPFSKSDNDMFKDGLRRAQSTDSLGTSSSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTVSLGSLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSETEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKEKQELEDFLKQSAEDSSHQISALVLRAQASEVLLEELQQSFSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQLAEDFILPDTVEVLRELVLKYRENIVHVRTAADHMEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEMKVNLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQLPET
| null | null |
apoptotic process [GO:0006915]; endocytosis [GO:0006897]; Golgi to plasma membrane transport [GO:0006893]; protein localization to ciliary membrane [GO:1903441]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]
|
early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; presynaptic cytosol [GO:0099523]; protein-containing complex [GO:0032991]; recycling endosome [GO:0055037]
|
growth factor activity [GO:0008083]; GTPase activator activity [GO:0005096]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]
|
PF09311;PF03528;
|
1.20.5.340;1.20.5.730;
|
Rabaptin family
|
PTM: Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex from the endoplasmic reticulum through the Golgi to the cilium (PubMed:25405894). {ECO:0000250|UniProtKB:Q15276, ECO:0000269|PubMed:25405894}.
|
Mus musculus (Mouse)
|
O35552
|
F263_RAT
|
MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCALAALRDVKSYLTKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRINCYEASYQPLDPDKCDRDLSFIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEYNVQGKIGGDSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVSTHRERSEAVKIQHFASVVRPSSYTELDFLSVESAKQDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQPLLGKACLRTVCHIFSKFSPY
|
2.7.1.105; 3.1.3.46
| null |
fructose 2,6-bisphosphate metabolic process [GO:0006003]; fructose metabolic process [GO:0006000]; regulation of glycolytic process [GO:0006110]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]
|
6-phosphofructo-2-kinase activity [GO:0003873]; ATP binding [GO:0005524]; fructose-2,6-bisphosphate 2-phosphatase activity [GO:0004331]
|
PF01591;PF00300;
|
3.40.50.300;3.40.50.1240;
|
Phosphoglycerate mutase family
|
PTM: Phosphorylation by AMPK stimulates activity. {ECO:0000250|UniProtKB:Q16875}.
| null |
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; Evidence={ECO:0000250|UniProtKB:Q16875}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17290; Evidence={ECO:0000250|UniProtKB:Q16875}; CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579, ChEBI:CHEBI:456216; EC=2.7.1.105; Evidence={ECO:0000250|UniProtKB:Q16875}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15654; Evidence={ECO:0000250|UniProtKB:Q16875};
| null | null | null | null |
FUNCTION: Catalyzes both the synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000250|UniProtKB:Q16875}.
|
Rattus norvegicus (Rat)
|
O35565
|
FGF10_MOUSE
|
MWKWILTHCASAFPHLPGCCCCFLLLFLVSSFPVTCQALGQDMVSQEATNCSSSSSSFSSPSSAGRHVRSYNHLQGDVRWRRLFSFTKYFLTIEKNGKVSGTKNEDCPYSVLEITSVEIGVVAVKAINSNYYLAMNKKGKLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRRGQKTRRKNTSAHFLPMTIQT
| null | null |
actin cytoskeleton organization [GO:0030036]; angiogenesis [GO:0001525]; animal organ formation [GO:0048645]; animal organ morphogenesis [GO:0009887]; blood vessel morphogenesis [GO:0048514]; blood vessel remodeling [GO:0001974]; branch elongation involved in salivary gland morphogenesis [GO:0060667]; branching involved in salivary gland morphogenesis [GO:0060445]; bronchiole morphogenesis [GO:0060436]; bud elongation involved in lung branching [GO:0060449]; bud outgrowth involved in lung branching [GO:0060447]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; cell-cell signaling [GO:0007267]; chemotaxis [GO:0006935]; determination of left/right symmetry [GO:0007368]; digestive tract development [GO:0048565]; embryonic camera-type eye development [GO:0031076]; embryonic digestive tract development [GO:0048566]; embryonic digestive tract morphogenesis [GO:0048557]; embryonic genitalia morphogenesis [GO:0030538]; embryonic pattern specification [GO:0009880]; endothelial cell proliferation [GO:0001935]; epidermis development [GO:0008544]; epidermis morphogenesis [GO:0048730]; epithelial cell differentiation [GO:0030855]; epithelial cell proliferation [GO:0050673]; epithelial cell proliferation involved in salivary gland morphogenesis [GO:0060664]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; ERK1 and ERK2 cascade [GO:0070371]; establishment of mitotic spindle orientation [GO:0000132]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; female genitalia morphogenesis [GO:0048807]; fibroblast growth factor receptor apoptotic signaling pathway [GO:1902178]; fibroblast growth factor receptor signaling pathway involved in mammary gland specification [GO:0060595]; fibroblast proliferation [GO:0048144]; hair follicle morphogenesis [GO:0031069]; Harderian gland development [GO:0070384]; induction of positive chemotaxis [GO:0050930]; inner ear morphogenesis [GO:0042472]; keratinocyte proliferation [GO:0043616]; lacrimal gland development [GO:0032808]; limb bud formation [GO:0060174]; limb development [GO:0060173]; limb morphogenesis [GO:0035108]; lung alveolus development [GO:0048286]; lung development [GO:0030324]; lung epithelium development [GO:0060428]; lung morphogenesis [GO:0060425]; lung proximal/distal axis specification [GO:0061115]; lung saccule development [GO:0060430]; male genitalia morphogenesis [GO:0048808]; mammary gland bud formation [GO:0060615]; mammary gland specification [GO:0060594]; mesenchymal cell differentiation involved in lung development [GO:0060915]; mesenchymal-epithelial cell signaling involved in lung development [GO:0060496]; mesonephros development [GO:0001823]; metanephros morphogenesis [GO:0003338]; mitotic cell cycle [GO:0000278]; muscle cell fate commitment [GO:0042693]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of stem cell proliferation [GO:2000647]; odontogenesis of dentin-containing tooth [GO:0042475]; organ growth [GO:0035265]; organ induction [GO:0001759]; otic vesicle formation [GO:0030916]; pancreas development [GO:0031016]; pituitary gland development [GO:0021983]; positive chemotaxis [GO:0050918]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of gene expression [GO:0010628]; positive regulation of hair follicle cell proliferation [GO:0071338]; positive regulation of keratinocyte migration [GO:0051549]; positive regulation of keratinocyte proliferation [GO:0010838]; positive regulation of lymphocyte proliferation [GO:0050671]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of urothelial cell proliferation [GO:0050677]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; positive regulation of white fat cell proliferation [GO:0070352]; positive regulation of Wnt signaling pathway [GO:0030177]; prostatic bud formation [GO:0060513]; protein localization to cell surface [GO:0034394]; radial glial cell differentiation [GO:0060019]; regulation of activin receptor signaling pathway [GO:0032925]; regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling [GO:0060665]; regulation of gene expression [GO:0010468]; regulation of saliva secretion [GO:0046877]; regulation of smoothened signaling pathway [GO:0008589]; respiratory system development [GO:0060541]; response to estradiol [GO:0032355]; response to lipopolysaccharide [GO:0032496]; salivary gland morphogenesis [GO:0007435]; secretion by lung epithelial cell involved in lung growth [GO:0061033]; semicircular canal fusion [GO:0060879]; semicircular canal morphogenesis [GO:0048752]; smooth muscle cell differentiation [GO:0051145]; somatic stem cell population maintenance [GO:0035019]; spleen development [GO:0048536]; stem cell proliferation [GO:0072089]; submandibular salivary gland formation [GO:0060661]; tear secretion [GO:0070075]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; tissue regeneration [GO:0042246]; type II pneumocyte differentiation [GO:0060510]; urothelial cell proliferation [GO:0050674]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; white fat cell differentiation [GO:0050872]; white fat cell proliferation [GO:0070343]; Wnt signaling pathway [GO:0016055]; wound healing [GO:0042060]
|
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; type 2 fibroblast growth factor receptor binding [GO:0005111]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing.
|
Mus musculus (Mouse)
|
O35567
|
PUR9_RAT
|
MASSQLALFSVSDKTGLVEFARNLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDAADMARLDFNLIRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYGAVAAEMQGSGNKDTSLETRRHLALKAFTHTAQYDEAISDYFRRQYSKGISQMPLRYGMNPHQTPAQLYTLKPKLPITVLNGAPGFINLCDALNAWQLVTELRGAVDIPAAASFKHVSPAGAAVGVPLSEDEARVCMVYDLYPTLTPLAIAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIVAPGYEEEALKILSKKKNGSYCVLQMDQSYKPDENEVRTLFGLRLSQKRNNGVVDKSLFSNIVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKDGQVIGIGAGQQSRIHCTRLAGDKANSWWLRHHPRVLSMKFKAGVKRAEVSNAIDQYVTGTIGEGEDLVKWKALFEEVPELLTEAEKKEWVDKLSGVSVSSDAFFPFRDNVDRAKRSGVAYIVAPSGSTADKVVIEACDELGIVLAHTDLRLFHH
|
2.1.2.3; 3.5.4.10
| null |
'de novo' AMP biosynthetic process [GO:0044208]; 'de novo' IMP biosynthetic process [GO:0006189]; 'de novo' XMP biosynthetic process [GO:0097294]; animal organ regeneration [GO:0031100]; brainstem development [GO:0003360]; cellular response to interleukin-7 [GO:0098761]; cerebellum development [GO:0021549]; cerebral cortex development [GO:0021987]; dihydrofolate metabolic process [GO:0046452]; GMP biosynthetic process [GO:0006177]; response to inorganic substance [GO:0010035]; tetrahydrofolate biosynthetic process [GO:0046654]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
IMP cyclohydrolase activity [GO:0003937]; phosphoribosylaminoimidazolecarboxamide formyltransferase activity [GO:0004643]; protein homodimerization activity [GO:0042803]
|
PF01808;PF02142;
|
1.10.287.440;3.40.140.20;3.40.50.1380;
|
PurH family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54113}.
|
CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3; Evidence={ECO:0000250|UniProtKB:P31939}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22193; Evidence={ECO:0000250|UniProtKB:P31939}; CATALYTIC ACTIVITY: Reaction=10-formyldihydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate; Xref=Rhea:RHEA:59144, ChEBI:CHEBI:57451, ChEBI:CHEBI:57452, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; Evidence={ECO:0000250|UniProtKB:P31939}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59145; Evidence={ECO:0000250|UniProtKB:P31939}; CATALYTIC ACTIVITY: Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377, ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10; Evidence={ECO:0000250|UniProtKB:P31939}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18447; Evidence={ECO:0000250|UniProtKB:P31939};
| null |
PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. {ECO:0000250|UniProtKB:P31939}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1. {ECO:0000250|UniProtKB:P31939}.
| null | null |
FUNCTION: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction. Also catalyzes the cyclization of FAICAR to IMP (By similarity). Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (PubMed:25687571). {ECO:0000250|UniProtKB:P31939, ECO:0000269|PubMed:25687571}.
|
Rattus norvegicus (Rat)
|
O35568
|
FBLN3_RAT
|
MLQTVFLTMLTLALVKSQVTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGGYLCLPKTAQIIVNNEQPQQETPAAEASSGAATGTIAARSMATSGVIPGGGFIASATAVAGPEVQTGRNNFVIRRNPADPQRIPSNPSHRIQCAAGYEQSEHNVCQDIDECTSGTHNCRLDQVCINLRGSFTCHCLPGYQKRGEQCVDIDECSVPPYCHQGCVNTPGSFYCQCNPGFQLAANNYTCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPQNPCQDPYVLTSENRCVCPVSNTMCRDVPQSIVYKYMNIRSDRSVPSDIFQIQATTIYANTINTFRIKSGNENGEFYLRQTSPVSAMLVLVKSLTGPREHIVGLEMLTVSSIGTFRTSSVLRLTIIVGPFSF
| null | null |
camera-type eye development [GO:0043010]; embryonic eye morphogenesis [GO:0048048]; epidermal growth factor receptor signaling pathway [GO:0007173]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of neuron projection development [GO:0010977]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell projection organization [GO:0031346]; post-embryonic eye morphogenesis [GO:0048050]; regulation of DNA-templated transcription [GO:0006355]; regulation of glial cell migration [GO:1903975]
|
basement membrane [GO:0005604]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; epidermal growth factor receptor activity [GO:0005006]; epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]
|
PF12662;PF07645;
|
2.10.25.10;
|
Fibulin family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:18803302}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18803302}. Note=Localizes to the lamina propria underneath the olfactory epithelium.
| null | null | null | null | null |
FUNCTION: Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth. {ECO:0000269|PubMed:18803302}.
|
Rattus norvegicus (Rat)
|
O35569
|
NRG2_RAT
|
MRQVCCSALPPPLEKARCSSYSYSDSSSSSSSNNSSSSTSSRSSSRSSSRSSRGSTTTTSSSENSGSNSGSIFRPAAPPEPRPQPQPQPRSPAARRAAARSRAAAAGGMRRDPAPGSSMLLFGVSLACYSPSLKSVQDQAYKAPVVVEGKVQGLAPAGGSSSNSTREPPASGRVALVKVLDKWPLRSGGLQREQVISVGSCAPLERNQRYIFFLEPTEQPLVFKTAFAPVDPNGKNIKKEVGKILCTDCATRPKLKKMKSQTGEVGEKQSLKCEAAAGNPQPSYRWFKDGKELNRSRDIRIKYGNGRKNSRLQFNKVKVEDAGEYVCEAENILGKDTVRGRLHVNSVSTTLSSWSGHARKCNETAKSYCVNGGVCYYIEGINQLSCKCPNGFFGQRCLEKLPLRLYMPDPKQKHLGFELKEAEELYQKRVLTITGICVALLVVGIVCVVAYCKTKKQRRQMHHHLRQNMCPAHQNRSLANGPSHPRLDPEEIQMADYISKNVPATDHVIRREAETTFSGSHSCSPSHHCSTATPTSSHRHESHTWSLERSESLTSDSQSGIMLSSVGTSKCNSPACVEARARRAAAYSQEERRRAAMPPYHDSIDSLRDSPHSERYVSALTTPARLSPVDFHYSLATQVPTFEITSPNSAHAVSLPPAAPISYRLAEQQPLLRHPAPPGPGPGPGADMQRSYDSYYYPAAGPGPRRGACALGGSLGSLPASPFRIPEDDEYETTQECAPPPPPRPRTRGASRRTSAGPRRWRRSRLNGLAAQRARAARDSLSLSSGSGCGSASASDDDADDADGALAAESTPFLGLRAAHDALRSDSPPLCPAADSRTYYSLDSHSTRASSRHSRGPPTRAKQDSGPL
| null | null |
animal organ development [GO:0048513]; cell surface receptor signaling pathway [GO:0007166]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERBB2-ERBB3 signaling pathway [GO:0038133]; ERBB4 signaling pathway [GO:0038130]; ERBB4-ERBB4 signaling pathway [GO:0038138]; intracellular signal transduction [GO:0035556]; nervous system development [GO:0007399]; regulation of synapse assembly [GO:0051963]; regulation of synapse maturation [GO:0090128]
|
extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]
|
epidermal growth factor receptor activity [GO:0005006]; epidermal growth factor receptor binding [GO:0005154]; ErbB-3 class receptor binding [GO:0043125]; ErbB-4 class receptor binding [GO:1990631]; growth factor activity [GO:0008083]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102]
|
PF07679;PF02158;
|
2.60.40.10;2.10.25.10;
|
Neuregulin family
|
PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form. {ECO:0000250}.; PTM: Extensive glycosylation precedes the proteolytic cleavage. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Pro-neuregulin-2, membrane-bound isoform]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: [Neuregulin-2]: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor.
|
Rattus norvegicus (Rat)
|
O35587
|
TMEDA_MESAU
|
MSGSSGPLSWPGPRPCALLFLLLLGPSSVLAISFHLPVNSRKCLREEIHKDLLVTGAYEITDQSGGAGGLRTHLKITDSAGHILYAKEDATKGKFAFTTEDYDMFEVCFESKGTGRIPDQLVILDMKHGVEAKNYEEIAKVEKLKPLEVELRRLEDLSESIVNDFAYMKKREEEMRDTNESTNTRVLYFSIFSMLCLIGLATWQVFYLRRFFKAKKLIE
| null | null |
COPI-coated vesicle budding [GO:0035964]; cytosol to ERGIC protein transport [GO:0106273]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; positive regulation of interleukin-1 production [GO:0032732]; positive regulation of protein secretion [GO:0050714]; protein localization to ERGIC [GO:0106272]; regulated exocytosis [GO:0045055]; regulation of amyloid-beta formation [GO:1902003]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
COPI-coated vesicle [GO:0030137]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; gamma-secretase complex [GO:0070765]; Golgi membrane [GO:0000139]; melanosome [GO:0042470]; plasma membrane [GO:0005886]; trans-Golgi network transport vesicle [GO:0030140]; transport vesicle membrane [GO:0030658]; zymogen granule membrane [GO:0042589]
|
protein transmembrane transporter activity [GO:0008320]; syntaxin binding [GO:0019905]
|
PF01105;
| null |
EMP24/GP25L family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49755}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P49755}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:9382861, ECO:0000269|PubMed:9527489}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:9382861}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:9527489}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P49755}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q63584}; Single-pass type I membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P49755}.
| null | null | null | null | null |
FUNCTION: Cargo receptor involved in protein vesicular trafficking and quality control in the endoplasmic reticulum (ER) and Golgi (PubMed:9382861). The p24 protein family is a group of transmembrane proteins that bind coat protein complex I/COPI and coat protein complex II/COPII involved in vesicular trafficking between the membranes. Acts at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and involved in vesicle coat formation at the cytoplasmic side (By similarity). Mainly functions in the early secretory pathway and cycles between the ER, ER-Golgi intermediate compartment (ERGIC) and Golgi, mediating cargo transport through COPI and COPII-coated vesicles (PubMed:9382861). In COPII vesicle-mediated anterograde transport, involved in the transport of GPI-anchored proteins by acting together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER (By similarity). Recognizes GPI anchors structural remodeled in the ER by the GPI inositol-deacylase/PGAP1 and the metallophosphoesterase MPPE1/PGAP5 (By similarity). In COPI vesicle-mediated retrograde transport, involved in the biogenesis of COPI vesicles and vesicle coat recruitment. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent from the modulation of gamma-secretase activity) (By similarity). Involved in the KDELR2-mediated retrograde transport of the toxin A subunit (CTX-A-K63)together with COPI and the COOH terminus of KDELR2 (By similarity). On Golgi membranes, acts as a primary receptor for ARF1-GDP, a GTP-binding protein involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2 which mediates the hydrolysis of ARF1-bound GTP and therefore modulates protein trafficking from the Golgi apparatus. Involved in the exocytic trafficking of G protein-coupled receptors F2LR1/PAR2 (trypsin and tryspin-like enzyme receptor), OPRM1 (opioid receptor) and P2RY4 (UTD and UDP receptor) from the Golgi to the plasma membrane, thus contributing to receptor resensitization. In addition to its cargo receptor activity, may also act as a protein channel after oligomerization, facilitating the post-translational entry of leaderless cytoplasmic cargo into the ERGIC. Involved in the translocation into ERGIC, the vesicle entry and the secretion of leaderless cargos (lacking the secretion signal sequence), including the mature form of interleukin 1/IL-1 family members, the alpha-crystallin B chain HSPB5, the carbohydrate-binding proteins galectin-1/LGALS1 and galectin-3/LGALS3, the microtubule-associated protein Tau/MAPT, and the annexin A1/ANXA1; the translocation process is dependent on cargo protein unfolding and enhanced by chaperones HSP90AB1 and HSP90B1/GRP9. Could also associates with the presenilin-dependent gamma-secretase complex in order to regulate gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40/Abeta40 (By similarity). {ECO:0000250|UniProtKB:P49755, ECO:0000250|UniProtKB:Q28735, ECO:0000250|UniProtKB:Q63584, ECO:0000269|PubMed:9382861}.
|
Mesocricetus auratus (Golden hamster)
|
O35593
|
PSDE_MOUSE
|
MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK
|
3.4.19.-
| null |
double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K63-linked deubiquitination [GO:0070536]; regulation of proteasomal protein catabolic process [GO:0061136]; response to ethanol [GO:0045471]
|
cytosolic proteasome complex [GO:0031597]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]
|
endopeptidase activator activity [GO:0061133]; endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; proteasome binding [GO:0070628]
|
PF01398;
|
3.40.140.10;
|
Peptidase M67A family, PSMD14 subfamily
| null | null | null | null | null | null | null |
FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading. {ECO:0000250|UniProtKB:O00487}.
|
Mus musculus (Mouse)
|
O35594
|
IFT81_MOUSE
|
MSDQIKFIVDSLNKEPFKKNYNLITFDSLGPMQLLQVLNDVLAEIDPKQDVDIREEMPEQTAKRMLNLLGILKYKPPGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRSNELKKRAYLARFLIKLEVPSEFLQDETVADTNKQYEELMEAFKTLHKECEQLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEIKFNSYMVTEKFPKELESKKKELHFLQKVVSEPAMGHSDLLELETKVNEVNTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLVSEKKSALAPVIKELRQLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHYTNCMIKNLEVELRRATDEMKAYVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAVRESHGPNMKQAKMWRDLEQLMECKKQCFLKQQSPASIGQVIQEGGEDRLVL
| null | null |
cilium assembly [GO:0060271]; intraciliary anterograde transport [GO:0035720]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735]; regulation of smoothened signaling pathway [GO:0008589]; sperm flagellum assembly [GO:0120316]; spermatogenesis [GO:0007283]
|
centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; intraciliary transport particle B [GO:0030992]; sperm midpiece [GO:0097225]; sperm principal piece [GO:0097228]
|
tubulin binding [GO:0015631]
|
PF18383;
|
1.10.418.70;
|
IFT81 family
| null |
SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19253336}. Cytoplasm {ECO:0000269|PubMed:32233951}.
| null | null | null | null | null |
FUNCTION: Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region. Required for ciliogenesis. Required for proper regulation of SHH signaling (By similarity). Plays an important role during spermatogenesis by modulating the assembly and elongation of the sperm flagella (PubMed:32233951). {ECO:0000250|UniProtKB:Q8WYA0, ECO:0000269|PubMed:32233951}.; FUNCTION: [Isoform CDV-1]: May be involved in cardiac hypertrophy caused by carnitine deficiency. {ECO:0000269|PubMed:10210276}.; FUNCTION: [Isoform CDV-1R]: May play a role in development of the testis and spermatogenesis. {ECO:0000269|PubMed:12549821}.
|
Mus musculus (Mouse)
|
O35595
|
PTC2_MOUSE
|
MVRPLSLGELPPSYTPPARSSAPHILAGSLQAPLWLRAYFQGLLFSLGCRIQKHCGKVLFLGLVAFGALALGLRVAVIETDLEQLWVEVGSRVSQELHYTKEKLGEEAAYTSQMLIQTAHQEGGNVLTPEALDLHLQAALTASKVQVSLYGKSWDLNKICYKSGVPLIENGMIERMIEKLFPCVILTPLDCFWEGAKLQGGSAYLPGRPDIQWTNLDPQQLLEELGPFASLEGFRELLDKAQVGQAYVGRPCLDPDDPHCPPSAPNRHSRQAPNVAQELSGGCHGFSHKFMHWQEELLLGGTARDLQGQLLRAEALQSTFLLMSPRQLYEHFRGDYQTHDIGWSEEQASMVLQAWQRRFVQLAQEALPANASQQIHAFSSTTLDDILRAFSEVSTTRVVGGYLLMLAYACVTMLRWDCAQSQGAVGLAGVLLVALAVASGLGLCALLGITFNAATTQVLPFLALGIGVDDIFLLAHAFTKAPPDTPLPERMGECLRSTGTSVALTSVNNMVAFFMAALVPIPALRAFSLQAAIVVGCNFAAVMLVFPAILSLDLRRRHRQRLDVLCCFSSPCSAQVIQMLPQELGDRAVPVGIAHLTATVQAFTHCEASSQHVVTILPPQAHLLSPASDPLGSELYSPGGSTRDLLSQEEGTGPQAACRPLLCAHWTLAHFARYQFAPLLLQTRAKALVLLFFGALLGLSLYGATLVQDGLALTDVVPRGTKEHAFLSAQLRYFSLYEVALVTQGGFDYAHSQRALFDLHQRFSSLKAVLPPPATQAPRTWLHYYRSWLQGIQAAFDQDWASGRITCHSYRNGSEDGALAYKLLIQTGNAQEPLDFSQLTTRKLVDKEGLIPPELFYMGLTVWVSSDPLGLAASQANFYPPPPEWLHDKYDTTGENLRIPAAQPLEFAQFPFLLHGLQKTADFVEAIEGARAACTEAGQAGVHAYPSGSPFLFWEQYLGLRRCFLLAVCILLVCTFLVCALLLLSPWTAGLIVLVLAMMTVELFGIMGFLGIKLSAIPVVILVASIGIGVEFTVHVALGFLTSHGSRNLRAASALEQTFAPVTDGAVSTLLGLLMLAGSNFDFIIRYFFVVLTVLTLLGLLHGLLLLPVLLSILGPPPQVVQVYKESPQTLNSAAPQRGGLRWDRPPTLPQSFARVTTSMTVALHPPPLPGAYVHPASEEPT
| null | null |
cell fate determination [GO:0001709]; epidermal cell fate specification [GO:0009957]; epidermis development [GO:0008544]; hair cycle [GO:0042633]; negative regulation of smoothened signaling pathway [GO:0045879]; positive regulation of epidermal cell differentiation [GO:0045606]; regulation of cell growth [GO:0001558]; skin development [GO:0043588]
|
plasma membrane [GO:0005886]
|
hedgehog family protein binding [GO:0097108]; hedgehog receptor activity [GO:0008158]; smoothened binding [GO:0005119]
|
PF02460;PF12349;
|
1.20.1640.10;
|
Patched family
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Plays a role in the control of cellular growth (By similarity). May have a role in epidermal development. May act as a receptor for Sonic hedgehog (SHH). {ECO:0000250|UniProtKB:Q9Y6C5}.
|
Mus musculus (Mouse)
|
O35598
|
ADA10_MOUSE
|
MVLPTVLILLLSWAAGLGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLLLDFHAHGRQFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIKTRGGTFYIEPAERYIKDRILPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEGARAHPEKHAASSGPELLRKKRTTLAERNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTSDEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDDCCFDANQPEGKKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAKEGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYDLEECTCASSDGKDDKELCHVCCMKKMAPSTCASTGSLQWSKQFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPQLYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPPRQRPRESYQMGHMRR
|
3.4.24.81
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O14672}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O14672};
|
adherens junction organization [GO:0034332]; amyloid-beta formation [GO:0034205]; cochlea development [GO:0090102]; constitutive protein ectodomain proteolysis [GO:0051089]; epidermal growth factor receptor ligand maturation [GO:0038004]; in utero embryonic development [GO:0001701]; membrane protein ectodomain proteolysis [GO:0006509]; monocyte activation [GO:0042117]; negative regulation of cell adhesion [GO:0007162]; negative regulation of gene expression [GO:0010629]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; nucleocytoplasmic transport [GO:0006913]; pore complex assembly [GO:0046931]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of T cell chemotaxis [GO:0010820]; postsynapse organization [GO:0099173]; protein catabolic process at postsynapse [GO:0140249]; protein phosphorylation [GO:0006468]; protein processing [GO:0016485]; regulation of dendritic spine morphogenesis [GO:0061001]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of Notch signaling pathway [GO:0008593]; regulation of postsynapse organization [GO:0099175]; regulation of vasculature development [GO:1901342]; response to tumor necrosis factor [GO:0034612]; signaling receptor ligand precursor processing [GO:0140448]; toxin transport [GO:1901998]
|
adherens junction [GO:0005912]; axon [GO:0030424]; cell surface [GO:0009986]; clathrin-coated vesicle [GO:0030136]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle [GO:0005798]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]; pore complex [GO:0046930]; postsynapse [GO:0098794]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; synaptic membrane [GO:0097060]; synaptic vesicle [GO:0008021]; tetraspanin-enriched microdomain [GO:0097197]; trans-Golgi network [GO:0005802]
|
endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metallodipeptidase activity [GO:0070573]; metalloendopeptidase activity [GO:0004222]; metalloendopeptidase activity involved in amyloid precursor protein catabolic process [GO:1902945]; metallopeptidase activity [GO:0008237]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; SH2 domain binding [GO:0042169]; SH3 domain binding [GO:0017124]
|
PF21299;PF00200;PF13574;
|
3.40.390.10;4.10.70.10;
| null |
PTM: The precursor is cleaved by furin and PCSK7. {ECO:0000250|UniProtKB:Q10741}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:26668317, ECO:0000269|PubMed:30463011}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O14672}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O14672}. Cell projection, axon {ECO:0000269|PubMed:29325091}. Cell projection, dendrite {ECO:0000269|PubMed:29325091}. Cell junction, adherens junction {ECO:0000269|PubMed:30463011, ECO:0000269|PubMed:30639848}. Cytoplasm {ECO:0000269|PubMed:30463011}. Note=Is localized in the plasma membrane but is also expressed in the Golgi apparatus and in clathrin-coated vesicles derived likely from the Golgi (By similarity). During long term depression, it is recruited to the cell membrane by DLG1 (PubMed:23676497). The immature form is mainly located near cytoplasmic fibrillar structures, while the mature form is predominantly located at zonula adherens and the cell membrane (PubMed:30463011). The localization and clustering of mature ADAM10 to zonula adherens is regulated by AFDN, TSPAN33, PLEKHA7 and PDZD11 (PubMed:30463011). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:30463011}.
|
CATALYTIC ACTIVITY: Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81; Evidence={ECO:0000269|PubMed:17245433, ECO:0000269|PubMed:29325091, ECO:0000269|PubMed:29430990, ECO:0000269|PubMed:30639848};
| null | null | null | null |
FUNCTION: Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins, including adhesion proteins, growth factor precursors and cytokines being essential for development and tissue homeostasis (PubMed:17245433, PubMed:29325091, PubMed:29430990, PubMed:30639848). Associates with six members of the tetraspanin superfamily TspanC8 which regulate its exit from the endoplasmic reticulum and its substrate selectivity (PubMed:26668317, PubMed:30463011, PubMed:9244301). Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (By similarity). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) at '687-Lys-|-Leu-688' (By similarity). Contributes to the normal cleavage of the cellular prion protein (By similarity). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (By similarity). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (PubMed:9244301). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (By similarity). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (PubMed:17245433). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (PubMed:26876177). Enhances the cleavage of CHL1 by BACE1 (PubMed:29325091). Cleaves NRCAM (PubMed:29430990). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (By similarity). Involved in the development and maturation of glomerular and coronary vasculature (PubMed:29397483, PubMed:30446855). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (PubMed:30639848). May regulate the EFNA5-EPHA3 signaling (By similarity). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:17245433, ECO:0000269|PubMed:26668317, ECO:0000269|PubMed:29325091, ECO:0000269|PubMed:29397483, ECO:0000269|PubMed:29430990, ECO:0000269|PubMed:30446855, ECO:0000269|PubMed:30463011, ECO:0000269|PubMed:30639848, ECO:0000269|PubMed:9244301}.
|
Mus musculus (Mouse)
|
O35599
|
OPSG_MOUSE
|
MAQRLTGEQTLDHYEDSTHASIFTYTNSNSTKGPFEGPNYHIAPRWVYHLTSTWMILVVVASVFTNGLVLAATMRFKKLRHPLNWILVNLAVADLAETIIASTISVVNQIYGYFVLGHPLCVIEGYIVSLCGITGLWSLAIISWERWLVVCKPFGNVRFDAKLATVGIVFSWVWAAIWTAPPIFGWSRYWPYGLKTSCGPDVFSGTSYPGVQSYMMVLMVTCCIFPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVFAYCLCWGPYTFFACFATAHPGYAFHPLVASLPSYFAKSATIYNPIIYVFMNRQFRNCILHLFGKKVDDSSELSSTSKTEVSSVSSVSPA
| null | null |
cellular response to light stimulus [GO:0071482]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; visual perception [GO:0007601]
|
photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
|
G protein-coupled photoreceptor activity [GO:0008020]; identical protein binding [GO:0042802]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: N-glycosylated (PubMed:30948514). O-glycosylated (PubMed:30948514). {ECO:0000269|PubMed:30948514}.; PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04001}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light. {ECO:0000269|PubMed:11055434}.
|
Mus musculus (Mouse)
|
O35600
|
ABCA4_MOUSE
|
MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGLLPWLQGIFCNMNNPCFQNPTPGESPGTVSNYNNSILARVYRDFQELFMDTPEVQHLGQVWAELRTLSQFMDTLRTHPERFAGRGLQIRDILKDEEALTLFLMRNIGLSDSVAHLLVNSQVRVEQFAYGVPDLELTDIACSEALLQRFIIFSQRRGAQTVRDALCPLSQVTLQWIEDTLYADVDFFKLFHVLPTLLDSSSQGINLRFWGGILSDLSPRMQKFIHRPSVQDLLWVSRPLLQNGGPETFTQLMSILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPAYSYDKRTTSFCNSLIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRIMKNANSTFEELDRVRKLVKAWEEVGPQIWYFFEKSTQMTVIRDTLQHPTVKDFINRQLGEEGITTEAVLNFFSNGPQEKQADDMTSFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPGMYPWASSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGIVKSQMQAEPPIGVYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKGIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMALSIFLLTLFIMHGRILHYSDPFILFLFLLAFATATIMQSFLLSTLFSKASLAAACSGVIYFTLYLPHVLCFAWQDRMTADLKTTVSLLSSVAFGFGTEYLVRFEEQGLGLQWSNIGKSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEEMEDPEHPEGMNDSFFERELPGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGVCSCTSKGFSTRCPTRVDEITEEQVLDGDVQELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDAGAGSMFVGGAQQKREQAGLRHPCSAPTEKLRQYAQAPHTCSPGQVDPPKGQPSPEPEDPGVPFNTGARLILQHVQALLVKRFHHTIRSRKDFVAQIVLPATFVFLALMLSIIVPPFGEFPALTLHPWMYGHQYTFFSMDEPNNEHLEVLADVLLNRPGFGNRCLKEEWLPEYPCINATSWKTPSVSPNITHLFQKQKWTAAHPSPSCKCSTREKLTMLPECPEGAGGLPPPQRTQRSTEVLQDLTNRNISDYLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPISGEALVGFLSGLGQMMNVSGGPVTREASKEMLDFLKHLETTDNIKVWFNNKGWHALVSFLNVAHNAILRASLPRDRDPEEYGITVISQPLNLTKEQLSDITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVTKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPDNLPALVSLLMLYGWAVIPMMYPASFLFEVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEYSANPFQWDLIGKNLVAMAIEGVVYFLLTLLIQHHFFLTRWIAEPAREPVFDEDDDVAEERQRVMSGGNKTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKFGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHHSMLQFQVPSSSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYDLPLHPRAAGASWQAKLEEKSGRLQTQEPLPAGSEQLANGSNPTAAEDKHTRSPQ
|
7.6.2.1
| null |
lipid transport [GO:0006869]; phospholipid transfer to membrane [GO:0006649]; phospholipid translocation [GO:0045332]; photoreceptor cell maintenance [GO:0045494]; response to stimulus [GO:0050896]; retinal metabolic process [GO:0042574]; retinoid metabolic process [GO:0001523]; visual perception [GO:0007601]
|
cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; rod photoreceptor disc membrane [GO:0120202]
|
11-cis retinal binding [GO:0005502]; ABC-type transporter activity [GO:0140359]; all-trans retinal binding [GO:0005503]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; ATPase-coupled transmembrane transporter activity [GO:0042626]; flippase activity [GO:0140327]; GTPase activity [GO:0003924]; N-retinylidene-phosphatidylethanolamine flippase activity [GO:0140347]; phosphatidylethanolamine flippase activity [GO:0090555]; phospholipid transporter activity [GO:0005548]; retinoid binding [GO:0005501]
|
PF12698;PF00005;
|
3.40.50.300;
|
ABC transporter superfamily, ABCA family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:F1MWM0}.; PTM: Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal fragment and a 115-kDa C-terminal fragment that are linked through disulfide bonds. {ECO:0000250|UniProtKB:F1MWM0}.; PTM: Phosphorylation is independent of light exposure and modulates ATPase activity. {ECO:0000250|UniProtKB:F1MWM0}.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P78363}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:9202155}. Note=Localized to the rim and incisures of rod outer segments disks. {ECO:0000269|PubMed:9202155}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + N-all-trans-retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-all-trans-retinylidenephosphatidylethanolamine(in) + phosphate; Xref=Rhea:RHEA:67188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167884, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10412977, ECO:0000269|PubMed:10852960, ECO:0000269|PubMed:22735453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67189; Evidence={ECO:0000305|PubMed:22735453}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:22735453}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22735453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000305|PubMed:22735453}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-11-cis-retinylidenephosphatidylethanolamine(in) + phosphate; Xref=Rhea:RHEA:67192, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167887, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:F1MWM0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67193; Evidence={ECO:0000250|UniProtKB:F1MWM0};
| null | null | null | null |
FUNCTION: Flippase that catalyzes in an ATP-dependent manner the transport of retinal-phosphatidylethanolamine conjugates like the 11-cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine from the lumen to the cytoplasmic leaflet of photoreceptor outer segment disk membranes, where N-cis-retinylidene-phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-retinol (all-trans-rol) and therefore prevents the accumulation of excess of 11-cis-retinal and its schiff-base conjugate and the formation of toxic bisretinoid (PubMed:10412977, PubMed:10852960, PubMed:22735453). Displays both ATPase and GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (By similarity). Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine with high affinity in the absence of ATP and ATP binding and hydrolysis induce a protein conformational change that causes the dissociation of N-retinylidene-phosphatidylethanolamine (By similarity). {ECO:0000250|UniProtKB:F1MWM0, ECO:0000269|PubMed:10412977, ECO:0000269|PubMed:10852960, ECO:0000269|PubMed:22735453}.
|
Mus musculus (Mouse)
|
O35601
|
FYB1_MOUSE
|
MAKFNTGSNPTEEAATSSRPFKVAGQSSPSGIQSRKNLFDNQGNASPPAGPSSMPKFGTTKPPLAAKPTYEEKPEKEPKPPFLKPTGGSPRFGTQPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVVLRPPGNKLHNLNQESDLKTPGPKPGPAPPVPENELKPGFSKVAGAKSKFMPAAQDTDSKPRFPRHTFGQKPSLSTEDSQEENTSKNVPVQKGSPVQLGAKSKGAPFKPPKEDPEDKDHGAPSSPFPGVVLKPAASRGSPGLSKNFEEKKEDRKTDLAKNIFLNKLNQEEPARFPKAPSKLTAGTPWGQSQEKEGDKNSATPKQKALPPLSVLGPPPPKPNRPPNVDLTRFRKADSANSATKSQTPYSTTSLPPPPPTHPASQPPLPASHPAHPPVPSLPPRNIKPPLDLKHPINDENQDGVMHSDGTGNLEEEQESEGETYEDIDSSKERDKKREKEEKKRLELERKEQKEREKKEQELKKKFKLTGPIQVIHHAKACCDVKGGKNELSFKQGEDIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEIDYDSLKRKKNSLNAVPPRLVEDDQDVYDDVAEQDAPNSHGQSGSGGMFPPPPTDDEIYDGIEEEDDDDGSVPQVDEKTNAWSWGILKMLKGKDDRKKSIREKPKVSESDNNEGSSLPSQHKQLDVGEEVYDDVDASDFPPPPAEMSQGMSVGRAKTEEKDPKKLKKQEKEEKDLRKKFKYDGEIRVLYSTKVASSLTSKKWGARDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDIADGCIYDND
| null | null |
integrin-mediated signaling pathway [GO:0007229]; protein localization to plasma membrane [GO:0072659]; T cell receptor signaling pathway [GO:0050852]
|
anchoring junction [GO:0070161]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
lipid binding [GO:0008289]; protein-containing complex binding [GO:0044877]
|
PF14603;PF07653;
|
2.30.30.40;
| null |
PTM: T-cell receptor ligation leads to increased tyrosine phosphorylation.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15117}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction {ECO:0000269|PubMed:21881001}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000269|PubMed:21881001}.
| null | null | null | null | null |
FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (PubMed:10497204, PubMed:9207119). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Modulates the expression of IL2 (PubMed:10497204, PubMed:9207119). Involved in platelet activation (PubMed:17003372). Prevents the degradation of SKAP1 and SKAP2 (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (PubMed:12681493). {ECO:0000250|UniProtKB:O15117, ECO:0000269|PubMed:10497204, ECO:0000269|PubMed:12681493, ECO:0000269|PubMed:17003372, ECO:0000269|PubMed:9207119}.
|
Mus musculus (Mouse)
|
O35604
|
NPC1_MOUSE
|
MGAHHPALGLLLLLLCPAQVFSQSCVWYGECGIATGDKRYNCKYSGPPKPLPKDGYDLVQELCPGLFFDNVSLCCDIQQLQTLKSNLQLPLQFLSRCPSCFYNLMTLFCELTCSPHQSQFLNVTATEDYFDPKTQENKTNVKELEYFVGQSFANAMYNACRDVEAPSSNEKALGLLCGRDARACNATNWIEYMFNKDNGQAPFTIIPVFSDLSILGMEPMRNATKGCNESVDEVTGPCSCQDCSIVCGPKPQPPPPPMPWRIWGLDAMYVIMWVTYVAFLFVFFGALLAVWCHRRRYFVSEYTPIDSNIAFSVNSSDKGEASCCDPLGAAFDDCLRRMFTKWGAFCVRNPTCIIFFSLAFITVCSSGLVFVQVTTNPVELWSAPHSQARLEKEYFDKHFGPFFRTEQLIIQAPNTSVHIYEPYPAGADVPFGPPLNKEILHQVLDLQIAIESITASYNNETVTLQDICVAPLSPYNKNCTIMSVLNYFQNSHAVLDSQVGDDFYIYADYHTHFLYCVRAPASLNDTSLLHGPCLGTFGGPVFPWLVLGGYDDQNYNNATALVITFPVNNYYNDTERLQRAWAWEKEFISFVKNYKNPNLTISFTAERSIEDELNRESNSDVFTVIISYVVMFLYISLALGHIQSCSRLLVDSKISLGIAGILIVLSSVACSLGIFSYMGMPLTLIVIEVIPFLVLAVGVDNIFILVQTYQRDERLQEETLDQQLGRILGEVAPTMFLSSFSETSAFFFGALSSMPAVHTFSLFAGMAVLIDFLLQITCFVSLLGLDIKRQEKNHLDILCCVRGADDGQGSHASESYLFRFFKNYFAPLLLKDWLRPIVVAVFVGVLSFSVAVVNKVDIGLDQSLSMPNDSYVIDYFKSLAQYLHSGPPVYFVLEEGYNYSSRKGQNMVCGGMGCDNDSLVQQIFNAAELDTYTRVGFAPSSWIDDYFDWVSPQSSCCRLYNVTHQFCNASVMDPTCVRCRPLTPEGKQRPQGKEFMKFLPMFLSDNPNPKCGKGGHAAYGSAVNIVGDDTYIGATYFMTYHTILKTSADYTDAMKKARLIASNITETMRSKGSDYRVFPYSVFYVFYEQYLTIIDDTIFNLSVSLGSIFLVTLVVLGCELWSAVIMCITIAMILVNMFGVMWLWGISLNAVSLVNLVMSCGISVEFCSHITRAFTMSTKGSRVSRAEEALAHMGSSVFSGITLTKFGGIVVLAFAKSQIFEIFYFRMYLAMVLLGATHGLIFLPVLLSYIGPSVNKAKRHTTYERYRGTERERLLNF
| null | null |
adult walking behavior [GO:0007628]; autophagy [GO:0006914]; bile acid metabolic process [GO:0008206]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to steroid hormone stimulus [GO:0071383]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol storage [GO:0010878]; cholesterol transport [GO:0030301]; cyclodextrin metabolic process [GO:2000900]; endocytosis [GO:0006897]; establishment of localization in cell [GO:0051649]; establishment of protein localization to membrane [GO:0090150]; gene expression [GO:0010467]; intestinal cholesterol absorption [GO:0030299]; intracellular cholesterol transport [GO:0032367]; intracellular lipid transport [GO:0032365]; liver development [GO:0001889]; lysosomal transport [GO:0007041]; macroautophagy [GO:0016236]; membrane raft organization [GO:0031579]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of macroautophagy [GO:0016242]; negative regulation of TORC1 signaling [GO:1904262]; neurogenesis [GO:0022008]; programmed cell death [GO:0012501]; protein glycosylation [GO:0006486]; response to cadmium ion [GO:0046686]; response to xenobiotic stimulus [GO:0009410]; sterol metabolic process [GO:0016125]; sterol transport [GO:0015918]; symbiont entry into host cell [GO:0046718]
|
endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; vesicle [GO:0031982]
|
cholesterol binding [GO:0015485]; lipid transporter activity [GO:0005319]
|
PF16414;PF02460;PF12349;
|
1.20.1640.10;
|
Patched family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:21896731, ECO:0000269|PubMed:22065762}.
|
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:O15118}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15118}. Lysosome membrane {ECO:0000269|PubMed:21896731, ECO:0000269|PubMed:22065762, ECO:0000269|PubMed:27551080}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15118}.
|
CATALYTIC ACTIVITY: Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, ChEBI:CHEBI:16113; Evidence={ECO:0000250|UniProtKB:O15118};
| null | null | null | null |
FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment (PubMed:21896731, PubMed:22048958, PubMed:27551080). Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket (By similarity). May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals (Probable). Inhibits cholesterol-mediated mTORC1 activation throught its interaction with SLC38A9 (By similarity). {ECO:0000250|UniProtKB:O15118, ECO:0000269|PubMed:21896731, ECO:0000269|PubMed:22048958, ECO:0000269|PubMed:27551080, ECO:0000305}.
|
Mus musculus (Mouse)
|
O35607
|
BMPR2_MOUSE
|
MTSSLHRPFRVPWLLWAVLLVSTTAASQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDETIIIALASVSVLAVLIVALCFGYRMLTGDRKQGLHSMNMMEAAAAEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERLTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGACVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEVFMRCTDLFPGESVPDYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGMTTISEMPYPDETHLHATNVAQSIGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEVTGQQDFTQAANGQACLIPDVPPAQIYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGNKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRSHNVNSHAATTQYANGAVPAGQAANIVAHRSQEMLQNQFIGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDILTQGVTSTAADPGPSKPRRAQRPNSLDLSATNILDGSSIQIGESTQDGKSGSGEKIKRRVKTPYSLKRWRPSTWVISTEPLDCEVNNNGSDRAVHSKSSTAVYLAEGGTATTTVSKDIGMNCL
|
2.7.11.30
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
anterior/posterior pattern specification [GO:0009952]; aortic valve development [GO:0003176]; artery development [GO:0060840]; atrial septum morphogenesis [GO:0060413]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; BMP signaling pathway [GO:0030509]; cellular response to growth factor stimulus [GO:0071363]; cellular response to starvation [GO:0009267]; chondrocyte development [GO:0002063]; endocardial cushion development [GO:0003197]; endochondral bone morphogenesis [GO:0060350]; endothelial cell apoptotic process [GO:0072577]; endothelial cell proliferation [GO:0001935]; limb development [GO:0060173]; lung alveolus development [GO:0048286]; lung vasculature development [GO:0060426]; lymphangiogenesis [GO:0001946]; lymphatic endothelial cell differentiation [GO:0060836]; maternal placenta development [GO:0001893]; mesoderm formation [GO:0001707]; mitral valve morphogenesis [GO:0003183]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation involved in heart valve morphogenesis [GO:0003252]; negative regulation of chondrocyte proliferation [GO:1902731]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of systemic arterial blood pressure [GO:0003085]; negative regulation of vasoconstriction [GO:0045906]; osteoblast differentiation [GO:0001649]; outflow tract morphogenesis [GO:0003151]; outflow tract septum morphogenesis [GO:0003148]; pharyngeal arch artery morphogenesis [GO:0061626]; phosphorylation [GO:0016310]; positive regulation of axon extension involved in axon guidance [GO:0048842]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cartilage development [GO:0061036]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of gene expression [GO:0010628]; positive regulation of ossification [GO:0045778]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteoglycan biosynthetic process [GO:0030166]; pulmonary valve development [GO:0003177]; regulation of lung blood pressure [GO:0014916]; retina vasculature development in camera-type eye [GO:0061298]; semi-lunar valve development [GO:1905314]; tricuspid valve morphogenesis [GO:0003186]; venous blood vessel development [GO:0060841]; ventricular septum morphogenesis [GO:0060412]
|
adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; basal plasma membrane [GO:0009925]; caveola [GO:0005901]; cell body [GO:0044297]; cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; receptor complex [GO:0043235]
|
activin receptor activity, type II [GO:0016362]; ATP binding [GO:0005524]; BMP binding [GO:0036122]; BMP receptor activity [GO:0098821]; cadherin binding [GO:0045296]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase binding [GO:1990782]; transforming growth factor beta receptor activity [GO:0005024]
|
PF01064;PF00069;
|
2.10.60.10;1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family, TGFB receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13873}; Single-pass type I membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.30;
| null | null | null | null |
FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Can also mediate signaling through the activation of the p38MAPK cascade (By similarity). Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6 (PubMed:23527555). {ECO:0000250|UniProtKB:Q13873, ECO:0000269|PubMed:23527555}.
|
Mus musculus (Mouse)
|
O35608
|
ANGP2_MOUSE
|
MWQIIFLTFGWDLVLASAYSNFRKSVDSTGRRQYQVQNGPCSYTFLLPETDSCRSSSSPYMSNAVQRDAPLDYDDSVQRLQVLENILENNTQWLMKLENYIQDNMKKEMVEIQQNVVQNQTAVMIEIGTSLLNQTAAQTRKLTDVEAQVLNQTTRLELQLLQHSISTNKLEKQILDQTSEINKLQNKNSFLEQKVLDMEGKHSEQLQSMKEQKDELQVLVSKQSSVIDELEKKLVTATVNNSLLQKQQHDLMETVNSLLTMMSSPNSKSSVAIRKEEQTTFRDCAEIFKSGLTTSGIYTLTFPNSTEEIKAYCDMDVGGGGWTVIQHREDGSVDFQRTWKEYKEGFGSPLGEYWLGNEFVSQLTGQHRYVLKIQLKDWEGNEAHSLYDHFYLAGEESNYRIHLTGLTGTAGKISSISQPGSDFSTKDSDNDKCICKCSQMLSGGWWFDACGPSNLNGQYYPQKQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF
| null | null |
angiogenesis [GO:0001525]; animal organ regeneration [GO:0031100]; blood vessel morphogenesis [GO:0048514]; blood vessel remodeling [GO:0001974]; cellular response to growth factor stimulus [GO:0071363]; endoderm development [GO:0007492]; gene expression [GO:0010467]; germ cell development [GO:0007281]; glomerulus vasculature development [GO:0072012]; hemopoiesis [GO:0030097]; maternal process involved in female pregnancy [GO:0060135]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of positive chemotaxis [GO:0050928]; positive regulation of angiogenesis [GO:0045766]; regulation of angiogenesis [GO:0045765]; response to activity [GO:0014823]; response to glucose [GO:0009749]; response to hypoxia [GO:0001666]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; Tie signaling pathway [GO:0048014]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cell projection [GO:0042995]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; receptor antagonist activity [GO:0048019]; receptor tyrosine kinase binding [GO:0030971]; vascular endothelial growth factor receptor binding [GO:0005172]
|
PF00147;
|
3.90.215.10;4.10.530.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O15123}.
| null | null | null | null | null |
FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (By similarity). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1 (By similarity). In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression (By similarity). In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (By similarity). Involved in the regulation of lymphangiogenesis (PubMed:28179430, PubMed:32908006). {ECO:0000250|UniProtKB:O15123, ECO:0000269|PubMed:28179430, ECO:0000269|PubMed:32908006}.
|
Mus musculus (Mouse)
|
O35609
|
SCAM3_MOUSE
|
MAQSRDTGNPFPDSGELDNPFQDPAVIQHRPSQQYATLDVYNPFENREPPPAYEPPAPAPAPLPPPSAPSVQSSRKLSPTEPRNYGSYSTQASAAAATAELLKKQEELNRKAEELDRRERELQHVALGGAGTRQNNWPPLPSFCPVKPCFFQDISMEIPQEFQKTVSTMYYLWMCSTLALLLNFFACLARFCVDTGSGSGFGLSMLWLLLFTPCSFVCWYRPMYKAFRSDSSFNFFVFFFIFFVQDVFFVLQAIGIPGWGFSGWVTALVVVGSKPAVAVLMLLVALLFTGIAVLGIVMLKRIHSLYRQTGASFQKAQQEFAAGVFSNPAVRTAAANAAAGAAENAFRAP
| null | null |
intracellular protein transport [GO:0006886]; protein transport [GO:0015031]; response to organic substance [GO:0010033]; response to retinoic acid [GO:0032526]
|
Golgi membrane [GO:0000139]; recycling endosome membrane [GO:0055038]; trans-Golgi network membrane [GO:0032588]
| null |
PF04144;
| null |
SCAMP family
|
PTM: Monoubiquitinated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.
|
Mus musculus (Mouse)
|
O35613
|
DAXX_MOUSE
|
MATDDSIIVLDDDDEDEAAAQPGPSNLPPNPASTGPGPGLSQQATGLSEPRVDGGSSNSGSRKCYKLDNEKLFEEFLELCKTETSDHPEVVPFLHKLQQRAQSVFLASAEFCNILSRVLARSRKRPAKIYVYINELCTVLKAHSIKKKLNLAPAASTTSEASGPNPPTEPPSDLTNTENTASEASRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSSYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGLDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPTLARRLRENRTLAMNRLDEVISKYAMMQDKTEEGERQKRRARLLGTAPQPSDPPQASSESGEGPSGMASQECPTTSKAETDDDDDDDDDDDEDNEESEEEEEEEEEEKEATEDEDEDLEQLQEDQGGDEEEEGGDNEGNESPTSPSDFFHRRNSEPAEGLRTPEGQQKRGLTETPASPPGASLDPPSTDAESSGEQLLEPLLGDESPVSQLAELEMEALPEERDISSPRKKSEDSLPTILENGAAVVTSTSVNGRVSSHTWRDASPPSKRFRKEKKQLGSGLLGNSYIKEPMAQQDSGQNTSVQPMPSPPLASVASVADSSTRVDSPSHELVTSSLCSPSPSLLLQTPQAQSLRQCIYKTSVATQCDPEEIIVLSDSD
| null | null |
androgen receptor signaling pathway [GO:0030521]; apoptotic signaling pathway [GO:0097190]; cell population proliferation [GO:0008283]; cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to diamide [GO:0072738]; cellular response to heat [GO:0034605]; cellular response to sodium arsenite [GO:1903936]; cellular response to type II interferon [GO:0071346]; cellular response to unfolded protein [GO:0034620]; mitotic cytokinesis [GO:0000281]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cellular response to hypoxia [GO:1900038]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of myotube differentiation [GO:0010832]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334]; PML body organization [GO:0030578]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to chromatin [GO:0071168]; regulation of apoptotic process [GO:0042981]; regulation of DNA-templated transcription [GO:0006355]; regulation of multicellular organism growth [GO:0040014]; regulation of protein ubiquitination [GO:0031396]
|
cell body [GO:0044297]; cell cortex [GO:0005938]; chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; heterochromatin [GO:0000792]; microtubule [GO:0005874]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605]; XY body [GO:0001741]
|
histone binding [GO:0042393]; JUN kinase binding [GO:0008432]; kinesin binding [GO:0019894]; nuclear androgen receptor binding [GO:0050681]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]
|
PF03344;PF20920;
|
1.20.58.2170;1.10.8.810;
|
DAXX family
|
PTM: Sumoylated with SUMO1 on multiple lysine residues. {ECO:0000250}.; PTM: Repressor activity is down-regulated upon Ser-669 phosphorylation. Upon neuronal activation dephosphorylated by calcineurin in a Ca2+ dependent manner at Ser-669; dephosphorylation positively affects histone H3.3 loading and transcriptional activation. {ECO:0000269|PubMed:12529400}.; PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10684855}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22500635}. Nucleus, PML body {ECO:0000269|PubMed:10684855}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UER7}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9UER7}. Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. {ECO:0000250|UniProtKB:Q9UER7}.
| null | null | null | null | null |
FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (By similarity). {ECO:0000250|UniProtKB:Q9UER7, ECO:0000269|PubMed:10684855, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:22500635}.
|
Mus musculus (Mouse)
|
O35615
|
FOG1_MOUSE
|
MSRRKQSNPRQIKRSLRDMEAGEEAKAMDSSPKEQEAPDPEAPAIEEPPSPPREDVSPPAVPAPPESPEDPEDMEGQELEMRPQDEEKEEKEEEAAMASPWSGPEELELALQDGQRCVRARLSLTEGLSWGPFYGSIQTRALSPEREEPGPAVTLMVDESCWLRMLPQVLTEEAANSEIYRKDDALWCRVTKVVPSGGLLYVRLVTEPHGAPRHPVQEPVEPGGLAPVHTDIQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQRAGSPVSATEEKPKETYPNERVCPFPQCRKSCPSASSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLSGVCHNCGFISTTRDILYSHLVTNHMVCQPGSKGEIYSPGAGHPAAKLPPDSLAGFQQHSLMHSPLVPADKAPTPSSGLDSKAEVTNGETRVPPQNGGSSESPAAPRTIKVEAAEEPEATRASGPGEPGPQAPSRTPSPHSPNPVRVKTELSSPTPGSSPGPGELTMAGTLFLPQYVFSPDAGTTTVPTAPQASEILAKMSELVHNRLQQGAGSSGAAGTPTGLFSGTKGATCFECEITFNNINNFYVHKRLYCSGRRAPEDPPTVRRPKAATGPARAPAGAAAEPDPSRSSPGPGPREEEASGTTTPEAEAAGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPPAPTTAPGPAAPALTAPPVRTRRRRKLYELPAAGAPPPAAGPAPVPVVPSPTAELPSSPRPGSASAGPAPALSPSPVPDGPIDLSKRPRRQSPDAPTALPALADYHECTACRVSFHSLEAYLAHKKYSCPAAPLRTTALCPYCPPNGRVRGDLVEHLRQAHGLQVAKPAASPGAEPRTPAERAPRDSPDGRAPRSPSPAPENTPSDPADQGARTPSKGPPAPAPAPGGGGGHRYCRLCNIRFSSLSTFIAHKKYYCSSHAAEHVK
| null | null |
atrial septum morphogenesis [GO:0060413]; atrioventricular valve morphogenesis [GO:0003181]; cardiac muscle tissue morphogenesis [GO:0055008]; definitive erythrocyte differentiation [GO:0060318]; embryonic hemopoiesis [GO:0035162]; erythrocyte differentiation [GO:0030218]; granulocyte differentiation [GO:0030851]; heart development [GO:0007507]; homeostasis of number of cells [GO:0048872]; megakaryocyte development [GO:0035855]; megakaryocyte differentiation [GO:0030219]; mitral valve formation [GO:0003192]; negative regulation of interleukin-4 production [GO:0032713]; negative regulation of mast cell differentiation [GO:0060377]; negative regulation of protein binding [GO:0032091]; negative regulation of transcription by RNA polymerase II [GO:0000122]; outflow tract morphogenesis [GO:0003151]; platelet formation [GO:0030220]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type II interferon production [GO:0032729]; primitive erythrocyte differentiation [GO:0060319]; regulation of chemokine production [GO:0032642]; regulation of definitive erythrocyte differentiation [GO:0010724]; tricuspid valve formation [GO:0003195]; ventricular septum morphogenesis [GO:0060412]
|
nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription corepressor activity [GO:0003714]
|
PF21182;PF00096;PF12874;
|
3.30.160.60;
|
FOG (Friend of GATA) family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9230307}.
| null | null | null | null | null |
FUNCTION: Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. The heterodimer formed with GATA proteins is essential to activate expression of genes such as NFE2, ITGA2B, alpha- and beta-globin, while it represses expression of KLF1. May be involved in regulation of some genes in gonads. May also be involved in cardiac development, in a non-redundant way with ZFPM2/FOG2. {ECO:0000269|PubMed:10078204, ECO:0000269|PubMed:10329627, ECO:0000269|PubMed:11940669, ECO:0000269|PubMed:12356738, ECO:0000269|PubMed:14614148, ECO:0000269|PubMed:9230307, ECO:0000269|PubMed:9553047}.
|
Mus musculus (Mouse)
|
O35618
|
MDM4_MOUSE
|
MTSHSTSAQCSASDSACRISSEQISQVRPKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRKNLVTSASINTDAAQTLALAQDHTMDFPSQDRLKHGATEYSNPRKRTEEEDTHTLPTSRHKCRDSRADEDLIEHLSQDETSRLDLDFEEWDVAGLPWWFLGNLRNNCIPKSNGSTDLQTNQDIGTAIVSDTTDDLWFLNETVSEQLGVGIKVEAANSEQTSEVGKTSNKKTVEVGKDDDLEDSRSLSDDTDVELTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSNITAIPEKKDNEGIDVPDCRRTISAPVVRPKDGYLKEEKPRFDPCNSVGFLDLAHSSESQEIISSAREQTDIFSEQKAETESMEDFQNVLKPCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVFIA
| null | null |
atrial septum development [GO:0003283]; atrioventricular valve morphogenesis [GO:0003181]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; endocardial cushion morphogenesis [GO:0003203]; heart valve development [GO:0003170]; negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902254]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell population proliferation [GO:0008284]; protein ubiquitination [GO:0016567]; regulation of cell cycle [GO:0051726]; regulation of heart rate [GO:0002027]; ventricular septum development [GO:0003281]
|
nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; ubiquitin-protein transferase activity [GO:0004842]
|
PF02201;PF13920;PF00641;
|
1.10.245.10;3.30.40.10;2.30.30.380;
|
MDM2/MDM4 family
|
PTM: Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-341 also induces ubiquitination and degradation but to a lower extent (By similarity). {ECO:0000250}.; PTM: Ubiquitinated and degraded by MDM2. Deubiquitination by USP2 on the other hand stabilizes the MDM4 protein (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. The short isoform is a more potent inhibitor of TP53 activity than the long isoform.
|
Mus musculus (Mouse)
|
O35621
|
PMM1_MOUSE
|
MAVAVEGARRKERILCLFDVDGTLTPARQKIDPEVSAFLQKLRSRVQIGVVGGSDYSKIAEQLGEGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLRLPKKRGTFIEFRNGMLNVSPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDEDSFDIIHFFGNETSPGGNDFEIYADPRTVGHSVVSPQDTVQRCRELFFPETAHEA
|
5.4.2.8
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cellular response to leukemia inhibitory factor [GO:1990830]; GDP-mannose biosynthetic process [GO:0009298]; mannose metabolic process [GO:0006013]; protein N-linked glycosylation [GO:0006487]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]
|
metal ion binding [GO:0046872]; phosphomannomutase activity [GO:0004615]
|
PF03332;
|
3.30.1240.20;3.40.50.1000;
|
Eukaryotic PMM family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16847318}.
|
CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for glucose-1,6-bisphosphate in the presence of 1 uM IMP {ECO:0000269|PubMed:18927083}; KM=40 uM for glucose-1,6-bisphosphate in the presence of 20 uM IMP {ECO:0000269|PubMed:18927083}; Vmax=2.1 umol/min/mg enzyme with glucose-1,6-bisphosphate as substrate {ECO:0000269|PubMed:18927083};
|
PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
| null | null |
FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain. {ECO:0000269|PubMed:18927083}.
|
Mus musculus (Mouse)
|
O35622
|
FGF15_MOUSE
|
MARKWNGRAVARALVLATLWLAVSGRPLAQQSQSVSDEDPLFLYGWGKITRLQYLYSAGPYVSNCFLRIRSDGSVDCEEDQNERNLLEFRAVALKTIAIKDVSSVRYLCMSADGKIYGLIRYSEEDCTFREEMDCLGYNQYRSMKHHLHIIFIQAKPREQLQDQKPSNFIPVFHRSFFETGDQLRSKMFSLPLESDSMDPFRMVEDVDHLVKSPSFQK
| null | null |
animal organ morphogenesis [GO:0009887]; bile acid and bile salt transport [GO:0015721]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; heart development [GO:0007507]; negative regulation of bile acid biosynthetic process [GO:0070858]; neural crest cell migration [GO:0001755]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cell migration [GO:0030334]; response to bacterium [GO:0009617]; response to ethanol [GO:0045471]; response to organic cyclic compound [GO:0014070]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression. {ECO:0000269|PubMed:16213224, ECO:0000269|PubMed:23747249}.
|
Mus musculus (Mouse)
|
O35625
|
AXIN1_MOUSE
|
MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDPLPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESIQVNGRVPLPHIPRTYRMPKEIRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGEMPSGPMASHKLPSVPAWHHFPPRYVDMGCSGLRDAHEENPESILDEHVQRVMRTPGCQSPGPGHRSPDSGHVAKTAVLGGTASGHGKHVPKLGLKLDTAGLHHHRHVHHHVHHNSARPKEQMEAEVARRVQSSFSWGPETHGHAKPRSYSENAGTTLSAGDLAFGGKTSAPSKRNTKKAESGKNANAEVPSTTEDAEKNQKIMQWIIEGEKEISRHRKAGHGSSGLRKQQAHESSRPLSIERPGAVHPWVSAQLRNSVQPSHLFIQDPTMPPNPAPNPLTQLEEARRRLEEEEKRANKLPSKQRYVQAVMQRGRTCVRPACAPVLSVVPAVSDLELSETETKSQRKAGGGSAPPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD
| null | null |
apoptotic process [GO:0006915]; axial mesoderm development [GO:0048318]; axial mesoderm formation [GO:0048320]; canonical Wnt signaling pathway [GO:0060070]; cell development [GO:0048468]; cytoplasmic microtubule organization [GO:0031122]; dorsal/ventral axis specification [GO:0009950]; dorsal/ventral pattern formation [GO:0009953]; epigenetic programming in the zygotic pronuclei [GO:0044725]; head development [GO:0060322]; in utero embryonic development [GO:0001701]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of protein metabolic process [GO:0051248]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; negative regulation of Wnt signaling pathway [GO:0030178]; nucleocytoplasmic transport [GO:0006913]; positive regulation of JNK cascade [GO:0046330]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; post-anal tail morphogenesis [GO:0036342]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein catabolic process [GO:0030163]; protein polyubiquitination [GO:0000209]; protein-containing complex assembly [GO:0065003]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of protein phosphorylation [GO:0001932]; sensory perception of sound [GO:0007605]; Wnt signaling pathway [GO:0016055]
|
beta-catenin destruction complex [GO:0030877]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; lateral plasma membrane [GO:0016328]; microtubule cytoskeleton [GO:0015630]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202]; Wnt signalosome [GO:1990909]
|
armadillo repeat domain binding [GO:0070016]; beta-catenin binding [GO:0008013]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; p53 binding [GO:0002039]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; R-SMAD binding [GO:0070412]; signaling receptor binding [GO:0005102]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625]
|
PF16646;PF08833;PF00778;PF00615;
|
1.10.196.10;2.40.240.130;1.10.167.10;
| null |
PTM: Phosphorylation and dephosphorylation of AXIN1 regulates assembly and function of the beta-catenin complex. Phosphorylated by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA. Phosphorylation by CK1 enhances binding of GSK3B to AXIN1 (By similarity). Also phosphorylated by CDK2 which regulates interaction with CTNBB1. {ECO:0000250, ECO:0000269|PubMed:10581160, ECO:0000269|PubMed:15063782}.; PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt signaling pathway (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important for nuclear accumulation during Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription (By similarity). Sumoylation at Lys-858 and Lys-861 prevents ubiquitination and degradation. Sumoylation is required for AXIN1-mediated JNK activation. Ubiquitination by SIAH1 and SIAH2 induces its proteasomal degradation as part of the activation of the Wnt signaling pathway (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O15169, ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:18632848}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16815997, ECO:0000269|PubMed:19141611}. Nucleus {ECO:0000250|UniProtKB:O15169}. Cell membrane {ECO:0000269|PubMed:16815997}. Membrane {ECO:0000269|PubMed:19141611}. Note=On UV irradiation, translocates to the nucleus and colocalizes with DAAX (By similarity). MACF1 is required for its translocation to cell membrane (PubMed:16815997). {ECO:0000250|UniProtKB:O15169, ECO:0000269|PubMed:16815997}.
| null | null | null | null | null |
FUNCTION: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity). Also a component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development. {ECO:0000250|UniProtKB:O15169, ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:15526030, ECO:0000269|PubMed:17681137}.
|
Mus musculus (Mouse)
|
O35626
|
RASD1_MOUSE
|
MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLKQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVEQREIEQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGDHGDAFGILAPFARRPSVHSDLMYIREKTSVGSQAKDKERCVIS
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]; nitric oxide mediated signal transduction [GO:0007263]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; sarcoplasmic reticulum [GO:0016529]
|
G-protein beta-subunit binding [GO:0031681]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, RasD family
|
PTM: S-nitrosylation stimulates guanine-nucleotide exchange activity. {ECO:0000269|PubMed:11086993}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35627
|
NR1I3_MOUSE
|
MTAMLTLETMASEEEYGPRNCVVCGDRATGYHFHALTCEGCKGFFRRTVSKTIGPICPFAGRCEVSKAQRRHCPACRLQKCLNVGMRKDMILSAEALALRRARQAQRRAEKASLQLNQQQKELVQILLGAHTRHVGPMFDQFVQFKPPAYLFMHHRPFQPRGPVLPLLTHFADINTFMVQQIIKFTKDLPLFRSLTMEDQISLLKGAAVEILHISLNTTFCLQTENFFCGPLCYKMEDAVHAGFQYEFLESILHFHKNLKGLHLQEPEYVLMAATALFSPDRPGVTQREEIDQLQEEMALILNNHIMEQQSRLQSRFLYAKLMGLLADLRSINNAYSYELQRLEELSAMTPLLGEICS
| null | null |
cell differentiation [GO:0030154]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast differentiation [GO:0001649]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
|
PTM: Phosphorylated at Thr-48 by PKC, dephosphorylation of Thr-48 is required for nuclear translocation and activation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Recruited to the cytoplasm by DNAJC7.
| null | null | null | null | null |
FUNCTION: Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element (By similarity). {ECO:0000250, ECO:0000269|PubMed:10462436}.
|
Mus musculus (Mouse)
|
O35632
|
HYAL2_MOUSE
|
MRAGLGPIITLALVLEVAWAGELKPTAPPIFTGRPFVVAWNVPTQECAPRHKVPLDLRAFDVKATPNEGFFNQNITTFYYDRLGLYPRFDAAGTSVHGGVPQNGSLCAHLPMLKESVERYIQTQEPGGLAVIDWEEWRPVWVRNWQEKDVYRQSSRQLVASRHPDWPSDRVMKQAQYEFEFAARQFMLNTLRYVKAVRPQHLWGFYLFPDCYNHDYVQNWESYTGRCPDVEVARNDQLAWLWAESTALFPSVYLDETLASSVHSRNFVSFRVREALRVAHTHHANHALPVYVFTRPTYTRGLTGLSQVDLISTIGESAALGSAGVIFWGDSEDASSMETCQYLKNYLTQLLVPYIVNVSWATQYCSWTQCHGHGRCVRRNPSANTFLHLNASSFRLVPGHTPSEPQLRPEGQLSEADLNYLQKHFRCQCYLGWGGEQCQRNYKGAAGNASRAWAGSHLTSLLGLVAVALTWTL
|
3.2.1.35
| null |
carbohydrate metabolic process [GO:0005975]; cartilage development [GO:0051216]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to interleukin-1 [GO:0071347]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to UV-B [GO:0071493]; defense response to virus [GO:0051607]; fusion of virus membrane with host plasma membrane [GO:0019064]; glycosaminoglycan catabolic process [GO:0006027]; hematopoietic progenitor cell differentiation [GO:0002244]; hyaluronan catabolic process [GO:0030214]; monocyte activation [GO:0042117]; multicellular organismal-level iron ion homeostasis [GO:0060586]; negative regulation of cell growth [GO:0030308]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of protein tyrosine kinase activity [GO:0061099]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of urine volume [GO:0035810]; renal water absorption [GO:0070295]; response to antibiotic [GO:0046677]; response to reactive oxygen species [GO:0000302]; response to virus [GO:0009615]; skeletal system morphogenesis [GO:0048705]; symbiont entry into host cell [GO:0046718]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; membrane raft [GO:0045121]; microvillus [GO:0005902]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; RNA polymerase II transcription regulator complex [GO:0090575]; side of membrane [GO:0098552]
|
enzyme binding [GO:0019899]; hyaluronic acid binding [GO:0005540]; hyaluronoglucuronidase activity [GO:0033906]; hyalurononglucosaminidase activity [GO:0004415]; receptor signaling protein tyrosine kinase inhibitor activity [GO:0030294]; receptor tyrosine kinase binding [GO:0030971]; transforming growth factor beta binding [GO:0050431]; virus receptor activity [GO:0001618]
|
PF01630;
|
3.20.20.70;
|
Glycosyl hydrolase 56 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
| null | null | null | null |
FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35633
|
VIAAT_MOUSE
|
MATLLRSKLTNVATSVSNKSQAKVSGMFARMGFQAATDEEAVGFAHCDDLDFEHRQGLQMDILKSEGEPCGDEGAEAPVEGDIHYQRGGAPLPPSGSKDQAVGAGGEFGGHDKPKITAWEAGWNVTNAIQGMFVLGLPYAILHGGYLGLFLIIFAAVVCCYTGKILIACLYEENEDGEVVRVRDSYVAIANACCAPRFPTLGGRVVNVAQIIELVMTCILYVVVSGNLMYNSFPGLPVSQKSWSIIATAVLLPCAFLKNLKAVSKFSLLCTLAHFVINILVIAYCLSRARDWAWEKVKFYIDVKKFPISIGIIVFSYTSQIFLPSLEGNMQQPSEFHCMMNWTHIAACVLKGLFALVAYLTWADETKEVITDNLPGSIRAVVNLFLVAKALLSYPLPFFAAVEVLEKSLFQEGSRAFFPACYGGDGRLKSWGLTLRCALVVFTLLMAIYVPHFALLMGLTGSLTGAGLCFLLPSLFHLRLLWRKLLWHQVFFDVAIFVIGGICSVSGFVHSLEGLIEAYRTNAED
| null | null |
beta-alanine transport [GO:0001762]; gamma-aminobutyric acid import [GO:0051939]; gamma-aminobutyric acid transport [GO:0015812]; glycine transport [GO:0015816]; hippocampus development [GO:0021766]; neurotransmitter loading into synaptic vesicle [GO:0098700]
|
cell surface [GO:0009986]; cell tip [GO:0051286]; cone cell pedicle [GO:0044316]; dendrite [GO:0030425]; dendrite terminus [GO:0044292]; GABA-ergic synapse [GO:0098982]; inhibitory synapse [GO:0060077]; neuron projection [GO:0043005]; neuron projection terminus [GO:0044306]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; vacuolar membrane [GO:0005774]
|
gamma-aminobutyric acid transmembrane transporter activity [GO:0015185]; gamma-aminobutyric acid:proton antiporter activity [GO:0140800]; glycine transmembrane transporter activity [GO:0015187]; glycine:proton antiporter activity [GO:0140799]
|
PF01490;
| null |
Amino acid/polyamine transporter 2 family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O35458}; Multi-pass membrane protein {ECO:0000255}. Presynapse {ECO:0000269|PubMed:19052203}. Note=Presents in glycine-, GABA- or GABA- and glycine-containing boutons. {ECO:0000250|UniProtKB:O35458}.
|
CATALYTIC ACTIVITY: Reaction=4-aminobutanoate(out) + n H(+)(in) = 4-aminobutanoate(in) + n H(+)(out); Xref=Rhea:RHEA:70979, ChEBI:CHEBI:15378, ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:16701208, ECO:0000269|PubMed:26912364, ECO:0000269|PubMed:27601664, ECO:0000305|PubMed:9395291}; CATALYTIC ACTIVITY: Reaction=glycine(out) + n H(+)(in) = glycine(in) + n H(+)(out); Xref=Rhea:RHEA:70983, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305; Evidence={ECO:0000269|PubMed:16701208, ECO:0000269|PubMed:26912364, ECO:0000305|PubMed:9395291}; CATALYTIC ACTIVITY: Reaction=beta-alanine(out) + n H(+)(in) = beta-alanine(in) + n H(+)(out); Xref=Rhea:RHEA:70987, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966; Evidence={ECO:0000250|UniProtKB:O35458};
| null | null | null | null |
FUNCTION: Antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals (PubMed:16701208, PubMed:26912364, PubMed:27601664, PubMed:9395291). The transport is equally dependent on the chemical and electrical components of the proton gradient (PubMed:27601664, PubMed:9395291). May also transport beta-alanine (By similarity). Acidification of GABAergic synaptic vesicles is a prerequisite for 4-aminobutanoate uptake (PubMed:27601664). {ECO:0000250|UniProtKB:O35458, ECO:0000269|PubMed:16701208, ECO:0000269|PubMed:26912364, ECO:0000269|PubMed:27601664, ECO:0000269|PubMed:9395291}.
|
Mus musculus (Mouse)
|
O35638
|
STAG2_MOUSE
|
MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKSGNGGGKPPSGSNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSRRDPEEDGLMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDDRTRITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCAHYVILWQLAKITESTSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDSNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGMSSRGSTVRSKKSKPSTGKRKVVEGMQLALPEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMSVYPMQAEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPPSKNRRERTELKPDFFDPASIMDESVLGVSMF
| null | null |
cell division [GO:0051301]; chromosome segregation [GO:0007059]; meiotic cell cycle [GO:0051321]; sister chromatid cohesion [GO:0007062]; stem cell population maintenance [GO:0019827]
|
chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; cohesin complex [GO:0008278]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]
|
PF21581;PF08514;
| null |
SCC3 family
|
PTM: Phosphorylated by PLK1. The large dissociation of cohesin from chromosome arms during prophase is partly due to its phosphorylation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35639
|
ANXA3_MOUSE
|
MASIWVGPRGTIKDYPGFSPSVDAEAIRKAIRGLGTDEKTLINILTERSNAQRQLIVKQYQAAYEQELKDDLKGDLSGHFEHVMVALVTAPALFDAKQLKKSMKGTGTDEDALIEILTTRSSRQMKEISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKKDAQILYNAGENKWGTDEDKFTEVLCLRSFPQLKLTFDEYRNISQKDIEDSIKGELSGHFEDLLLAIVHCARNTPAFLAERLHQALKGAGTDEFTLNRIMVSRSEIDLLDIRHEFKKHYGYSLYSAIQSDTSGDYRTVLLKICGEDD
| null | null |
animal organ regeneration [GO:0031100]; defense response to bacterium [GO:0042742]; hippocampus development [GO:0021766]; neutrophil degranulation [GO:0043312]; phagocytosis [GO:0006909]; positive regulation of angiogenesis [GO:0045766]; positive regulation of DNA metabolic process [GO:0051054]; positive regulation of endothelial cell migration [GO:0010595]; response to glucocorticoid [GO:0051384]; response to growth factor [GO:0070848]
|
axon [GO:0030424]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; specific granule [GO:0042581]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]
|
PF00191;
|
1.10.220.10;
|
Annexin family
| null | null | null | null | null | null | null |
FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant properties.
|
Mus musculus (Mouse)
|
O35643
|
AP1B1_MOUSE
|
MTDSKYFTTTKKGEIFELKAELNSDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNTFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQLVEDQGFLDTLKDLISDSNPMVVANAVAALSEIAESHPSSNLLDLNPQSINKLLTALNECTEWGQIFILDCLANYMPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFMEMLSKDLDYYATLLKKLAPPLVTLLSAEPELQYVALRNINLIVQKRPEILKHEMKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESVIATLCENLDSLDEPEARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLQLLTAIVKLFLKKPTETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVAAKEVVLAEKPLISEETDLIEPTLLDELICYIGTLASVYHKPPNAFVEGGRGVVHKSLPPRTASSESTESPETAPAGAPAGDQPDVIPAQGDLLGDLLNLDLGPPVSGPPLAASSVQMGAVDLLGGGLDSLIGDSNFGAPSASVAAAPAPARLGAPISSGLSDLFDLTSGVGTLSGSYVAPKAVWLPAMKAKGLEISGTFTRQAGSISMDLQLTNKALQVMTDFAIQFNRNSFGLAPAAPLQVHVPLSPNQTVEISLPLNTVGSVLKMEPLNNLQVAVKNNIDVFYFSTLYPLHVLFVEDGKMDRQMFLATWKDIANENEAQFQIRDCPLNTEAASNKLQSSNIFTVAKRNVEGQDMLYQSLKLTNGIWVLAELRIQPGNPSFTLSLKCRAPEVSQHVYQAYETILKN
| null | null |
basolateral protein secretion [GO:0110010]; clathrin coat assembly [GO:0048268]; determination of left/right symmetry [GO:0007368]; heart development [GO:0007507]; intracellular protein transport [GO:0006886]; kidney development [GO:0001822]; melanosome assembly [GO:1903232]; platelet dense granule organization [GO:0060155]; vesicle-mediated transport [GO:0016192]
|
AP-1 adaptor complex [GO:0030121]; cytosol [GO:0005829]; early endosome [GO:0005769]; lysosomal membrane [GO:0005765]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]
|
clathrin binding [GO:0030276]; protein kinase binding [GO:0019901]; protein serine/threonine kinase binding [GO:0120283]
|
PF01602;PF02883;PF09066;
|
2.60.40.1150;1.25.10.10;3.30.310.10;
|
Adaptor complexes large subunit family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
|
Mus musculus (Mouse)
|
O35646
|
CAN6_MOUSE
|
MGPPLKLFKNQKYQELKQECMKDGRLFCDPTFLPENDSLFFNRLLPGKVVWKRPQDISDDPHLIVGNISNHQLIQGRLGNKAMISAFSCLAVQESHWTKAIPNHKDQEWDPRKPEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLGCYEALDGLTITDIIMDFTGTLAEIIDMQKGRYTDLVEEKYKLFGELYKTFTKGGLICCSIESPSQEEQEVETDWGLLKGYTYTMTDIRKLRLGERLVEVFSTEKLYMVRLRNPLGRQEWSGPWSEISEEWQQLTVTDRKNLGLVMSDDGEFWMSLEDFCHNFHKLNVCRNVNNPVFGRKELESVVGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIMSLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRRFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGSYVLVPTMFQHGRTSEFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEGLEKKYANETVNPYLIIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIIQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTEL
| null | null |
microtubule bundle formation [GO:0001578]; regulation of cytoskeleton organization [GO:0051493]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]; perinuclear region of cytoplasm [GO:0048471]; spindle microtubule [GO:0005876]
|
microtubule binding [GO:0008017]
|
PF00168;PF01067;PF00648;
|
2.60.120.380;2.60.40.150;3.90.70.10;
|
Peptidase C2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:20814968}.
| null | null | null | null | null |
FUNCTION: Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues. {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:21406564}.
|
Mus musculus (Mouse)
|
O35648
|
CETN3_MOUSE
|
MSLALRGELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDQAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; mRNA transport [GO:0051028]; protein transport [GO:0015031]
|
centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nuclear pore nuclear basket [GO:0044615]; nucleolus [GO:0005730]; photoreceptor connecting cilium [GO:0032391]; transcription export complex 2 [GO:0070390]
|
calcium ion binding [GO:0005509]; G-protein beta/gamma-subunit complex binding [GO:0031683]; microtubule binding [GO:0008017]
|
PF13499;
|
1.10.238.10;
|
Centrin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O15182}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O15182}. Nucleus envelope {ECO:0000250|UniProtKB:O15182}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15182}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O15182}. Note=Centrosome of interphase and mitotic cells. Localizes to centriole distal lumen (By similarity). Localization at the nuclear pore complex requires NUP153 and TPR (By similarity). {ECO:0000250|UniProtKB:O15182}.
| null | null | null | null | null |
FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function.; FUNCTION: As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000250|UniProtKB:O15182}.
|
Mus musculus (Mouse)
|
O35652
|
LHX8_MOUSE
|
MYWKSDQMFVCKLEGKEVPELAVPREKCPGLMSEECGRPAALAAGRTRKGAGEEGLVNPEGAGDEDSCSSSAPLSPSSSPQSMASGSVCPPGKCVCSSCGLEIVDKYLLKVNDLCWHVRCLSCSVCRTSLGRHTSCYIKDKDIFCKLDYFRRYGTRCSRCGRHIHSTDWVRRAKGNVYHLACFACFSCKRQLSTGEEFALVEEKVLCRVHFDCMLDNLKREVENGNGISVEGALLTEQDVNHPKPAKRARTSFTADQLQVMQAQFAQDNNPDAQTLQKLAERTGLSRRVIQVWFQNCRARHKKHVSPNHSSSAPVTAVPSSRLSPPMLEEMAYSAYVPQDGTMLTALHSYMDAHQQLLDSSPCYPIQ
| null | null |
female gonad development [GO:0008585]; forebrain neuron development [GO:0021884]; forebrain neuron differentiation [GO:0021879]; learning or memory [GO:0007611]; neuron differentiation [GO:0030182]; odontogenesis of dentin-containing tooth [GO:0042475]; regulation of transcription by RNA polymerase II [GO:0006357]
|
female germ cell nucleus [GO:0001674]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00046;PF00412;
|
2.10.110.10;1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcription factor involved in differentiation of certain neurons and mesenchymal cells.
|
Mus musculus (Mouse)
|
O35655
|
PPE1_MOUSE
|
MGCGTSSKKGNKSKKVIKAALVIQNWYRRYRARLRVRQHYALAIFQSIEYSDEQGQMQLSSFFSFMLENYTKTNNEDSALVTRIFDNTRRESQIKDRDDFLGLIEVPDSYDGPRLQFPLTFTDIHILLQAFKQQQILHAHYVLEVLFEARKVLKQMPNFSHVKTFPAKEITICGDLHGKLDDLMLIFYKNGLPSENNPYVFNGDFVDRGNNSMEILMILLVCFLVYPSDLHLNRGNHEDFMMNLRYGFTKEILQKYKLHGRKILQVLEEVYTWLPIGTIIDNEILVIHGGISESTDLNTLHQLQRNKMKSVLMPPVLGNQETGEKRNKSASNYVEPRKVEPDKTPSEDLTKQEWEQIVDILWSDPRGKKGCYPNTSRGGGCYFGPDVTSKVLSKNQLKMLIRSHECKPDGYEVSHDGKVITVFSASNYYEEGSNRGAYIRLSYGTMPQFFQYQVTSTSCLNPLHQRMNAMESSAFKILKEKMISRKTDLINAFELRDHSRSGRISLAEWAFSMENILGLNLPWRSLSSHLVTIDSSGSVDYMSSFDDIRIEKPTKDMKSNLTETMYRYRSDLKIIFNIIDSDQSGLISMDEFRTMWKLFNAHYKAHIDDSQIDELASIVDFNKDGNIDFNEFLKAFYVVHKYDKPGTSLA
|
3.1.3.16
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
detection of stimulus involved in sensory perception [GO:0050906]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; iron ion binding [GO:0005506]; manganese ion binding [GO:0030145]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF13499;PF00149;PF08321;
|
3.60.21.10;1.10.238.10;
|
PPP phosphatase family
| null | null |
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; 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;
| null | null | null | null |
FUNCTION: May have a role in the recovery or adaptation response of photoreceptors. May have a role in diverse sensory neurons and in development.
|
Mus musculus (Mouse)
|
O35657
|
NEUR1_MOUSE
|
MVGADPTRPRGPLSYWAGRRGQGLAAIFLLLVSAAESEARAEDDFSLVQPLVTMEQLLWVSGKQIGSVDTFRIPLITATPRGTLLAFAEARKKSASDEGAKFIAMRRSTDQGSTWSSTAFIVDDGEASDGLNLGAVVNDVDTGIVFLIYTLCAHKVNCQVASTMLVWSKDDGISWSPPRNLSVDIGTEMFAPGPGSGIQKQREPGKGRLIVCGHGTLERDGVFCLLSDDHGASWHYGTGVSGIPFGQPKHDHDFNPDECQPYELPDGSVIINARNQNNYHCRCRIVLRSYDACDTLRPRDVTFDPELVDPVVAAGALATSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWQKERVQVWPGPSGYSSLTALENSTDGKKQPPQLFVLYEKGLNRYTESISMVKISVYGTL
|
3.2.1.18
| null |
ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313]; positive regulation of neuron projection development [GO:0010976]; regulation of myoblast proliferation [GO:2000291]
|
cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; exo-alpha-sialidase activity [GO:0004308]
|
PF13088;
|
2.120.10.10;
|
Glycosyl hydrolase 33 family
|
PTM: N-glycosylated. {ECO:0000305}.; PTM: Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane.
|
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:9384611}; Peripheral membrane protein {ECO:0000269|PubMed:9384611}; Lumenal side {ECO:0000269|PubMed:9384611}. Lysosome lumen {ECO:0000269|PubMed:9384611}. Cell membrane {ECO:0000269|PubMed:9384611}. Cytoplasmic vesicle {ECO:0000269|PubMed:9384611}. Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000269|PubMed:9363440, ECO:0000269|PubMed:9384611};
| null | null | null | null |
FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage. {ECO:0000269|PubMed:9363440, ECO:0000269|PubMed:9384611}.
|
Mus musculus (Mouse)
|
O35658
|
C1QBP_MOUSE
|
MLPLLRCVPRSLGAASGLRTAIPAQPLRHLLQPAPRPCLRPFGLLSVRAGSARRSGLLQPPVPCACGCGALHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPERTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQATGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKNQ
| null | null |
apoptotic process [GO:0006915]; complement activation, classical pathway [GO:0006958]; cytosolic ribosome assembly [GO:0042256]; innate immune response [GO:0045087]; mRNA processing [GO:0006397]; negative regulation of defense response to virus [GO:0050687]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of interleukin-12 production [GO:0032695]; negative regulation of MDA-5 signaling pathway [GO:0039534]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of RIG-I signaling pathway [GO:0039536]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of type II interferon production [GO:0032689]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell adhesion [GO:0045785]; positive regulation of dendritic cell chemotaxis [GO:2000510]; positive regulation of mitochondrial translation [GO:0070131]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of trophoblast cell migration [GO:1901165]; regulation of complement activation [GO:0030449]; RNA splicing [GO:0008380]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; presynaptic active zone [GO:0048786]
|
adrenergic receptor binding [GO:0031690]; complement component C1q complex binding [GO:0001849]; enzyme inhibitor activity [GO:0004857]; hyaluronic acid binding [GO:0005540]; kininogen binding [GO:0030984]; mitochondrial ribosome binding [GO:0097177]; mRNA binding [GO:0003729]; protein kinase C binding [GO:0005080]; transcription corepressor activity [GO:0003714]
|
PF02330;
|
3.10.280.10;
|
MAM33 family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172}. Nucleus {ECO:0000250|UniProtKB:Q07021}. Cell membrane {ECO:0000250|UniProtKB:Q07021}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q07021}; Extracellular side {ECO:0000250|UniProtKB:Q07021}. Secreted {ECO:0000250|UniProtKB:Q07021}. Cytoplasm {ECO:0000250|UniProtKB:Q07021}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q07021}. Note=Seems to be predominantly localized to mitochondria (PubMed:17486078, PubMed:18166172). Secreted by activated lymphocytes (By similarity). {ECO:0000250|UniProtKB:Q07021, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172}.
| null | null | null | null | null |
FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93 (PubMed:9414106). In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria (PubMed:22904065, PubMed:28942965). In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity (PubMed:22904065, PubMed:28942965). May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4 (PubMed:18460468). Involved in regulation of CDKN2A- and HRK-mediated apoptosis. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense (By similarity). Acts as a regulator of DNA repair via homologous recombination by inhibiting the activity of MRE11: interacts with unphosphorylated MRE11 and RAD50 in absence of DNA damage, preventing formation and activity of the MRN complex (By similarity). Following DNA damage, dissociates from phosphorylated MRE11, allowing formation of the MRN complex (By similarity). {ECO:0000250|UniProtKB:Q07021, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172, ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:22904065, ECO:0000269|PubMed:28942965}.
|
Mus musculus (Mouse)
|
O35659
|
GLP1R_MOUSE
|
MASTPSLLRLALLLLGAVGRAGPRPQGTTVSLSETVQKWREYRRQCQRFLTEAPLLATGLFCNRTFDDYACWPDGPPGSFVNVSCPWYLPWASSVLQGHVYRFCTAEGLWLHKDNSSLPWRDLSECEESKRGERNFPEEQLLSLYIIYTVGYALSFSALVIASAILVGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLGCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFKLYLSIGWGVPLLFVIPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFIRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFIKLFTELSFTSFQGLMVAILYCFVNNEVQMEFRKCWERWRLEHLNIQRDCSMKPLKCPTSSVSSGATVGSSVYAATCQSSYS
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; associative learning [GO:0008306]; cAMP-mediated signaling [GO:0019933]; cell surface receptor signaling pathway [GO:0007166]; feeding behavior [GO:0007631]; hormone secretion [GO:0046879]; insulin secretion [GO:0030073]; learning or memory [GO:0007611]; memory [GO:0007613]; negative regulation of apoptotic process [GO:0043066]; negative regulation of blood pressure [GO:0045776]; negative regulation of neuron apoptotic process [GO:0043524]; neuropeptide signaling pathway [GO:0007218]; positive regulation of blood pressure [GO:0045777]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of insulin secretion [GO:0032024]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-translational protein targeting to membrane, translocation [GO:0031204]; regulation of calcium ion transport [GO:0051924]; regulation of heart contraction [GO:0008016]; release of sequestered calcium ion into cytosol [GO:0051209]; response to glucose [GO:0009749]; response to psychosocial stress [GO:1990911]
|
plasma membrane [GO:0005886]
|
G protein-coupled peptide receptor activity [GO:0008528]; glucagon receptor activity [GO:0004967]; glucagon-like peptide 1 receptor activity [GO:0044508]; peptide hormone binding [GO:0017046]; peptide receptor activity [GO:0001653]; signaling receptor activity [GO:0038023]
|
PF00002;PF02793;
|
4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family
|
PTM: N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER. {ECO:0000250|UniProtKB:P43220}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9568699}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P43220}.
| null | null | null | null | null |
FUNCTION: G-protein coupled receptor for glucagon-like peptide 1 (GLP-1) (PubMed:9568699). Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels (By similarity). Plays a role in regulating insulin secretion in response to GLP-1 (PubMed:9568699). {ECO:0000250|UniProtKB:P43220, ECO:0000269|PubMed:9568699}.
|
Mus musculus (Mouse)
|
O35664
|
INAR2_MOUSE
|
MRSRCTVSAVGLLSLCLVVSASLETITPSAFDGYPDEPCTINITIRNSRLILSWELENKSGPPANYTLWYTVMSKDENLTKVKNCSDTTKSSCDVTDKWLEGMESYVVAIVIVHRGDLTVCRCSDYIVPANAPLEPPEFEIVGFTDHINVTMEFPPVTSKIIQEKMKTTPFVIKEQIGDSVRKKHEPKVNNVTGNFTFVLRDLLPKTNYCVSLYFDDDPAIKSPLKCIVLQPGQESGLSESAIVGITTSCLVVMVFVSTIVMLKRIGYICLKDNLPNVLNFRHFLTWIIPERSPSEAIDRLEIIPTNKKKRLWNYDYEDGSDSDEEVPTASVTGYTMHGLTGKPLQQTSDTSASPEDPLHEEDSGAEESDEAGAGAGAEPELPTEAGAGPSEDPTGPYERRKSVLEDSFPREDNSSMDEPGDNIIFNVNLNSVFLRVLHDEDASETLSLEEDTILLDEGPQRTESDLRIAGGDRTQPPLPSLPSQDLWTEDGSSEKSDTSDSDADVGDGYIMR
| null | null |
defense response to virus [GO:0051607]; immature T cell proliferation in thymus [GO:0033080]; regulation of transcription by RNA polymerase II [GO:0006357]; response to interferon-alpha [GO:0035455]; response to interferon-beta [GO:0035456]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
interleukin-22 receptor activity [GO:0042018]; type I interferon receptor activity [GO:0004905]
|
PF09294;PF01108;
|
2.60.40.10;
|
Type II cytokine receptor family
|
PTM: Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-335 or Tyr-510 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types (By similarity). {ECO:0000250|UniProtKB:P48551}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}; Single-pass type I membrane protein {ECO:0000305|PubMed:9322767}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305|PubMed:9322767}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}.
| null | null | null | null | null |
FUNCTION: Together with IFNAR1, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response. Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another. The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (STAT1, STAT2 and STAT). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes. {ECO:0000250|UniProtKB:P48551}.; FUNCTION: [Isoform 2]: May be potent inhibitors of type I IFN receptor activity. {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}.; FUNCTION: [Isoform 3]: May be potent inhibitors of type I IFN receptor activity. {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}.
|
Mus musculus (Mouse)
|
O35668
|
HAP1_MOUSE
|
MRPKEQVQSGAGDGTGSGDPAAGTPTTQPAVGPAPEPSAEPKPAPAQGTGSGQKSGSRTKTGSFCRSMIIGDSDAPWTRYVFQGPYGPRATGLGTGKAEGIWKTPAAYIGRRPGVSGPERAAFIRELQEALCPNPPPTKKITEDDVKVMLYLLEEKERDLNTAARIGQSLVKQNSVLMEENNKLETMLGSAREEILHLRKQVNLRDDLLQLYSDSDDDDDEEDEEDEEEGEEEEREGQRDQDQQHDHPYGAPKPHPKAETAHRCPQLETLQQKLRLLEEENDHLREEASHLDNLEDEEQMLILECVEQFSEASQQMAELSEVLVLRLEGYERQQKEITQLQAEITKLQQRCQSYGAQTEKLQQMLASEKGIHSESLRAGSYMQDYGSRPRDRQEDGKSHRQRSSMPAGSVTHYGYSVPLDALPSFPETLAEELRTSLRKFITDPAYFMERRDTHCREGRKKEQRAMPPPPAQDLKPPEDFEAPEELVPEEELGAIEEVGTAEDGQAEENEQASEETEAWEEVEPEVDETTRMNVVVSALEASGLGPSHLDMKYVLQQLSNWQDAHSKRQQKQKVVPKDSPTPQQQTNMGGGILEQQPRVPTQDSQRLEEDRATHSPSAREEEGPSGAT
| null | null |
anterograde axonal transport [GO:0008089]; anterograde axonal transport of mitochondrion [GO:0098957]; autophagy [GO:0006914]; cerebellum development [GO:0021549]; exocytosis [GO:0006887]; hypothalamus cell differentiation [GO:0021979]; mitochondrion distribution [GO:0048311]; negative regulation of amyloid-beta formation [GO:1902430]; neurogenesis [GO:0022008]; neuron projection development [GO:0031175]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of inclusion body assembly [GO:0090261]; positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity [GO:0031587]; positive regulation of neurogenesis [GO:0050769]; positive regulation of neuron projection development [GO:0010976]; positive regulation of neurotrophin production [GO:0032901]; positive regulation of non-motile cilium assembly [GO:1902857]; positive regulation of synaptic transmission, GABAergic [GO:0032230]; protein targeting [GO:0006605]; protein transport [GO:0015031]; regulation of exocytosis [GO:0017157]; regulation of organelle transport along microtubule [GO:1902513]; regulation of postsynaptic neurotransmitter receptor internalization [GO:0099149]; retrograde axonal transport [GO:0008090]; vesicle transport along microtubule [GO:0047496]
|
autophagosome [GO:0005776]; axon cytoplasm [GO:1904115]; axon terminus [GO:0043679]; centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; GABA-ergic synapse [GO:0098982]; growth cone [GO:0030426]; inclusion body [GO:0016234]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic cytosol [GO:0099524]; presynaptic cytosol [GO:0099523]; synaptic vesicle [GO:0008021]
|
brain-derived neurotrophic factor binding [GO:0048403]; identical protein binding [GO:0042802]; myosin binding [GO:0017022]; protein domain specific binding [GO:0019904]; signaling receptor binding [GO:0005102]; transmembrane transporter binding [GO:0044325]
|
PF04849;
| null | null |
PTM: Isoform A is phosphorylated on Thr-598. {ECO:0000250|UniProtKB:P54256}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54256}. Presynapse {ECO:0000250|UniProtKB:P54256}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P54256}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P54256}. Cell projection, dendrite {ECO:0000250|UniProtKB:P54256}. Cell projection, axon {ECO:0000250|UniProtKB:P54256}. Lysosome {ECO:0000250|UniProtKB:P54256}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P54256}. Mitochondrion {ECO:0000250|UniProtKB:P54256}. Nucleus {ECO:0000250|UniProtKB:P54256}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24453320}. Early endosome {ECO:0000250|UniProtKB:P54256}. Cell projection, growth cone {ECO:0000250|UniProtKB:P54256}. Note=Localizes to large nonmembrane-bound cytoplasmic bodies found in various types of neurons, called stigmoid bodies (STBs); STB formation is regulated by the ratio of isoform A to isoform B. In the nucleus localizes to nuclear rods. {ECO:0000250|UniProtKB:P54256}.; SUBCELLULAR LOCATION: [Isoform B]: Cytoplasm {ECO:0000250|UniProtKB:P54256}. Note=In NGF-stimulated PC2 cells isoform A can move anterogradely fom neurite cell body to neurite terminal and is localized to growth cone tips whereas isoform B stays in the cell body. {ECO:0000250|UniProtKB:P54256}.; SUBCELLULAR LOCATION: [Isoform A]: Cell projection, growth cone {ECO:0000250|UniProtKB:P54256}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54256}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P54256}. Presynapse {ECO:0000250|UniProtKB:P54256}. Note=In NGF-stimulated PC2 cells isoform A can move anterogradely fom neurite cell body to neurite terminal and is localized to growth cone tips whereas isoform B stays in the cell body. Localization to neuronal processes and neurite tips is decreased by YWHAZ. {ECO:0000250|UniProtKB:P54256}.
| null | null | null | null | null |
FUNCTION: Originally identified as neuronal protein that specifically associates with HTT/huntingtin and the binding is enhanced by an expanded polyglutamine repeat within HTT possibly affecting HAP1 interaction properties. Both HTT and HAP1 are involved in intracellular trafficking and HAP1 is proposed to link HTT to motor proteins and/or transport cargos. Seems to play a role in vesicular transport within neurons and axons such as from early endosomes to late endocytic compartments and to promote neurite outgrowth. The vesicular transport function via association with microtubule-dependent transporters can be attenuated by association with mutant HTT. Involved in the axonal transport of BDNF and its activity-dependent secretion; the function seems to involve HTT, DCTN1 and a complex with SORT1. Involved in APP trafficking and seems to facilitate APP anterograde transport and membrane insertion thereby possibly reducing processing into amyloid beta. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptors to synapses; the function is dependent on kinesin motor protein KIF5 and is disrupted by HTT with expanded polyglutamine repeat. Involved in regulation of autophagosome motility by promoting efficient retrograde axonal transport. Seems to be involved in regulation of membrane receptor recycling and degradation, and respective signal transduction, including GABA(A) receptors, tyrosine kinase receptors, EGFR, IP3 receptor and androgen receptor. Among others suggested to be involved in control of feeding behavior (involving hypothalamic GABA(A) receptors), cerebellar and brainstem development (involving AHI1 and NTRK1/TrkA), postnatal neurogenesis (involving hypothalamic NTRK2/TrkB regulating the number of Npyr1-expressing cells), and ITPR1/InsP3R1-mediated Ca(2+) release (involving HTT and possibly the effect of mutant HTT). Via association with DCTN1/dynactin p150-glued and HTT/huntingtin involved in cytoplasmic retention of REST in neurons. May be involved in ciliogenesiss; however, reports are conflicting: PubMed:21985783 reports that Hap1 is required for ciliogenesis in primary cortical neurons and proposes that HTT interacts with PCM1 through HAP1; PubMed:23532844 reports that mice with disrupted Hap1 display normal cilium formation and function. Involved in regulation of exocytosis. Isoform A but not isoform B seems to be involved in formation of cytoplasmic inclusion bodies (STBs). In case of anomalous expression of TBP, can sequester a subset of TBP into STBs; sequestration is enhanced by an expanded polyglutamine repeat within TBP. {ECO:0000269|PubMed:12890790, ECO:0000269|PubMed:15379999, ECO:0000269|PubMed:17868456, ECO:0000269|PubMed:18636121, ECO:0000269|PubMed:21985783, ECO:0000269|PubMed:24355921, ECO:0000269|PubMed:24366265, ECO:0000269|PubMed:24453320}.
|
Mus musculus (Mouse)
|
O35671
|
ITBP1_MOUSE
|
MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNSNLDTCAEFRIKYVGAIEKLAVSEGKSLEGPLDLINYIDVAQQDGKLPFVPLEEEFILGVSKYGIKVSTTDQHGVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSDKS
| null | null |
activation of protein kinase B activity [GO:0032148]; biomineral tissue development [GO:0031214]; blood vessel diameter maintenance [GO:0097746]; blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; cell differentiation [GO:0030154]; cell-matrix adhesion [GO:0007160]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; integrin activation [GO:0033622]; integrin-mediated signaling pathway [GO:0007229]; myoblast migration [GO:0051451]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of protein binding [GO:0032091]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein targeting to membrane [GO:0090315]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; Notch signaling pathway [GO:0007219]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to plasma membrane [GO:0072659]; receptor clustering [GO:0043113]; regulation of cell adhesion [GO:0030155]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of GTPase activity [GO:0043087]; regulation of integrin-mediated signaling pathway [GO:2001044]; tube formation [GO:0035148]
|
cell periphery [GO:0071944]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; nuclear body [GO:0016604]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
|
GDP-dissociation inhibitor activity [GO:0005092]; integrin binding [GO:0005178]; kinase binding [GO:0019900]; protein kinase binding [GO:0019901]
|
PF10480;
|
6.20.360.10;
| null |
PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16741948}. Cell membrane {ECO:0000269|PubMed:16741948}. Cell projection, lamellipodium {ECO:0000269|PubMed:16741948}. Cell projection, ruffle {ECO:0000269|PubMed:16741948}. Note=Nucleocytoplasmic shuttling protein; shuttles between nucleus and cytoplasm in an integrin-dependent manner; probably sequestered in the cytosol by ITGB1. Its localization is dependent on the stage of cell spreading on fibronectin; cytoplasmic in case of round cells, corresponding to the initial step of cell spreading, or nuclear in case of well spread cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-rich peripheral ruffles and lamellipodia during initial cell spreading on fibronectin and/or collagen (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter. {ECO:0000269|PubMed:16741948, ECO:0000269|PubMed:17567669, ECO:0000269|PubMed:17654484, ECO:0000269|PubMed:18227284, ECO:0000269|PubMed:21768292}.
|
Mus musculus (Mouse)
|
O35674
|
ADA19_MOUSE
|
MPGRAGVARFCLLALALQLHWPLAACEPGWTTRGSQEGSPPLQHELIIPQWRTSESPGRGKHPLRAELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYHGTVRDVDESSVTLSTCRGIRGLIIVRSNLSYIIEPVPNSDSQHRIYRSEHLTLPPGNCGFEHSGPTSKDWALQFTHQTKKQPRRMKREDLHSMKYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRKLLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHCCSASAADGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMPDTRTLYGGRRCGNGYLEDGEECDCGEEEECKNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYYQMDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGLNGQYRKCSPRDAKCGKIQCQSTQARPLESNAVSIDTTITLNGRRIHCRGTHVYRGPEEEEGEGDMLDPGLVMTGTKCGHNHICFEGQCRNTSFFETEGCGKKCNGHGVCNNNKNCHCFPGWSPPFCNTPGDGGSVDSGPLPPKSVGPVIAGVFSALFVLAVLVLLCHCYRQSHKLGKPSALPFKLRHQFSCPFRVSQSGGTGHANPTFKLQTPQGKRKVTNTPESLRKPSHPPPRPPPDYLRVESPPAPLPAHLNRAAGSSPEAGARIERKESARRPPPSRPMPPAPNCLLSQDFSRPRPPQKALPANPVPGQRTGPRSGGTSLLQPPTSGPQPPRPPAVPVPKLPEYRSQRVGAIISSKI
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
heart development [GO:0007507]; membrane protein ectodomain proteolysis [GO:0006509]; placenta development [GO:0001890]; positive regulation of cell-cell adhesion mediated by cadherin [GO:2000049]; positive regulation of gene expression [GO:0010628]
|
collagen-containing extracellular matrix [GO:0062023]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; SH3 domain binding [GO:0017124]
|
PF08516;PF00200;PF01562;PF01421;
|
3.40.390.10;4.10.70.10;2.60.120.260;
| null |
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteoblast activity in bone (By similarity). {ECO:0000250, ECO:0000269|PubMed:11116142}.
|
Mus musculus (Mouse)
|
O35678
|
MGLL_MOUSE
|
MPEASSPRRTPQNVPYQDLPHLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRIAAAGAGCPP
|
3.1.1.23
| null |
acylglycerol catabolic process [GO:0046464]; arachidonic acid metabolic process [GO:0019369]; fatty acid biosynthetic process [GO:0006633]; long-term synaptic depression [GO:0060292]; monoacylglycerol catabolic process [GO:0052651]; positive regulation of vasoconstriction [GO:0045907]; regulation of axon extension [GO:0030516]; regulation of endocannabinoid signaling pathway [GO:2000124]; regulation of inflammatory response [GO:0050727]; regulation of sensory perception of pain [GO:0051930]; regulation of signal transduction [GO:0009966]; triglyceride catabolic process [GO:0019433]
|
axon [GO:0030424]; cytosol [GO:0005829]; membrane [GO:0016020]; synapse [GO:0045202]; varicosity [GO:0043196]
|
acylglycerol lipase activity [GO:0047372]; hydrolase activity [GO:0016787]
|
PF12146;
|
3.40.50.1820;
|
AB hydrolase superfamily, Monoacylglycerol lipase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18096503}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:18096503}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21454566, ECO:0000269|PubMed:9341166}; CATALYTIC ACTIVITY: Reaction=a 1-acylglycerol + H2O = a fatty acid + glycerol + H(+); Xref=Rhea:RHEA:34019, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868, ChEBI:CHEBI:35759; Evidence={ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21454566}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34020; Evidence={ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21454566}; CATALYTIC ACTIVITY: Reaction=a 2-acylglycerol + H2O = a fatty acid + glycerol + H(+); Xref=Rhea:RHEA:44688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:20554061}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44689; Evidence={ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:20554061}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000269|PubMed:18096503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000269|PubMed:18096503}; CATALYTIC ACTIVITY: Reaction=1-octanoylglycerol + H2O = glycerol + H(+) + octanoate; Xref=Rhea:RHEA:44328, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25646, ChEBI:CHEBI:85241; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44329; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+); Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44321; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+); Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44317; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807, ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44313; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:75455; Evidence={ECO:0000269|PubMed:20554061}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964; Evidence={ECO:0000269|PubMed:20554061}; 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:0000269|PubMed:20554061, ECO:0000269|PubMed:21454566}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21454566}; 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:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75457; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44733; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75568; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48429; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:20554061}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960; Evidence={ECO:0000269|PubMed:20554061}; CATALYTIC ACTIVITY: Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629, ChEBI:CHEBI:75555; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38364; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) + prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48297; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin D2-1-glycerol ester = glycerol + H(+) + prostaglandin D2; Xref=Rhea:RHEA:45412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57406, ChEBI:CHEBI:85232; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45413; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 + H2O = 15-deoxy-Delta(12,14)-prostaglandin J2 + glycerol + H(+); Xref=Rhea:RHEA:45416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:85236, ChEBI:CHEBI:85238; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45417; Evidence={ECO:0000250|UniProtKB:Q99685}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H(+) + prostaglandin F2alpha; Xref=Rhea:RHEA:48300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57404, ChEBI:CHEBI:90233; Evidence={ECO:0000250|UniProtKB:Q99685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48301; Evidence={ECO:0000250|UniProtKB:Q99685};
| null |
PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:9341166}.
| null | null |
FUNCTION: Converts monoacylglycerides to free fatty acids and glycerol (PubMed:17700715, PubMed:18096503, PubMed:19029917, PubMed:20554061, PubMed:20729846, PubMed:21454566, PubMed:9341166). Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (PubMed:17700715, PubMed:18096503, PubMed:19029917, PubMed:20554061, PubMed:20729846, PubMed:21454566, PubMed:9341166). Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (By similarity). {ECO:0000250|UniProtKB:Q99685, ECO:0000269|PubMed:17700715, ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:19029917, ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:20729846, ECO:0000269|PubMed:21454566, ECO:0000269|PubMed:9341166}.
|
Mus musculus (Mouse)
|
O35681
|
SYT3_MOUSE
|
MSGDYEDDLCRRALILVSDLCARVRDADTNDRCQEFNELRIRGYPRGPDADISVSLLSVIVTFCGIVLLGVSLFVSWKLCWVPWRDKGGSAVGGGPLRKDLAPGVGLAGLVGGGGHHLGASLGGHPLLGGPHHHGHTAHHPPFAELLEPGGLGGSEPPEPSYLDMDSYPEAAVASVVAAGVKPSQTSPELPSEGGTGSGLLLLPPSGGGLPSAQSHQQVTSLAPTTRYPALPRPLTQQTLTTQADPSTEERPPALPLPLPGGEEKAKLIGQIKPELYQGTGPGGRRGGGSGEAGAPCGRISFALRYLYGSDHLVVRILQALDLPAKDSNGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFSVPLAELAQRKLHFSVYDFDRFSRHDLIGQVVLDNLLELAEQPPDRPLWRDILEGGSEKADLGELNFSLCYLPTAGRLTVTIIKASNLKAMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALVFDVAPESVENVGLSIAVVDYDCIGHNEVIGVCRVGPEAADPHGREHWAEMLANPRKPVEHWHQLVEEKTLSSFTKGGKGLSEKENSE
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. {ECO:0000250|UniProtKB:P40748};
|
calcium-ion regulated exocytosis [GO:0017156]; cell differentiation [GO:0030154]; cellular response to calcium ion [GO:0071277]; positive regulation of vesicle fusion [GO:0031340]; regulation of calcium ion-dependent exocytosis [GO:0017158]; regulation of dopamine secretion [GO:0014059]; response to calcium ion [GO:0051592]
|
exocytic vesicle [GO:0070382]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060]; transport vesicle membrane [GO:0030658]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; clathrin binding [GO:0030276]; identical protein binding [GO:0042802]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
|
PF00168;
|
2.60.40.150;
|
Synaptotagmin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P40748}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain. Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis. Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:P40748, ECO:0000250|UniProtKB:Q9BQG1}.
|
Mus musculus (Mouse)
|
O35685
|
NUDC_MOUSE
|
MGGEQEEERFDGMLLAMAQQHEGGVQELVNTFFSFLRRKTDFFIGGEEGMAEKLITQTFNHHNQLAQKARREKRARQETERREKAERAARLAKEAKAETPGPQIKELTDEEAERLQLEIDQKKDAEDQEAQLKNGSLDSPGKQDAEDEEDEEDEKDKGKLKPNLGNGADLPNYRWTQTLAELDLAVPFRVSFRLKGKDVVVDIQRRHLRVGLKGQPPVVDGELYNEVKVEESSWLIEDGKVVTVHLEKINKMEWWNRLVTSDPEINTKKINPENSKLSDLDSETRSMVEKMMYDQRQKSMGLPTSDEQKKQEILKKFMDQHPEMDFSKAKFN
| null | null |
cell division [GO:0051301]; mitotic metaphase chromosome alignment [GO:0007080]; mitotic spindle organization [GO:0007052]; nuclear migration [GO:0007097]; protein folding [GO:0006457]; response to peptide hormone [GO:0043434]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]
|
unfolded protein binding [GO:0051082]
|
PF04969;PF16273;PF14050;
|
2.60.40.790;
|
NudC family
|
PTM: Reversibly phosphorylated on serine residues during the M phase of the cell cycle. Phosphorylation on Ser-275 and Ser-327 is necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Phosphorylated by PLK and other kinases (By similarity). {ECO:0000250|UniProtKB:Q9Y266}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Y266}. Midbody {ECO:0000250|UniProtKB:Q9Y266}. Note=A small proportion is nuclear, in a punctate pattern (By similarity). In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migrating cells (By similarity). Localizes to the mitotic spindle in a EML4-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9Y266}.
| null | null | null | null | null |
FUNCTION: Plays a role in neurogenesis and neuronal migration (PubMed:11734602). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (By similarity). Necessary for cytokinesis and cell proliferation (By similarity). {ECO:0000250|UniProtKB:Q9Y266, ECO:0000269|PubMed:11734602}.
|
Mus musculus (Mouse)
|
O35690
|
PHX2B_MOUSE
|
MYKMEYSYLNSSAYESCMAGMDTSSLASAYADFSSCSQASGFQYNPIRTTFGATSGCPSLTPGSCSLGTLRDHQSSPYAAVPYKLFTDHGGLNEKRKQRRIRTTFTSAQLKELERVFAETHYPDIYTREELALKIDLTEARVQVWFQNRRAKFRKQERAAAAAAAAAKNGSSGKKSDSSRDDESKEAKSTDPDSTGGPGPNPNPTPSCGANGGGGGGPSPAGAPGAAGPGGPGGEPGKGGAAAAAAAAAAAAAAAAAAAAGGLAAAGGPGQGWAPGPGPITSIPDSLGGPFASVLSSLQRPNGAKAALVKSSMF
| null | null |
brainstem development [GO:0003360]; cell development [GO:0048468]; cell differentiation in hindbrain [GO:0021533]; cell population proliferation [GO:0008283]; cellular response to BMP stimulus [GO:0071773]; cellular response to carbon dioxide [GO:0071244]; dopaminergic neuron differentiation [GO:0071542]; efferent axon development in a lateral line nerve [GO:0048894]; enteric nervous system development [GO:0048484]; glial cell differentiation [GO:0010001]; hindbrain tangential cell migration [GO:0021934]; inner ear development [GO:0048839]; medullary reticular formation development [GO:0021723]; membrane depolarization [GO:0051899]; motor neuron migration [GO:0097475]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of type B pancreatic cell proliferation [GO:1904691]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; neuron differentiation [GO:0030182]; noradrenergic neuron development [GO:0003358]; noradrenergic neuron differentiation [GO:0003357]; parasympathetic nervous system development [GO:0048486]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; regulation of transcription by RNA polymerase II [GO:0006357]; respiratory system development [GO:0060541]; response to activity [GO:0014823]; retrotrapezoid nucleus neuron differentiation [GO:0061452]; skeletal muscle cell differentiation [GO:0035914]; sympathetic ganglion development [GO:0061549]; sympathetic nervous system development [GO:0048485]; type B pancreatic cell proliferation [GO:0044342]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
O35696
|
SIA8B_MOUSE
|
MQLQFRSWMLAALTLLVVFLIFADISEIEEEIGNSGGRGTIRSAVNSLHSKSNRAEVVINGSSPPAVADRSNESLKHNIQPASSKWRHNQTLSLRIRKQILKFLDAEKDISVLKGTLKPGDIIHYIFDRDSTMNVSQNLYELLPRTSPLKNKHFQTCAIVGNSGVLLNSGCGQEIDTHSFVIRCNLAPVQEYARDVGLKTDLVTMNPSVIQRAFEDLVNATWREKLLQRLHGLNGSILWIPAFMARGGKERVEWVNALILKHHVNVRTAYPSLRLLHAVRGYWLTNKVHIKRPTTGLLMYTLATRFCNQIYLYGFWPFPLDQNQNPVKYHYYDSLKYGYTSQASPHTMPLEFKALKSLHEQGALKLTVGQCDGAT
|
2.4.3.-
| null |
ganglioside biosynthetic process [GO:0001574]; N-glycan processing [GO:0006491]; neuron projection extension [GO:1990138]; oligosaccharide metabolic process [GO:0009311]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of synapse assembly [GO:0051965]; protein glycosylation [GO:0006486]; response to cocaine [GO:0042220]; sialylation [GO:0097503]
|
early endosome [GO:0005769]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]
|
alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity [GO:0003828]; nucleotide binding [GO:0000166]; sialyltransferase activity [GO:0008373]
|
PF00777;
|
3.90.1480.20;
|
Glycosyltransferase 29 family
|
PTM: Autopolysialylated. Autopolysialylation is not a prerequisite for the polysialylation acitity, but enhances the polysialylation acitity. {ECO:0000250|UniProtKB:Q92186}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92186}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q92186}. Secreted {ECO:0000250|UniProtKB:Q92186}. Cell membrane {ECO:0000250|UniProtKB:Q92186}. Note=Also trafficks to the cell surface. {ECO:0000250|UniProtKB:Q92186}.
|
CATALYTIC ACTIVITY: Reaction=[N-acetyl-alpha-D-neuraminosyl-(2->8)](n) + CMP-N-acetyl-beta-neuraminate = [N-acetyl-alpha-D-neuraminosyl-(2->8)](n+1) + CMP + H(+); Xref=Rhea:RHEA:77367, Rhea:RHEA-COMP:14315, Rhea:RHEA-COMP:18878, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:139252; Evidence={ECO:0000269|PubMed:7875291}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77368; Evidence={ECO:0000269|PubMed:7875291};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:7875291}.
| null | null |
FUNCTION: Catalyzes the transfer of a sialic acid from a CMP-linked sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid of an N-linked glycan acceptor through alpha-2,8-linkages (PubMed:7875291). Therefore, participates in polysialic acid synthesis on various sialylated N-acetyllactosaminyl oligosaccharides (alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid), including NCAM1, NCAM1 N-glycans, FETUB N-glycans, and to a lesser extent sialylparagloboside (SPG) and AHSG, which does not require the initial addition of an alpha 2,8-sialic acid (By similarity). However, does not exhibit sialic acid-polymerase activity (PubMed:7875291). Catalyzes polysialic acid synthesis in the hippocampal on NCAM1 and supports neurite outgrowth (PubMed:7875291). ST8SIA2-mediated polysialylation influences on oligodendrocyte differentiation and may promote the integrity of myelin and axons (PubMed:27534376). {ECO:0000250|UniProtKB:Q92186, ECO:0000269|PubMed:27534376, ECO:0000269|PubMed:7875291}.
|
Mus musculus (Mouse)
|
O35701
|
MATN3_MOUSE
|
MLLSAPLRHLPGLLLLLWPLLLLPSLAAPGRLARASVRRLGTRVPGGSPGHLSALATSTRAPYSGGRGAGVCKSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTMSGLAIQTAMEEAFTVEAGARGPMSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLEEHVFYVETYGVIEKLSARFQETFCALDQCMLGTHQCQHVCVSDGDGKHHCECSQGYTLNADGKTCSAIDKCALSTHGCEQICVNDRNGSYHCECYGGYALNADRRTCAALDKCASGTHGCQHICVNDGAGSHHCECFEGYTLNADKKTCSVRNKCALGTHGCQHICVSDGAVAYHCDCFPGYTLNDDKKTCSDIEEARSLISIEDACGCGATLAFQEKVSSHLQKLNTKLDNILKKLKVTEYGQVHR
| null | null |
cartilage development [GO:0051216]; extracellular matrix organization [GO:0030198]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; matrilin complex [GO:0120216]
|
calcium ion binding [GO:0005509]
|
PF12662;PF07645;PF10393;PF00092;
|
1.20.5.30;2.10.25.10;3.40.50.410;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10660556, ECO:0000269|PubMed:23956175}.
| null | null | null | null | null |
FUNCTION: Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks. {ECO:0000269|PubMed:10660556}.
|
Mus musculus (Mouse)
|
O35704
|
SPTC1_MOUSE
|
MATVAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSKNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVSGLKVVGESLSPALHLQLEESTGSREKDVKLLQAIVDQCMDKGIALTQARYLDKEEKCLPPPSIRVVVTVEQTEEELQRAASTIREAAQAVLL
|
2.3.1.50
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250};
|
ceramide biosynthetic process [GO:0046513]; lipophagy [GO:0061724]; positive regulation of lipophagy [GO:1904504]; regulation of fat cell apoptotic process [GO:1904649]; sphinganine biosynthetic process [GO:0046511]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; sphingomyelin biosynthetic process [GO:0006686]; sphingosine biosynthetic process [GO:0046512]
|
endoplasmic reticulum [GO:0005783]; 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:1317856, ECO:0000269|PubMed:26301690}; Single-pass membrane protein {ECO:0000269|PubMed:1317856}.
|
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. {ECO:0000269|PubMed:28100772}.
| 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 (PubMed:28100772). 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 (PubMed:28100772). {ECO:0000250|UniProtKB:O15269, ECO:0000269|PubMed:28100772}.
|
Mus musculus (Mouse)
|
O35710
|
NOCT_MOUSE
|
MYQSPRRLCSALLLRDAPGLRRTLVPGPRRTLAPPVLGSRPKSPQLQAAAASGAARSRPRTVSSMGNGTSRLYSALAKTVNSSAAAQHPEYLVSTDPEHLEPIDPKELLEECRAVLHTRPPRYQRDFVDLRTDCSSSHSPIRVMQWNILAQALGEGKDNFVQCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFFLQNRFKLISSTNIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITQGAKIPLIVCGDFNAEPTEEVYKHFASSSLNLNSAYKLLSPDGQSEPPYTTWKIRTSGECRHTLDYIWYSRHALSVTSALDLLTEEQIGPNRLPSFHYPSDHLSLVCDFSFNEEPHELF
|
3.1.3.108
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UK39}; Note=Binds 2 magnesium ions, but the ions are only loosely bound to the protein. {ECO:0000250|UniProtKB:Q9UK39};
|
circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; mRNA stabilization [GO:0048255]; NADP metabolic process [GO:0006739]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoblast differentiation [GO:0045668]; P-body assembly [GO:0033962]; positive regulation of fat cell differentiation [GO:0045600]; regulation of circadian rhythm [GO:0042752]; regulation of embryonic development [GO:0045995]; response to extracellular stimulus [GO:0009991]; response to lipopolysaccharide [GO:0032496]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; P-body [GO:0000932]; perinuclear region of cytoplasm [GO:0048471]
|
3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; NADP phosphatase activity [GO:0019178]; NADPH phosphatase activity [GO:0102757]; poly(A)-specific ribonuclease activity [GO:0004535]
|
PF03372;
|
3.60.10.10;
|
CCR4/nocturin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23449310}. Nucleus {ECO:0000269|PubMed:23449310}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20498072}. Mitochondrion {ECO:0000250|UniProtKB:Q9UK39}.
|
CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = NAD(+) + phosphate; Xref=Rhea:RHEA:28050, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:58349; EC=3.1.3.108; Evidence={ECO:0000250|UniProtKB:Q9UK39}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28051; Evidence={ECO:0000250|UniProtKB:Q9UK39}; CATALYTIC ACTIVITY: Reaction=H2O + NADPH = NADH + phosphate; Xref=Rhea:RHEA:60664, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57945; EC=3.1.3.108; Evidence={ECO:0000250|UniProtKB:Q9UK39}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60665; Evidence={ECO:0000250|UniProtKB:Q9UK39};
| null | null | null | null |
FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Represses translation and promotes degradation of target mRNA molecules (By similarity). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control (PubMed:20498072, PubMed:20685873). Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis (PubMed:20498072, PubMed:21820310, PubMed:22073225, PubMed:22082366, PubMed:22331129). Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance (PubMed:20498072, PubMed:22082366). Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity (PubMed:20498072). Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone (PubMed:20685873, PubMed:22073225). Critical for proper development of early embryos (PubMed:23449310). {ECO:0000250|UniProtKB:Q9UK39, ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:20685873, ECO:0000269|PubMed:21820310, ECO:0000269|PubMed:22073225, ECO:0000269|PubMed:22082366, ECO:0000269|PubMed:22331129, ECO:0000269|PubMed:23449310}.
|
Mus musculus (Mouse)
|
O35714
|
TNR18_MOUSE
|
MGAWAMLYGVSMLCVLDLGQPSVVEEPGCGPGKVQNGSGNNTRCCSLYAPGKEDCPKERCICVTPEYHCGDPQCKICKHYPCQPGQRVESQGDIVFGFRCVACAMGTFSAGRDGHCRLWTNCSQFGFLTMFPGNKTHNAVCIPEPLPTEQYGHLTVIFLVMAACIFFLTTVQLGLHIWQLRRQHMCPRETQPFAEVQLSAEDACSFQFPEEERGEQTEEKCHLGGRWP
| null | null |
apoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell adhesion [GO:0045785]
|
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]
|
tumor necrosis factor receptor activity [GO:0005031]
| null |
2.10.50.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform A]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform B]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform C]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform D]: Secreted.
| null | null | null | null | null |
FUNCTION: Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35716
|
SOCS1_MOUSE
|
MVARNQVAADNAISPAAEPRRRSEPSSSSSSSSPAAPVRPRPCPAVPAPAPGDTHFRTFRSHSDYRRITRTSALLDACGFYWGPLSVHGAHERLRAEPVGTFLVRDSRQRNCFFALSVKMASGPTSIRVHFQAGRFHLDGSRETFDCLFELLEHYVAAPRRMLGAPLRQRRVRPLQELCRQRIVAAVGRENLARIPLNPVLRDYLSSFPFQI
| null | null |
cellular response to amino acid stimulus [GO:0071230]; cellular response to cytokine stimulus [GO:0071345]; cellular response to organic cyclic compound [GO:0071407]; cytokine-mediated signaling pathway [GO:0019221]; fat cell differentiation [GO:0045444]; intracellular signal transduction [GO:0035556]; macrophage differentiation [GO:0030225]; negative regulation of CD8-positive, alpha-beta T cell differentiation [GO:0043377]; negative regulation of hepatic stellate cell proliferation [GO:1904898]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; negative regulation of tyrosine phosphorylation of STAT protein [GO:0042532]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; positive regulation of CD4-positive, alpha-beta T cell differentiation [GO:0043372]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of regulatory T cell differentiation [GO:0045591]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of cytokine production [GO:0001817]; regulation of protein phosphorylation [GO:0001932]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]; regulation of tyrosine phosphorylation of STAT protein [GO:0042509]
|
cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; phosphatidylinositol 3-kinase complex [GO:0005942]
|
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; insulin-like growth factor receptor binding [GO:0005159]; kinase inhibitor activity [GO:0019210]; protein kinase binding [GO:0019901]
|
PF00017;PF07525;
|
3.30.505.10;1.10.750.20;
|
SOCS1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15524}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O15524}. Note=Detected in perinuclear cytoplasmic vesicles upon interaction with FGFR3. {ECO:0000250|UniProtKB:O15524}.
| null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Essential negative regulator of type I and type II interferon (IFN) signaling, as well as that of other cytokines, including IL2, IL4, IL6 and leukemia inhibitory factor (LIF) (PubMed:10064597, PubMed:15169905, PubMed:15522878, PubMed:9202125). Downregulates cytokine signaling by inhibiting the JAK/STAT signaling pathway. Acts by binding to JAK proteins and to IFNGR1 and inhibiting their kinase activity (PubMed:10064597, PubMed:15522878, PubMed:9202125). In vitro, suppresses Tec protein-tyrosine activity (By similarity). Regulates IFN-gamma (IFNG)-mediated sensory neuron survival. Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250|UniProtKB:O15524, ECO:0000269|PubMed:10064597, ECO:0000269|PubMed:15169905, ECO:0000269|PubMed:15522878, ECO:0000269|PubMed:9202125}.
|
Mus musculus (Mouse)
|
O35717
|
SOCS2_MOUSE
|
MTLRCLEPSGNGADRTRSQWGTAGLPEEQSPEAARLAKALRELSQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPTLQHFCRLAINKCTGTIWGLPLPTRLKDYLEEYKFQV
| null | null |
growth hormone receptor signaling pathway [GO:0060396]; intracellular signal transduction [GO:0035556]; lactation [GO:0007595]; mammary gland alveolus development [GO:0060749]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; positive regulation of neuron differentiation [GO:0045666]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of multicellular organism growth [GO:0040014]; response to estradiol [GO:0032355]
|
phosphatidylinositol 3-kinase complex [GO:0005942]
|
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; growth hormone receptor binding [GO:0005131]; insulin-like growth factor receptor binding [GO:0005159]
|
PF00017;PF07525;
|
3.30.505.10;1.10.750.20;
| null |
PTM: Ubiquitinated; mediated by AREL1 and leading to its subsequent proteasomal degradation (PubMed:31578312). Ubiquitination is dependent on phosphorylation at Ser-52, by PKC and is stimulated by LPS (PubMed:31578312). {ECO:0000269|PubMed:31578312}.; PTM: Phosphorylation at Ser-52 by PKC facilitates its ubiquitination and proteasomal degradation. {ECO:0000269|PubMed:31578312}.
| null | null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35718
|
SOCS3_MOUSE
|
MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGTPSFSLPPTEPSSEVPEQPPAQALPGSTPKRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL
| null | null |
branching involved in labyrinthine layer morphogenesis [GO:0060670]; cell differentiation [GO:0030154]; cellular response to interleukin-17 [GO:0097398]; cellular response to leukemia inhibitory factor [GO:1990830]; intracellular signal transduction [GO:0035556]; negative regulation of inflammatory response [GO:0050728]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of signal transduction [GO:0009968]; negative regulation of tyrosine phosphorylation of STAT protein [GO:0042532]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; placenta blood vessel development [GO:0060674]; positive regulation of cell differentiation [GO:0045597]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of protein phosphorylation [GO:0001932]; signal transduction [GO:0007165]
|
cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; phosphatidylinositol 3-kinase complex [GO:0005942]
|
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; miRNA binding [GO:0035198]; phosphotyrosine residue binding [GO:0001784]; protein tyrosine kinase inhibitor activity [GO:0030292]
|
PF00017;
|
3.30.505.10;1.10.750.20;
| null |
PTM: Phosphorylated on tyrosine residues after stimulation by the cytokines, IL-2, EPO or IGF1. {ECO:0000250}.
| null | null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors (PubMed:10821852, PubMed:12754505, PubMed:9889194). Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling (PubMed:12754505, PubMed:9889194). Suppresses fetal liver erythropoiesis (PubMed:10490101). Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells (PubMed:12847520). Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250|UniProtKB:O14543, ECO:0000269|PubMed:10490101, ECO:0000269|PubMed:10821852, ECO:0000269|PubMed:12754505, ECO:0000269|PubMed:12847520, ECO:0000269|PubMed:9889194}.
|
Mus musculus (Mouse)
|
O35719
|
RA51B_MOUSE
|
MSSKKLRRVGLSPELCDRLSRYQIVNCQHFLSLSPLELMKVTGLSYRGVHELLHTVSKACAPQMQTAYELKTRRSAHLSPAFLSTTLCALDEALHGGVPCGSLTEITGPPGCGKTQFCIMMSVLATLPTSLGGLEGAVVYIDTESAFTAERLVEIAESRFPQYFNTEEKLLLTSSRVHLCRELTCEGLLQRLESLEEEIISKGVKLVIVDSIASVVRKEFDPKLQGNIKERNKFLGKGASLLKYLAGEFSIPVILTNQITTHLSGALPSQADLVSPADDLSLSEGTSGSSCLVAALGNTWGHCVNTRLILQYLDSERRQILIAKSPLAAFTSFVYTIKGEGLVLQGHERP
| null | null |
blastocyst growth [GO:0001832]; double-strand break repair via homologous recombination [GO:0000724]; in utero embryonic development [GO:0001701]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; somite development [GO:0061053]
|
Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; single-stranded DNA binding [GO:0003697]
|
PF08423;
|
3.40.50.300;
|
RecA family, RAD51 subfamily
|
PTM: Phosphorylated on tyrosine residues by BCR-ABL. {ECO:0000250|UniProtKB:O15315}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15315}.
| null | null | null | null | null |
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. {ECO:0000250|UniProtKB:O15315}.
|
Mus musculus (Mouse)
|
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