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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O95989
|
NUDT3_HUMAN
|
MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPSVAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVNIGRKREWFKIEDAIKVLQYHKPVQASYFETLRQGYSANNGTPVVATTYSVSAQSSMSGIR
|
3.6.1.10; 3.6.1.52; 3.6.1.59; 3.6.1.61; 3.6.1.62
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19585659, ECO:0000269|PubMed:34788624}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:34788624}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:34788624}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:19585659};
|
adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; cell-cell signaling [GO:0007267]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diadenosine polyphosphate catabolic process [GO:0015961]; diphosphoinositol polyphosphate catabolic process [GO:0071544]; diphosphoinositol polyphosphate metabolic process [GO:0071543]; RNA decapping [GO:0110154]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity [GO:0140932]; 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; endopolyphosphatase activity [GO:0000298]; inositol diphosphate pentakisphosphate diphosphatase activity [GO:0052842]; inositol diphosphate tetrakisphosphate diphosphatase activity [GO:0052840]; inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity [GO:0052848]; inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity [GO:0052845]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; zinc ion binding [GO:0008270]
|
PF00293;
|
3.90.79.10;
|
Nudix hydrolase family, DIPP subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34788624}. Nucleus {ECO:0000269|PubMed:34788624}.
|
CATALYTIC ACTIVITY: Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:10585413, ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:34788624, ECO:0000269|PubMed:9822604}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O = 1D-myo-inositol hexakisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:22384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:10585413, ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:34788624, ECO:0000269|PubMed:9822604}; CATALYTIC ACTIVITY: Reaction=3,5-bis(diphospho)-1D-myo-inositol 1,2,4,6-tetrakisphosphate + H2O = 3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:56312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:140372, ChEBI:CHEBI:140374; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:10585413, ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:34788624, ECO:0000269|PubMed:9822604}; CATALYTIC ACTIVITY: Reaction=[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate; Xref=Rhea:RHEA:22452, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.10; Evidence={ECO:0000269|PubMed:34788624}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = ADP + ATP + 2 H(+); Xref=Rhea:RHEA:30527, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:62041, ChEBI:CHEBI:456216; EC=3.6.1.61; Evidence={ECO:0000269|PubMed:10419486, ECO:0000269|PubMed:10585413, ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:34788624}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = 2 ATP + 2 H(+); Xref=Rhea:RHEA:32043, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:63740; EC=3.6.1.61; Evidence={ECO:0000269|PubMed:10419486, ECO:0000269|PubMed:10585413, ECO:0000269|PubMed:12370170}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = AMP + ATP + 2 H(+); Xref=Rhea:RHEA:32039, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58141, ChEBI:CHEBI:456215; EC=3.6.1.61; Evidence={ECO:0000269|PubMed:10419486, ECO:0000269|PubMed:10585413, ECO:0000269|PubMed:12370170}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616; EC=3.6.1.59; Evidence={ECO:0000269|PubMed:32727897}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461; EC=3.6.1.62; Evidence={ECO:0000269|PubMed:32727897};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.9 uM for Ap6A {ECO:0000269|PubMed:10419486, ECO:0000269|PubMed:12370170}; KM=7.7 uM for Ap5A {ECO:0000269|PubMed:10419486}; KM=38 mM for 5-phosphoribose 1-diphosphate {ECO:0000269|PubMed:12370170}; KM=4.2 nM for PP-InsP5 {ECO:0000269|PubMed:12370170};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5 for PP-InsP5 hydrolysis. Displays strong endopolyphosphatase activity at pH 6.8 and 7.4. {ECO:0000269|PubMed:34788624, ECO:0000269|PubMed:9822604};
| null |
FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (PubMed:10585413, PubMed:12370170, PubMed:9822604). InsP6 (inositol hexakisphosphate) is not a substrate (PubMed:9822604). Acts as a negative regulator of the ERK1/2 pathway (By similarity). Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) and diadenosine 5',5'''- P1,P5-pentaphosphate (Ap5A) being the preferred substrates (PubMed:10419486, PubMed:12370170). The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A (PubMed:12370170). Also able to hydrolyze 5-phosphoribose 1-diphosphate (PubMed:12370170). Acts as a decapping enzyme that modulates the stability of a subset of mRNAs implicated in cell motility (PubMed:26932476). Hydrolyzes monomethylated capped RNA after both the alpha- and beta-phosphates generating m7GMP + ppRNA and m7GDP + pRNA (PubMed:32727897). Can hydrolyze unmethylated capped RNAs (By similarity). Divalent cations zinc, magnesium and manganese determine its substrate specificity (PubMed:34788624). Exhibits diphosphoinositol polyphosphate phosphohydrolase in the presence of magnesium ions, diadenosine hexaphosphate hydrolase activity in the presence of manganese ions and endopolyphosphatase activity in the presence of zinc ions (PubMed:34788624). Plays an important role in limiting DNA damage and maintaining cell survival upon oxidative stress via its endopolyphosphatase activity (PubMed:34788624). {ECO:0000250|UniProtKB:Q9JI46, ECO:0000269|PubMed:10419486, ECO:0000269|PubMed:10585413, ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:34788624, ECO:0000269|PubMed:9822604, ECO:0000305|PubMed:26932476}.
|
Homo sapiens (Human)
|
O95990
|
F107A_HUMAN
|
MYSEIQRERADIGGLMARPEYREWNPELIKPKKLLNPVKASRSHQELHRELLMNHRRGLGVDSKPELQRVLEHRRRNQLIKKKKEELEAKRLQCPFEQELLRRQQRLNQLEKPPEKEEDHAPEFIKVRENLRRIATLTSEEREL
| null | null |
actin filament bundle assembly [GO:0051017]; actin filament polymerization [GO:0030041]; cell cycle [GO:0007049]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to nutrient levels [GO:0031669]; cognition [GO:0050890]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of long-term synaptic potentiation [GO:1900272]; positive regulation of cell migration [GO:0030335]; positive regulation of protein ubiquitination [GO:0031398]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell growth [GO:0001558]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of protein stability [GO:0031647]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; neuron projection [GO:0043005]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; ruffle membrane [GO:0032587]; stress fiber [GO:0001725]; synapse [GO:0045202]
|
actin binding [GO:0003779]
|
PF06625;
| null |
FAM107 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10564580, ECO:0000269|PubMed:11256614, ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}. Cell junction, focal adhesion {ECO:0000269|PubMed:20543869}. Cell projection, ruffle membrane {ECO:0000269|PubMed:20543869}. Synapse {ECO:0000250|UniProtKB:Q78TU8}. Note=Colocalizes with F-actin and COMMD1 in the nucleus (PubMed:28604741). Colocalizes with MAP1A along actin stress fibers and membrane ruffles (PubMed:20543869). {ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}.
| null | null | null | null | null |
FUNCTION: Stress-inducible actin-binding protein that plays a role in synaptic and cognitive functions by modulating actin filamentous (F-actin) dynamics. Mediates polymerization of globular actin to F-actin. Also binds to, stabilizes and bundles F-actin. Involved in synaptic function by regulating neurite outgrowth in an actin-dependent manner and for the acquisition of hippocampus-dependent cognitive function, such as learning and long-term memory (By similarity). Plays a role in the actin and microtubule cytoskeleton organization; negatively regulates focal adhesion (FA) assembly promoting malignant glial cell migration in an actin-, microtubule- and MAP1A-dependent manner (PubMed:20543869). Also involved in neuroblastoma G1/S phase cell cycle progression and cell proliferation inhibition by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a COMMD1- and actin-dependent manner (PubMed:10564580, PubMed:28604741). May play a role in tumor development (PubMed:10564580). {ECO:0000250|UniProtKB:Q78TU8, ECO:0000269|PubMed:10564580, ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}.
|
Homo sapiens (Human)
|
O95992
|
CH25H_HUMAN
|
MSCHNCSDPQVLCSSGQLFLQPLWDHLRSWEALLQSPFFPVIFSITTYVGFCLPFVVLDILCSWVPALRRYKIHPDFSPSAQQLLPCLGQTLYQHVMFVFPVTLLHWARSPALLPHEAPELLLLLHHILFCLLLFDMEFFVWHLLHHKVPWLYRTFHKVHHQNSSSFALATQYMSVWELFSLGFFDMMNVTLLGCHPLTTLTFHVVNIWLSVEDHSGYNFPWSTHRLVPFGWYGGVVHHDLHHSHFNCNFAPYFTHWDKILGTLRTASVPAR
|
1.14.99.38
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:Q9Z0F5};
|
B cell chemotaxis [GO:0035754]; cholesterol metabolic process [GO:0008203]; lipid metabolic process [GO:0006629]; negative regulation of cholesterol metabolic process [GO:0090206]; negative regulation of fusion of virus membrane with host plasma membrane [GO:1903914]; response to type I interferon [GO:0034340]; sterol biosynthetic process [GO:0016126]
|
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]
|
C-4 methylsterol oxidase activity [GO:0000254]; cholesterol 25-hydroxylase activity [GO:0001567]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395]
|
PF04116;
| null |
Sterol desaturase family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9852097}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z0F5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z0F5}.
|
CATALYTIC ACTIVITY: Reaction=AH2 + cholesterol + O2 = 25-hydroxycholesterol + A + H2O; Xref=Rhea:RHEA:21104, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:17499, ChEBI:CHEBI:42977; EC=1.14.99.38; Evidence={ECO:0000269|PubMed:33239446, ECO:0000269|PubMed:9852097}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21105; Evidence={ECO:0000269|PubMed:33239446, ECO:0000305|PubMed:9852097}; CATALYTIC ACTIVITY: Reaction=cholesterol + H(+) + NADPH + O2 = 25-hydroxycholesterol + H2O + NADP(+); Xref=Rhea:RHEA:46132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:42977, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:9852097}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46133; Evidence={ECO:0000305|PubMed:9852097};
| null | null | null | null |
FUNCTION: Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes (PubMed:9852097). Plays a key role in cell positioning and movement in lymphoid tissues: 25-hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC), an oxysterol that acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (By similarity). May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing (PubMed:9852097). As an interferon-stimulated gene, has broad antiviral activities against a wide range of enveloped viruses, such as vesicular stomatitis virus (VSV) and SARS coronavirus-2 (SARS-CoV-2). Its product, 25-hydroxycholesterol, activates the ER-localized enzyme ACAT to induce internalization of accessible cholesterol on the plasma membrane and restricts SARS-CoV-2 S protein-mediated fusion which inhibits virus replication (PubMed:32944968, PubMed:33239446). In testis, production of 25-hydroxycholesterol by macrophages plays a role in Leydig cell differentiation (By similarity). Required to restrain inflammation in macrophages: production of 25-hydroxycholesterol protects macrophages from cholesterol overload, thereby preventing mitochondrial DNA release and subsequent activation of the AIM2 inflammasome (By similarity). {ECO:0000250|UniProtKB:Q4QQV7, ECO:0000250|UniProtKB:Q9Z0F5, ECO:0000269|PubMed:32944968, ECO:0000269|PubMed:33239446, ECO:0000269|PubMed:9852097}.
|
Homo sapiens (Human)
|
O95994
|
AGR2_HUMAN
|
MEKIPVSAFLLLVALSYTLARDTTVKPGAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPADTALLLDNMKKALKLLKTEL
| null | null |
digestive tract morphogenesis [GO:0048546]; inflammatory response [GO:0006954]; lung goblet cell differentiation [GO:0060480]; mucus secretion [GO:0070254]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of developmental growth [GO:0048639]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of gene expression [GO:0010628]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896]; positive regulation of PERK-mediated unfolded protein response [GO:1903899]; positive regulation of protein localization to plasma membrane [GO:1903078]
|
endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
dystroglycan binding [GO:0002162]; epidermal growth factor receptor binding [GO:0005154]; identical protein binding [GO:0042802]
|
PF13899;
|
3.40.30.10;
|
AGR family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15834940}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O88312}.
| null | null | null | null | null |
FUNCTION: Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion (PubMed:23274113). {ECO:0000250, ECO:0000269|PubMed:18199544, ECO:0000269|PubMed:23274113}.
|
Homo sapiens (Human)
|
O95995
|
DRC4_HUMAN
|
MAPKKKGKKGKAKGTPIVDGLAPEDMSKEQVEEHVSRIREELDREREERNYFQLERDKIHTFWEITRRQLEEKKAELRNKDREMEEAEERHQVEIKVYKQKVKHLLYEHQNNLTEMKAEGTVVMKLAQKEHRIQESVLRKDMRALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKMLRDELDLRRKTELHEVEERKNGQIHTLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILLCTKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEKKEVQFNEVLAASNLDPAALTLVSRKLEDVLESKNSTIKDLQYELAQVCKAHNDLLRTYEAKLLAFGIPLDNVGFKPLETAVIGQTLGQGPAGLVGTPT
| null | null |
axoneme assembly [GO:0035082]; brain development [GO:0007420]; cilium movement involved in cell motility [GO:0060294]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; flagellated sperm motility [GO:0030317]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of protein localization to cilium [GO:1903566]; positive regulation of smoothened signaling pathway [GO:0045880]; protein localization [GO:0008104]; regulation of microtubule binding [GO:1904526]
|
axoneme [GO:0005930]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; motile cilium [GO:0031514]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]
|
microtubule binding [GO:0008017]; small GTPase binding [GO:0031267]
|
PF13851;
| null |
DRC4 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10969087}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:16643277, ECO:0000269|PubMed:26387594}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q60779}. Golgi apparatus {ECO:0000269|PubMed:16643277}. Cell projection, cilium {ECO:0000269|PubMed:27120127}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q7XJ96}. Note=Associates with microtubules (PubMed:10969087). Localized to the cytoplasm of round spermatids, the tails of elongating spermatids, and mature spermatid tail bundles protruding into the lumen, and in the flagellum of epididymal spermatozoa (By similarity). {ECO:0000250|UniProtKB:Q60779, ECO:0000269|PubMed:10969087}.
| null | null | null | null | null |
FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dual roles at both the primary (or non-motile) cilia to regulate hedgehog signaling and in motile cilia to coordinate cilia movement. Required for proper motile cilia functioning (PubMed:26387594, PubMed:27120127, PubMed:27472056). Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by facilitating the trafficking of SMO into the cilium and the stimulation of SMO activity in a GRK2-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q60779, ECO:0000250|UniProtKB:Q7XJ96, ECO:0000269|PubMed:26387594, ECO:0000269|PubMed:27120127, ECO:0000269|PubMed:27472056}.
|
Homo sapiens (Human)
|
O95996
|
APCL_HUMAN
|
MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQMDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQGLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQILHGTEAAAGGRAGAPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDGGPEGGGAGSAPIPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVANKATLCARRGCMEAIVAQLASDSEELHQVVSSILRNLSWRADINSKKVLREAGSVTALVQCVLRATKESTLKSVLSALWNLSAHSTENKAAICQVDGALGFLVSTLTYKCQSNSLAIIESGGGILRNVSSLVATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACGTLWNLSARSARDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKHQAAATAVSPGSCVPSLYVRKQRALEAELDARHLAQALEHLEKQGPPAAEAATKKPLPPLRHLDGLAQDYASDSGCFDDDDAPSSLAAAAATGEPASPAALSLFLGSPFLQGQALARTPPTRRGGKEAEKDTSGEAAVAAKAKAKLALAVARIDQLVEDISALHTSSDDSFSLSSGDPGQEAPREGRAQSCSPCRGPEGGRREAGSRAHPLLRLKAAHASLSNDSLNSGSASDGYCPREHMLPCPLAALASRREDPRCGQPRPSRLDLDLPGCQAEPPAREATSADARVRTIKLSPTYQHVPLLEGASRAGAEPLAGPGISPGARKQAWLPADHLSKVPEKLAAAPLSVASKALQKLAAQEGPLSLSRCSSLSSLSSAGRPGPSEGGDLDDSDSSLEGLEEAGPSEAELDSTWRAPGATSLPVAIPAPRRNRGRGLGVEDATPSSSSENYVQETPLVLSRCSSVSSLGSFESPSIASSIPSEPCSGQGSGTISPSELPDSPGQTMPPSRSKTPPLAPAPQGPPEATQFSLQWESYVKRFLDIADCRERCRLPSELDAGSVRFTVEKPDENFSCASSLSALALHEHYVQQDVELRLLPSACPERGGGAGGAGLHFAGHRRREEGPAPTGSRPRGAADQELELLRECLGAAVPARLRKVASALVPGRRALPVPVYMLVPAPAPAQEDDSCTDSAEGTPVNFSSAASLSDETLQGPPRDQPGGPAGRQRPTGRPTSARQAMGHRHKAGGAGRSAEQSRGAGKNRAGLELPLGRPPSAPADKDGSKPGRTRGDGALQSLCLTTPTEEAVYCFYGNDSDEEPPAAAPTPTHRRTSAIPRAFTRERPQGRKEAPAPSKAAPAAPPPARTQPSLIADETPPCYSLSSSASSLSEPEPSEPPAVHPRGREPAVTKDPGPGGGRDSSPSPRAAEELLQRCISSALPRRRPPVSGLRRRKPRATRLDERPAEGSRERGEEAAGSDRASDLDSVEWRAIQEGANSIVTWLHQAAAATREASSESDSILSFVSGLSVGSTLQPPKHRKGRQAEGEMGSARRPEKRGAASVKTSGSPRSPAGPEKPRGTQKTTPGVPAVLRGRTVIYVPSPAPRAQPKGTPGPRATPRKVAPPCLAQPAAPAKVPSPGQQRSRSLHRPAKTSELATLSQPPRSATPPARLAKTPSSSSSQTSPASQPLPRKRPPVTQAAGALPGPGASPVPKTPARTLLAKQHKTQRSPVRIPFMQRPARRGPPPLARAVPEPGPRGRAGTEAGPGARGGRLGLVRVASALSSGSESSDRSGFRRQLTFIKESPGLRRRRSELSSAESAASAPQGASPRRGRPALPAVFLCSSRCEELRAAPRQGPAPARQRPPAARPSPGERPARRTTSESPSRLPVRAPAARPETVKRYASLPHISVARRPDGAVPAAPASADAARRSSDGEPRPLPRVAAPGTTWRRIRDEDVPHILRSTLPATALPLRGSTPEDAPAGPPPRKTSDAVVQTEEVAAPKTNSSTSPSLETREPPGAPAGGQLSLLGSDVDGPSLAKAPISAPFVHEGLGVAVGGFPASRHGSPSRSARVPPFNYVPSPMVVAATTDSAAEKAPATASATLLE
| null | null |
activation of GTPase activity [GO:0090630]; cell fate specification [GO:0001708]; cell migration [GO:0016477]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of microtubule depolymerization [GO:0007026]; nervous system development [GO:0007399]; pattern specification process [GO:0007389]; positive regulation of protein catabolic process [GO:0045732]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of cell differentiation [GO:0045595]; Wnt signaling pathway [GO:0016055]
|
actin filament [GO:0005884]; beta-catenin destruction complex [GO:0030877]; catenin complex [GO:0016342]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intercellular bridge [GO:0045171]; lamellipodium membrane [GO:0031258]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]
|
beta-catenin binding [GO:0008013]; gamma-catenin binding [GO:0045295]; microtubule binding [GO:0008017]
|
PF05956;PF16689;PF05923;PF18797;PF00514;PF16629;PF05924;PF11414;
|
1.20.5.10;1.10.287.450;1.25.10.10;
|
Adenomatous polyposis coli (APC) family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}. Golgi apparatus {ECO:0000269|PubMed:11691822}. Cytoplasm {ECO:0000269|PubMed:11691822}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10646860}. Note=Associated with actin filaments (PubMed:11691822, PubMed:25753423). Associated with microtubule network (PubMed:10644998, PubMed:11691822, PubMed:25753423). {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}.
| null | null | null | null | null |
FUNCTION: Stabilizes microtubules and may regulate actin fiber dynamics through the activation of Rho family GTPases (PubMed:25753423). May also function in Wnt signaling by promoting the rapid degradation of CTNNB1 (PubMed:10021369, PubMed:11691822, PubMed:9823329). {ECO:0000269|PubMed:10021369, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423, ECO:0000269|PubMed:9823329}.
|
Homo sapiens (Human)
|
O95997
|
PTTG1_HUMAN
|
MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPFNPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQSPSSILSTLDVELPPVCCDIDI
| null | null |
cell division [GO:0051301]; chromosome organization [GO:0051276]; DNA repair [GO:0006281]; homologous chromosome segregation [GO:0045143]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; molecular function activator activity [GO:0140677]; SH3 domain binding [GO:0017124]
|
PF04856;
| null |
Securin family
|
PTM: Phosphorylated at Ser-165 by CDK1 during mitosis. {ECO:0000269|PubMed:10656688}.; PTM: Phosphorylated in vitro by ds-DNA kinase. {ECO:0000269|PubMed:10656688}.; PTM: Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation. 'Lys-11'-linked ubiquitination is mediated by the E2 ligase UBE2C/UBCH10. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:18485873}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
| null | null | null | null | null |
FUNCTION: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of TP53. The negative regulation of TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:11238996, ECO:0000269|PubMed:11371342, ECO:0000269|PubMed:12355087}.
|
Homo sapiens (Human)
|
O95998
|
I18BP_HUMAN
|
MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG
| null | null |
cellular response to hydrogen peroxide [GO:0070301]; cellular response to tumor necrosis factor [GO:0071356]; response to lipopolysaccharide [GO:0032496]; T-helper 1 type immune response [GO:0042088]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
interleukin-18 binding [GO:0042007]; receptor antagonist activity [GO:0048019]
| null |
2.60.40.10;
| null |
PTM: N- and O-glycosylated. O-glycosylated with core 1-like and core 2-like glycans. O-glycan heterogeneity at Ser-53: HexHexNAc (major) and Hex2HexNAc2 (minor). N-glycan heterogeneity at Asn-103: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (major) and Hex6HexNAc5 (minor); N-glycan at Asn-147: dHex1Hex5HexNAc4. {ECO:0000269|PubMed:22171320}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31213488}.
| null | null | null | null | null |
FUNCTION: Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response. {ECO:0000269|PubMed:10023777, ECO:0000269|PubMed:10655506, ECO:0000269|PubMed:31213488}.
|
Homo sapiens (Human)
|
O95999
|
BCL10_HUMAN
|
MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLDTLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGESSTTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ
| null | null |
adaptive immune response [GO:0002250]; antifungal innate immune response [GO:0061760]; B cell apoptotic process [GO:0001783]; canonical NF-kappaB signal transduction [GO:0007249]; cellular defense response [GO:0006968]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to mechanical stimulus [GO:0071260]; immunoglobulin mediated immune response [GO:0016064]; innate immune response [GO:0045087]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; negative regulation of mature B cell apoptotic process [GO:0002906]; neural tube closure [GO:0001843]; non-canonical NF-kappaB signal transduction [GO:0038061]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of lymphotoxin A production [GO:0032761]; positive regulation of mast cell cytokine production [GO:0032765]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell receptor signaling pathway [GO:0050862]; programmed cell death [GO:0012501]; protein homooligomerization [GO:0051260]; response to food [GO:0032094]; T cell apoptotic process [GO:0070231]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor signaling pathway [GO:0002224]
|
CBM complex [GO:0032449]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; immunological synapse [GO:0001772]; lysosome [GO:0005764]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; polkadots [GO:0002096]; protein-containing complex [GO:0032991]
|
CARD domain binding [GO:0050700]; general transcription initiation factor binding [GO:0140296]; identical protein binding [GO:0042802]; kinase activator activity [GO:0019209]; NF-kappaB binding [GO:0051059]; protease binding [GO:0002020]; protein kinase B binding [GO:0043422]; protein self-association [GO:0043621]; protein-containing complex binding [GO:0044877]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase binding [GO:0031625]
|
PF00619;
|
1.10.533.10;
| null |
PTM: Phosphorylated. Phosphorylation results in dissociation from TRAF2 and binding to BIRC2/c-IAP2 (PubMed:11466612). Phosphorylated by IKBKB/IKKB (PubMed:17213322). {ECO:0000269|PubMed:11466612, ECO:0000269|PubMed:17213322}.; PTM: Ubiquitinated via both 'Lys-63'-linked and linear ('Met-1'-linked) polyubiquitin chains in response to T-cell receptor (TCR) activation (PubMed:18287044, PubMed:27777308). Ubiquitination is recognized by IKBKG/NEMO, the regulatory subunit of I-kappa-B kinase (IKK), and is required for TCR-induced NF-kappa-B activation (PubMed:18287044, PubMed:27777308). Linear ubiquitination at Lys-17, Lys-31 and Lys-63 is mediated by RNF31/HOIP; linear ubiquitination is recognized with much higher affinity than 'Lys-63'-linked ubiquitin by IKBKG/NEMO (PubMed:27777308). CARD11 is required for linear ubiquitination by HOIP by promoting the targeting of BCL10 to RNF31/HOIP (PubMed:27777308). {ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:27777308}.; PTM: Proteolytically cleaved by MALT1; required for T-cell activation. {ECO:0000269|PubMed:18264101}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17287217}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Appears to have a perinuclear, compact and filamentous pattern of expression. Also found in the nucleus of several types of tumor cells. Colocalized with DPP4 in membrane rafts. {ECO:0000269|PubMed:17287217}.
| null | null | null | null | null |
FUNCTION: Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation (PubMed:10187770, PubMed:10364242, PubMed:10400625, PubMed:24074955, PubMed:25365219). Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing proteins CARD9, CARD11 and CARD14 to activate NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:24074955). Recruited by activated CARD domain-containing proteins: homooligomerized CARD domain-containing proteins form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10, subsequent recruitment of MALT1 and formation of a CBM complex (PubMed:24074955). This leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:18287044, PubMed:24074955, PubMed:27777308). Activated by CARD9 downstream of C-type lectin receptors; CARD9-mediated signals are essential for antifungal immunity (PubMed:26488816). Activated by CARD11 downstream of T-cell receptor (TCR) and B-cell receptor (BCR) (PubMed:18264101, PubMed:18287044, PubMed:24074955, PubMed:27777308). Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK (PubMed:10187815). {ECO:0000269|PubMed:10187770, ECO:0000269|PubMed:10187815, ECO:0000269|PubMed:10364242, ECO:0000269|PubMed:10400625, ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:24074955, ECO:0000269|PubMed:25365219, ECO:0000269|PubMed:26488816, ECO:0000269|PubMed:27777308}.
|
Homo sapiens (Human)
|
O96000
|
NDUBA_HUMAN
|
MPDSWDKDVYPEPPRRTPVQPNPIVYMMKAFDLIVDRPVTLVREFIERQHAKNRYYYYHRQYRRVPDITECKEEDIMCMYEAEMQWKRDYKVDQEIINIMQDRLKACQQREGQNYQQNCIKEVEQFTQVAKAYQDRYQDLGAYSSARKCLAKQRQRMLQERKAAKEAAAATS
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF10249;
| null |
Complex I NDUFB10 subunit family
|
PTM: The formation of intramolecular disulfide bonds is assisted by CHCHD4 and ensures folding, import into the mitochondrion and is required for the function in mitochondrial respiratory chain complex I assembly. {ECO:0000269|PubMed:28040730}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:28040730, ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory subunit that is involved in the functional assembly of the mitochondrial respiratory chain complex I. Complex I has an NADH dehydrogenase activity with ubiquinone as an immediate electron acceptor and mediates the transfer of electrons from NADH to the respiratory chain. {ECO:0000269|PubMed:27626371, ECO:0000269|PubMed:28040730}.
|
Homo sapiens (Human)
|
O96004
|
HAND1_HUMAN
|
MNLVGSYAHHHHHHHPHPAHPMLHEPFLFGPASRCHQERPYFQSWLLSPADAAPDFPAGGPPPAAAAAATAYGPDARPGQSPGRLEALGGRLGRRKGSGPKKERRRTESINSAFAELRECIPNVPADTKLSKIKTLRLATSYIAYLMDVLAKDAQSGDPEAFKAELKKADGGRESKRKRELQQHEGFPPALGPVEKRIKGRTGWPQQVWALELNQ
| null | null |
angiogenesis [GO:0001525]; blastocyst development [GO:0001824]; cardiac left ventricle formation [GO:0003218]; cardiac right ventricle formation [GO:0003219]; cardiac septum morphogenesis [GO:0060411]; cartilage morphogenesis [GO:0060536]; embryonic heart tube development [GO:0035050]; embryonic heart tube formation [GO:0003144]; heart development [GO:0007507]; heart looping [GO:0001947]; mesenchyme development [GO:0060485]; mesoderm formation [GO:0001707]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding [GO:1903026]; negative regulation of transcription by RNA polymerase II [GO:0000122]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; trophectodermal cell differentiation [GO:0001829]; trophoblast giant cell differentiation [GO:0060707]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
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]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coregulator binding [GO:0001221]
|
PF00010;
|
4.10.280.10;
| null |
PTM: Phosphorylation by PLK4 disrupts the interaction with MDFIC and leads to translocation into the nucleoplasm, allowing dimerization and transcription factor activity. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Interaction with MDFIC sequesters it into the nucleolus, preventing the transcription factor activity. Phosphorylation by PLK4 disrupts the interaction with MDFIC and releases it from the nucleolus, leading to transcription factor activity (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcription factor that plays an essential role in both trophoblast giant cell differentiation and in cardiac morphogenesis (By similarity). Binds the DNA sequence 5'-NRTCTG-3' (non-canonical E-box) (By similarity). Acts as a transcriptional repressor of SOX15 (By similarity). In the adult, could be required for ongoing expression of cardiac-specific genes (PubMed:9931445). {ECO:0000250|UniProtKB:Q64279, ECO:0000269|PubMed:9931445}.
|
Homo sapiens (Human)
|
O96005
|
CLPT1_HUMAN
|
MAAAQEADGARSAVVAAGGGSSGQVTSNGSIGRDPPAETQPQNPPAQPAPNAWQVIKGVLFRIFIIWAISSWFRRGPAPQDQAGPGGAPRVASRNLFPKDTLMNLHVYISEHEHFTDFNATSALFWEQHDLVYGDWTSGENSDGCYEHFAELDIPQSVQQNGSIYIHVYFTKSGFHPDPRQKALYRRLATVHMSRMINKYKRRRFQKTKNLLTGETEADPEMIKRAEDYGPVEVISHWHPNITINIVDDHTPWVKGSVPPPLDQYVKFDAVSGDYYPIIYFNDYWNLQKDYYPINESLASLPLRVSFCPLSLWRWQLYAAQSTKSPWNFLGDELYEQSDEEQDSVKVALLETNPYLLALTIIVSIVHSVFEFLAFKNDIQFWNSRQSLEGLSVRSVFFGVFQSFVVLLYILDNETNFVVQVSVFIGVLIDLWKITKVMDVRLDREHRVAGIFPRLSFKDKSTYIESSTKVYDDMAFRYLSWILFPLLGCYAVYSLLYLEHKGWYSWVLSMLYGFLLTFGFITMTPQLFINYKLKSVAHLPWRMLTYKALNTFIDDLFAFVIKMPVMYRIGCLRDDVVFFIYLYQRWIYRVDPTRVNEFGMSGEDPTAAAPVAEVPTAAGALTPTPAPTTTTATREEASTSLPTKPTQGASSASEPQEAPPKPAEDKKKD
| null | null |
cell differentiation [GO:0030154]; regulation of T cell differentiation in thymus [GO:0033081]
|
endomembrane system [GO:0012505]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
GABA receptor binding [GO:0050811]
|
PF05602;
| null |
CLPTM1 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Involved in GABAergic but not glutamatergic transmission. Binds and traps GABAA receptors in the endoplasmic reticulum (ER). Modulates postsynaptic GABAergic transmission, and therefore inhibitory neurotransmission, by reducing the plasma membrane expression of these receptors. Altered GABAergic signaling is one among many causes of cleft palate (By similarity). Might function as a lipid scramblase, translocating lipids in membranes from one leaflet to the other one (By similarity). Required for efficient glycosylphosphatidylinositol (GPI) inositol deacylation in the ER, which is a crucial step to switch GPI-anchored proteins (GPI-APs) from protein folding to transport states (PubMed:29255114). May play a role in T-cell development (By similarity). {ECO:0000250|UniProtKB:Q8VBZ3, ECO:0000250|UniProtKB:Q96KA5, ECO:0000269|PubMed:29255114}.
|
Homo sapiens (Human)
|
O96006
|
ZBED1_HUMAN
|
MENKSLESSQTDLKLVAHPRAKSKVWKYFGFDTNAEGCILQWKKIYCRICMAQIAYSGNTSNLSYHLEKNHPEEFCEFVKSNTEQMREAFATAFSKLKPESSQQPGQDALAVKAGHGYDSKKQQELTAAVLGLICEGLYPASIVDEPTFKVLLKTADPRYELPSRKYISTKAIPEKYGAVREVILKELAEATWCGISTDMWRSENQNRAYVTLAAHFLGLGAPNCLSMGSRCLKTFEVPEENTAETITRVLYEVFIEWGISAKVFGATTNYGKDIVKACSLLDVAVHMPCLGHTFNAGIQQAFQLPKLGALLSRCRKLVEYFQQSAVAMYMLYEKQKQQNVAHCMLVSNRVSWWGSTLAMLQRLKEQQFVIAGVLVEDSNNHHLMLEASEWATIEGLVELLQPFKQVAEMLSASRYPTISMVKPLLHMLLNTTLNIKETDSKELSMAKEVIAKELSKTYQETPEIDMFLNVATFLDPRYKRLPFLSAFERQQVENRVVEEAKGLLDKVKDGGYRPAEDKIFPVPEEPPVKKLMRTSTPPPASVINNMLAEIFCQTGGVEDQEEWHAQVVEELSNFKSQKVLGLNEDPLKWWSDRLALFPLLPKVLQKYWCVTATRVAPERLFGSAANVVSAKRNRLAPAHVDEQVFLYENARSGAEAEPEDQDEGEWGLDQEQVFSLGDGVSGGFFGIRDSSFL
|
2.3.2.-
| null |
negative regulation by host of viral genome replication [GO:0044828]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein autosumoylation [GO:1990466]; protein sumoylation [GO:0016925]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
centrosome [GO:0005813]; chromatin [GO:0000785]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]
|
PF05699;PF02892;
| null | null |
PTM: Autosumoylated with SUMO1, SUMO2, and SUMO3. {ECO:0000269|PubMed:25210186, ECO:0000269|PubMed:27068747}.
|
SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:25210186, ECO:0000269|PubMed:27068747}. Nucleus {ECO:0000269|PubMed:12663651, ECO:0000269|PubMed:17209048}. Note=In granular structures. {ECO:0000269|PubMed:12663651, ECO:0000269|PubMed:17209048}.; SUBCELLULAR LOCATION: Nucleus, PML body. Note=(Microbial infection) Upon interaction with human adenovirus early E1A protein, the protein is redistributed to the peripheral areas of PML bodies. {ECO:0000269|PubMed:25210186}.
| null | null |
PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:27068747}.
| null | null |
FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase which sumoylates CHD3/Mi2-alpha, causing its release from DNA (PubMed:27068747). This results in suppression of CHD3/Mi2-alpha transcription repression, increased recruitment of RNA polymerase II to gene promoters and positive regulation of transcription including H1-5 and ribosomal proteins such as: RPS6, RPL10A, and RPL12 (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747). The resulting increased transcriptional activity drives cell proliferation (PubMed:12663651, PubMed:17220279). Binds to 5'-TGTCG[CT]GA[CT]A-3' consensus sequences in gene promoters of ribosomal proteins (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747). {ECO:0000269|PubMed:12663651, ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:17220279, ECO:0000269|PubMed:27068747}.; FUNCTION: (Microbial infection) Binds to human adenovirus gene promoters and contributes to transcriptional repression and virus growth inhibition during early stages of infection. {ECO:0000269|PubMed:25210186}.
|
Homo sapiens (Human)
|
O96007
|
MOC2B_HUMAN
|
MSSLEISSSCFSLETKLPLSPPLVEDSAFEPSRKDMDEVEEKSKDVINFTAEKLSVDEVSQLVISPLCGAISLFVGTTRNNFEGKKVISLEYEAYLPMAENEVRKICSDIRQKWPVKHIAVFHRLGLVPVSEASIIIAVSSAHRAASLEAVSYAIDTLKAKVPIWKKEIYEESSTWKGNKECFWASNS
|
2.8.1.12
| null |
Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; molybdopterin cofactor biosynthetic process [GO:0032324]
|
cytosol [GO:0005829]; molybdopterin synthase complex [GO:0019008]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]
|
molybdopterin synthase activity [GO:0030366]
|
PF02391;
|
3.90.1170.40;
|
MoaE family, MOCS2B subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:15073332}.
|
CATALYTIC ACTIVITY: Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58698, ChEBI:CHEBI:59648, ChEBI:CHEBI:90619, ChEBI:CHEBI:90778; EC=2.8.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:12732628, ECO:0000269|PubMed:15073332};
| null |
PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03052}.
| null | null |
FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group. {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:12732628, ECO:0000269|PubMed:15073332}.
|
Homo sapiens (Human)
|
O96008
|
TOM40_HUMAN
|
MGNVLAASSPPAGPPPPPAPALVGLPPPPPSPPGFTLPPLGGSLGAGTSTSRSSERTPGAATASASGAAEDGACGCLPNPGTFEECHRKCKELFPIQMEGVKLTVNKGLSNHFQVNHTVALSTIGESNYHFGVTYVGTKQLSPTEAFPVLVGDMDNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSGILVAHYLQSITPCLALGGELVYHRRPGEEGTVMSLAGKYTLNNWLATVTLGQAGMHATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDLPKANLLFKGSVDSNWIVGATLEKKLPPLPLTLALGAFLNHRKNKFQCGFGLTIG
| null | null |
monoatomic ion transport [GO:0006811]; protein import into mitochondrial matrix [GO:0030150]; protein insertion into mitochondrial outer membrane [GO:0045040]; protein targeting to mitochondrion [GO:0006626]
|
cytosol [GO:0005829]; membrane [GO:0016020]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]; pore complex [GO:0046930]; TOM complex [GO:0140596]
|
porin activity [GO:0015288]; protein transmembrane transporter activity [GO:0008320]
|
PF01459;
|
2.40.160.10;
|
Tom40 family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:15644312, ECO:0000269|PubMed:31206022}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with the mitochondria-associated ER membrane via interaction with BCAP31. {ECO:0000269|PubMed:31206022}.
| null | null | null | null | null |
FUNCTION: Channel-forming protein essential for import of protein precursors into mitochondria (PubMed:15644312, PubMed:31206022). Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by forming a complex with BCAP31 and mediating the translocation of Complex I components from the cytosol to the mitochondria (PubMed:31206022). {ECO:0000269|PubMed:15644312, ECO:0000269|PubMed:31206022}.
|
Homo sapiens (Human)
|
O96009
|
NAPSA_HUMAN
|
MSPPPLLQPLLLLLPLLNVEPSGATLIRIPLHRVQPGRRILNLLRGWREPAELPKLGAPSPGDKPIFVPLSNYRDVQYFGEIGLGTPPQNFTVAFDTGSSNLWVPSRRCHFFSVPCWLHHRFDPKASSSFQANGTKFAIQYGTGRVDGILSEDKLTIGGIKGASVIFGEALWEPSLVFAFAHFDGILGLGFPILSVEGVRPPMDVLVEQGLLDKPVFSFYLNRDPEEPDGGELVLGGSDPAHYIPPLTFVPVTVPAYWQIHMERVKVGPGLTLCAKGCAAILDTGTSLITGPTEEIRALHAAIGGIPLLAGEYIILCSEIPKLPAVSFLLGGVWFNLTAHDYVIQTTRNGVRLCLSGFQALDVPPPAGPFWILGDVFLGTYVAVFDRGDMKSSARVGLARARTRGADLGWGETAQAQFPG
|
3.4.23.-
| null |
membrane protein proteolysis [GO:0033619]; proteolysis [GO:0006508]; surfactant homeostasis [GO:0043129]
|
alveolar lamellar body [GO:0097208]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lysosome [GO:0005764]; multivesicular body lumen [GO:0097486]
|
aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]
|
PF00026;
|
2.40.70.10;
|
Peptidase A1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in processing of pneumocyte surfactant precursors.
|
Homo sapiens (Human)
|
O96011
|
PX11B_HUMAN
|
MDAWVRFSAQSQARERLCRAAQYACSLLGHALQRHGASPELQKQIRQLESHLSLGRKLLRLGNSADALESAKRAVHLSDVVLRFCITVSHLNRALYFACDNVLWAGKSGLAPRVDQEKWAQRSFRYYLFSLIMNLSRDAYEIRLLMEQESSACSRRLKGSGGGVPGGSETGGLGGPGTPGGGLPQLALKLRLQVLLLARVLRGHPPLLLDVVRNACDLFIPLDKLGLWRCGPGIVGLCGLVSSILSILTLIYPWLRLKP
| null | null |
peroxisome fission [GO:0016559]; peroxisome organization [GO:0007031]; regulation of peroxisome size [GO:0044375]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]
|
identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF05648;
| null |
Peroxin-11 family
| null |
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670, ECO:0000269|PubMed:9826565}; Single-pass membrane protein {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:9792670, ECO:0000269|PubMed:9826565}.
| null | null | null | null | null |
FUNCTION: Involved in peroxisomal proliferation (PubMed:9792670). May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane (PubMed:12618434). Promotes membrane protrusion and elongation on the peroxisomal surface (PubMed:20826455). {ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670}.
|
Homo sapiens (Human)
|
O96013
|
PAK4_HUMAN
|
MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEEPATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPLSGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIPQSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell migration [GO:0016477]; cellular response to organic cyclic compound [GO:0071407]; cytoskeleton organization [GO:0007010]; dendritic spine development [GO:0060996]; intracellular signal transduction [GO:0035556]; negative regulation of endothelial cell apoptotic process [GO:2000352]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; regulation of cell growth [GO:0001558]; regulation of MAPK cascade [GO:0043408]; signal transduction [GO:0007165]
|
adherens junction [GO:0005912]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]
|
ATP binding [GO:0005524]; cadherin binding involved in cell-cell adhesion [GO:0098641]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00786;PF00069;
|
3.90.810.10;1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Autophosphorylated on serine residues when activated by CDC42/p21 (Ref.32). Phosphorylated on tyrosine residues upon stimulation of FGFR2 (By similarity). Methylated by SETD6. {ECO:0000250|UniProtKB:Q8BTW9, ECO:0000269|PubMed:30189201, ECO:0000269|Ref.32}.; PTM: Polyubiquitinated, leading to its proteasomal degradation. {ECO:0000269|PubMed:24130170}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12356872}. Note=Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways. {ECO:0000269|PubMed:12356872}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN. {ECO:0000269|PubMed:11278822, ECO:0000269|PubMed:11313478, ECO:0000269|PubMed:14560027, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:20507994, ECO:0000269|PubMed:20631255, ECO:0000269|PubMed:20805321, ECO:0000269|PubMed:26607847}.
|
Homo sapiens (Human)
|
O96014
|
WNT11_HUMAN
|
MRARPQVCEALLFALALQTGVCYGIKWLALSKTPSALALNQTQHCKQLEGLVSAQVQLCRSNLELMHTVVHAAREVMKACRRAFADMRWNCSSIELAPNYLLDLERGTRESAFVYALSAAAISHAIARACTSGDLPGCSCGPVPGEPPGPGNRWGGCADNLSYGLLMGAKFSDAPMKVKKTGSQANKLMRLHNSEVGRQALRASLEMKCKCHGVSGSCSIRTCWKGLQELQDVAADLKTRYLSATKVVHRPMGTRKHLVPKDLDIRPVKDSELVYLQSSPDFCMKNEKVGSHGTQDRQCNKTSNGSDSCDLMCCGRGYNPYTDRVVERCHCKYHWCCYVTCRRCERTVERYVCK
| null | null |
adrenal gland development [GO:0030325]; artery morphogenesis [GO:0048844]; atrial septum development [GO:0003283]; bicellular tight junction assembly [GO:0070830]; bone mineralization [GO:0030282]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cellular response to mechanical stimulus [GO:0071260]; cellular response to retinoic acid [GO:0071300]; cloacal septation [GO:0060197]; convergent extension involved in axis elongation [GO:0060028]; embryonic skeletal system development [GO:0048706]; epithelial cell apoptotic process [GO:1904019]; epithelial to mesenchymal transition [GO:0001837]; lung-associated mesenchyme development [GO:0060484]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; mesenchymal cell proliferation [GO:0010463]; mesonephric duct development [GO:0072177]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cartilage development [GO:0061037]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fibroblast growth factor production [GO:0090272]; negative regulation of mesenchymal cell proliferation [GO:0072201]; negative regulation of stem cell proliferation [GO:2000647]; neuroendocrine cell differentiation [GO:0061101]; neuron differentiation [GO:0030182]; notochord morphogenesis [GO:0048570]; osteoblast differentiation [GO:0001649]; outflow tract morphogenesis [GO:0003151]; paraxial mesoderm formation [GO:0048341]; planar cell polarity pathway involved in axis elongation [GO:0003402]; planar cell polarity pathway involved in gastrula mediolateral intercalation [GO:0060775]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell apoptotic process [GO:1904037]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein kinase C signaling [GO:0090037]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transforming growth factor beta2 production [GO:0032915]; primary heart field specification [GO:0003138]; protein localization to cell surface [GO:0034394]; protein phosphorylation [GO:0006468]; response to nutrient levels [GO:0031667]; secondary heart field specification [GO:0003139]; secondary palate development [GO:0062009]; signal transduction [GO:0007165]; somite development [GO:0061053]; stem cell proliferation [GO:0072089]; ureteric bud morphogenesis [GO:0060675]; ventricular septum morphogenesis [GO:0060412]; Wnt signaling pathway, calcium modulating pathway [GO:0007223]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]
|
cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; GTPase activator activity [GO:0005096]; protein kinase activator activity [GO:0030295]
|
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.
| null | null | null | null | null |
FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.
|
Homo sapiens (Human)
|
O96015
|
DNAL4_HUMAN
|
MGETEGKKDEADYKRLQTFPLVRHSDMPEEMRVETMELCVTACEKFSNNNESAAKMIKETMDKKFGSSWHVVIGEGFGFEITHEVKNLLYLYFGGTLAVCVWKCS
| null | null |
microtubule-based movement [GO:0007018]
|
cilium [GO:0005929]; cytoplasm [GO:0005737]; dynein complex [GO:0030286]; microtubule [GO:0005874]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; microtubule motor activity [GO:0003777]
|
PF01221;
|
3.30.740.10;
|
Dynein light chain family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O96017
|
CHK2_HUMAN
|
MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCAAVL
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
cell division [GO:0051301]; cellular response to gamma radiation [GO:0071480]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:0006978]; double-strand break repair [GO:0006302]; G2/M transition of mitotic cell cycle [GO:0000086]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; mitotic spindle assembly [GO:0090307]; positive regulation of DNA-templated transcription [GO:0045893]; protein autophosphorylation [GO:0046777]; protein catabolic process [GO:0030163]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of DNA-templated transcription [GO:0006355]; regulation of protein catabolic process [GO:0042176]; regulation of signal transduction by p53 class mediator [GO:1901796]; replicative senescence [GO:0090399]; signal transduction in response to DNA damage [GO:0042770]; thymocyte apoptotic process [GO:0070242]
|
cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ubiquitin protein ligase binding [GO:0031625]
|
PF00498;PF00069;
|
2.60.200.20;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CHK2 subfamily
|
PTM: Phosphorylated. Phosphorylated at Ser-73 by PLK3 in response to DNA damage, promoting phosphorylation at Thr-68 by ATM and the G2/M transition checkpoint. Phosphorylation at Thr-68 induces homodimerization. Autophosphorylates at Thr-383 and Thr-387 in the T-loop/activation segment upon dimerization to become fully active and phosphorylate its substrates like for instance CDC25C. DNA damage-induced autophosphorylation at Ser-379 induces CUL1-mediated ubiquitination and regulates the pro-apoptotic function. Phosphorylation at Ser-456 also regulates ubiquitination. Phosphorylated by PLK4. {ECO:0000269|PubMed:10973490, ECO:0000269|PubMed:11390408, ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:16311512, ECO:0000269|PubMed:16481012, ECO:0000269|PubMed:17715138, ECO:0000269|PubMed:18644861, ECO:0000269|PubMed:19164942}.; PTM: Ubiquitinated. CUL1-mediated ubiquitination regulates the pro-apoptotic function. Ubiquitination may also regulate protein stability. Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination.
|
SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Note=Isoform 10 is present throughout the cell.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 7]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 9]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 12]: Nucleus.; SUBCELLULAR LOCATION: Nucleus, PML body. Nucleus, nucleoplasm. Note=Recruited into PML bodies together with TP53.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:37943659}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates numerous effectors preferentially at the consensus sequence [L-X-R-X-X-S/T] (PubMed:37943659). Regulates cell cycle checkpoint arrest through phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their activity. Inhibition of CDC25 phosphatase activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. May also phosphorylate NEK6 which is involved in G2/M cell cycle arrest. Regulates DNA repair through phosphorylation of BRCA2, enhancing the association of RAD51 with chromatin which promotes DNA repair by homologous recombination. Also stimulates the transcription of genes involved in DNA repair (including BRCA2) through the phosphorylation and activation of the transcription factor FOXM1. Regulates apoptosis through the phosphorylation of p53/TP53, MDM4 and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may alleviate inhibition by MDM2, leading to accumulation of active p53/TP53. Phosphorylation of MDM4 may also reduce degradation of p53/TP53. Also controls the transcription of pro-apoptotic genes through phosphorylation of the transcription factor E2F1. Tumor suppressor, it may also have a DNA damage-independent function in mitotic spindle assembly by phosphorylating BRCA1. Its absence may be a cause of the chromosomal instability observed in some cancer cells. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition (PubMed:25361978). Under oxidative stress, promotes ATG7 ubiquitination by phosphorylating the E3 ubiquitin ligase TRIM32 at 'Ser-55' leading to positive regulation of the autophagosme assembly (PubMed:37943659). {ECO:0000250|UniProtKB:Q9Z265, ECO:0000269|PubMed:10097108, ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11298456, ECO:0000269|PubMed:12402044, ECO:0000269|PubMed:12607004, ECO:0000269|PubMed:12717439, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:16163388, ECO:0000269|PubMed:17101782, ECO:0000269|PubMed:17380128, ECO:0000269|PubMed:17715138, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:18644861, ECO:0000269|PubMed:18728393, ECO:0000269|PubMed:20364141, ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:25619829, ECO:0000269|PubMed:37943659, ECO:0000269|PubMed:9836640, ECO:0000269|PubMed:9889122}.; FUNCTION: (Microbial infection) Phosphorylates herpes simplex virus 1/HHV-1 protein ICP0 and thus activates its SUMO-targeted ubiquitin ligase activity. {ECO:0000269|PubMed:32001251}.
|
Homo sapiens (Human)
|
O96018
|
APBA3_HUMAN
|
MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAPCPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASAEQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTSTRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQDHGRRLYKMLCHVFYAEDAQLIAQAIGQAFAAAYSQFLRESGIDPSQVGVHPSPGACHLHNGDLDHFSNSDNCREVHLEKRRGEGLGVALVESGWGSLLPTAVIANLLHGGPAERSGALSIGDRLTAINGTSLVGLPLAACQAAVRETKSQTSVTLSIVHCPPVTTAIIHRPHAREQLGFCVEDGIICSLLRGGIAERGGIRVGHRIIEINGQSVVATPHARIIELLTEAYGEVHIKTMPAATYRLLTGQEQPVYL
| null | null |
chemical synaptic transmission [GO:0007268]; in utero embryonic development [GO:0001701]; negative regulation of catalytic activity [GO:0043086]; protein transport [GO:0015031]; regulation of gene expression [GO:0010468]
|
cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
amyloid-beta binding [GO:0001540]; enzyme binding [GO:0019899]; enzyme inhibitor activity [GO:0004857]
|
PF00595;PF00640;
|
2.30.42.10;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19726677}.
| null | null | null | null | null |
FUNCTION: May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN. {ECO:0000269|PubMed:19726677}.
|
Homo sapiens (Human)
|
O96019
|
ACL6A_HUMAN
|
MSGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGDKGKQGGPTYYIDTNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHPVLMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKRKEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGAERLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQSFTDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP
| null | null |
blastocyst formation [GO:0001825]; chromatin remodeling [GO:0006338]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; negative regulation of cell differentiation [GO:0045596]; nervous system development [GO:0007399]; neural retina development [GO:0003407]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of telomere maintenance in response to DNA damage [GO:1904507]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle [GO:0051726]; regulation of chromosome organization [GO:0033044]; regulation of DNA repair [GO:0006282]; regulation of DNA replication [GO:0006275]; regulation of DNA strand elongation [GO:0060382]; regulation of DNA-templated transcription [GO:0006355]; regulation of double-strand break repair [GO:2000779]; regulation of embryonic development [GO:0045995]; regulation of G0 to G1 transition [GO:0070316]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357]; signal transduction [GO:0007165]; spinal cord development [GO:0021510]; telomere maintenance [GO:0000723]
|
brahma complex [GO:0035060]; chromatin [GO:0000785]; GBAF complex [GO:0140288]; Ino80 complex [GO:0031011]; kinetochore [GO:0000776]; npBAF complex [GO:0071564]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514]
|
chromatin binding [GO:0003682]; transcription coactivator activity [GO:0003713]
|
PF00022;
|
3.30.420.40;
|
Actin family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18026119}.
| null | null | null | null | null |
FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000250|UniProtKB:Q9Z2N8, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:15196461, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
|
Homo sapiens (Human)
|
O96020
|
CCNE2_HUMAN
|
MSRRSSRLQAKQQPQPSQTESPQEAQIIQAKKRKTTQDVKKRREEVTKKHQYEIRNCWPPVLSGGISPCIIIETPHKEIGTSDFSRFTNYRFKNLFINPSPLPDLSWGCSKEVWLNMLKKESRYVHDKHFEVLHSDLEPQMRSILLDWLLEVCEVYTLHRETFYLAQDFFDRFMLTQKDINKNMLQLIGITSLFIASKLEEIYAPKLQEFAYVTDGACSEEDILRMELIILKALKWELCPVTIISWLNLFLQVDALKDAPKVLLPQYSQETFIQIAQLLDLCILAIDSLEFQYRILTAAALCHFTSIEVVKKASGLEWDSISECVDWMVPFVNVVKSTSPVKLKTFKKIPMEDRHNIQTHTNYLAMLEEVNYINTFRKGGQLSPVCNGGIMTPPKSTEKPPGKH
| null | null |
cell division [GO:0051301]; DNA replication initiation [GO:0006270]; G1/S transition of mitotic cell cycle [GO:0000082]; homologous chromosome pairing at meiosis [GO:0007129]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of protein localization [GO:0032880]; telomere maintenance [GO:0000723]
|
centrosome [GO:0005813]; cyclin E1-CDK2 complex [GO:0097134]; cyclin E2-CDK2 complex [GO:0097135]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]; protein kinase binding [GO:0019901]
|
PF02984;PF00134;
|
1.10.472.10;
|
Cyclin family, Cyclin E subfamily
|
PTM: Phosphorylation by CDK2 triggers its release from CDK2 and degradation via the ubiquitin proteasome pathway. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9840943}.
| null | null | null | null | null |
FUNCTION: Essential for the control of the cell cycle at the late G1 and early S phase.
|
Homo sapiens (Human)
|
O96024
|
B3GT4_HUMAN
|
MQLRLFRRLLLAALLLVIVWTLFGPSGLGEELLSLSLASLLPAPASPGPPLALPRLLIPNQEACSGPGAPPFLLILVCTAPENLNQRNAIRASWGGLREARGLRVQTLFLLGEPNAQHPVWGSQGSDLASESAAQGDILQAAFQDSYRNLTLKTLSGLNWAEKHCPMARYVLKTDDDVYVNVPELVSELVLRGGRWGQWERSTEPQREAEQEGGQVLHSEEVPLLYLGRVHWRVNPSRTPGGRHRVSEEQWPHTWGPFPPYASGTGYVLSASAVQLILKVASRAPLLPLEDVFVGVSARRGGLAPTQCVKLAGATHYPLDRCCYGKFLLTSHRLDPWKMQEAWKLVGGSDGERTAPFCSWFQGVLGILRCRAIAWLQS
|
2.4.1.62
| null |
ganglioside biosynthetic process [GO:0001574]; glycosphingolipid biosynthetic process [GO:0006688]; oligosaccharide biosynthetic process [GO:0009312]; protein O-linked glycosylation [GO:0006493]
|
Golgi membrane [GO:0000139]
|
ganglioside galactosyltransferase activity [GO:0047915]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]
|
PF01762;
|
3.90.550.50;
|
Glycosyltransferase 31 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z0F0}; Single-pass type II membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 (d18:1(4E)) + UDP-alpha-D-galactose = a ganglioside GM1 (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:16773, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:71502, ChEBI:CHEBI:77709; EC=2.4.1.62; Evidence={ECO:0000269|PubMed:9582303}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16774; Evidence={ECO:0000269|PubMed:9582303}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 + UDP-alpha-D-galactose = a ganglioside GM1 + H(+) + UDP; Xref=Rhea:RHEA:48280, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:79218, ChEBI:CHEBI:82639; Evidence={ECO:0000250|UniProtKB:Q9Z0F0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48281; Evidence={ECO:0000250|UniProtKB:Q9Z0F0}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD2 (d18:1(4E)) + UDP-alpha-D-galactose = a ganglioside GD1b (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:47568, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:78542, ChEBI:CHEBI:87785; Evidence={ECO:0000250|UniProtKB:O88178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47569; Evidence={ECO:0000250|UniProtKB:O88178}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA2 (d18:1(4E)) + UDP-alpha-D-galactose = a ganglioside GA1 (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41960, ChEBI:CHEBI:15378, ChEBI:CHEBI:27731, ChEBI:CHEBI:27938, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; Evidence={ECO:0000250|UniProtKB:O88178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41961; Evidence={ECO:0000250|UniProtKB:O88178};
| null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis. {ECO:0000269|PubMed:9582303}.
|
Homo sapiens (Human)
|
O96028
|
NSD2_HUMAN
|
MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEGVMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNGSPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLEQGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQAPTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVAKEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGKSTPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASGEEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKRNRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVCKESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKGKMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKNALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKPTDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAKRDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSGFLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCTKAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGRSYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK
|
2.1.1.357
| null |
atrial septum primum morphogenesis [GO:0003289]; atrial septum secundum morphogenesis [GO:0003290]; bone development [GO:0060348]; double-strand break repair [GO:0006302]; membranous septum morphogenesis [GO:0003149]; methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; regulation of DNA-templated transcription [GO:0006355]; regulation of double-strand break repair via nonhomologous end joining [GO:2001032]; regulation of establishment of protein localization [GO:0070201]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; histone H3 methyltransferase activity [GO:0140938]; histone H3K36 dimethyltransferase activity [GO:0140954]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K36 trimethyltransferase activity [GO:0140955]; histone H4K20 methyltransferase activity [GO:0042799]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565]
|
PF17907;PF17982;PF00505;PF00628;PF00855;PF00856;
|
2.30.30.140;1.10.30.10;2.170.270.10;3.30.40.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, SET2 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}. Chromosome {ECO:0000250|UniProtKB:Q8BVE8}. Note=In embryonic stem (ES) cells, localizes to small foci, probably corresponding to euchromatin (By similarity). In B-cells, localizes to Ig heavy chain switch region during class switch recombination (By similarity). {ECO:0000250|UniProtKB:Q8BVE8}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}. Chromosome {ECO:0000269|PubMed:15677557}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}. Nucleus, nucleolus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(36)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60312, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9786, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:19808676, ECO:0000269|PubMed:22099308}; CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60308, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.357; Evidence={ECO:0000269|PubMed:19808676, ECO:0000269|PubMed:22099308, ECO:0000269|PubMed:27571355, ECO:0000269|PubMed:29728617};
| null | null | null | null |
FUNCTION: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:19808676, PubMed:22099308, PubMed:27571355, PubMed:29728617, PubMed:33941880). Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro (PubMed:22099308). Does not trimethylate nucleosomal histone H3 at 'Lys-36' (H3K36me3) (PubMed:22099308). However, specifically trimethylates histone H3 at 'Lys-36' (H3K36me3) at euchromatic regions in embryonic stem (ES) cells (By similarity). By methylating histone H3 at 'Lys-36', involved in the regulation of gene transcription during various biological processes (PubMed:16115125, PubMed:22099308, PubMed:29728617). In ES cells, associates with developmental transcription factors such as SALL1 and represses inappropriate gene transcription mediated by histone deacetylation (By similarity). During heart development, associates with transcription factor NKX2-5 to repress transcription of NKX2-5 target genes (By similarity). Plays an essential role in adipogenesis, by regulating expression of genes involved in pre-adipocyte differentiation (PubMed:29728617). During T-cell receptor (TCR) and CD28-mediated T-cell activation, promotes the transcription of transcription factor BCL6 which is required for follicular helper T (Tfh) cell differentiation (By similarity). During B-cell development, required for the generation of the B1 lineage (By similarity). During B2 cell activation, may contribute to the control of isotype class switch recombination (CRS), splenic germinal center formation, and the humoral immune response (By similarity). Plays a role in class switch recombination of the immunoglobulin heavy chain (IgH) locus during B-cell activation (By similarity). By regulating the methylation of histone H3 at 'Lys-36' and histone H4 at 'Lys-20' at the IgH locus, involved in TP53BP1 recruitment to the IgH switch region and promotes the transcription of IgA (By similarity). {ECO:0000250|UniProtKB:Q8BVE8, ECO:0000269|PubMed:16115125, ECO:0000269|PubMed:19808676, ECO:0000269|PubMed:22099308, ECO:0000269|PubMed:27571355, ECO:0000269|PubMed:29728617, ECO:0000269|PubMed:33941880}.; FUNCTION: [Isoform 1]: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2). {ECO:0000269|PubMed:22099308}.; FUNCTION: [Isoform 4]: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:22099308). Methylation of histone H3 at 'Lys-27' is controversial (PubMed:18172012, PubMed:22099308). Mono-, di- or tri-methylates histone H3 at 'Lys-27' (H3K27me, H3K27me2 and H3K27me3) (PubMed:18172012). Does not methylate histone H3 at 'Lys-27' (PubMed:22099308). May act as a transcription regulator that binds DNA and suppresses IL5 transcription through HDAC recruitment (PubMed:11152655, PubMed:18172012). {ECO:0000269|PubMed:11152655, ECO:0000269|PubMed:18172012, ECO:0000269|PubMed:22099308}.
|
Homo sapiens (Human)
|
O96033
|
MOC2A_HUMAN
|
MVPLCQVEVLYFAKSAEITGVRSETISVPQEIKALQLWKEIETRHPGLADVRNQIIFAVRQEYVELGDQLLVLQPGDEIAVIPPISGG
| null | null |
Mo-molybdopterin cofactor biosynthetic process [GO:0006777]
|
cytosol [GO:0005829]; molybdopterin synthase complex [GO:0019008]
|
molybdopterin synthase activity [GO:0030366]; nucleotide binding [GO:0000166]
|
PF02597;
|
3.10.20.30;
|
MoaD family, MOCS2A subfamily
|
PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3. {ECO:0000255|HAMAP-Rule:MF_03051, ECO:0000269|PubMed:12732628, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:15910006, ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18491921}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03051, ECO:0000269|PubMed:15073332}.
| null | null |
PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03051}.
| null | null |
FUNCTION: Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin. {ECO:0000255|HAMAP-Rule:MF_03051, ECO:0000269|PubMed:12732628}.
|
Homo sapiens (Human)
|
O96390
|
RACF1_DICDI
|
MQNIKCVVVGDGAVGKTCMLISYTTNGFPSEYIPTVFDNYCANLMLEGKPYSLGLWDTAGQEDYDRLRPLSYPHTDVFLICFSIISQASFENVTTKWFKEVNHHAPGVPIILVGTKQDIRNDNDSIKKLKEKNIELVPYEKGLEKAKEINAIYLEASALTQRGIKDVFDQCIRSVIYPNKLIKKPKKKSCTIM
| null | null |
actin filament organization [GO:0007015]; cortical cytoskeleton organization [GO:0030865]; engulfment of apoptotic cell [GO:0043652]; establishment or maintenance of cell polarity [GO:0007163]; mitotic cytokinesis [GO:0000281]; motor neuron axon guidance [GO:0008045]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; response to imidacloprid [GO:1902351]; sexual reproduction [GO:0019953]; signal transduction [GO:0007165]; small GTPase-mediated signal transduction [GO:0007264]
|
cell cortex [GO:0005938]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; macropinosome [GO:0044354]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rho family
| null |
SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
| null | null | null | null | null |
FUNCTION: Might act in concert and/or share functions with other members of the RHO family in the regulation of a subset of cytoskeletal rearrangements that are required for these processes.
|
Dictyostelium discoideum (Social amoeba)
|
O96433
|
CCNT_DROME
|
MSLLATPMPQAATASSSSSASAAASASGIPITANNNLPFEKDKIWYFSNDQLANSPSRRCGIKGDDELQYRQMTAYLIQEMGQRLQVSQLCINTAIVYMHRFYAFHSFTHFHRNSMASASLFLAAKVEEQPRKLEHVIRAANKCLPPTTEQNYAELAQELVFNENVLLQTLGFDVAIDHPHTHVVRTCQLVKACKDLAQTSYFLASNSLHLTSMCLQYRPTVVACFCIYLACKWSRWEIPQSTEGKHWFYYVDKTVSLDLLKQLTDEFIAIYEKSPARLKSKLNSIKAIAQGASNRTANSKDKPKEDWKITEMMKGYHSNITTPPELLNGNDSRDRDRDRERERERERDPSSLLPPPAMVPQQRRQDGGHQRSSSVSGVPGSSSSSSSSSHKMPNYPGGMPPDAHTDHKSKQPGYNNRMPSSHQRSSSSGLGSSGSGSQRSSSSSSSSSQQPGRPSMPVDYHKSSRGMPPVGVGMPPHGSHKMTSGSKPQQPQQQPVPHPSASNSSASGMSSKDKSQSNKMYPNAPPPYSNSAPQNPLMSRGGYPGASNGSQPPPPAGYGGHRSKSGSTVHGMPPFEQQLPYSQSQSYGHMQQQPVPQSQQQQMPPEASQHSLQSKNSLFSPEWPDIKKEPMSQSQPQPFNGLLPPPAPPGHDYKLNSHPRDKESPKKERLTPTKKDKHRPVMPPVGSGNSSSGSGSSKPMLPPHKKQIPHGGDLLTNPGESGSLKRPNEISGSQYGLNKLDEIDNSNMPREKLRKLDTTTGLPTYPNYEEKHTPLNMSNGIETTPDLVRSLLKESLCPSNASLLKPDALTMPGLKPPAELLEPMPAPATIKKEQGITPMTSLASGPAPMDLEVPTKQAGEIKEESSSKSEKKKKKDKHKHKEKDKSKDKTEKEERKKHKKDKQKDRSGSGGSKDSSLPNEPLKMVIKNPNGSLQAGASAPIKLKISKNKVEPNNYSAAAGLPGAIGYGLPPTTATTTSASIGAAAPVLPPYGAGGGGYSSSGGSSSGGSSKKKHSDRDRDKESKKNKSQDYAKYNGAGGGIFNPLGGAGAAPNMSGGMGAPMSTAVPPSMLLAPTGAVPPSAAGLAPPPMPVYNKK
| null | null |
DNA-templated transcription [GO:0006351]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of transcription by RNA polymerase II [GO:0006357]; response to heat [GO:0009408]; ventral cord development [GO:0007419]
|
cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nucleus [GO:0005634]; P-TEFb complex [GO:0070691]; polytene chromosome [GO:0005700]; polytene chromosome puff [GO:0005703]; super elongation complex [GO:0032783]; transcription elongation factor complex [GO:0008023]
|
cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]
|
PF00134;PF21797;
|
1.10.472.10;
|
Cyclin family, Cyclin C subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II).
|
Drosophila melanogaster (Fruit fly)
|
O96553
|
C1TC_DROME
|
MSAQYQRFLKVLEKWPAEKSKVGSGEWTAEPAIKMSGAKIISGTAVAKSIREELRNEVTAMSKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKINDLNEDPRVHGIIVQMPLDCDTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLERLAKSQWALQTLPLKPQRPVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQALGAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTQKDKALYDRLVPAIKGQRKFSPIQLRRLQKLGITKTDPDTLTADEYGPFARLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVHAGPFANIAHGCNSIIADEVGLKLVGKNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVTPGAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAVVSTHWADGGAGAVQLADAVIKACEQGNQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGDAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGLF
|
1.5.1.5; 3.5.4.9; 6.3.4.3
| null |
amino acid biosynthetic process [GO:0008652]; histidine biosynthetic process [GO:0000105]; methionine biosynthetic process [GO:0009086]; purine nucleotide biosynthetic process [GO:0006164]; tetrahydrofolate interconversion [GO:0035999]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; formate-tetrahydrofolate ligase activity [GO:0004329]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488]
|
PF01268;PF00763;PF02882;
|
1.10.8.770;3.10.410.10;3.40.50.10860;3.40.50.720;3.40.50.300;
|
Tetrahydrofolate dehydrogenase/cyclohydrolase family; Formate--tetrahydrofolate ligase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000250|UniProtKB:P11586}; CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, ChEBI:CHEBI:195366; EC=3.5.4.9; Evidence={ECO:0000250|UniProtKB:P11586}; CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221, ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216; EC=6.3.4.3; Evidence={ECO:0000250|UniProtKB:P11586};
| null |
PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
| null | null | null |
Drosophila melanogaster (Fruit fly)
|
O96621
|
ARP2_DICDI
|
MDSNKVIVMDNGTGFVKCGFAGANFPTAIFPSMVGRPILRSEEKVENVEIKDIMVGDEAAKLRSMLQITYPLENGIIRNWDDITHVWDYALKEKLKVSDPTECKILLTEPPMNPVANRQKMIECMFEKYGFQAVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIIPVYEGYSIPHLTRRLDVAGRDVTRYLIKLLLLRGYAFNRTADFETIRQIKEKLCYVAYDVQQEMKLASETTVLVENYTLPDGRVIKVGQERFQASEALFNPSLVDVEGGGVHEQLFDCITKADRDLQQGFYQHIVLSGGSSMYPGLPSRLEKEIRSLYLERVLKGNKEGLAKFKCRIEDPPRRKHMVFLGGAVLADLTKDRDDFWITKAEYMEKGFGALDKLTKLSV
| null | null |
actin filament polymerization [GO:0030041]; aggregation involved in sorocarp development [GO:0031152]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; bleb assembly [GO:0032060]; chemotaxis to cAMP [GO:0043327]; exocytosis [GO:0006887]; hyperosmotic response [GO:0006972]; phagocytosis [GO:0006909]; response to mercury ion [GO:0046689]
|
Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytosol [GO:0005829]; polyphosphate kinase complex [GO:0009358]; pseudopodium [GO:0031143]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]
|
PF00022;
|
3.30.420.40;
|
Actin family, ARP2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11807934}. Cytoplasm, cytosol {ECO:0000269|PubMed:11425877}. Cytoplasm, cell cortex {ECO:0000269|PubMed:11425877}. Cell projection, pseudopodium {ECO:0000269|PubMed:11425877}.
| null | null | null | null | null |
FUNCTION: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions. {ECO:0000269|PubMed:11807934, ECO:0000269|PubMed:17553489}.
|
Dictyostelium discoideum (Social amoeba)
|
O96622
|
ARPC1_DICDI
|
MSAFEIEHLASCITAHAWNADRSRVALCPNNNEVHIYAKQGTSWVVEHVLAEHDQLVTSIDWAPKTNRILTSSQDRNAYVWTFKDGQWKPVLVLLRINRAATHVKWSPQENKFAVATGAKLVCICFFEEEHDWWASNHIKKHKSTVLKVDWHPNNLLLATSSSDYKVRVFDAYIKKADGRSVTRPYGEVAFGEPVFEFDQCASWVHALKWSPSGSTLAYSSHDGVFAVANFSTNPPTIEKLRVRNLPLRDLLYITENSIAGVGYDCAPLLITNQNGWKYSGEMDKASEGGAAAGSETSARKLFQNKVDLGESKSADKKLTTVHQNCITSIVPFKSVGGVVSDFSTSGLDGNIVVWHVKALEAKNKFKVI
| null | null |
actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]
|
Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cell projection [GO:0042995]; clathrin-coated pit [GO:0005905]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; filopodium [GO:0030175]; phagocytic cup [GO:0001891]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; pseudopodium [GO:0031143]
|
actin filament binding [GO:0051015]
|
PF00400;
|
2.130.10.10;
|
WD repeat ARPC1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium.
| null | null | null | null | null |
FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions. {ECO:0000269|PubMed:11807934}.
|
Dictyostelium discoideum (Social amoeba)
|
O96623
|
ARPC2_DICDI
|
MLLLETHNRILYDEVISHFEGDRRVNNIFADFDGVKFNVQTSDDKSSLMVSVSLHAAADLLKNGGSALLKSVYGDMLQAKPEGGYDVTLVIQSSFSGNKEELAKKVSLLKRHLVAAPFLMVFEGIEAKKPLPEIIAINYRTDETFYLKPQGDNVIVIFDIAFKDADDVILSKIFLQSFVDVRKTISNVPSITFSQKDPPLELKGVKGVRAGQANHGFVSFVLFPAHIKKPQESADLIQTFRDYLHYHIKCAKGYMHTSMRNRVESLIQVLNRAKPEPVNTVKRTITGKFFKQN
| null | null |
actin filament depolymerization [GO:0030042]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]
|
Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytosol [GO:0005829]; pseudopodium [GO:0031143]
|
actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200]
|
PF04045;
|
3.30.1460.20;
|
ARPC2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium.
| null | null | null | null | null |
FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions. {ECO:0000269|PubMed:11807934, ECO:0000269|PubMed:17553489}.
|
Dictyostelium discoideum (Social amoeba)
|
O96624
|
ARPC3_DICDI
|
MVYHSQFNDESAGFRLVGNVPILPLKTTHKGPAPKGDANSVDIIDEALDLFKANILFRNFEVQGNGDRVLIYLTLYITKCLLKIAPMNKADAEKALFLIAQEQFSIPGESAFPLGGLVTVPNTRDAADTLRQYFTQLRLELGVRLCQRVYAVDPSKANKWWICFSKRKFLNKAL
| null | null |
actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]; regulation of actin filament polymerization [GO:0030833]
|
Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytosol [GO:0005829]; pseudopodium [GO:0031143]
|
actin filament binding [GO:0051015]
|
PF04062;
|
1.10.1760.10;
|
ARPC3 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium.
| null | null | null | null | null |
FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions. {ECO:0000269|PubMed:11807934}.
|
Dictyostelium discoideum (Social amoeba)
|
O96625
|
ARPC4_DICDI
|
MSTAQVPYLNCIRNTLTASMCLQNFGSQIVERHNKPEVEVKTSKELVLNPVIIARNKNERVLIETSINSIRISVSIKKSDEVDVILAKKFVRFLQQRAENFIILRRKPVEGYDISFLVTNFHTENMFKHKLVDFIIQFMEDIDREISDLKLTLNARGRIVASEYLKNFA
| null | null |
actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]
|
Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytosol [GO:0005829]; pathogen-containing vacuole [GO:0140220]; pseudopodium [GO:0031143]
|
actin filament binding [GO:0051015]
|
PF05856;
|
3.30.1460.20;
|
ARPC4 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium.
| null | null | null | null | null |
FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions. {ECO:0000269|PubMed:11807934}.
|
Dictyostelium discoideum (Social amoeba)
|
O96626
|
ARPC5_DICDI
|
MNYEDDNVESGQAGKSDAEYKADIANREKEVTKALNAGKPQDALNVALADPPIYTKTGAIKDQNATIVLNLLGSFKDKDVETSVETLNDDQLDILMKYVYRGLATGENSPIFFKWHECVLKKGGAGTIIRVISEKKTV
| null | null |
actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; cell migration [GO:0016477]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]; regulation of actin filament polymerization [GO:0030833]
|
Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; pseudopodium [GO:0031143]
|
actin filament binding [GO:0051015]
|
PF04699;
|
1.25.40.190;
|
ARPC5 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium.
| null | null | null | null | null |
FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions. {ECO:0000269|PubMed:11807934}.
|
Dictyostelium discoideum (Social amoeba)
|
O96690
|
PDF_DROME
|
MARYTYLVALVLLAICCQWGYCGAMAMPDEERYVRKEYNRDLLDWFNNVGVGQFSPGQVATLCRYPLILENSLGPSVPIRKRNSELINSLLSLPKNMNDAGK
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; circadian rhythm [GO:0007623]; circadian sleep/wake cycle [GO:0042745]; eclosion rhythm [GO:0008062]; entrainment of circadian clock by photoperiod [GO:0043153]; gravitaxis [GO:0042332]; locomotor rhythm [GO:0045475]; mating behavior [GO:0007617]; neuropeptide signaling pathway [GO:0007218]; positive regulation of circadian sleep/wake cycle, wakefulness [GO:0010841]; regulation of circadian sleep/wake cycle [GO:0042749]; regulation of locomotor rhythm [GO:1904059]; response to paraquat [GO:1901562]
|
extracellular space [GO:0005615]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]
|
neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102]
|
PF06324;
| null |
Arthropod PDH family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Neuropeptide PDF is the main transmitter regulating circadian locomotor rhythms. Required to maintain behavioral rhythms under constant conditions by coordinating pacemaker interactions in the circadian system (PubMed:10619432, PubMed:10777797, PubMed:15356209). Together with CCHa1, involved in regulating intensity and periodicity of daytime activity, possibly by modulating rhythmic expression of circadian protein PER/period in a subset of clock neurons, but not TIM/timeless (PubMed:36786215). Acts on small and large ventral lateral neurons to control sleep and regulates the state transition from sleep to wake (PubMed:19038223, PubMed:19230663). {ECO:0000269|PubMed:10619432, ECO:0000269|PubMed:10777797, ECO:0000269|PubMed:15356209, ECO:0000269|PubMed:19038223, ECO:0000269|PubMed:19230663, ECO:0000269|PubMed:36786215}.
|
Drosophila melanogaster (Fruit fly)
|
O96693
|
DXR_PLAFX
|
MKKYIYIYFFFITITINDLVINNTSKCVSIERRKNNAYINYGIGYNGPDNKITKSRRCKRIKLCKKDLIDIGAIKKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDYKPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEHSAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGLEVIETHFLFDVDYNDIEVIVHKECIIHSCVEFIDKSVISQMYYPDMQIPILYSLTWPDRIKTNLKPLDLAQVSTLTFHKPSLEHFPCIKLAYQAGIKGNFYPTVLNASNEIANNLFLNNKIKYFDISSIISQVLESFNSQKVSENSEDLMKQILQIHSWAKDKATDIYNKHNSS
|
1.1.1.267
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22355528}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:22355528}; Note=Binds 1 divalent cation per subunit. Mg(2+) or Mn(2+). {ECO:0000269|PubMed:22355528};
|
isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process [GO:0051484]
|
apicoplast [GO:0020011]
|
1-deoxy-D-xylulose-5-phosphate reductoisomerase activity [GO:0030604]; manganese ion binding [GO:0030145]; NADPH binding [GO:0070402]
|
PF08436;PF02670;PF13288;
|
1.10.1740.10;3.40.50.720;
|
DXR family
| null |
SUBCELLULAR LOCATION: Plastid, apicoplast {ECO:0000269|PubMed:10477522}.
|
CATALYTIC ACTIVITY: Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000269|PubMed:10477522}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719; Evidence={ECO:0000305|PubMed:10477522};
| null |
PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000305|PubMed:10477522}.
| null | null |
FUNCTION: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000269|PubMed:10477522}.
|
Plasmodium falciparum (isolate HB3)
|
O96759
|
ADAS_DICDI
|
MSGEKKEYPKEHIDLYQQIKWNGWGDTRKFLHQLKPSGTIAMTTPEVSSVPLPSLRGFIKKELTLPGEEDKPFVLDETPALQIENIHVDPPKQYPEFVRELKAFFLPDQLKDDKLARITHTFGKSLRDLIRVRIGQVKNAPDLIVLPHSHEEVERLVQLAHKYNVVIIPMGGGSNIVGAIEPVSNERFTVSIDMRRMNKVLWVDRREMTACIQVGIMGPELEKQLHKQGVSLGHDPDSFEFSTLGGWLATCSSGHQSDKYGDIEDMAVSFRTVTPTGTLELRNGARSGAGINYKHIILGSEGTLGIITEAVMKVHAVPQAVEYYGFLFPTFAHAVSALQQIRSSEVIPTMIRVYDPEETQLSFAWKPSKGAVSEFTSAMVKKYLHYIRSFDFKNVCLSIIGFEGPKKVVDFHRTSVFDILSKNAAFGLGSAPGKTWAEKRYDLPYIRDFLLDHNMWVDVAETTVSYANLQTLWKDAKQTFVKHFKDQGIPAWICAHISHTYTNGVCLYFIFASKQNENKDMAQYIEAKKLMTDIIFKYGGSLSHHHGVGYEHVPWMTRYATRGWINVYRSLKETIDPKDICNPRKLIPTIKEENNKEPFLFDVVNVKYPKL
|
2.5.1.26
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17562315};
|
ether lipid biosynthetic process [GO:0008611]
|
peroxisome [GO:0005777]
|
alcohol binding [GO:0043178]; alkylglycerone-phosphate synthase activity [GO:0008609]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]
|
PF02913;PF01565;
|
3.40.462.40;3.30.43.10;
|
FAD-binding oxidoreductase/transferase type 4 family
| null |
SUBCELLULAR LOCATION: Peroxisome.
|
CATALYTIC ACTIVITY: Reaction=a 1-acylglycerone 3-phosphate + a long chain fatty alcohol = 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+); Xref=Rhea:RHEA:36171, ChEBI:CHEBI:15378, ChEBI:CHEBI:17135, ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:73315; EC=2.5.1.26; Evidence={ECO:0000269|PubMed:17562315};
| null |
PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
| null | null |
FUNCTION: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids. {ECO:0000269|PubMed:17562315}.
|
Dictyostelium discoideum (Social amoeba)
|
O96821
|
CDK2H_PLAKH
|
MEKYHGLEKIGEGTYGVVYKAQNNYGETFALKKIRLEKEDEGIPSTAIREISILKELKHSNIVKLYDVIHTKKRLILVFEHLDQDLKKLLDVCDGGLESVTAKSFLLQLLSGIAYCHEHRVLHRDLKPQNLLINREGELKIADFGLARAFGIPVRKYTHEVVTLWYRAPDILMGSKKYSTPIDIWSVGCIFAEMVNGRPLFPGVSETDQLMRIFRILGTPNSANWPSVTELPKYDPDFIVYEPLPWETFLKGLDDTGIDLLSKMLRLDPNQRITAKEALQHAYFKESS
|
2.7.11.22; 2.7.11.23
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P61075};
|
axonogenesis [GO:0007409]; cell cycle [GO:0007049]; cell division [GO:0051301]; phosphorylation [GO:0016310]; synaptic vesicle transport [GO:0048489]; vesicle-mediated transport [GO:0016192]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04551}.
|
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; Evidence={ECO:0000250|UniProtKB:P61075}; 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; Evidence={ECO:0000250|UniProtKB:P61075}; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; Evidence={ECO:0000250|UniProtKB:P61075};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase (By similarity). Involved in the control of the cell cycle. Required for entry into S-phase and mitosis (By similarity). Probable component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity). {ECO:0000250|UniProtKB:P04551, ECO:0000250|UniProtKB:P61075}.
|
Plasmodium knowlesi (strain H)
|
O96838
|
FYV1_DROME
|
MTSNNQNNSSSHQHLHSPSKLTEFARNFEDKPESLFGRVVNKIQNVYNQSYNTVNDISSGSSSSSSTQPVQVVGKSQFFSDSQTSTAEIADVETSSQSSVRPQPPTTLSIRTNSETRGTSTSSNTAAEDSETSDRVETLPLPTSEANQGRTVSNVLKHISNIVATKNNNDLRNYKDTELQRFWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYCSKIVLTFLKSSSSEMGQDMQELQQHLSNKLEVQDSGSSLAKHPQMQRAPLPRKTSVGYQEERFSSHPTYTTLSIDDRKNILQQSNSLITLHEEMQRDLPAQNCGQRLIEFLNSNNKSANEVQAVAILNAMLAAGFLEPIVPDPEQMDFDSSLHYKFSKSSSSDTSRTMSPQFEANPHAEPQPPKSMDQSAEEKEKELENELENDRCYTTATSKLLASYCEHEEQLLAQMLRAHNLDQEWDKVLQMLCSTAANHFKPEHCSNDLMDIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIEGKFVTIETVLLQEKEYLRNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIESNITMPKLGYCNDFYIRNYNGKTLMFFEKLTNPRGYTCLLRGGSNAELTRVKRVASALLFARYNWRLEMSFLLNEFAQPLSPKPSIFDSKETSPKTETEAELRSKRPIILERKSEDKITTIVSENVSDFTDPLRASQAEALSTSPCAPPVVEALAVEPRYDNRFRTALSSTLLSVSPFLTFPLPYLETEQGRKCKLRKLFPAELYFSKQWSRTGLERPDSMGDGEAGKSEPGNKENQMQLLPAHDFVLMKITAPASSRDIQSKLAEFRSFGGRLPKGKAPMLRPKKKNAEVIQRPQKVSEEQLYKDALDPQNHQRLPVLFCSFHYNPKGVSSFCKLPMLLDMKFYGQYDIMLEQFLQRYCCLFNSMCPSCNLPMLGHVRRYVHSLGCVHVYLTEDLTRSDPTRIYFTSWCSICNATTPTIPLSDAAKCLSLAKYLEMRFHGHAYKRRPPSTDAEQGGTVCEHSLHRDYVHHFSFRGVGAKFQYTPVEVWETDLPSLTVQLDLPQPFQSAQVQEEIKNFSIKGHEVYNRIHERIADLATEEENSPLVQHLKTMLTHDQFIFKQKIEIVHTLLTDNRATAYDTSDALAMARRALAESIELWGPRLQEIEKLTAKQAHHIDSGTICTEELRPEQVQTADSSKVTTSSLPKENDPLECPSEDTETGASNSQTVLDKNFSIDQMLASTVNVYSDKKSIRKILTQLLPSGNQVNPLQSPFPAQDHLTLPLGSIPIHVRETDLSSVIAYSLTSMDYQKAIDEAEANSNAAHSSPQLKRKIPLAESVSDAEDSPSLSRTSSNTSAAPNASVPSPATAASESEEKSKERIKQPPSPHITLAFQDHSCQFQCKIYFAREFDAMRSKSLKPPKLDKSLYRRLEKSKMREELRISQSRTGSEMELVRKPSDVGAPRTTEDDSNQEEDARIALARSLCKSVQWEARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQQQQPTLLAKIFGVFRVSVKKKDSFVERSVMVMENLFYGCNIENKFDLKGSERNRLVDPSNQQGEIVLLDENLVQMSWSKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMDYSLLVGLDKKNGVLVLGIIDYIRTFTLDKRVESIIKGSGILGGKGKDPTVVNPERYKQRFIDAMDRYFLTVPDRWEGLSKV
|
2.7.1.150
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
|
autophagosome maturation [GO:0097352]; endosome to lysosome transport [GO:0008333]; intracellular signal transduction [GO:0035556]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]
|
endosome [GO:0005768]; endosome membrane [GO:0010008]; vesicle membrane [GO:0012506]
|
1-phosphatidylinositol-3-phosphate 5-kinase activity [GO:0000285]; 1-phosphatidylinositol-5-kinase activity [GO:0052810]; ATP binding [GO:0005524]; zinc ion binding [GO:0008270]
|
PF00118;PF01363;PF01504;
|
3.30.810.10;3.50.7.10;3.30.800.10;3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:16837550}. Note=Mainly associated with membranes of the late endocytic pathway.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.150; Evidence={ECO:0000305|PubMed:16837550}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13610; Evidence={ECO:0000305|PubMed:16837550};
| null | null | null | null |
FUNCTION: Regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) or PtdIns(3,5)P2) (PubMed:16837550). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)) on the fifth hydroxyl of the myo-inositol ring, to form PtdIns(3,5)P2 (PubMed:16837550). Required for endocytic-vacuolar pathway and nuclear migration. Has a role at a late stage in endosome-related membrane trafficking, at a point when signal termination has occurred. Is not required for receptor silencing. {ECO:0000269|PubMed:16837550}.
|
Drosophila melanogaster (Fruit fly)
|
O96923
|
GNRA_DICDI
|
MEEDNIVDSKEIENNVEDKKEETPSSSPSPSSSLQQQQEEGGVVKQAVSNLVSSSITLHDDAKLIQVTGKDEPFHFISVPMSVEFLNLEDVFIMQSDAYIFVWCSEQANIKKKAKAVQMAQKLKVEIGCQRAVQVLEIGEEHPTFLFCLGVPKGTKLNVTKEKNDIFQVDEDDEEQVLEPEFFLFKIFTGTDGKPSIKPMEEDEGINQEMLESSACFILDCEHEMYIWLGKGVKKSTKDTLIPVAKKIWTQYDRPEYYGKLKLQPIITWVFDGAESCLFKSKFSKWVEKAQPLQTSYLSLSSKKKEALNFDVSSMHQDKEVPVINIGAASDYSNGKLLVWCSGGGSGNKWNKVEEDDFGIFYSNKSYVCHFIYKPENKNSIRSVIFFWEGLYSNQRNYIGYKFGLYKEIQKKMEGLKSDDPVEYRISQNKEPQEFINLFGTELLVLNEELALKPMIFQVRANRGTQLFPDPDSCNAKLLNSLDSFVFLFPNKYIIVWHGKVSTEHQRELAADLFTFLPPEYEAGVKEFDQGKESDNFWKIIGGNSNDIVINTFINENKEEKEKEEEEKEEEEEEEEEEEEEEEEEKDNNKTTTIIKHLRPKKIKLFLCTDNSGIFKADQINPFSQVDLNSQECVLLDVYHKVFLWKGSKSTDQKLNDTQDLAKQYIETANDQRPSDCSVELVEQYNESPLFKSYFHSWKVTPPKVFIDPIISYKQKLAERLQKEKEDLEKLKQQQEQEQEQQQKENNKIVEEVKEEVKEEDVKEEVKEEEVKEEEVKEEEVKEVAKEETKEEIKEEVNDEATEVKEVNQVEEEVKEEEVKEEVKVEVKEEEVKGEAKEEEVKEEEVKEEEVKEEVKEVKEEVKEEVKQDKEEEVNEEIKEETKEEETKEDDNKEDEKVNEENETVNEENEVGIIVSPPSEKVDEANSSSTISSPENEGSVSVKDKRKSNEPITPSVVSSSGDLLFAYEPYHGPPIHSSNSPKQGRKGGRKSHGKNQPQHKKNHSVDQSPLSSPIIPNKSLNLDIDNQSFDLNSINNNNSVEVLDGASSPLSFSSSSINSNSTHNTPSKKNKNKNKKKHNRSSSLTHA
| null | null |
actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]; phototaxis [GO:0042331]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]
|
actin filament binding [GO:0051015]; filamin binding [GO:0031005]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; small GTPase binding [GO:0031267]
|
PF00626;
|
3.40.20.10;
|
Villin/gelsolin family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:9880334}.
| null | null | null | null | null |
FUNCTION: Involved in phototaxis. Required for coupling photodetection to the locomotory machinery of slugs. May be essential in the natural environment for the propagation of spores. {ECO:0000269|PubMed:9880334}.
|
Dictyostelium discoideum (Social amoeba)
|
O96935
|
AMPN_PLAF7
|
MKLTKGCAYKYIIFTVLILANILYDNKKRCMIKKNLRISSCGIISRLLKSNSNYNSFNKNYNFTSAISELQFSNFWNLDILQKDIFSNIHNNKNKPQSYIIHKRLMSEKGDNNNNNHQNNNGNDNKKRLGSVVNNEENTCSDKRMKPFEEGHGITQVDKMNNNSDHLQQNGVMNLNSNNVENNNNNNSVVVKKNEPKIHYRKDYKPSGFIINNVTLNINIHDNETIVRSVLDMDISKHNVGEDLVFDGVGLKINEISINNKKLVEGEEYTYDNEFLTIFSKFVPKSKFAFSSEVIIHPETNYALTGLYKSKNIIVSQCEATGFRRITFFIDRPDMMAKYDVTVTADKEKYPVLLSNGDKVNEFEIPGGRHGARFNDPHLKPCYLFAVVAGDLKHLSATYITKYTKKKVELYVFSEEKYVSKLQWALECLKKSMAFDEDYFGLEYDLSRLNLVAVSDFNVGAMENKGLNIFNANSLLASKKNSIDFSYARILTVVGHEYFHNYTGNRVTLRDWFQLTLKEGLTVHRENLFSEEMTKTVTTRLSHVDLLRSVQFLEDSSPLSHPIRPESYVSMENFYTTTVYDKGSEVMRMYLTILGEEYYKKGFDIYIKKNDGNTATCEDFNYAMEQAYKMKKADNSANLNQYLLWFSQSGTPHVSFKYNYDAEKKQYSIHVNQYTKPDENQKEKKPLFIPISVGLINPENGKEMISQTTLELTKESDTFVFNNIAVKPIPSLFRGFSAPVYIEDNLTDEERILLLKYDSDAFVRYNSCTNIYMKQILMNYNEFLKAKNEKLESFNLTPVNAQFIDAIKYLLEDPHADAGFKSYIVSLPQDRYIINFVSNLDTDVLADTKEYIYKQIGDKLNDVYYKMFKSLEAKADDLTYFNDESHVDFDQMNMRTLRNTLLSLLSKAQYPNILNEIIEHSKSPYPSNWLTSLSVSAYFDKYFELYDKTYKLSKDDELLLQEWLKTVSRSDRKDIYEILKKLENEVLKDSKNPNDIRAVYLPFTNNLRRFHDISGKGYKLIAEVITKTDKFNPMVATQLCEPFKLWNKLDTKRQELMLNEMNTMLQEPNISNNLKEYLLRLTNKL
|
3.4.11.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:19196988, ECO:0000269|PubMed:21366301}; Note=Binds 1 zinc ion per subunit (PubMed:12166515, PubMed:19196988, PubMed:21366301, PubMed:21844374, PubMed:23713488, PubMed:23897806, PubMed:25299353, PubMed:25645579, PubMed:26406322, PubMed:26807544, PubMed:30537832, PubMed:32182520, Ref.21, Ref.24). Also, can use Mn(2+), Mg(2+) and Co(2+) with less efficiency (PubMed:12166515). {ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:19196988, ECO:0000269|PubMed:21366301, ECO:0000269|PubMed:21844374, ECO:0000269|PubMed:23713488, ECO:0000269|PubMed:23897806, ECO:0000269|PubMed:25299353, ECO:0000269|PubMed:25645579, ECO:0000269|PubMed:26406322, ECO:0000269|PubMed:26807544, ECO:0000269|PubMed:30537832, ECO:0000269|PubMed:32182520, ECO:0000269|Ref.21, ECO:0000269|Ref.24};
|
proteolysis [GO:0006508]
|
chloroplast [GO:0009507]; cytoplasm [GO:0005737]; food vacuole [GO:0020020]; membrane [GO:0016020]; nucleus [GO:0005634]; symbiont-containing vacuole membrane [GO:0020005]; vacuolar lumen [GO:0005775]
|
aminopeptidase activity [GO:0004177]; dipeptidase activity [GO:0016805]; metalloaminopeptidase activity [GO:0070006]; zinc ion binding [GO:0008270]
|
PF11940;PF17432;PF01433;PF17900;
|
2.60.40.1840;3.30.2010.30;1.10.390.10;1.25.50.10;2.60.40.1730;
|
Peptidase M1 family
|
PTM: The full length protein appears to be cleaved into a 120 kDa precursor. This precursor is then proteolytically cleaved at the N-terminus generating a 96 kDa form which is further processed at the C-terminus into 68 kDa and 35 kDa forms that remain associated. {ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:20591164, ECO:0000269|PubMed:21659511, ECO:0000269|PubMed:33536500, ECO:0000269|PubMed:9879894}.
|
SUBCELLULAR LOCATION: [Aminopeptidase N]: Parasitophorous vacuole membrane {ECO:0000269|PubMed:20591164}; Peripheral membrane protein {ECO:0000305}. Note=In trophozoites, partially localizes to the parasitophorous vacuole membrane. {ECO:0000269|PubMed:20591164}.; SUBCELLULAR LOCATION: [p120 form]: Nucleus {ECO:0000269|PubMed:21659511}.; SUBCELLULAR LOCATION: [p96 form]: Cytoplasm {ECO:0000269|PubMed:33536500}.; SUBCELLULAR LOCATION: [p68 form]: Cytoplasm {ECO:0000269|PubMed:33536500}. Vacuole lumen {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:20591164}. Note=In trophozoites, partially localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:20591164}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:9879894}. Note=In trophozoite and schizonts, localizes to the cytoplasm (PubMed:12166515). In trophozoites, also localizes around the digestive vacuole (PubMed:12166515). In schizonts, also localizes to discrete vesicle-like structures and in released merozoites localizes to a single discrete structure (PubMed:12166515). In ruptured schizonts, localizes around the digestive vacuole (PubMed:12166515). {ECO:0000269|PubMed:12166515}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=110 uM for Arg-betaNA (at pH 7.5 and 27 degrees Celsius) {ECO:0000269|PubMed:21659511}; KM=170 uM for Arg-betaNA (at pH 7.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=1100 uM for Arg-betaNA (at pH 5.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=210 uM for Ala-betaNA (at pH 7.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=4400 uM for Ala-betaNA (at pH 5.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=22 uM for Met-Phe (at pH 7.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=65 uM for Met-Phe (at pH 5.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=380 uM for Met-Phe (at pH 5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=130 uM for Leu-Leu (at pH 7.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=410 uM for Leu-Leu (at pH 5.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=1200 uM for Leu-Leu (at pH 5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; Note=kcat is 9.3 sec(-1) with for Arg-betaNA as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:21659511). kcat is 21 sec(-1) with for Arg-betaNA as substrate (at pH 7.5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 9.4 sec(-1) with for Arg-betaNA as substrate (at pH 5.5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 36 sec(-1) with for Ala-betaNA as substrate (at pH 7.5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 16 sec(-1) with for Ala-betaNA as substrate (at pH 5.5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 5.9 sec(-1) with for Met-Phe as substrate (at pH 7.5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 7.5 sec(-1) with for Met-Phe as substrate (at pH 5.5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 7.4 sec(-1) with for Met-Phe as substrate (at pH 5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 12 sec(-1) with for Leu-Leu as substrate (at pH 7.5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 7.9 sec(-1) with for Leu-Leu as substrate (at pH 5.5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). kcat is 1.4 sec(-1) with for Leu-Leu as substrate (at pH 5 and 37 degrees Celsius, recombinant protein) (PubMed:21659511). {ECO:0000269|PubMed:21659511}; Kinetic parameters: KM=86 uM for Arg-betaNA (at pH 7.5 and 27 degrees Celsius) {ECO:0000269|PubMed:21659511}; Note=kcat is 11 sec(-1) with for Arg-betaNA as substrate (at pH 7.5 and 37 degrees Celsius). {ECO:0000269|PubMed:21659511}; Kinetic parameters: KM=197 uM for H-Ala-NHMec (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:33536500}; KM=1276 uM for H-Ala-NHMec (at pH 5.2 and 37 degrees Celsius) {ECO:0000269|PubMed:33536500}; KM=197 uM for H-Leu-NHMec (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:33536500}; KM=1714 uM for H-Leu-NHMec (at pH 5.2 and 37 degrees Celsius) {ECO:0000269|PubMed:33536500}; KM=308 uM for H-Arg-NHMec (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:33536500}; KM=980 uM for H-Arg-NHMec (at pH 5.2 and 37 degrees Celsius) {ECO:0000269|PubMed:33536500}; KM=240.6 uM for Ala-ACC (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:22359643}; KM=214.3 uM for Arg-ACC (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:22359643}; KM=140.9 uM for Leu-ACC (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:22359643}; KM=218 uM for Phe-ACC (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:22359643}; KM=138.2 uM for Met-ACC (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:22359643}; KM=144.4 uM for Trp-ACC (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:22359643}; KM=173 uM for Leu-Mec (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:34133730}; Note=kcat is 0.9 sec(-1) with for H-Ala-NHMec as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:33536500). kcat is 0.4 sec(-1) with for H-Ala-NHMec as substrate (at pH 5.2 and 37 degrees Celsius) (PubMed:33536500). kcat is 0.8 sec(-1) with for H-Leu-NHMec as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:33536500). kcat is 0.7 sec(-1) with for H-Leu-NHMec as substrate (at pH 5.2 and 37 degrees Celsius) (PubMed:33536500). kcat is 0.7 sec(-1) with for H-Arg-NHMec as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:33536500). kcat is 0.4 sec(-1) with for H-Arg-NHMec as substrate (at pH 5.2 and 37 degrees Celsius) (PubMed:33536500). kcat is 1.054 sec(-1) with for Ala-ACC as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:22359643). kcat is 0.876 sec(-1) with for Arg-ACC as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:22359643). kcat is 0.868 sec(-1) with for Leu-ACC as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:22359643). kcat is 0.422 sec(-1) with for Phe-ACC as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:22359643). kcat is 0.887 sec(-1) with for Met-ACC as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:22359643). kcat is 0.444 sec(-1) with for Trp-ACC as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:22359643). kcat is 0.12 sec(-1) with for Leu-Mec as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:34133730). {ECO:0000269|PubMed:22359643, ECO:0000269|PubMed:33536500, ECO:0000269|PubMed:34133730};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 (PubMed:21659511). Active between 5-8.5 (PubMed:21659511). {ECO:0000269|PubMed:21659511}; pH dependence: Optimum pH is 7-7.5 (PubMed:19196988, PubMed:20591164, PubMed:33536500). Active from pH 5 to 9 (PubMed:19196988, PubMed:33536500). Has less than 20% of normal activity at pH 6.0 (PubMed:19196988). {ECO:0000269|PubMed:19196988, ECO:0000269|PubMed:20591164, ECO:0000269|PubMed:33536500};
| null |
FUNCTION: Displays aminopeptidase activity with a broad substrate specificity (PubMed:12166515, PubMed:19196988, PubMed:21659511, PubMed:21844374, PubMed:22359643, PubMed:23897806, PubMed:33536500, PubMed:34133730, PubMed:9879894). Preferentially, cleaves after Leu and Met, but cleaves also after Ala and Arg (PubMed:12166515, PubMed:21844374, PubMed:22359643, PubMed:33536500). Low activity towards Lys, Phe, Tyr, Trp, Gln, Ser and Gly and negligible activity towards Glu, Asp, Pro, Ile, Thr, Val, His and Asn (PubMed:22359643). Has dipeptidase activity (PubMed:21659511, PubMed:23897806). Plays a role in the terminal stages of host hemoglobin digestion by cleaving the N-terminal residue of small hemoglobin-derived oligopeptides (PubMed:21659511, PubMed:21844374, PubMed:34133730). {ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:19196988, ECO:0000269|PubMed:21659511, ECO:0000269|PubMed:21844374, ECO:0000269|PubMed:22359643, ECO:0000269|PubMed:23897806, ECO:0000269|PubMed:33536500, ECO:0000269|PubMed:34133730, ECO:0000269|PubMed:9879894}.
|
Plasmodium falciparum (isolate 3D7)
|
O97101
|
CBFA_DICDI
|
MEELIKAPNSNFIIMSNQPYQTTSPEIVEDYIIKRGQPFVLTGTTQGWSRSNMFTLDFLSERYSEMELINSPRNNETHTDLQGWRMKDFISYLQVSPEERNPKHLYGKDIACPREWQEYLSHKLQPQYSYKSRFDLVSHLPDYLQPETLLVYIGSNGTYTPGHIDMCGSLSQNLMVSSDQDAFAWWFIVPTEYKDEALKFWGDKGGDVYNESRFIRPIDLLGAPFPIYVFKQRPGDFIFVPPDSVHQVVNCGPGISTKVAWNSISLKSLPISYFSSLPHTRRMAKPELFRIKAIAYYTLRKIMGDVENTNFNTIDVNDVIDIIAPLLEIFHNILQTESILIPKPNYPYCNGETIPFLQPFKYFNGDRIQDRRCDHCNSDIFNRCYHCETCKTDDGQGKDFCFDCVSSGIGCEFHFKVMVLKEFISHSKLKKELSSFYEIYKNLLAHSGRRPKEVDDIITKSTDRVSDECGFLTTATVAYHVVFYSSQKKIKCHRCEKRFKKFSIIFCTNCNARFCEQCVVNTFGQNFQVLMKRNEWECFCCKGLCDCSNCTSNSNSSNHPRILNNNQQLGLPYNNNNNSNNNNNNNINNNNNNNNNNINNNNNNMNNNNSINNNNNNNNNNNINNNNINNNNHHNNNGNNNLNSSYSSLNALSSLSQQQSYGSYDNYNNNNNNNNYNNNNNNNGHIQILKSGRQYDDEQSSSSGSGSSNSTPTKPRPRNGGDDGLMSHFSGNNNNNNNHHNNNNNNNNNHHMMSHHHHNNNNNNNNNNNPTTSSLSSLSTSLSSSSTSTQKPMDVHSKKRPIVLDNDKPKGRPPKNLKEWTSTHKFIISLIELFRSSNNAILGKPNPHYKPIENLPPLVQLYLSQRKAFGGVLWAKTNSCPLLPCIWVKDLSVIPPNTKLLPSLIQGKKIVVLFFGDQDQEEYVGIVGKKSIFSFDEVNQTLLLKCGEVPLAQLEDLFNTTEPEIAMKKDIAAFNYKNQIEEKEEGLYVKQELYNNKKII
| null | null |
aggregation involved in sorocarp development [GO:0031152]; chromatin organization [GO:0006325]; negative regulation of gene expression [GO:0010629]; phagocytosis [GO:0006909]; pinocytosis [GO:0006907]; positive regulation of gene expression [GO:0010628]; positive regulation of translational termination [GO:0045905]; transposition [GO:0032196]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565]
|
PF02373;PF10497;
|
2.60.120.650;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10491202, ECO:0000269|PubMed:11162086, ECO:0000269|PubMed:16607013, ECO:0000269|PubMed:19343174, ECO:0000269|PubMed:8898890}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator involved in phagocytosis and pinocytosis. Both activates and represses transcription. Regulates expression of acaA, carA, pkaC, csaA, cotB and lagC (PubMed:11162086, PubMed:15470262, PubMed:16607013, PubMed:19343174, PubMed:23355006, PubMed:26339297). Promotes amplification of the tRNA gene-associated retrotransposon TRE5-A, a mobile genetic element formerly called as Dictyostelium repetitive element (DRE). Suppresses agnC and agnE encoding argonaute proteins which are part of a RNA interference pathway controlling TRE5-A amplification. Required for amplification of both sense and antisense RNA transcripts, but does not activate their promoters found in A-module and C-module of the TRE5-A, respectively (PubMed:21076008, PubMed:26339297). Nevertheless, binds to distinct DNA sequences containing A and T stretches within the C-module in vitro (PubMed:10491202, PubMed:11162086, PubMed:8898890). {ECO:0000269|PubMed:10491202, ECO:0000269|PubMed:11162086, ECO:0000269|PubMed:15470262, ECO:0000269|PubMed:16607013, ECO:0000269|PubMed:19343174, ECO:0000269|PubMed:21076008, ECO:0000269|PubMed:23355006, ECO:0000269|PubMed:26339297, ECO:0000269|PubMed:8898890}.
|
Dictyostelium discoideum (Social amoeba)
|
O97143
|
PLK4_DROME
|
MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRTSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSAPGALNVFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIREEFKQVHHKLPYEQTGLFGQASTGLAEPNWPGAAKSSAFCMEAGNVPNSKQASLKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFLKFRPTYNEDRINDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYDNLPSKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPSEGLKVYDRNGMLLSDYSCSESRSLIEHGNECFTHCVNISNALEVAQTKDNSCFPVTIGRRPITDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSLSTISSTRNTSDFGTNCSRSNMLAAHQNIPIKRINVPEIGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKGDDLPFPVRDRVGQIPNIQLKLKTAPLLGSGRKTDYNNAMTPKTTTPYYNRMLL
|
2.7.11.21
| null |
centriole replication [GO:0007099]; centrosome cycle [GO:0007098]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; positive regulation of protein catabolic process [GO:0045732]; protein autophosphorylation [GO:0046777]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm axoneme assembly [GO:0007288]; syncytial blastoderm mitotic cell cycle [GO:0035186]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF18190;PF18409;
|
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
|
PTM: Ubiquitinated by the SCF-slmb ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000269|PubMed:19084407, ECO:0000269|PubMed:19171756}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:19171756, ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:32965218}. Note=Colocalizes with Sas-4 and Patronin at the microtubule organizing center (PubMed:20946984). Colocalizes with Alms1a at the mother centrosome in male germ stem cells (PubMed:32965218). {ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:32965218}.
|
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=2.7.11.21; 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=2.7.11.21;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers. {ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:17463247, ECO:0000269|PubMed:18555779}.
|
Drosophila melanogaster (Fruit fly)
|
O97148
|
MTH_DROME
|
MKTLLVLRISTVILVVLVIQKSYADILECDYFDTVDISAAQKLQNGSYLFEGLLVPAILTGEYDFRILPDDSKQKVARHIRGCVCKLKPCVRFCCPHDHIMDNGVCYDNMSDEELAELDPFLNVTLDDGSVSRRHFKNELIVQWDLPMPCDGMFYLDNREEQDKYTLFENGTFFRHFDRVTLRKREYCLQHLTFADGNATSIRIAPHNCLIVPSITGQTVVMISSLICMVLTIAVYLFVKKLQNLHGKCFICYMVCLFMGYLFLLLDLWQISISFCKPAGFLGYFFVMAAFFWLSVISLHLWNTFRGSSHKANRFLFEHRFLAYNTYAWGMAVVLTGITVLADNIVENQDWNPRVGHEGHCWIYTQAWSAMLYFYGPMVFLIAFNITMFILTAKRILGVKKDIQNFAHRQERKQKLNSDKQTYTFFLRLFIIMGLSWSLEIGSYFSQSNQTWANVFLVADYLNWSQGIIIFILFVLKRSTWRLLQESIRGEGEEVNNSEEEISLENTTTRNVLL
| null | null |
cell surface receptor signaling pathway [GO:0007166]; determination of adult lifespan [GO:0008340]; G protein-coupled receptor signaling pathway [GO:0007186]; response to heat [GO:0009408]; response to paraquat [GO:1901562]; response to reactive oxygen species [GO:0000302]; response to starvation [GO:0042594]; synaptic vesicle exocytosis [GO:0016079]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
G protein-coupled peptide receptor activity [GO:0008528]; G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277]
|
PF00002;PF06652;
|
2.30.160.11;2.170.180.11;1.20.1070.10;
|
G-protein coupled receptor 2 family, Mth subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12367510}; Multi-pass membrane protein {ECO:0000269|PubMed:12367510}. Note=Plasma membrane of presynaptic terminals and innervating axons.
| null | null | null | null | null |
FUNCTION: Involved in biological aging and stress response. Essential for adult survival. Required in the presynaptic motor neuron to up-regulate neurotransmitter exocytosis at larval glutamatergic neuromuscular junctions (NMJs). Regulates a step associated with docking and clustering of vesicles at release sites. SP/Acp70A and sun are agonists that activate mth in vitro. {ECO:0000269|PubMed:12367510, ECO:0000269|PubMed:15133470, ECO:0000269|PubMed:19672878, ECO:0000269|PubMed:9794765}.
|
Drosophila melanogaster (Fruit fly)
|
O97159
|
CHDM_DROME
|
MASEEENDDNFQEEEEAQEDNAPAAELSNDSDAPLKPNNDEDDDYDPEDSRRKKKGKKRKTRKGEEKGRKKKKRKKNESEEDSDFVQHDEEVEYPSTSKRGRKRKEEKQAAKEKESASSGMPSVEDVCSAFSVCNVEIEYSEEELQSLTTYKAFMHHVRPILQKENPKIAAPKLVMLVAAKWREFCESNPHIQQEGGAAGSGGSAGQARSVTGDEPEEPRSSRSSRNEKPDDIYEEAVEEEEEEEEEEKKPRRKRSGRGKKGRRPSGKVPTLKIKLLGKRKRDSSDEEQDASGASERDSDLEFERMLQKSDDSADEKEAPVSSKADNSAPAAQDDGSGAPVVRKKAKTKIGNKFKKKNKLKKTKNFPEGEDGEHEHQDYCEVCQQGGEIILCDTCPRAYHLVCLEPELDEPPEGKWSCPHCEADGGAAEEEDDDEHQEFCRVCKDGGELLCCDSCPSAYHTFCLNPPLDTIPDGDWRCPRCSCPPLTGKAEKIITWRWAQRSNDDGPSTSKGSKNSNSRVREYFIKWHNMSYWHCEWVPEVQLDVHHPLMIRSFQRKYDMEEPPKFEESLDEADTRYKRIQRHKDKVGMKANDDAEVLEERFYKNGVKPEWLIVQRVINHRTARDGSTMYLVKWRELPYDKSTWEEEGDDIQGLRQAIDYYQDLRAVCTSETTQSRSKKSKKGRKSKLKVEDDEDRPVKHYTPPPEKPTTDLKKKYEDQPAFLEGTGMQLHPYQIEGINWLRYSWGQGIDTILADEMGLGKTIQTVTFLYSLYKEGHCRGPFLVAVPLSTLVNWEREFELWAPDFYCITYIGDKDSRAVIRENELSFEEGAIRGSKVSRLRTTQYKFNVLLTSYELISMDAACLGSIDWAVLVVDEAHRLKSNQSKFFRILNSYTIAYKLLLTGTPLQNNLEELFHLLNFLSRDKFNDLQAFQGEFADVSKEEQVKRLHEMLGPHMLRRLKTDVLKNMPSKSEFIVRVELSAMQKKFYKFILTKNYEALNSKSGGGSCSLINIMMDLKKCCNHPYLFPSAAEEATTAAGGLYEINSLTKAAGKLVLLSKMLKQLKAQNHRVLIFSQMTKMLDILEDFLEGEQYKYERIDGGITGTLRQEAIDRFNAPGAQQFVFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQANKVMIYRFVTRNSVEERVTQVAKRKMMLTHLVVRPGMGGKGANFTKQELDDILRFGTEDLFKEDDKEEAIHYDDKAVAELLDRTNRGIEEKESWANEYLSSFKVASYATKEEEEEEETEIIKQDAENSDPAYWVKLLRHHYEQHQEDVGRSLGKGKRVRKQVNYTDGGVVAADTTRDDSNWQDNGSEYNSEYSAGSDEDGGDDDFDDQNGAERKAKRRLERRDDRPLPPLLARVGGNIEVLGFNARQRKSFLNAIMRYGMPPQDAFNSQWLVRDLRGKSERNFKAYVSLFMRHLCEPGADNAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHINGYYSMPELILKPCEPVRSALKQDVAALEAPPTGGNVDKSATTSNSVTPATSAAPSPAPASEKGEDKDKDSEKEKDKTSAEKSEVKQEQEAEEDKKPGDVKQENPVEEAAGDTKPSDAEVKTEVAKTEPKEETKDPEVKEEPKTEEKEKEKVDDKKPIPPTTVIDDDDDDVMIVKEDGELEKPSASSPKDQKAVAAATSAATGATGKGAEDSLEVLKRKFMFNIADGGFTELHTLWLNEEKAAVPGREYEIWHRRHDYWLLAGIVTHGYGRWQDIQNDIRFAIINEPFKMDVGKGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNLAQDPSHPAMSLNARFAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKSDVSRLPATLARIPPVAQRLQMSERSILSRLAATAGNASNAAQLMAQFPAGFQGTTLPAFTSGPAGNFANFRPQFSVPGQLSNNSGV
|
3.6.4.12
| null |
chromatin remodeling [GO:0006338]; chromosome condensation [GO:0030261]; chromosome organization [GO:0051276]; mitotic sister chromatid cohesion [GO:0007064]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome organization [GO:0034728]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; euchromatin [GO:0000791]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; polytene chromosome [GO:0005700]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; nucleosome array spacer activity [GO:0140750]; zinc ion binding [GO:0008270]
|
PF08074;PF06461;PF08073;PF00385;PF06465;PF00271;PF00628;PF00176;
|
2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810;3.30.40.10;
|
SNF2/RAD54 helicase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18250149}. Chromosome {ECO:0000269|PubMed:18250149}. Note=During embryogenesis, detected in nuclei before and after their migration to the membrane of the preblastoderm embryo (PubMed:18250149). Expression is diffuse in mitotic nuclei and is still detectable in nuclei at postgastrulation (PubMed:18250149). In polytene chromosomes of third instar larvae, weakly expressed at the chromocenter and fourth chromosome (PubMed:18250149). {ECO:0000269|PubMed:18250149}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:18250149};
| null | null | null | null |
FUNCTION: Helicase which acts in nucleosome-remodeling by catalyzing ATP-dependent nucleosome mobilization (PubMed:18250149). Involved in regulating transcription (PubMed:18250149, PubMed:9836641). Plays a vital role in development (PubMed:9836641). Binds to a portion of Hunchback (HB) protein that is critical for repression of bithorax complex (BXC) genes (PubMed:9836641). May also function in polycomb group (PcG) repression of Hox genes (PubMed:9836641). May also act as part of the nucleosome remodeling and deacetylase complex (the NuRD complex) which participates in the remodeling of chromatin by deacetylating histones (PubMed:18250149). {ECO:0000269|PubMed:18250149, ECO:0000269|PubMed:9836641}.
|
Drosophila melanogaster (Fruit fly)
|
O97240
|
APEX_PLAF7
|
MKITSLHFLIFHKNLNYVSSKVKAKKIFYQRALNNIYLCTIRTMIVDIAEIKKRDNHALDTQESQELVNKIKEIKNSDEQNNSNNNNNNSSSSNFCSNNNSPFSHKETKLMVKEEVPNSIVKNILNNNSCATSIINNKFYTQINNIIPVKPEAMKEENINVSTVNTENDISKEKKENSHYFCDEIKVMKKEYSKDDFVTDVKLEMNDKEEEEEEKQKIGQESTHINIKVEKDTFNECNNSNVNEKKRNRSVDIHNELSNKRILTEDVVVKCNIKNDVKIIVTWNMNSITVRYKNKKKWDEFMNFFNNLNADVLCFQEVRLPAMNLSEPCDNKNKNKNKNDGIRDRGKIKNSDQKSLADYEIMEQILNDDFKDYNAYFSLANIKYSGQLVLVKKNIHIESIRYNLFFENNAHIHHDEGRVILVEFSNFFLLSTYTPNNGFDHVKFERRRLFDEQLQKFVTILRNEKQKPLVWTGDLNIAPEDIDLSHPAEFRRMKKGNVPKEFIGQPGCTDFERKNFQKILTAGNLVDSYRYLQNIKLNEDKKNNIKHTPNINDNIYTWRCPFLLGKSCNKAMRIDHFIVSKEFLNRINKIHIQGFSVFHNNFYGSDHCPVILYLKNE
|
3.1.11.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU362131, ECO:0000269|PubMed:33743509}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|RuleBase:RU362131, ECO:0000269|PubMed:33743509}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000255|RuleBase:RU362131};
|
base-excision repair [GO:0006284]; DNA repair [GO:0006281]; nucleotide-excision repair [GO:0006289]
|
mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; RNA exonuclease activity [GO:0004532]
|
PF03372;
|
3.60.10.10;
|
DNA repair enzymes AP/ExoA family
|
PTM: May be proteolytically cleaved into a 64 kDa form. {ECO:0000269|PubMed:33743509}.
|
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:33743509}.
|
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000269|PubMed:33743509};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.69 uM for DNA gapped template with 3'-OH at the gap (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:33743509}; Note=kcat is 0.169 sec(-1) with DNA gapped template with 3'-OH at the gap as substrate (at pH 7.5 and 37 degrees Celsius). {ECO:0000269|PubMed:33743509};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8.5 for apurinic/apyrimidinic (AP) endonuclease activity (PubMed:33743509). Optimum pH is 8-8.5 for 3'-5' exonuclease activity (PubMed:33743509). Optimum pH is 8-8.5 for nucleotide incision repair (NIR) cleavage activity (PubMed:33743509). {ECO:0000269|PubMed:33743509};
| null |
FUNCTION: Multifunctional protein that plays a central role in mitochondrial DNA base excision repair (BER) pathway induced by oxidative stress. Has apurinic/apyrimidinic (AP) endonuclease activity towards double-stranded DNA (dsDNA) (PubMed:33743509). Has nucleotide incision repair (NIR) activity; acts on dsDNA with oxidized bases thymine glycol and 5,6-dihydro-2'-deoxyuridine (PubMed:33743509). Has 3'-5' exonuclease; can use dsDNA templates with 3'-OH termini including blunt-end, gapped and mismatched 3'-recessed (PubMed:33743509). Has 3'-phosphatase activity; cleaves 3'-phosphate from blunt, recessed and gapped dsDNA templates, followed by 3'-5' exonuclease activity (PubMed:33743509). Has RNase H-like activity; cleaves RNA on 3'-recessed RNA-DNA duplex (PubMed:33743509). Plays a role in merosome infection of host erythrocytes (By similarity). {ECO:0000250|UniProtKB:A0A509ADV9, ECO:0000269|PubMed:33743509}.
|
Plasmodium falciparum (isolate 3D7)
|
O97302
|
RH5IP_PLAF7
|
MFRIFFTLLIIILIKKTSAIDLIEGIFYEKNEIDKLTFSLDHRVRDNLKTDLILNNNGENDYAYLNKYVYTILNRDSTEKIKTFFSHNKDMKSCDYFISKEYNSSDKTNQICYKKTFCGVVIPNSEEIKTNKITNDKLYCAHFNSTHIIIYYISQPLLLEPHVVYEETFFEKGKNDQINCQGMYISLRSVHVHTHNAILQQETLTYIKNLCDGKNNCKFDFDSIKYENKSLTHYLFFINIQYQCISPLNLQENEMCDVYNDDTHKATCKYGFNKIELLKNVCEENYRCTQDICSVNQFCDGENETCTCKTSLLPSAKNNCEYNDLCTVLNCPENSTCEQIGNGKKAECKCENGKYYHNNKCYTKNDLELAIKIEPHKKEKFYKNNLYQGKALKPEYIFMQCENGFSIEVINAYVSCYRVSFNLNKLKYVTESLKKMCDGKTKCAYGNTIDPIDDLNHHNICNNFNTIFKYDYLCVFNNQNITSDKNSHLHSNIPSLYNSSILPDINKSKFHLISRNSRTNQYPHNNISMLEIQNEISSHNSNQFSTDPHTNSNNINNMNIKKVEIFRSRFSSKLQCQGGKINIDKAILKGGEGCNDLLLTNSLKSYCNDLSECDIGLIYHFDTYCINDQYLFVSYSCSNLCNKCHNNSTCYGNRFNYDCFCDNPYISKYGNKLCERPNDCESVLCSQNQVCQILPNDKLICQCEEGYKNVKGKCVPDNKCDLSCPSNKVCVIENGKQTCKCSERFVLENGVCICANDYKMEDGINCIAKNKCKRKEYENICTNPNEMCAYNEETDIVKCECKEHYYRSSRGECILNDYCKDINCKENEECSIVNFKPECVCKENLKKNNKGECIYENSCLINEGNCPKDSKCIYREYKPHECVCNKQGHVAVNGKCVLEDKCVHNKKCSENSICVNVMNKEPICVCTYNYYKKDGVCLIQNPCLKDNGGCSRNSECTFKYSKINCTCKENYKNKDDSCVPNTNEYDESFTFQYNDDASIILGACGMIEFSYIYNQIIWKINNSKESYVFYYDYPTAGNIEVQIKNEIFHTIIYLKKKIGNSVIYDDFQVDHQTCIYENVFYYSNQN
| null | null |
symbiont entry into host [GO:0044409]
|
cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; host cell membrane [GO:0033644]; host cell plasma membrane [GO:0020002]; host extracellular space [GO:0043655]; membrane [GO:0016020]; microneme [GO:0020009]; microneme lumen [GO:0034494]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
| null | null |
2.90.20.10;
| null |
PTM: Proteolytically cleaved into two chains of 125kDa and 65kDa which remain associated. The cleavage occurs at the schizont stage prior to the release of merozoites. {ECO:0000269|PubMed:21909261}.; PTM: Contains disulfide bonds. {ECO:0000269|PubMed:21909261}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518}. Cytoplasmic vesicle, secretory vesicle, microneme lumen {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406, ECO:0000269|PubMed:27692771}. Cell membrane {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406}; Peripheral membrane protein {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406}; Extracellular side {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406}. Host cell membrane {ECO:0000269|PubMed:30542156}. Note=In late schizonts, colocalizes with CyRPA in the microneme lumen (PubMed:21909261, PubMed:25583518, PubMed:27374406, PubMed:27692771). During merozoite invasion of host erythrocytes, secreted at the merozoite apical surface where it colocalizes with CyPRA and RH5 at the interface between the merozoite and the erythrocyte (PubMed:21909261, PubMed:25583518, PubMed:27374406). {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406, ECO:0000269|PubMed:27692771}.
| null | null | null | null | null |
FUNCTION: Essential for the invasion of host erythrocytes by blood stage merozoites (PubMed:21909261, PubMed:25583518, PubMed:27374406, PubMed:27692771). As part of the PfRH5 adhesion complex, facilitates the interaction of RH5 and human BSG required for the Ca(2+) release into the erythrocyte (PubMed:27374406). {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406, ECO:0000269|PubMed:27692771}.
|
Plasmodium falciparum (isolate 3D7)
|
O97336
|
EPTP7_PLAF7
|
MAKDSQKNLNVSNNNNVQCTMGRSSQNINKSDSKGKIKRCTYAYKILLCTIFIWICQCFYNKSYYVYKKDGRRNKGKKILGIRINKSLAEMDHTKYHPEYYDEVQENYDPYYGVNQYSDECESYKSEDDDSEEEYYNSTPRVTVLEPQTENSEDEENYEKTIVDELNELPNDKKALILSYIRNGNDNNMQLLPYANNNKQNTQENISRNKEFFRHFVDFIKGYKLFDSPVLNALLPFIFIAFVYCTITMLVGNVRYIIALYILAKILKMHYDYKHKENNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKKSKKN
| null | null |
symbiont intracellular protein transport in host [GO:0030581]; vesicle-mediated transport [GO:0016192]
|
exon-exon junction complex [GO:0035145]; host cell [GO:0043657]; Maurer's cleft [GO:0020036]; membrane [GO:0016020]; vesicle [GO:0031982]
| null | null | null | null | null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:35930605}. Vesicle {ECO:0000269|PubMed:35930605}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Note=In the host erythrocyte cytoplasm, localizes to Maurer's clefts, chaperone-containing structures known as J-dots, and EMP1-containing electron dense vesicles (EDVs). {ECO:0000269|PubMed:35930605}.
| null | null | null | null | null |
FUNCTION: During the asexual blood stage, plays an essential role in the recruitment and/or formation of EMP1-containing vesicles at the Maurer's clefts and their subsequent transfer to the host erythrocyte cell membrane. {ECO:0000269|PubMed:35930605}.
|
Plasmodium falciparum (isolate 3D7)
|
O97364
|
SUB2_PLAFA
|
MLNIIYVVSLILIKFIFYKECNNNNNYYLSNIELYNYKLRKRNRILNNNINDRKSFLSDLEQNYKPLFDIYELSANFEKRRKELEKKTKGEENEIEKKKENDLEEKKENEIEKKKENDLEKEYNDVINLLELSLSSEYKELNADVSNNDNSGHEENNKHKLNKKNSSNYKNDKSLDELIKGAILKLKQNPNIKNKNMLDYDKIFKIIKEKLINKNLASNKIKGGDNEKLKEEKKQSDISTNVEVKKDIINDQLNKGIPTKIENKDDMINKESNKEDITNEGKSNSLNNLNTLNNDGNIITKVYDHYTIVTNSNDILNDISIDASDISKNSIGGINIPFNENDNSSFTHQRYIVLSNNGEKKYKIVLMTKNPKFMDMDGIYDEEEKKESLIELNQKVNKEENTNLYDGTGTLYYGKKSKKEKENTQQKGGNNPNVDINILNNNNNNNNNNNNNSNNNSNSMNDEEINYNNNNNKESPSMFRRFINFLSFSGNENETEDTLIYHNKNDNSYKNKKEGTGKNNDNNDPNNNNNKKILLNVDKLVDQYLLNLKNNHTSKQELILVLKGELDLHSKNMKNVINNAKKNLEKYFKEHFKEFDKISYDISTPINFLCIFIPTLFDMNNMDLLKQALLILHNDLHEYVENWSFSSTYHTYEADYIKEQDSVYDRSPKKKYIKASKKLYNNKYSFLNKFLNIEPLILFAKKLNSKRSNIEKEILNFLPKELRDYSTWNLSIIRVFNAWFLAGYGNKNVKVCVVDSGADIKHVDLNGNLYIPEYNEKYEMTQDFYNFMVKNPTDASGHGTHVTGIIGGVANDLGVVGVAPNITLISLRFIDGKKYGGSFHAIKALNVCILNKAPIINASWGSSHFDVNLHLAVERLKYTLNGKGSVLIAASGNKSNDNDISPLYPATFTFPHVYSVASISRNFEISPFSNYGHKSVHILAPGHHIYSTIPNNSYKIFTGTSMAAPHVCGVSALVYSVCYNQGFIPQAEEVLDILTRTSIKIISTKKRTINDSLVNAEGAVLTTLLGGLWMQMDCYFVKFNLEKGKKKHIPVVFSAYKKGVYETDIVIAIIPIDGKSKIYGEIHIPIKIVTDVNIPNFQESPRRGKNYTIDSNEAQHDEVLSYICENALYNLYEYDSHYLLASVILFFLALLSIFVGMIYMKSRKHSDKKCSKNLMKSNYIPEMDDGMEETQQLQQERRQYFRELFGENLEKNYDQHFVQDFGQDFRQDFKLGSTPDLKQYSDIDLQNKIQQPERKTVKIIINNFEDRKKETKRRLLKGLNYDGENAKKHDFTNESISNSRKNFKFSNNTEMKKNTIKSEDVKIASDDNVNKAMNQLDDMFMK
|
3.4.21.62
| null |
membrane protein ectodomain proteolysis [GO:0006509]; peptide hormone processing [GO:0016486]
|
cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; microneme membrane [GO:0033163]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
serine-type endopeptidase activity [GO:0004252]
|
PF00082;PF18513;
|
3.30.70.2370;3.40.50.200;
|
Peptidase S8 family
|
PTM: Proteolytically cleaved at the N-terminus to generate a 74kDa intermediate which is further processed into a 72kDa form (PubMed:10551362, PubMed:16322767). The first maturation cleavage is autocatalytic, occurs in the ER and is necessary for the subsequent SUB2 trafficking to the microneme (By similarity). The second cleavage may be mediated by PMX/plasmepsin X (By similarity). {ECO:0000250|UniProtKB:Q8IHZ5, ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Note=In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:10551362, PubMed:16322767). Immediately after schizont rupture, secreted from the micronemes to the merozoite surface where it redistributes in an actin-dependent manner to accumulate at the posterior end of newly released merozoites (PubMed:16322767). {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000305|PubMed:16322767};
| null | null | null | null |
FUNCTION: Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite (PubMed:16322767). May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion (By similarity). {ECO:0000250|UniProtKB:Q8IHZ5, ECO:0000269|PubMed:16322767}.
|
Plasmodium falciparum
|
O97366
|
PPAF1_HOLDI
|
MKQVHFFILWFFVLNLYSIKAQAGCRTPNGENARCVPINNCKILYDSVLTSDPEVIRFLRASQCGYNGQPLVCCGSSASYQPPPTSASIRNRRPELLPNDCGYQVEADKILNGDDTVPEEFPWTAMIGYKNSSNFEQFACGGSLINNRYIVTAAHCVAGRVLRVVGALNKVRLGEWNTATDPDCYGAVRVCVPDKPIDLGIEETIQHPDYVDGSKDRYHDIALIRLNRQVEFTNYIRPVCLPQPNEEVQVGQRLTVVGWGRTETGQYSTIKQKLAVPVVHAEQCAKTFGAAGVRVRSSQLCAGGEKAKDSCGGDSGGPLLAERANQQFFLEGLVSFGATCGTEGWPGIYTKVGKYRDWIEGNIRP
|
3.4.21.-
| null |
innate immune response [GO:0045087]; proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]
|
PF12032;PF00089;
|
3.30.1640.30;2.40.10.10;
|
Peptidase S1 family, CLIP subfamily
|
PTM: Cleaved following the recognition of pathogen-derived products, probably by a lysyl endopeptidase. {ECO:0000269|PubMed:11012672, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:17287215, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}.
| null | null | null | null | null |
FUNCTION: Serine endopeptidase which, by cleaving prophenoloxidase PPO1 and PPO2, is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:17287215, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}.
|
Holotrichia diomphalia (Korean black chafer)
|
O97394
|
SDK_DROME
|
MLKSAASSLRRRRPKTTITATLAIEMPSQPKLASLLAVLVLLCYCDSCFFCYADANLQQQNSIVQQQQLQAPRFTTHPSSSGSIVSEGSTKILQCHALGYPQPTYRWLKDGVPVGDFSSSQFYRFHSTRREDAGSYQCIARNDAGSIFSEKSDVVVAYMGIFENTTEGRLTVISGHPAIFDMPPIESIPVPSVMWQSEDGPLNYDIKYAFTHANQLIILSADENDRKGYRAKAINTQLGKEESSAFVHLNVSGDPYIEVAPEIIVRPQDVKVKVGTGVVELQCIANARPLHELETLWLKDGLAVETAGVRHTLNDPWNRTLALLQANSSHSGEYTCQVRLRSGGYPAVSASARLQILEPPLFFTPMRAETFGEFGGQVQLTCDVVGEPTPQVKWFRNAESVDAHIESGRYTLNTDNTLVIKKLILDDAAMFQCLAINEAGENSASTWLRVKTSAPIMELPPQNVTALDGKDATISCRAVGSPNPNITWIYNETQLVDISSRVQILESGDLLISNIRSVDAGLYICVRANEAGSVKGEAYLSVLVRTQIIQPPVDTTVLLGLTATLQCKVSSDPSVPYNIDWYREGQSSTPISNSQRIGVQADGQLEIQAVRASDVGSYACVVTSPGGNETRAARLSVIELPFPPSNVKVERLPEPQQRSINVSWTPGFDGNSPISKFIIQRREVSELEKFVGPVPDPLLNWITELSNVSADQRWILLENLKAATVYQFRVSAVNRVGEGSPSEPSNVVELPQEAPSGPPVGFVGSARSMSEIITQWQPPLEEHRNGQILGYILRYRLFGYNNVPWSYQNITNEAQRNFLIQELITWKDYIVQIAAYNNMGVGVYTEGSKIKTKEGVPEAPPTNVKVEAINSTAARCRWTPPNPQQINGINQGYKIQAWQRRLIDGEWRDIERRMKTVPPSLIDPLAEQTAILGGLEKFTEYNISVLCFTDPGDGVASSQVAVMTMDDVPDEVTGLHFDDVSDRSVKVLWAPPRASNGILTGYTVRYQVKDRPDTLKSFNLTADDTELTVNQLQATTHYWFEIVAWTRVGSGIPKTATIQSGVEPVLPHAPTALALSNIEAFSVVLQFTPGFDGNSSITKWKVEGQTARNMTWFTICEINDPDAETLTVTGLVPFTQYRLRLSASNVVGSSKPSEATKDFQTIQARPKHPPFNVTVRAMSAQQLRVRWIPLQQTEWYGNPRGYNISYKQLVKTPGTIKYVPRSVVIEDHTANSHVLDSLEEWTLYEVKMNACNDVGCSKESDTAVERTREAVPSYGPLDVQANATSSTTVVVQWGEVPRQHRNGQIDGYKVFYAAADRGQQVLHKTIPNNATFTTTLTELKKYVVYHVQVLAYTRLGNGALSTPPIRVQTFEDTPGVPSNVSFPDVSLTMARIIWDVPVDPNGKILAYQVTYTLNGSAMLNYSREFPPSDRTFRATELLPGKYYSFSCTAQTRLGWGKIATALVYTTNNRERPQAPSVPQISRSQIQAHQITFSWTPGRDGFAPLRYYTVEMRENEGRWQPLPERVDPSLSSFTAVGLRPYMTYQFRIQATNDLGPSAFSRESVIVRTLPAAPAVGVGGLKVVPITTTSVRVQWSALETALWNGDASTGGYRILYQQLSDFPTALQSTPKTDVHGINENSVVLSDLQQDRNYEIVVLPFNSQGPGPATPPAAVYVGEAVPTGEPRAVDAAPISSTEVRLLWKPPKQSMQNGDILGYKIYYLVTYSPQALEPGRKWEEEIEVVSATATSHSLVFLDKFTEYRIQLLAFNPAGDGPRSAPITVKTLPGVPSAPLHLRFSDITMQSLEVTWDPPKFLNGEILGYLVTYETTEENEKFSKQVKQKVSNTTLRVQNLEEEVTYTFTVRAQTSVDYGPGISENVTTGPQDGSPVAPRDLILTKTLSSVEMHWINGPSGRGPILGYLIEAKKRDDSRWTKIEQTRKGMMQDFTVSYHILMPSTAYTFRVIAYNRYGISFPVYSKDSILTPSKLHLEYGYLQHKPFYRQTWFMVSLAATSIVIIVMVIAVLCVKSKSYKYKQEAQKTLEESMAMSIDERQELALELYRSRHGVGTGTLNSVGTLRSGTLGTLGRKSTSRPPPGVHLGKSPPRPSPASVAYHSDEESLKCYDENPDDSSVTEKPSEVSSSEASQHSESENESVRSDPHSFVNHYANVNDSLRQSWKKTKPVRNYSSYTDSEPEGSAVMSLNGGQIIVNNMARSRAPLPGFSSFV
| null | null |
cell-cell adhesion [GO:0098609]; compound eye cone cell differentiation [GO:0042675]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of photoreceptor cell differentiation [GO:0046533]; pigment cell differentiation [GO:0050931]
|
apical part of cell [GO:0045177]; perivitelline space [GO:0098595]; plasma membrane [GO:0005886]
|
cell adhesion receptor activity [GO:0004895]
|
PF00041;PF07679;PF13927;
|
2.60.40.10;
|
Sidekick family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Participates in homotypic or heterotypic interactions in the eye during pattern formation to prevent extra cells from joining the precluster and differentiating as photoreceptor cells. {ECO:0000269|PubMed:9310325}.
|
Drosophila melanogaster (Fruit fly)
|
O97422
|
B3GI_DROME
|
MSEVRIRPRQVLILIIVFLVVLMMVHRNGKRTCQGPEYLQAMFVQGDTLPTIYAVTPTYPRPAQKAELTRLSHLFMLLPHLHWIIVEDTNATTPLVRNLLDRAGLEKRSTLLNIKTPSEFKLKGKDPNWIKPRGVEQRNLALAWLRNHVDVDRHSIVFFMDDDNSYSTELFAEMSKIERGRVGVWPVGLVGGLMVERPLLTEDGTKVTGFNAAWRPERPFPIDMAAFAISMDLFIRNPQATFSYEVQRGYQESEILRHLTTRDQLQPLANRCTDVLVWHTRTEKTKLAAEEALLKKGQRSDGGMEV
|
2.4.1.135
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:12511570};
|
carbohydrate metabolic process [GO:0005975]; chondroitin sulfate proteoglycan biosynthetic process [GO:0050650]; protein glycosylation [GO:0006486]; proteoglycan biosynthetic process [GO:0030166]
|
Golgi membrane [GO:0000139]
|
galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity [GO:0015018]; metal ion binding [GO:0046872]
|
PF03360;
| null |
Glycosyltransferase 43 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571, Rhea:RHEA-COMP:12573, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132090, ChEBI:CHEBI:132093; EC=2.4.1.135; Evidence={ECO:0000250|UniProtKB:O35789};
| null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates. {ECO:0000269|PubMed:12511570}.
|
Drosophila melanogaster (Fruit fly)
|
O97531
|
KCNQ1_FELCA
|
RVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFAVFLIVLVCLIFSVLSTIEQYVALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGVWGRLRFARKPISIIDLIVVLASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGQVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPESSTWNIYVRKPTRSHTLLSPSPKPKKSVMVKKKKFKLDKDNGVSPGEKTLTVPHITCEPVSEKRRPDHFSVDTCDSSVKSPMLLEVSTTHFLRTNSVAEDLDLEGETPLVPITHVSQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVAQLDQRLVLITDMLQQLLSLHHGGPPGSRPPSGGGAQVQPCGPTNPELFLPGNALPTYEQLTVPRRGPEEGS
| null | null |
inner ear development [GO:0048839]; intestinal absorption [GO:0050892]; membrane repolarization [GO:0086009]; membrane repolarization during ventricular cardiac muscle cell action potential [GO:0098915]; potassium ion export across plasma membrane [GO:0097623]; regulation of gastric acid secretion [GO:0060453]; renal absorption [GO:0070293]
|
basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; membrane raft [GO:0045121]; monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
|
calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; outward rectifier potassium channel activity [GO:0015271]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization [GO:0086089]; voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization [GO:1902282]
|
PF00520;PF03520;
|
1.10.287.70;6.10.140.1910;1.20.120.350;
|
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.1/KCNQ1 sub-subfamily
|
PTM: Phosphorylated by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9. {ECO:0000250|UniProtKB:P51787}.; PTM: Ubiquitinated by NEDD4L; promotes internalization. The ubiquitinylated form is internalized through a clathrin-mediated endocytosis by interacting with AP2M1 and is recycled back to the cell membrane via RAB4A and RAB11A. {ECO:0000250|UniProtKB:P51787}.; PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restores the membrane localization. {ECO:0000250|UniProtKB:P51787}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51787}. Early endosome {ECO:0000250|UniProtKB:P51787}. Membrane raft {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51787}. Note=Colocalized with KCNE3 at the plasma membrane. Upon 17beta-oestradiol treatment, colocalizes with RAB5A at early endosome. Heterotetramer with KCNQ5 is highly retained at the endoplasmic reticulum and is localized outside of lipid raft microdomains. During the early stages of epithelial cell polarization induced by the calcium switch it is removed from the plasma membrane to the endoplasmic reticulum, where it is retained, and redistributed to the basolateral cell surface in a PI3K-dependent manner at a later stage. {ECO:0000250|UniProtKB:P51787}.
| null | null | null | null | null |
FUNCTION: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity). Also forms a heterotetramer with KCNQ5 that has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity). {ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:P97414, ECO:0000250|UniProtKB:Q9Z0N7}.
|
Felis catus (Cat) (Felis silvestris catus)
|
O97554
|
PGH1_RABIT
|
MSRSSPSLRLPVLLLLLLLLLLPPPPPVLPADPGAPAPVNPCCYFPCQHQGVCVRVALDRYQCDCTRTGYSGPNCTVPDLWTWLRSSLRPSPTFVHYLLTHVRWFWEFVNATFIRDTLMRLVLTVRSNLIPSPPTYNLDYDYISWEAFSNVSYYTRVLPSVPKDCPTPMGTKGKKQLPDAQVLAHRFLLRRTFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDSLERQYHLRLFKDGKLKYQVLDGEVYPPSVEEAPVLMHYPRGVPPRSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWDDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPEMLFSVQFQYRNRIAMEFNHLYHWHPLMPDSFQVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQSAGRIGGGRNIDHHVLHVAVEVIKESREMRLQPFNEYRKRFGLKPYASFQELTGETEMAAELEELYGDIDALEFYPGLLLEKCQPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGSNLIKTATLKKLVCLNTKTCPYVSFRVPRSSGDDGPAAERRSTEL
|
1.14.99.1
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000250};
|
cyclooxygenase pathway [GO:0019371]; response to oxidative stress [GO:0006979]
|
endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]
|
PF03098;
|
1.10.640.10;2.10.25.10;
|
Prostaglandin G/H synthase family
| null |
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000250|UniProtKB:P23219}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000250|UniProtKB:P23219}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P23219}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000250|UniProtKB:P23219}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P23219}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000250|UniProtKB:P23219}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000250|UniProtKB:P05979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000250|UniProtKB:P05979}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000250|UniProtKB:P05979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000250|UniProtKB:P05979}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P05979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000250|UniProtKB:P05979}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000250|UniProtKB:P05979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000250|UniProtKB:P05979};
| null |
PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P23219}.
| null | null |
FUNCTION: Dual cyclooxygenase and peroxidase that plays an important role in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells. Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products. {ECO:0000250|UniProtKB:P05979}.
|
Oryctolagus cuniculus (Rabbit)
|
O97562
|
UCP2_PIG
|
MVGFKATEVPPTATVKFLGAGTAACIADLITFPLDTAKVRLQIQGERRGPVQAAASAQYRGVLGTILTMVRNEGPRSLYNGLVAGLQRQMSFASVRIGLYDSVKHFYTKGSEHAGIGSRLLAGSTTGALAVAVAQPTDVVKVRFQAQARAGGGRRYRSTVDAYKTIAREEGLRGLWKGTSPNVARNAIVNCAELVTYDLIKDTLLKADLMTDDLPCHFTSAFGAGFCTTVIASPVDVVKTRYMNSAPGQYSSAGHCALTMLQKEGPRAFYKGFTPSFLRLGSWNVVMFVTYEQLKRALMAARASREAPF
| null | null |
adaptive thermogenesis [GO:1990845]; C4-dicarboxylate transport [GO:0015740]; cellular response to glucose stimulus [GO:0071333]; glutamine metabolic process [GO:0006541]; glycolytic process [GO:0006096]; macrophage differentiation [GO:0030225]; mitochondrial fission [GO:0000266]; mitochondrial transmembrane transport [GO:1990542]; reactive oxygen species metabolic process [GO:0072593]; response to cold [GO:0009409]
|
mitochondrial inner membrane [GO:0005743]
|
antiporter activity [GO:0015297]; L-aspartate transmembrane transporter activity [GO:0015183]; malate transmembrane transporter activity [GO:0015140]; oxaloacetate transmembrane transporter activity [GO:0015131]; oxidative phosphorylation uncoupler activity [GO:0017077]; phosphate ion uniporter activity [GO:0140787]; protein homodimerization activity [GO:0042803]; proton transmembrane transporter activity [GO:0015078]; secondary active sulfate transmembrane transporter activity [GO:0008271]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P70406}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-aspartate(out) + phosphate(in) = H(+)(out) + L-aspartate(in) + phosphate(out); Xref=Rhea:RHEA:73307, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + oxaloacetate(out) + phosphate(in) = H(+)(out) + oxaloacetate(in) + phosphate(out); Xref=Rhea:RHEA:73303, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=(S)-malate(out) + H(+)(in) + phosphate(in) = (S)-malate(in) + H(+)(out) + phosphate(out); Xref=Rhea:RHEA:73299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + malonate(out) + phosphate(in) = H(+)(out) + malonate(in) + phosphate(out); Xref=Rhea:RHEA:73387, ChEBI:CHEBI:15378, ChEBI:CHEBI:15792, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + phosphate(in) + sulfate(out) = H(+)(out) + phosphate(out) + sulfate(in); Xref=Rhea:RHEA:73391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=(S)-malate(out) = (S)-malate(in); Xref=Rhea:RHEA:74555, ChEBI:CHEBI:15589; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=L-aspartate(out) = L-aspartate(in); Xref=Rhea:RHEA:66332, ChEBI:CHEBI:29991; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P55851, ECO:0000250|UniProtKB:P70406}; CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid(out) = a long-chain fatty acid(in); Xref=Rhea:RHEA:39283, ChEBI:CHEBI:57560; Evidence={ECO:0000250|UniProtKB:P70406};
| null | null | null | null |
FUNCTION: Antiporter that exports dicarboxylate intermediates of the Krebs cycle in exchange for phosphate plus a proton across the inner membrane of mitochondria, a process driven by mitochondrial motive force with an overall impact on glycolysis, glutaminolysis and glutathione-dependent redox balance. Continuous export of oxaloacetate and related four-carbon dicarboxylates from mitochondrial matrix into the cytosol negatively regulates the oxidation of acetyl-CoA substrates via the Krebs cycle lowering the ATP/ADP ratio and reactive oxygen species (ROS) production (By similarity). May mediate inducible proton entry into the mitochondrial matrix affecting ATP turnover as a protection mechanism against oxidative stress. The proton currents are most likely associated with fatty acid flipping across the inner membrane of mitochondria in a metabolic process regulated by free fatty acids and purine nucleotides (By similarity). Regulates the use of glucose as a source of energy. Required for glucose-induced DRP1-dependent mitochondrial fission and neuron activation in the ventromedial nucleus of the hypothalamus (VMH). This mitochondrial adaptation mechanism modulates the VMH pool of glucose-excited neurons with an impact on systemic glucose homeostasis. Regulates ROS levels and metabolic reprogramming of macrophages during the resolution phase of inflammation. Attenuates ROS production in response to IL33 to preserve the integrity of the Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity). Can unidirectionally transport anions including L-malate, L-aspartate, phosphate and chloride ions (By similarity). Does not mediate adaptive thermogenesis (By similarity). {ECO:0000250|UniProtKB:P55851, ECO:0000250|UniProtKB:P70406}.
|
Sus scrofa (Pig)
|
O97572
|
RAB7A_RABIT
|
MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLSVAFYRGADCCVLVFDVTAPNTFKTLDSWRLEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWSYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPMKLDKNDRAKTSAESCSC
|
3.6.5.2
| null |
early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; endosome to plasma membrane protein transport [GO:0099638]; lipid catabolic process [GO:0016042]; lipophagy [GO:0061724]; phagosome acidification [GO:0090383]; phagosome-lysosome fusion [GO:0090385]
|
autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lipid droplet [GO:0005811]; lysosomal membrane [GO:0005765]; melanosome membrane [GO:0033162]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]
|
G protein activity [GO:0003925]; GTP binding [GO:0005525]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
|
PTM: Deubiquitination at Lys-191 and Lys-194 by USP32. {ECO:0000250|UniProtKB:P51149}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000250|UniProtKB:P51150}. Endosome membrane {ECO:0000250|UniProtKB:P51149}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P51150}. Mitochondrion membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}. Note=Colocalizes with OSBPL1A at the late endosome. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts. Recruited to phagosomes containing S.aureus or Mycobacterium. Lipid droplet localization is increased upon ADRB2 stimulation. Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner. {ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150}.
|
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:P51149}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P51149};
| null | null | null | null |
FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (By similarity). Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transporter-mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism (By similarity). Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes (By similarity). Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacteria (By similarity). Plays a role in the fusion of phagosomes with lysosomes (By similarity). Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses (By similarity). Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium) (By similarity). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts (By similarity). Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA (By similarity). Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation (By similarity). Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway.Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). Required for vesicular trafficking and cell surface expression of ACE2 (By similarity). May play a role in PRPH neuronal intermediate filament assembly (By similarity). {ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150}.
|
Oryctolagus cuniculus (Rabbit)
|
O97583
|
NDST2_BOVIN
|
MLKLWKVVRPARQLELHRLILLLIAFSLGSMGFLAYYVSTSPKAKEPLPLPLGDCSSSGAAGGPGPVRPPVPPRPPRPPETARTEPVVLVFVESAYSQLGQEIVAILESSRFRYSTELAPGRGDMPTLTDHTRGRYVLVIYENLLKYVNLDAWSRELLDRYCVEYGVGIIGFFRAHEHSLLSAQLKGFPLFLHSNLGLRDYQVNPTAPLLHLTRPSRLEPGPLPGDDWTIFQSNHRTYEPVLLGSLRPAEPPVPGPVARRARLPTVVQDLGVHDGIQRVLFGHGLSFWLHKLVFRDAGGYLTGKGLLWDLDRYILVDIDDIFVGKEGTRMKVADVEALLTTQNKLRTLVPNFTFNLGFSGKFYHTGTEEEDAGDDMLLNHRREFWWFPHMWSHMQPHLFHNRSVLADQMRLNKQFALEHGIPTDLGYAVAPHHSGVYPIHTQLYEAWKSVWGIQVTSTEEYPHLRPARYRRGFIHNGIMVLPRQTCGLFTHTIFYNEYPGGSRELDRSIRGGELFLTVLLNPISIFMTHLSNYGNDRLGLYTFESLVRFLQCWTSLRLQTLPPVPLGRKYFDLFPQERSPLWQNPCDDKRHKDIWSKEKTCDRLPKFLIVGPQKTGTTAIHFFLSLHPAVTSSFPSPSTFEEIQFFNGPNYHKGIDWYMDFFPVPSNASTDFLFEKSATYFDSEVVPRRGAALLPRAKIITVLTNPADRAYSWYQHQRAHGDPVALNYTFYQVITASSQDPPALRSLQNRCLVPGYYSTHLQRWLTYYPSGQLLIVDGQELRTNPAASMEIIQKFLGITPFLNYTRTLRFDEDKGFWCQGLEGGKTRCLGKSKGRKYPDMDAESRLFLTDFFRNHNLELSKLLSRLGQPVPSWLREELQHSSSG
|
2.8.2.-; 2.8.2.8; 3.-.-.-
| null |
heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0015014]; heparin biosynthetic process [GO:0030210]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
[heparan sulfate]-glucosamine N-sulfotransferase activity [GO:0015016]; deacetylase activity [GO:0019213]
|
PF12062;PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family, NDST subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:140572; EC=2.8.2.8;
| null |
PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.; PATHWAY: Glycan metabolism; heparin biosynthesis.
| null | null |
FUNCTION: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:P52849, ECO:0000269|PubMed:9712870}.
|
Bos taurus (Bovine)
|
O97593
|
SMC1A_BOVIN
|
MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRTSNIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ
| null | null |
cell division [GO:0051301]; DNA repair [GO:0006281]; meiotic cell cycle [GO:0051321]; response to DNA damage checkpoint signaling [GO:0072423]; response to radiation [GO:0009314]; sister chromatid cohesion [GO:0007062]
|
kinetochore [GO:0000776]; meiotic cohesin complex [GO:0030893]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]
|
PF06470;PF02463;
|
1.20.1060.20;3.30.70.1620;3.40.50.300;
|
SMC family, SMC1 subfamily
|
PTM: Phosphorylated upon ionizing radiation or DNA methylation. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation (By similarity). {ECO:0000250|UniProtKB:Q14683}.; PTM: Ubiquitinated by the DCX(DCAF15) complex, leading to its degradation. {ECO:0000250|UniProtKB:Q14683}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function (By similarity). Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex 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. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central component of cohesin complex. The cohesin complex is 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. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000250}.
|
Bos taurus (Bovine)
|
O97594
|
SMC3_BOVIN
|
MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKRRXERQSGLRMKEKGVVKGERGSGPQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG
| null | null |
cell division [GO:0051301]; DNA repair [GO:0006281]; meiotic cell cycle [GO:0051321]; mitotic sister chromatid cohesion [GO:0007064]; regulation of DNA replication [GO:0006275]
|
chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; meiotic cohesin complex [GO:0030893]; mitotic spindle pole [GO:0097431]; nuclear matrix [GO:0016363]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cohesin loader activity [GO:0061775]; double-stranded DNA binding [GO:0003690]; dynein complex binding [GO:0070840]
|
PF06470;PF02463;
|
1.10.287.1490;1.20.1060.20;3.30.70.1620;3.40.50.300;
|
SMC family, SMC3 subfamily
|
PTM: Phosphorylated at Ser-1082 in a SPO11-dependent manner. {ECO:0000250|UniProtKB:Q9CW03}.; PTM: Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion. Regulated by DSCC1, it is required for processive DNA synthesis, coupling sister chromatid cohesion establishment during S phase to DNA replication (By similarity). Deacetylation by HDAC8, regulates release of the cohesin complex from chromatin (By similarity). {ECO:0000250|UniProtKB:Q9UQE7}.; PTM: Ubiquitinated by the DCX(DCAF15) complex, leading to its degradation. {ECO:0000250|UniProtKB:Q9UQE7}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CW03}. Chromosome {ECO:0000250|UniProtKB:Q9CW03}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9CW03}. 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 PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. The phosphorylated form at Ser-1082 is preferentially associated with unsynapsed chromosomal regions (By similarity). {ECO:0000250|UniProtKB:Q9CW03}.
| null | null | null | null | null |
FUNCTION: Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form 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. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement.
|
Bos taurus (Bovine)
|
O97605
|
CD40L_FELCA
|
MIETYSQTAPRSVAPGPPVSMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLYEDFVFMKTLQKCNKGEGALSLLNCEEIKSRFEAFLKEIMLNKETKKEKNVAMQKGDQDPRVAAHVISEASSSTASVLQWAPKGYYTISSNLVTLENGKQLAVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLHSPSGSERVLLRAANARSSSKPCGQQSIHLGGVFELHPGASVFVNVTDPSQVSHGTGFTSFGLLKL
| null | null |
B cell proliferation [GO:0042100]; immune response [GO:0006955]; inflammatory response [GO:0006954]; platelet activation [GO:0030168]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of T cell proliferation [GO:0042102]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
CD40 receptor binding [GO:0005174]; cytokine activity [GO:0005125]; protein serine/threonine kinase activator activity [GO:0043539]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250|UniProtKB:P29965}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29965}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P29965}. Cell surface {ECO:0000250|UniProtKB:P29965}.; SUBCELLULAR LOCATION: [CD40 ligand, soluble form]: Secreted {ECO:0000250|UniProtKB:P29965}. Note=Release of soluble CD40L from platelets is partially regulated by GP IIb/IIIa, actin polymerization, and a matrix metalloproteinases (MMP) inhibitor-sensitive pathway. {ECO:0000250|UniProtKB:P29965}.
| null | null | null | null | null |
FUNCTION: Cytokine that acts as a ligand to CD40/TNFRSF5 (By similarity). Costimulates T-cell proliferation and cytokine production (By similarity). Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation (By similarity). Induces the activation of NF-kappa-B (By similarity). Induces the activation of kinases MAPK8 and PAK2 in T-cells (By similarity). Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4 (By similarity). Involved in immunoglobulin class switching (By similarity). {ECO:0000250|UniProtKB:P27548, ECO:0000250|UniProtKB:P29965}.; FUNCTION: [CD40 ligand, soluble form]: Acts as a ligand for integrins, specifically ITGA5:ITGB1 and ITGAV:ITGB3; both integrins and the CD40 receptor are required for activation of CD40-CD40LG signaling, which have cell-type dependent effects, such as B-cell activation, NF-kappa-B signaling and anti-apoptotic signaling. {ECO:0000250|UniProtKB:P29965}.
|
Felis catus (Cat) (Felis silvestris catus)
|
O97626
|
CD40L_CANLF
|
MIETYSQTAPRSVATGPPVSMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLYEDFVFMKTLQKCNKGEGSLSLLNCEEIKSQFEAFLKEIMLNNEMKKEENIAMQKGDQDPRIAAHVISEASSNPASVLRWAPKGYYTISSNLVSLENGKQLAVKRQGLYYVYAQVTFCSNRAASSQAPFVASLCLHSPSGTERVLLRAASSRGSSKPCGQQSIHLGGVFELHPGASVFVNVTDPSQVSHGTGFTSFGLLKL
| null | null |
B cell proliferation [GO:0042100]; immune response [GO:0006955]; inflammatory response [GO:0006954]; platelet activation [GO:0030168]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of T cell proliferation [GO:0042102]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
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CD40 receptor binding [GO:0005174]; cytokine activity [GO:0005125]; protein serine/threonine kinase activator activity [GO:0043539]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250|UniProtKB:P29965}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29965}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P29965}. Cell surface {ECO:0000250|UniProtKB:P29965}.; SUBCELLULAR LOCATION: [CD40 ligand, soluble form]: Secreted {ECO:0000250|UniProtKB:P29965}. Note=Release of soluble CD40L from platelets is partially regulated by GP IIb/IIIa, actin polymerization, and a matrix metalloproteinases (MMP) inhibitor-sensitive pathway. {ECO:0000250|UniProtKB:P29965}.
| null | null | null | null | null |
FUNCTION: Cytokine that acts as a ligand to CD40/TNFRSF5 (By similarity). Costimulates T-cell proliferation and cytokine production (By similarity). Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation (By similarity). Induces the activation of NF-kappa-B (By similarity). Induces the activation of kinases MAPK8 and PAK2 in T-cells (By similarity). Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4 (By similarity). Involved in immunoglobulin class switching (By similarity). {ECO:0000250|UniProtKB:P27548, ECO:0000250|UniProtKB:P29965}.; FUNCTION: [CD40 ligand, soluble form]: Acts as a ligand for integrins, specifically ITGA5:ITGB1 and ITGAV:ITGB3; both integrins and the CD40 receptor are required for activation of CD40-CD40LG signaling, which have cell-type dependent effects, such as B-cell activation, NF-kappa-B signaling and anti-apoptotic signaling. {ECO:0000250|UniProtKB:P29965}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O97627
|
ARBK1_DIDVI
|
MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFREFCLNHMEEAKPLVEFYDEIKKYEKLDSEEERTVKSREIFDLYIMKELLSCSHLFSKSATEHVQSRLLKKQVPTDLFQPYIEEICQRFRDDVFQKFIESEKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSESDMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRSLGCLGRGAQEVKEDPFFKAVDWQMVLLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTVNSETDRLEARKKAKNKQLGHEDDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRAEGEAPQSLLTMEEIQSVEETQIKDRKCILLKIRGGKQFILQCDSDPELVQWKKELRDVYREAQQLLQRVPKMKNKPRSPVVELSKMPLTQRGSANGL
|
2.7.11.15
| null |
desensitization of G protein-coupled receptor signaling pathway [GO:0002029]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of relaxation of smooth muscle [GO:1901081]; phosphorylation [GO:0016310]; regulation of the force of heart contraction [GO:0002026]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793]
|
ATP binding [GO:0005524]; beta-adrenergic receptor kinase activity [GO:0047696]; Edg-2 lysophosphatidic acid receptor binding [GO:0031755]; G protein-coupled receptor kinase activity [GO:0004703]
|
PF00169;PF00069;PF00615;
|
2.30.29.30;1.10.167.10;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, GPRK subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26817}. Cell membrane {ECO:0000250|UniProtKB:P21146}. Postsynapse {ECO:0000250|UniProtKB:P26817}. Presynapse {ECO:0000250|UniProtKB:P26817}.
|
CATALYTIC ACTIVITY: Reaction=[beta-adrenergic receptor] + ATP = [beta-adrenergic receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:19429, Rhea:RHEA-COMP:11222, Rhea:RHEA-COMP:11223, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.15; Evidence={ECO:0000250|UniProtKB:P26817}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19430; Evidence={ECO:0000250|UniProtKB:P26817};
| null | null | null | null |
FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them (PubMed:9892019). Does not act on HTR1B/5-hydroxytryptamine 1B receptor (PubMed:9892019). Key regulator of LPAR1 signaling (By similarity). Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor (By similarity). Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner (By similarity). Inhibits relaxation of airway smooth muscle in response to blue light (By similarity). {ECO:0000250|UniProtKB:P25098, ECO:0000250|UniProtKB:Q99MK8, ECO:0000269|PubMed:9892019}.
|
Didelphis virginiana (North American opossum) (Didelphis marsupialis virginiana)
|
O97666
|
APJ_MACMU
|
MEEGGDFDNYYGADNQSECEYTDWKSSGALIPAIYMLVFLLGTTGNGLVLWTVFRSSREKRRSADIFIASLAVADLTFVVTLPLWATYTYRDYDWPFGTFSCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAMPVMVFRTTGDLENTTKVQCYMDYSMVATVSSDWAWEVGLGVSSTTVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDLFLMNVFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCGQSRCAGTSHSSSGEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVVD
| null | null |
blood vessel development [GO:0001568]; brain development [GO:0007420]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; coronary vasculature development [GO:0060976]; G protein-coupled receptor signaling pathway [GO:0007186]; gastrulation [GO:0007369]; heart development [GO:0007507]; immune response [GO:0006955]; negative regulation of cAMP-mediated signaling [GO:0043951]; neurogenesis [GO:0022008]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903589]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of inhibitory G protein-coupled receptor phosphorylation [GO:1904325]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]
|
external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
|
apelin receptor activity [GO:0060182]; C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35414}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}. Note=After exposure to apelin (APLN) or apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:Q9JHG3}.
| null | null | null | null | null |
FUNCTION: Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone. May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis. Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development. Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure. {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:P79960, ECO:0000250|UniProtKB:Q7SZP9, ECO:0000250|UniProtKB:Q9WV08}.; FUNCTION: (Microbial infection) Alternative coreceptor with CD4 for HIV-1 infection; may be involved in the development of AIDS dementia.
|
Macaca mulatta (Rhesus macaque)
|
O97676
|
SRBP1_PIG
|
MDEPPFTEAALEQALAEPCELDAALLTDIEDMLQLINNQDSDFPGLFDAPYAGVAGGTDPTSPDASSPGSPTPPPSTMSSPLEGFLGGARTPPPPPVSPTQPAPTPLKMYPSVPAFSPGPGIKEEPVPLTILQPPTPQPLSGALLPQSLPALAPPQLSPAPVLGYPSPPGSFSSATPPGSTSQTLPGLPLASLPGVLPVSVHTQVQSAAPQQLLTATATPVVSPGTTTVTSQIQQVPVLLQPHFIKADSLLLTTMKTDMGTPVKAAGIGSLAPGTAVQAAPLQTLVSGGTILATVPLVVDTDKLPINRLAAGGKALSSGQSRGEKRTAHNAIEKRYRSSINDKIIELKDLVVGTEAKLNKSAVLRKAIDYIRFLQQSNQKLKQENLSLRTAAHKSKSLKDLVSCSSGGRTDVPMEGVKPEVVDTLSPPPSDAGSPSQSSPLSLGSRGSSSGGSGSDSEPDSPVFEDSQMKPEQLPAPHGRGMLDRSRLALCVLVFLCLSCNPLASLMGSWALPGPSDATSAYHGPWRSVLGAEGRDGPGWVLWLLPPLVWLTNGLLVLLFLALLFVYGEPVTRPHSDPAVRFWRHRKQADLDLARGDFAQAAQQLWLALRALGRPLPTSHLDLACSLLWNLIRHLLQRLWVGRWLAGRAGGLRRDSALEADTRTSACDAALVYHKLHQLHTMGKYPGGHLDAANLALSALNLAECAGDALSVAVLAEVYVAAALRVKTSLPRALHFLTRFFLSSARQACLAQSGSVPVAMQWLCHPVGHRFFVDGDWAVCGAPRDSLYSVAGNPVDPLAQVTQLFREHLLEQALHCVAQPSPGPGSADGDREFSEALGFLQLLNSCCDTAGAPACSFSIASSTAATAGTDPVAKWWASLTAVVTHWLGRDEEAAERLYPLVEHLPRALQESERPLPRAALHSFKAARALLGRGKAESGSASLAMCEKASGYLQDSLAATPAGSSIDKAMQLLLCDLLLVARTSLWQRQKPPPPSQASQGSSSGAQASALELRGFQRDLSGLRRLAQSFRPAMRRVFLHEATARLMAGASPARTHQLLDRSLRRRAGPCGRGGAAAAAAAELEPRPTRREQAEALLLASCYLPPGFLSAPGQRVGMLAEAARTLEKLGDRRLLHDCQQMLMRLGGGTTVTSS
| null | null |
cholesterol metabolic process [GO:0008203]; lipid biosynthetic process [GO:0008610]; positive regulation of triglyceride biosynthetic process [GO:0010867]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00010;
|
4.10.280.10;
|
SREBP family
|
PTM: [Sterol regulatory element-binding protein 1]: Processed in the Golgi apparatus, releasing the protein from the membrane. At low cholesterol the SCAP-SREBP complex is recruited into COPII vesicles for export from the endoplasmic reticulum. In the Golgi, complex SREBPs are cleaved sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain, releasing the transcription factor from the Golgi membrane. {ECO:0000250|UniProtKB:P36956}.; PTM: Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression. Phosphorylation at Ser-403 by SIK1 represses activity possibly by inhibiting DNA-binding. {ECO:0000250|UniProtKB:Q9WTN3}.; PTM: [Processed sterol regulatory element-binding protein 1]: Ubiquitinated; the nuclear form has a rapid turnover and is rapidly ubiquitinated and degraded by the proteasome in the nucleus. {ECO:0000250|UniProtKB:P36956}.
|
SUBCELLULAR LOCATION: [Sterol regulatory element-binding protein 1]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P36956}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WTN3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q9WTN3}; Multi-pass membrane protein {ECO:0000255}. Note=At high sterol concentrations, the SCAP-SREBP is retained in the endoplasmic reticulum. Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed. {ECO:0000250|UniProtKB:Q9WTN3}.; SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding protein 1]: Nucleus {ECO:0000250|UniProtKB:P36956}.
| null | null | null | null | null |
FUNCTION: [Sterol regulatory element-binding protein 1]: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 1), which is embedded in the endoplasmic reticulum membrane (By similarity). Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis and lipid homeostasis (By similarity). {ECO:0000250|UniProtKB:P36956, ECO:0000250|UniProtKB:Q9WTN3}.; FUNCTION: [Processed sterol regulatory element-binding protein 1]: Key transcription factor that regulates expression of genes involved in cholesterol biosynthesis and lipid homeostasis. Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3'). Regulates the promoters of genes involved in cholesterol biosynthesis and the LDL receptor (LDLR) pathway of sterol regulation. {ECO:0000250|UniProtKB:P36956}.
|
Sus scrofa (Pig)
|
O97703
|
CD81_CHLAE
|
MGVEGCTKCIKYLLFVFNFVFWLAGGVILGVALWLRHDPQTTNLLYLELGDKPAPNTFYVGIYILIAVGAVMMFVGFLGCYGAIQESQCLLGTFFTCLVILFACEVAAGIWGFVNKDQIAKDVKQFYDQALQQAVVDDDANNAKAVVKTFHETLDCCGSSTLAALTTSVLKNNLCPSGSNIISNLLKKDCHQKIDELFSGKLYLIGIAAIVVAVIMIFEMILSMVLCCGIRNSSVY
| null | null |
CD4-positive, alpha-beta T cell costimulation [GO:0035783]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunological synapse formation [GO:0001771]; macrophage fusion [GO:0034238]; myoblast fusion involved in skeletal muscle regeneration [GO:0014905]; osteoclast fusion [GO:0072675]; positive regulation of B cell activation [GO:0050871]; positive regulation of B cell receptor signaling pathway [GO:0050861]; positive regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000563]; positive regulation of inflammatory response to antigenic stimulus [GO:0002863]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of protein exit from endoplasmic reticulum [GO:0070863]; positive regulation of receptor clustering [GO:1903911]; positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell [GO:2001190]; positive regulation of T cell receptor signaling pathway [GO:0050862]; positive regulation of T-helper 2 cell cytokine production [GO:2000553]; protein localization to plasma membrane [GO:0072659]; receptor internalization [GO:0031623]; regulation of macrophage migration [GO:1905521]
|
basolateral plasma membrane [GO:0016323]; immunological synapse [GO:0001772]; membrane [GO:0016020]; plasma membrane [GO:0005886]; tetraspanin-enriched microdomain [GO:0097197]
|
cholesterol binding [GO:0015485]; integrin binding [GO:0005178]
|
PF00335;
|
1.10.1450.10;
|
Tetraspanin (TM4SF) family
|
PTM: Not glycosylated. {ECO:0000305}.; PTM: Likely constitutively palmitoylated at low levels. Protein palmitoylation is up-regulated upon coligation of BCR and CD9-C2R-CD81 complexes in lipid rafts. {ECO:0000250|UniProtKB:P60033}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35762}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P60033}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with CLDN1 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000250|UniProtKB:P60033}.
| null | null | null | null | null |
FUNCTION: Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Essential for trafficking and compartmentalization of CD19 receptor on the surface of activated B cells. Upon initial encounter with microbial pathogens, enables the assembly of CD19-CR2/CD21 and B cell receptor (BCR) complexes at signaling TERMs, lowering the threshold dose of antigen required to trigger B cell clonal expansion and antibody production. In T cells, facilitates the localization of CD247/CD3 zeta at antigen-induced synapses with B cells, providing for costimulation and polarization toward T helper type 2 phenotype. Present in MHC class II compartments, may also play a role in antigen presentation (By similarity). Can act both as positive and negative regulator of homotypic or heterotypic cell-cell fusion processes. Positively regulates sperm-egg fusion and may be involved in acrosome reaction. In myoblasts, associates with CD9 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD9 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (By similarity). Also prevents the fusion of mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). May regulate the compartmentalization of enzymatic activities. In T cells, defines the subcellular localization of dNTPase SAMHD1 and permits its degradation by the proteasome, thereby controlling intracellular dNTP levels (By similarity). Also involved in cell adhesion and motility. Positively regulates integrin-mediated adhesion of macrophages, particularly relevant for the inflammatory response in the lung (By similarity). {ECO:0000250|UniProtKB:P35762, ECO:0000250|UniProtKB:P60033}.
|
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
|
O97711
|
HYAS2_BOVIN
|
MHCERFLCILRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQSLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVIDGNSEDDLYMMDIFSEVMGRDKSATYIWKNNYHVKGPGETDESHKESSQHVTQLVLSNKSICTMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQEFMGSQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFREWLYNAMWFHKHHLWMTYEAVITGFFPFFLIATVIQLFYRGKIWNTLLFLLTVQLVGLIKSSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIPVSVWFTILLGGVIFTIYKESKKPFSESKQTVLIVGTLLYACYWVMLLTLYVVLINKCGRRKKGQQYDMVLDV
|
2.4.1.212
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
atrioventricular canal development [GO:0036302]; endocardial cushion to mesenchymal transition [GO:0090500]; extracellular matrix assembly [GO:0085029]; extracellular polysaccharide biosynthetic process [GO:0045226]; hyaluronan biosynthetic process [GO:0030213]; positive regulation of urine volume [GO:0035810]; renal water absorption [GO:0070295]; vasculogenesis [GO:0001570]
|
endoplasmic reticulum membrane [GO:0005789]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; plasma membrane [GO:0005886]
|
hyaluronan synthase activity [GO:0050501]
|
PF03142;
| null |
NodC/HAS family
|
PTM: Phosphorylation at Thr-328 is essential for hyaluronan synthase activity. {ECO:0000250|UniProtKB:Q92819}.; PTM: O-GlcNAcylation at Ser-221 increases the stability of HAS2 and plasma membrane localization. {ECO:0000250|UniProtKB:Q92819}.; PTM: Ubiquitination at Lys-190; this ubiquitination is essential for hyaluronan synthase activity and homo- or hetero-oligomerization. Can also be poly-ubiquitinated. Deubiquitinated by USP17 and USP4. USP17 efficiently removes 'Lys-63'- and 'Lys-48'-linked polyubiquitin chains, whereas USP4 preferentially removes monoubiquitination and, partially, both 'Lys-63'- and 'Lys-48'-linked polyubiquitin chain. {ECO:0000250|UniProtKB:Q92819}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000250|UniProtKB:Q92819}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Lysosome {ECO:0000250|UniProtKB:Q92819}. Note=Travels from endoplasmic reticulum (ER), Golgi to plasma membrane and either back to endosomes and lysosomes, or out into extracellular vesicles. Post-translational modifications control HAS2 trafficking. {ECO:0000250|UniProtKB:Q92819}.
|
CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP; Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212; Evidence={ECO:0000250|UniProtKB:Q92819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20466; Evidence={ECO:0000250|UniProtKB:Q92819}; CATALYTIC ACTIVITY: Reaction=N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP; Xref=Rhea:RHEA:12528, Rhea:RHEA-COMP:12585, Rhea:RHEA-COMP:12587, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212; Evidence={ECO:0000250|UniProtKB:Q92819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12529; Evidence={ECO:0000250|UniProtKB:Q92819};
| null |
PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis. {ECO:0000250|UniProtKB:Q92819}.
| null | null |
FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation (By similarity). This is one of three isoenzymes responsible for cellular hyaluronan synthesis and it is particularly responsible for the synthesis of high molecular mass hyaluronan (By similarity). {ECO:0000250|UniProtKB:P70312, ECO:0000250|UniProtKB:Q92819}.
|
Bos taurus (Bovine)
|
O97716
|
THA_PIG
|
MEQKPSKVECGSDPEENSARSPDGKRKRKNGQCSLKTSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHVATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQAVLLMSTDRSGLLCVDKIEKSQEAYLLAFEHYVNHRKHNIPHFWPKLLMKEREVQSSILYKGAAAEGRPGGSLGVHPEGQQLLGMHVVQGPQVRQLEQQLGEAGSLRGPVLQHQSPKSPQQRLLELLHRSGILHARAVCGEDDSSEAGSLTSSDEDPEVCEDAAQATQPLPEAPPRADGEGGGGGS
| null | null |
cell differentiation [GO:0030154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; retinoic acid receptor signaling pathway [GO:0048384]; thyroid hormone mediated signaling pathway [GO:0002154]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; thyroid hormone binding [GO:0070324]; 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.; SUBCELLULAR LOCATION: [Isoform Alpha-2]: Cytoplasm {ECO:0000250|UniProtKB:P63058}. Nucleus {ECO:0000250|UniProtKB:P63058}. Note=When overexpressed found in the cytoplasm where it colocalizes with TACC1. {ECO:0000250|UniProtKB:P63058}.
| null | null | null | null | null |
FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.
|
Sus scrofa (Pig)
|
O97741
|
SCNNA_RABIT
|
MKGDKREEQGPGPETVAPQQPTEDEEALIEFHRSYRELFQFFCNNTTIHGAIRLVCSKHNRMKTAFWAVLWLCTFGMMYWQFGLLFGEYFSYPVNLNINLNSDKLVFPAVTVCTLNPYRYPEITEQLKELDSITQQTLLDLFKYNASTLEAQPRHRRDVHPPLPHPLQRLRVPPPRLEARRARSSASSVRDNSPEVGRKDWMIGFQLCNQNRSDCFYQRYSSGVDAVREWYRFHYINILSRLSDTSLSREQLGNFIFTCRFNQAFCGDGNYSHFHHPMYGNCYTFNDKNNSSLWMSSMPGINNGLSLTLRTEQNDFIPLLSTVTGARVMVHGQDEPAFMDDGGFNLRPGVETSISMRKESLDRLGGDYGDCTQNGSDVPVKNLYRSKYTQQVCIHSCFQENMVKECGCAYIFYPLPEGVEYCDYRKHNSWGYCYYKLQDAFSSDRLGCFTKCRKPCSVTNYELSAGYSRWPSVTSQDWVFQMLSLQNNYTVSNKRNGVAKLNIYFKELNYKANSESPSVTMVTLLSNLGSQWSLWFGSSVLSVVEMAELLFDLSVITFLMLLRRFRSRYWSPGRGAGGAREVASSPVSALPSRFCPHPTSPSVPQPGPTLPPSLTAPPPAYATLGPCLSQSGSACAPGEP
| null | null |
multicellular organismal-level water homeostasis [GO:0050891]; response to stimulus [GO:0050896]; sensory perception of taste [GO:0050909]; sodium ion homeostasis [GO:0055078]; sodium ion transmembrane transport [GO:0035725]
|
acrosomal vesicle [GO:0001669]; apical plasma membrane [GO:0016324]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; motile cilium [GO:0031514]; plasma membrane [GO:0005886]; sodium channel complex [GO:0034706]; sperm principal piece [GO:0097228]
|
ligand-gated sodium channel activity [GO:0015280]
|
PF00858;
|
2.60.470.10;1.10.287.770;
|
Amiloride-sensitive sodium channel (TC 1.A.6) family, SCNN1A subfamily
|
PTM: Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation. {ECO:0000250|UniProtKB:P37089}.; PTM: ENaC cleavage by furin, and subsequently by prostasin (PRSS8), leads to a stepwise increase in the open probability of the channel as a result of release of the alpha and gamma subunit inhibitory tracts, respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects ENaC against proteolytic activation. {ECO:0000250|UniProtKB:P37088}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P37089}.
|
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P37089}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P37089}. Cell projection, cilium {ECO:0000250|UniProtKB:P37088}. Cytoplasmic granule {ECO:0000250|UniProtKB:P37088}. Cytoplasm {ECO:0000250|UniProtKB:P37088}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P37089}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:P37089}. Note=In the oviduct and bronchus, located on cilia in multi-ciliated cells. In endometrial non-ciliated epithelial cells, restricted to apical surfaces. In epidermis, located nearly uniformly in the cytoplasm in a granular distribution. In sebaceous glands, observed only in the cytoplasmic space in between the lipid vesicles. In eccrine sweat glands, mainly located at the apical surface of the cells facing the lumen. In skin, in arrector pili muscle cells and in adipocytes, located in the cytoplasm and colocalized with actin fibers. In spermatogonia, spermatocytes and round spermatids, located in the cytoplasm. Prior to spermiation, location shifts from the cytoplasm to the spermatid tail. In spermatozoa, localizes at the acrosome and the central region of the sperm flagellum. {ECO:0000250|UniProtKB:P37088, ECO:0000250|UniProtKB:P37089}.
| null | null | null | null | null |
FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and eccrine sweat glands. Also plays a role in taste perception. {ECO:0000250|UniProtKB:P37088}.
|
Oryctolagus cuniculus (Rabbit)
|
O97756
|
SNAT_MACMU
|
MSTQSTHPPKPEAPRLPPAISSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVLGVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKDRLMQESLTMHRPGGHIAHLHVLAVHCAFRQQGRGPILLWRYLHHLGSQPAVHRAALMCEDALVPFYERFGFHAMGPCAITVGSLSFTELHCSLQGHPFLRRNSGC
|
2.3.1.87
| null |
cellular response to cAMP [GO:0071320]; circadian rhythm [GO:0007623]; melatonin biosynthetic process [GO:0030187]; N-terminal protein amino acid acetylation [GO:0006474]; response to light stimulus [GO:0009416]
|
cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
|
aralkylamine N-acetyltransferase activity [GO:0004059]
|
PF00583;
|
3.40.630.30;
|
Acetyltransferase family, AANAT subfamily
|
PTM: cAMP-dependent phosphorylation regulates AANAT activity by promoting interaction with 14-3-3 proteins. Phosphorylation levels exhibit night/day variations, with an increase during nighttime. {ECO:0000269|PubMed:12364461}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16613}.
|
CATALYTIC ACTIVITY: Reaction=a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine + CoA + H(+); Xref=Rhea:RHEA:20497, ChEBI:CHEBI:15378, ChEBI:CHEBI:55469, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:77827; EC=2.3.1.87; Evidence={ECO:0000269|PubMed:12364461};
| null |
PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.
| null | null |
FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. {ECO:0000269|PubMed:12364461}.
|
Macaca mulatta (Rhesus macaque)
|
O97758
|
ZO1_CANLF
|
MSARAAAAKNTAMEETAIWEQHTVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSRPDPEPVSENEDSYDEEVHDPRSSRGGLVSRRSEKSWARDRSASRERSLSPRSDRRSVASSQPPKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSGRSHDRPPRHSRSRSPDQRSEPSDHSRHSPQQPSSGSLRSREEERISKPGAVSTPVKHADDHTHKTVEEVVVERNEKQAPSLPEPKPVYAQVGQPDVDLPVSPSDGVLPNSTHEDGILRPSMKLVKFRKGDSVGLRLAGGNDVGIFVAGVLEDSPAAKEGLEEGDQILRVNNVDFTNIIREEAVLFLLDLPKGEEVTILAQKKKDVYRRIVESDVGDSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNKNRAEQLASVQYTLPKTAGGDRADFWRFRGLRSSKRNLRKSREDLSAQPVQTKFPAYERVVLREAGFLRPVTIFGPIADVAREKLAREEPDIYQIAKSEPRDAGTDQRSSGIIRLHTIKQIIDQDKHALLDVTPNAVDRLNYAQWYPIVVFLNPDSKQGVKTMRMRLCPESRKSARKLYERSHKLRKNNHHLFTTTINLNSMNDGWYGALKEAIQQQQNQLVWVSEGKADGATSDDLDLHDDRLSYLSAPGSEYSMYSTDSRHTSDYEDTDTEGGAYTDQELDETLNDEVGTPPESAITRSSEPVREDSSGMHHENQTYPPYSPQAQPQPIHRIDSPGFKTASQQKAEASSPVPYLSPETNPASSTSAVNHNVTLTNVRLEGPTPAPSTSYSPQADSLRTPSTEAAHIMLRDQEPSLPSHVEPAKVYRKDPYPEEMMRQNHVLKQPAVGHPGQRPDKEPNLSYESQPPYVEKQANRDLEQPTYRYDSSSYTDQFSRNYDHRLRYEERIPTYEEQWSYYDDKQPYQPRPSLDNQHPRDLDSRQHPEESSERGSYPRFEEPAPLSYDSRPRYDQPPRTSTLRHEEQPTPGYDMHNRYRPEAQSYSSAGPKASEPKQYFDQYPRSYEQVPSQGFSSKAGHYEPLHGAAVVPPLIPASQHKPEVLPSNTKPLPPPPTLTEEEEDPAMKPQSVLTRVKMFENKRSASLENKKDENHTAGFKPPEVASKPPGAPIIGPKPTPQNQFSEHDKTLYRIPEPQKPQMKPPEDIVRSNHYDPEEDEEYYRKQLSYFDRRSFENKPSTHIPAGHLSEPAKPVHSQNQTNFSSYSSKGKSPEADAPDRSFGEKRYEPVQATPPPPPLPSQYAQPSQPGTSSSLALHTHAKGAHGEGNSISLDFQNSLVSKPDPPPSQNKPATFRPPNREDTVQSTFYPQKSFPDKAPVNGAEQTQKTVTPAYNRFTPKPYTSSARPFERKFESPKFNHNLLPSETAHKPDLSSKAPASPKTLAKAHSRAQPPEFDSGVETFSIHADKPKYQMNNLSTVPKAIPVSPSAVEEDEDEDGHTVVATARGVFNNNGGVLSSIETGVSIIIPQGAIPEGVEQEIYFKVCRDNSILPPLDKEKGETLLSPLVMCGPHGLKFLKPVELRLPHCASMTPDGWSFALKSSDSSSGDPKTWQNKCLPGDPNYLVGANCVSVLIDHF
| null | null |
bicellular tight junction assembly [GO:0070830]; cell-cell adhesion [GO:0098609]; cell-cell junction organization [GO:0045216]; cellular response to calcium ion [GO:0071277]; establishment of endothelial intestinal barrier [GO:0090557]; positive regulation of blood-brain barrier permeability [GO:1905605]; protein localization to cell-cell junction [GO:0150105]
|
bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; gap junction [GO:0005921]; plasma membrane [GO:0005886]; tight junction [GO:0070160]
|
calmodulin binding [GO:0005516]; cell adhesion molecule binding [GO:0050839]
|
PF00625;PF00595;PF07653;PF00791;
|
2.30.42.10;2.60.220.30;3.40.50.300;2.30.30.40;
|
MAGUK family
|
PTM: Phosphorylated at tyrosine redidues in response to epidermal growth factor (EGF) (By similarity). This response is dependent on an intact actin microfilament system (By similarity). Dephosphorylated by PTPRJ (By similarity). {ECO:0000250|UniProtKB:Q07157}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9792688}; Peripheral membrane protein {ECO:0000269|PubMed:9792688}; Cytoplasmic side {ECO:0000269|PubMed:9792688}. Cell junction, tight junction {ECO:0000269|PubMed:9792688}. Cell junction {ECO:0000250|UniProtKB:P12830}. Cell junction, gap junction {ECO:0000250|UniProtKB:Q07157}. Note=Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact (PubMed:9792688). Distributed over the entire lateral surface of the plasma membrane and other actin-rich structures (PubMed:9792688). Detected at the leading edge of migrating and wounded cells (By similarity). Colocalizes with SPEF1 at sites of cell-cell contact in intestinal epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:9792688}.
| null | null | null | null | null |
FUNCTION: TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:10575001, PubMed:27802160, PubMed:9792688). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (PubMed:27802160). Plays a role in the regulation of cell migration by targeting CDC42BPBb to the leading edge of migrating cells (By similarity). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (PubMed:24986862). {ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:24986862, ECO:0000269|PubMed:27802160, ECO:0000269|PubMed:9792688}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O97763
|
NPC2_PIG
|
MHFLAAAFLLLTLSASALAEPVHFRDCGSGVGVIKEVNVNPCPTQPCQLHKGQSYSVNVTFTSNTQSKGSKAVVHGIVMGVPIPFPIPDPDGCKSGINCPIQKDQTYSYLNKLPVKAEYPSIKLVVEWKLQDDNDQCLFCWQIPVQIES
| null | null |
cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; intracellular cholesterol transport [GO:0032367]
|
endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; lysosome [GO:0005764]
|
cholesterol binding [GO:0015485]
|
PF02221;
|
2.60.40.770;
|
NPC2 family
|
PTM: N-glycosylated. Found in the epididymal fluid as a 19 kDa glycoprotein that is processed during its passage through the epididymis into a 16 kDa protein. {ECO:0000269|PubMed:10366780}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10366780}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61916}. Lysosome {ECO:0000250|UniProtKB:P61916}. Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. {ECO:0000250|UniProtKB:P61916}.
|
CATALYTIC ACTIVITY: Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, ChEBI:CHEBI:16113; Evidence={ECO:0000250|UniProtKB:P79345};
| null | null | null | null |
FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment. 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. May bind and mobilize cholesterol that is associated with membranes (By similarity). NPC2 binds cholesterol with a 1:1 stoichiometry (PubMed:10366780). Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (By similarity). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport (By similarity). {ECO:0000250|UniProtKB:P61916, ECO:0000250|UniProtKB:Q9Z0J0, ECO:0000269|PubMed:10366780}.
|
Sus scrofa (Pig)
|
O97775
|
ANDR_PANTR
|
MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSAPECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQEGDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ
| null | null |
androgen receptor signaling pathway [GO:0030521]; intracellular receptor signaling pathway [GO:0030522]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of integrin biosynthetic process [GO:0045720]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phosphorylation [GO:0042327]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein localization to plasma membrane [GO:1903076]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
androgen binding [GO:0005497]; beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF02166;PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-526 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity). Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-81 by CDK9 regulates AR promoter selectivity and cell growth (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Sumoylated on Lys-385 (major) and Lys-512 (By similarity). Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250|UniProtKB:P10275}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. {ECO:0000250|UniProtKB:P10275}.
| null | null | null | null | null |
FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207}.
|
Pan troglodytes (Chimpanzee)
|
O97776
|
ANDR_EULFC
|
MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGARLQQQQETSPPQQQQQQQGEDGSPQAQSRGPTGYLALDEEQQPSQQQSALECHPESGCVPEPGAAAAASKGLQQQPPAPSDEDDSAVPSTLSLLGPTFPGLSSCSADLKDILSEAGTMQLLQQQQQEAVSEGSSSGRAREAAGAPTSSKDSYLGGTSTISDSAKELCKAVSVSMGLGVETLEHLSPGEQLRGDCMYAPLLGGPPAVRPTPCAPLAECKGSLLDDSADKGTEEPAEYTPFKGSYTQGLEGESLGCSGSSEAGSSGTLELPSTLSLYKSGALEEAASYQSRDYYNFPLALAGPPPPPLPPHPHARIKLENPLDYGSSWAAAAAQCRFGDLASLHGGGATGPGSGSPSAAAASSWHTLFTAEEGQLYGPCGGGGGGTSEAGAVTPYGYSRPPQGLAGQEGDFPAPDVWYPSGVVSRVPYPSPSCVKSEMGPWMESYSGPYGDVRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSATSPTEESSQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ
| null | null |
androgen receptor signaling pathway [GO:0030521]; intracellular receptor signaling pathway [GO:0030522]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of integrin biosynthetic process [GO:0045720]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phosphorylation [GO:0042327]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein localization to plasma membrane [GO:1903076]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
androgen binding [GO:0005497]; beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF02166;PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-499 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity). Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-61 by CDK9 regulates AR promoter selectivity and cell growth (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Sumoylated on Lys-367 (major) and Lys-485 (By similarity). Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation. {ECO:0000250|UniProtKB:P10275}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. {ECO:0000250|UniProtKB:P10275}.
| null | null | null | null | null |
FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207}.
|
Eulemur fulvus collaris (Collared brown lemur) (Eulemur collaris)
|
O97799
|
KIT_CANLF
|
MRGARGAWDFLCVLLLLLLLGVQTGSSQPSVSPGEPSLPSIHPAKSELIVSVGDELRLSCTDPGFVKWTFETLGQLNENTHNEWITEKAEAGHTGNYTCTNRDGLSRSIYVFVRDPAKLFLVDLPLYGKEGNDTLVRCPLTDPEVTNYSLRGCEGKPLPKDLTFVADPKAGITIRNVKREYHRLCLHCSADQKGRTVLSKKFTLKVRAAIRAVPVVSVSKTSSLLKEGEAFSVMCFIKDVSSFVDSMWIKENSQQTNAQTQSNSWHHGDFNFERQEKLIISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMMSTTIFVNDGENVDLIVEYEAYPKPEHQQWIYMNRTFTDKWEDYPKSDNESNIRYVSELHLTRLKGNEGGTYTFQVSNSDVNSSVTFNVYVNTKPEILTHESLTNGMLQCVVAGFPEPAVDWYFCPGAEQRCSVPIGPMDVQMQNSSLSPSGKLVVQSSIDYSAFKHNGTVECRAYNNVGRSSAFFNFAFKGNSKEQIHPHTLFTPLLIGFVIAAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHGEVALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSARIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISDSTNHIYSNLANCSPNPERPVVDHSVRINSVGSSASSTQPLLVHEDV
|
2.7.10.1
| null |
actin cytoskeleton organization [GO:0030036]; B cell differentiation [GO:0030183]; cell chemotaxis [GO:0060326]; cytokine-mediated signaling pathway [GO:0019221]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; digestive tract development [GO:0048565]; ectopic germ cell programmed cell death [GO:0035234]; embryonic hemopoiesis [GO:0035162]; erythrocyte differentiation [GO:0030218]; erythropoietin-mediated signaling pathway [GO:0038162]; Fc receptor signaling pathway [GO:0038093]; glycosphingolipid metabolic process [GO:0006687]; hematopoietic progenitor cell differentiation [GO:0002244]; hematopoietic stem cell migration [GO:0035701]; immature B cell differentiation [GO:0002327]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; Kit signaling pathway [GO:0038109]; lamellipodium assembly [GO:0030032]; lymphoid progenitor cell differentiation [GO:0002320]; male gonad development [GO:0008584]; mast cell chemotaxis [GO:0002551]; mast cell degranulation [GO:0043303]; mast cell differentiation [GO:0060374]; mast cell proliferation [GO:0070662]; megakaryocyte development [GO:0035855]; melanocyte adhesion [GO:0097326]; melanocyte differentiation [GO:0030318]; melanocyte migration [GO:0097324]; myeloid progenitor cell differentiation [GO:0002318]; negative regulation of developmental process [GO:0051093]; negative regulation of programmed cell death [GO:0043069]; negative regulation of reproductive process [GO:2000242]; ovarian follicle development [GO:0001541]; phosphorylation [GO:0016310]; pigmentation [GO:0043473]; positive regulation of cell migration [GO:0030335]; positive regulation of dendritic cell cytokine production [GO:0002732]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mast cell cytokine production [GO:0032765]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular associated smooth muscle cell differentiation [GO:1905065]; regulation of cell shape [GO:0008360]; response to radiation [GO:0009314]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283]; stem cell differentiation [GO:0048863]; T cell differentiation [GO:0030217]
|
cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrillar center [GO:0001650]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; SH2 domain binding [GO:0042169]; stem cell factor receptor activity [GO:0005020]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
|
PF00047;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
|
PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation. {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding promotes autophosphorylation. Phosphorylated tyrosine residues are important for interaction with specific binding partners (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
|
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=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1 (By similarity). {ECO:0000250}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O97817
|
AGRL2_BOVIN
|
MVSSGCRMRSLWFIIIISFLPNTEGFSRAALPFGLVRRELSCEGYSIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAFKIMTQRCNNRTQCIVVTGSDVFPDPCPGTYKYLEVQYECVPYMEQKVFVCPGTLKAIVDSPCIYEAEQKAGAWCKDPLQAADKIYFMPWTPYRTDTLIEYASLEDFQNSRQTTTYKLPNRVDGTGFVVYDGAVFFNKERTRNIVKYDLRTRIKSGEAIINYANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEQNNGMIVISQLNPYTLRFEATWETVYDKRAASNAFMICGVLYVVRSVYQDNESETGKNAIDYIYNTRLNRGEYVDVPFPNQYQYIAAVDYNPRDNQLYVWNNNFILRYSLEFGPPDPAQVPTTAVTITSSAEMFKTTVSTTSTTSQKGPMSTTVAGSQEGSKGTKAPPAVSTTKIPPVTNIFPLPERFCEALDARGIRWPQTQRGMMVERPCPKGTRGTASYLCVLSTGTWNPKGPDLSNCTSHWVNQLAQKIRSGENAASLANELAKHTKGPVFAGDVSSSVRLMEQLVDILDAQLQELKPSEKDSAGRSYNKLQKREKTCRAYLKAIVDTVDNLLRPEALESWKHMNSSEQAHTATMLLDTLEEGAFVLADNLVEPTRVSMPTENIVLEVAVLSTEGQVQDFKFPLGIKGAGSSIQLSANTVKQNSRNGLAKLVFIIYRSLGQFLSTENATIKLGADFIGRNSTIAVNSHVISVSINKESSRVYLTDPVLFTLPHIDPDNYFNANCSFWNYSERTMMGYWSTQGCKLVDTNKTRTTCACSHLTNFAILMAHREIAYKDGVHELLLTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTKYMIACPIFAGLLHFFFLAAFAWMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLHVDNYFIWSFIGPVTFIILLNIIFLVITLCKMVKHSNTLKPDSSRLENINNYRVCDGYYNTDLPGSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGVFIFIFHCALQKKVRKEYGKCFRHSYCCGGLPTESPHSSVKASTTRTSARYSSGTQSRIRRMWNDTVRKQSESSFISGDINSTSTLNQGMTGNYLLTNPLLRPHGTNNPYNTLLAETVVCNAPSAPVFNSPGHSLNNARDTSAMDTLPLNGNFNNSYSLRKGDYNDSVQVVDCGLSLNDTAFEKMIISELVHNNLRGSSKAHNLELTLPVKPVIGGSSSEDDAIVADASSLMHGDNPGLELHHKELEAPLIPQRTHSLLYQPQKKAKPEGTDSYVSQLTAEAEDHLQSPNRDSLYTSMPNLRDSPYQESSPDMEEDLSPSRRSENEDIYYKSMPNLGAGHQLQMCYQISRGNSDGYIIPINKEGCIPEGDVREGQMQLVTSL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; signal transduction [GO:0007165]
|
extracellular space [GO:0005615]; membrane [GO:0016020]
|
carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930]
|
PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191;
|
1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
|
PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Calcium-independent receptor of low affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. {ECO:0000250|UniProtKB:O88923}.
|
Bos taurus (Bovine)
|
O97827
|
AGRL3_BOVIN
|
MWPSQLLVFMMLLAPIIHGGKHSERHPALASPLRHAERGPGGALPPRHLLQQPAAERATAHRGPGPRGATRGVRGPGAHGAQISAQAFSRAPIPMAVVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDFGPLDSRSGQAHHGQVSYISPPIHLDSDLERPPVREISTTGPLGTGSTTTSTTLRTTTWSPGRSTTPSVSGRRNRSTSTPSPAIEVLNDITTHVPSASPQIPALEESCEAVEAREIMWFKTRQGQMAKQPCPAGTIGVSTYLCLAPDGIWDPQGPDLSNCSSPWVNHITQKLKSGETAANIARELAEQTRNHLNAGDITYSVRAMDQLVGLLDVQLRNLTPGGKDSAARSLNKLQKRERSCRAYVQAMVETVNNLLQPQALNAWRDLTTSDQLRAATMLLDTVEESAFVLADNLLKTDIVRENTDNIQLEVARLSTEGNLEDLKFPENTGHGSTIQLSANTLKQNGRNGEIRVAFVLYNNLGPYLSTENASMKLGTEAMSTNHSVIVNSPVITAAINKEFSNKVYLADPVVFTVKHIKQSEENFNPNCSFWSYSKRTMTGYWSTQGCRLLTTNKTHTTCSCNHLTNFAVLMAHVEVKHSDAVHDLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIFLGIALYKMFHHTAILKPESGCLDNINYEDNRPFIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRKEYGKCLRTHCCSGRSTESSIGSGKTSGSRTPGRYSTGSQSRIRRMWNDTVRKQSESSFITGDINSSASLNRGAMANHLISNALLRPHGTNNPYNTLLGEPAVCNNPSVSMYNAQEGLLNNARDTSVMDTLPLNGNHGNSYSIASGEYLSNCVQIIDRGYNHNETALEKKILKELTSNYIPSYLNNHERSSEQNRNLMNKLVNNLGSGSEDDAIVLDDATSFNHEESLGLELIHEESDAPLLPPRVYSTENHQLHHYTRRRIPQDHSESFFPLLTNEHTEDLQSPHRDSLYTSMPALAGVPTAESVTTSTQTEPPPAKCGDAEDVYYKSMPNLGSRNHVHQLHTYYQLGRGSSDGFIVPPNKDGTPPEGSSKGPAHLVTSL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; neuron migration [GO:0001764]; signal transduction [GO:0007165]; synapse assembly [GO:0007416]
|
axon [GO:0030424]; cell-cell junction [GO:0005911]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930]
|
PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191;
|
1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, LN-TM7 subfamily
|
PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250}.; PTM: O-glycosylated (major) and N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80TS3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80TS3}. Cell projection, axon {ECO:0000250|UniProtKB:Q80TS3}. Cell junction {ECO:0000250|UniProtKB:Q80TS3}.
| null | null | null | null | null |
FUNCTION: Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells. Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex. {ECO:0000250|UniProtKB:Q80TS3}.
|
Bos taurus (Bovine)
|
O97831
|
AGRL1_BOVIN
|
MARLAAVLWSLCVTAILVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVKQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLAFPNPYQFVSSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPAPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQAHTATMLLDVLEEGAFLLADNVREPARFLAAKQNVVLEVTVLNTEGQVQELVFPQEYPSENSIQLSANTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGSGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEAKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMVRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGAHGSLKTSAMRSNARYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGAPEPPRGRNLADAAAFEKMIISELVHNNLRGGSSGAKGPPPPEPPVPPVPGGSGEEEAGGPGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPSEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPDGDGQMQLVTSL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell surface receptor signaling pathway [GO:0007166]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; positive regulation of synapse maturation [GO:0090129]; signal transduction [GO:0007165]
|
axon [GO:0030424]; extracellular space [GO:0005615]; growth cone [GO:0030426]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synapse [GO:0045202]
|
carbohydrate binding [GO:0030246]; cell adhesion molecule binding [GO:0050839]; G protein-coupled receptor activity [GO:0004930]; latrotoxin receptor activity [GO:0016524]
|
PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191;
|
1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
|
PTM: Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus. {ECO:0000250|UniProtKB:O88917}.
|
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell projection, axon {ECO:0000250|UniProtKB:O88917}. Cell projection, growth cone {ECO:0000250|UniProtKB:O88917}. Synapse {ECO:0000250|UniProtKB:O88917}. Presynaptic cell membrane {ECO:0000250|UniProtKB:O88917}. Synapse, synaptosome {ECO:0000250|UniProtKB:O88917}. Note=Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. {ECO:0000250|UniProtKB:O88917}.
| null | null | null | null | null |
FUNCTION: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity). {ECO:0000250|UniProtKB:O88917}.
|
Bos taurus (Bovine)
|
O97859
|
NEUR3_BOVIN
|
MEEVTSCSFSSPLFQQEDKRGVTYRIPALIYVPPAHTFLAFAEKRSSSKDEDALHLVLRRGLRTGQSVQWEPLKSLMKATLPGHRTMNPCPVWERKSGYVYLFFICVQGHVTERQQIMSGRNPARLCFICSQDAGYSWSDVRDLTEEVIGPEVTHWATFAVGPGHGIQLQSGRLIIPAYAYYIPFWFFCFRLPYRARPHSLMIYSDDLGATWHHGRLIKPMVTVECEVAEVIGKAGHPVLYCSARTPNRHRAEALSIDHGECFQKPVLSHQLCEPPHGCQGSVVSFCPLEIPGGCQDLAGEDAPAIQQSPLLCSSVRPEPEAGTLSESWLLYSHPTNKKRRVDLGIYLNQSPLEAACWSRPWILHCGPCGYSDLAALENEGLFGCLFECGTKQECEQIAFRLFTDREILSHVQGDCSTPGMNSEPSKK
|
3.2.1.18
| null |
ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313]
|
caveola [GO:0005901]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]
|
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: Palmitoylated; may regulate intracellular trafficking and anchorage to plasma membrane and endomembranes. {ECO:0000250|UniProtKB:Q9UQ49}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9988745}; Peripheral membrane protein {ECO:0000269|PubMed:9988745}. Membrane, caveola {ECO:0000250|UniProtKB:Q9UQ49}. Early endosome membrane {ECO:0000250|UniProtKB:Q9UQ49}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UQ49}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9UQ49}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UQ49}. Lysosome membrane {ECO:0000250|UniProtKB:Q9UQ49}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UQ49}. Note=Associates with the external leaflet of the plasma membrane (By similarity). S-acylated NEU3 likely spans the lipid bilayer with a portion of C-terminus exposed to cytosol and the catalytic region facing the extracellular space (By similarity). {ECO:0000250|UniProtKB:Q9JMH7, ECO:0000250|UniProtKB:Q9UQ49}.
|
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:9988745}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD1a + H2O = a ganglioside GM1 + N-acetylneuraminate; Xref=Rhea:RHEA:47832, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:82637, ChEBI:CHEBI:82639; Evidence={ECO:0000269|PubMed:9988745}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47833; Evidence={ECO:0000305|PubMed:9988745}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD1a (d18:1(4E)) + H2O = a ganglioside GM1 (d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:47856, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; Evidence={ECO:0000250|UniProtKB:Q9UQ49}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47857; Evidence={ECO:0000250|UniProtKB:Q9UQ49}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD1b + H2O = a ganglioside GM1 + N-acetylneuraminate; Xref=Rhea:RHEA:47876, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:82639, ChEBI:CHEBI:82939; Evidence={ECO:0000269|PubMed:9988745}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47877; Evidence={ECO:0000305|PubMed:9988745}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD1b (d18:1(4E)) + H2O = a ganglioside GM1 (d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:48064, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:77709, ChEBI:CHEBI:87785; Evidence={ECO:0000250|UniProtKB:Q9UQ49}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48065; Evidence={ECO:0000250|UniProtKB:Q9UQ49}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD3 + H2O = a ganglioside GM3 + N-acetylneuraminate; Xref=Rhea:RHEA:48120, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:79210, ChEBI:CHEBI:79214; Evidence={ECO:0000269|PubMed:9988745}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48121; Evidence={ECO:0000305|PubMed:9988745}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD3 (d18:1(4E)) + H2O = a ganglioside GM3 (d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:48124, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:60065, ChEBI:CHEBI:78436; Evidence={ECO:0000250|UniProtKB:Q9UQ49}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48125; Evidence={ECO:0000250|UniProtKB:Q9UQ49}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM3 + H2O = a beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + N-acetylneuraminate; Xref=Rhea:RHEA:48136, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:79208, ChEBI:CHEBI:79210; Evidence={ECO:0000269|PubMed:9988745}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48137; Evidence={ECO:0000305|PubMed:9988745}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 + H2O = a ganglioside GA1 + N-acetylneuraminate; Xref=Rhea:RHEA:47872, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:82639, ChEBI:CHEBI:88069; Evidence={ECO:0000250|UniProtKB:Q9JMH7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47873; Evidence={ECO:0000250|UniProtKB:Q9JMH7}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 (d18:1(4E)) + H2O = a ganglioside GA1 (d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:48072, ChEBI:CHEBI:15377, ChEBI:CHEBI:27938, ChEBI:CHEBI:35418, ChEBI:CHEBI:77709; Evidence={ECO:0000250|UniProtKB:Q9JMH7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48073; Evidence={ECO:0000250|UniProtKB:Q9JMH7}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 (d18:1(4E)) + H2O = a ganglioside GA2 (d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:48068, ChEBI:CHEBI:15377, ChEBI:CHEBI:27731, ChEBI:CHEBI:35418, ChEBI:CHEBI:71502; Evidence={ECO:0000250|UniProtKB:Q9JMH7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48069; Evidence={ECO:0000250|UniProtKB:Q9JMH7}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM3 (d18:1(4E)) + H2O = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:47900, ChEBI:CHEBI:15377, ChEBI:CHEBI:17950, ChEBI:CHEBI:35418, ChEBI:CHEBI:60065; Evidence={ECO:0000250|UniProtKB:Q9UQ49}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47901; Evidence={ECO:0000250|UniProtKB:Q9UQ49}; CATALYTIC ACTIVITY: Reaction=a ganglioside GT1b + H2O = a ganglioside GD1b + N-acetylneuraminate; Xref=Rhea:RHEA:47828, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:82939, ChEBI:CHEBI:82940; Evidence={ECO:0000269|PubMed:9988745}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47829; Evidence={ECO:0000305|PubMed:9988745};
| null | null | null | null |
FUNCTION: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3 (PubMed:9988745). Plays a role in the regulation of transmembrane signaling through the modulation of ganglioside content of the lipid bilayer and by direct interaction with signaling receptors, such as EGFR. Desialylates EGFR and activates downstream signaling in proliferating cells. Contributes to clathrin-mediated endocytosis by regulating sorting of endocytosed receptors to early and recycling endosomes (By similarity). {ECO:0000250|UniProtKB:Q9UQ49, ECO:0000269|PubMed:9988745}.
|
Bos taurus (Bovine)
|
O97921
|
PTGDS_HORSE
|
MAASHTLWMGLVLLGVLGVLQTRAQAQPSLQPNFQQDKFLGRWFTSGLASNSSWFREKKKVLSMCTSVVAPTADGGFNLTSTFLRKDQCETRTLLLQPAGPPGCYSYTSPHWGMVHEVSVVETDYEEYALLYTHAESTKGLGGQDFRMATLYSRVQSPRPEVKEKFSTFAKAQGFTEDAIVFLPQTDKCMEEHN
|
5.3.99.2
| null |
gene expression [GO:0010467]; mast cell degranulation [GO:0043303]; negative regulation of male germ cell proliferation [GO:2000255]; prostaglandin biosynthetic process [GO:0001516]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum [GO:0005791]
|
fatty acid binding [GO:0005504]; prostaglandin-D synthase activity [GO:0004667]; retinoid binding [GO:0005501]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
|
CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000250|UniProtKB:P41222};
| null | null | null | null |
FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
|
Equus caballus (Horse)
|
O97939
|
ENAM_PIG
|
MLLSCRHGASSPKLDNLVPSGKMKILLVFLGLLCYSAAMPMQMPRMPGFSSKSEEMMRYGHFNFMNAPHMAHLGTLYGNGMQLPQFFPQYQMPMWPQPPPNKKHPQKPSASKQQSKTDPAPESQKPNQPQPKTPTPKQPLNEPSPTPTQPEEETQTPQAFPPFGNGLFPYQQPLWHVPHRIPPGYGRPPTSNEEGGNPYFGFFGYHGFGGRPPYYSEEMFEQDFEKPKEKDPPKTETPATEPSVNTTVPETNSTQPNAPNPRGNDTSPTGTSGQGPNPRSNPTGQNGPAVNVSGQGVPRSQSPWGPRQTIIHENYPNPNIRGFPARRQWRPPGPAMGHRRNGPFYRNQQIQRGPRWNSFTLEGKQAVRPGYPTYRRVYGSTARSNPPNYAGNSANLRRKPEGPNKNPMVTNVAPPGPKHGTVDQNENIQNPREKQVSQKERTVVPTRDPSGPWRNSQDYGINKSNYKLPQPEDNMLVPNFNSIDQRENSYYPRGESKRAPNSDGQTQTQIIPKGIVLEPRRIPYESETNQPELKHSAYQPVYTEGIPSPAKEHFPAGRNTWNQQEISPPFKEDPGRQEEHLPHLSHGSRVHVYYPDYNPYDPRENSPYLRSNTWYERDDSPNTMGQPENPHYPMNTPDPKETIPYNEEDPIDPTGDEHFPGQSRWDMEELSFKEDPTVRHYEGEQYTSNQPKEYLPYSLDNPSKPREDFLYGEFYPWNPEENFPSYNTAPTVSSPVESRGYYANNAVGQEESTMFPSWSSWDPRIQAQGQKEGRPYLNRNFWDQSTNLYKTPTSSPHQKENQPYSNNSPAGLQKNPTWHEGENLNYGMQITRLNSPERDHLAFPDLIPPDYPGGQKESHVFHLSQRGPCCAGGSMWPKNNPLALQDYTQSFGLAPGENPDTSIGYAEDSHIKYARQTVSPTSIVPGQRNSSEKILPGESQNPSPFKDDVSTLRRSTPCSVKSQLSQRGIMPLPEANSLQSKNTPCLTSDLGGDGNNVLEQIFEGNQLNERTVDLTPEQLVFGTPDKEPRPEGIPNEMQGNESERQQQRQSSILQLPCFGSKLANYHTSSIGTPSSLGRQDSFDGDPIMPTETPNSLAGLATGAQFQNINVDPLNEDEHTPFDSLQIGTNPQDQVQDCLLLQA
| null | null |
ameloblast differentiation [GO:0036305]; amelogenesis [GO:0097186]; biomineral tissue development [GO:0031214]; positive regulation of enamel mineralization [GO:0070175]
|
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]
|
structural constituent of tooth enamel [GO:0030345]
|
PF15362;
| null | null |
PTM: Proteolytically cleaved into several smaller polypeptides. Cleavage of N-terminal region of enamelin occurs soon after secretion. {ECO:0000269|PubMed:9206327}.; PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q9NRM1}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9206327}.
| null | null | null | null | null |
FUNCTION: Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation. {ECO:0000269|PubMed:9206327}.
|
Sus scrofa (Pig)
|
O97952
|
ANDR_MACFA
|
MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLQQQQQQQQETSPRQQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSAPECHPERGCVPEPGAAVAAGKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSTDLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPVLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGAGEAGAVAPYGYTRPPQGLAGQEGDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETAQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ
| null | null |
androgen receptor signaling pathway [GO:0030521]; intracellular receptor signaling pathway [GO:0030522]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of integrin biosynthetic process [GO:0045720]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phosphorylation [GO:0042327]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein localization to plasma membrane [GO:1903076]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
androgen binding [GO:0005497]; beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF02166;PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-510 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity). Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-65 by CDK9 regulates AR promoter selectivity and cell growth (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Sumoylated on Lys-371 (major) and Lys-496 (By similarity). Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation. {ECO:0000250|UniProtKB:P10275}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. {ECO:0000250|UniProtKB:P10275}.
| null | null | null | null | null |
FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207}.
|
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
|
O97960
|
ANDR_PAPHA
|
MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSAPECHPERGCVPEPGAAVAAGKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPVLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGELASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGAGEAGAVAPYGYTRPPQGLAGQEGDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETAQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ
| null | null |
androgen receptor signaling pathway [GO:0030521]; intracellular receptor signaling pathway [GO:0030522]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of integrin biosynthetic process [GO:0045720]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phosphorylation [GO:0042327]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein localization to plasma membrane [GO:1903076]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
androgen binding [GO:0005497]; beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF02166;PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-510 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity). Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-66 by CDK9 regulates AR promoter selectivity and cell growth (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Sumoylated on Lys-371 (major) and Lys-496 (By similarity). Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250|UniProtKB:P10275}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. {ECO:0000250|UniProtKB:P10275}.
| null | null | null | null | null |
FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207}.
|
Papio hamadryas (Hamadryas baboon)
|
O97980
|
HMHB1_HUMAN
|
MEEQPECREEKRGSLHVWKSELVEVEDDVYLRHSSSLTYRL
| null | null |
adaptive immune response [GO:0002250]; cellular response to tumor necrosis factor [GO:0071356]; positive regulation of type II interferon production [GO:0032729]; regulation of gene expression [GO:0010468]
| null | null | null | null | null | null | null | null | null | null | null | null |
FUNCTION: Precursor of the histocomplatibility antigen HB-1. More generally, minor histocomplatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocomplatibility antigen in HLA-matched sibling marrow transplants. HB-1 is presented on the cell surface by MHC class I HLA-B44. This complex specifically elicits donor-cytotoxic T lymphocyte (CTL) reactivity in B-cell acute lymphoblastic leukemia (B-ALL) after treatment by HLA-identical allogenic bone marrow transplantation (BMT). It induces cell recognition and lysis by CTL. However, HB-1 restricted expression in B-ALL cells and not in normal tissues may allow a specific CTL reactivity against B-ALL without the risk of evoking graft-versus-host disease. {ECO:0000269|PubMed:15102363, ECO:0000269|PubMed:8992968, ECO:0000269|PubMed:9892612}.
|
Homo sapiens (Human)
|
P00002
|
CYC_MACMU
|
MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGITWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
| null | null |
apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}.
|
Macaca mulatta (Rhesus macaque)
|
P00004
|
CYC_HORSE
|
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
| null | null |
apoptotic process [GO:0006915]; cytochrome c-heme linkage [GO:0018063]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity [GO:2001056]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]
|
cytochrome complex [GO:0070069]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}.
|
Equus caballus (Horse)
|
P00007
|
CYC_HIPAM
|
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQSPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKQATNE
| null | null |
apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}.
|
Hippopotamus amphibius (Hippopotamus)
|
P00008
|
CYC_RABIT
|
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKMIFAGIKKKDERADLIAYLKKATNE
| null | null |
apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}.
|
Oryctolagus cuniculus (Rabbit)
|
P00011
|
CYC_CANLF
|
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKKATKE
| null | null |
apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
P00012
|
CYC_MIRLE
|
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKIATKE
| null | null |
apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}.
|
Mirounga leonina (Southern elephant seal) (Phoca leonina)
|
P00014
|
CYC_MACGI
|
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLNGIFGRKTGQAPGFTYTDANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
| null | null |
apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}.
|
Macropus giganteus (Eastern gray kangaroo)
|
P00015
|
CYC2_MOUSE
|
MGDAEAGKKIFVQKCAQCHTVEKGGKHKTGPNLWGLFGRKTGQAPGFSYTDANKNKGVIWSEETLMEYLENPKKYIPGTKMIFAGIKKKSEREDLIKYLKQATSS
| null | null |
apoptotic process [GO:0006915]; hydrogen peroxide metabolic process [GO:0042743]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]
|
mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
P00044
|
CYC1_YEAST
|
MTEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
| null |
COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:18390544}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:18390544};
|
mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
|
PTM: Methylation may enhance its transport into mitochondria. Methylation occurs in fungi, plants, and some protozoa, but not in animals. The precise role of methylation at Lys-79 is unknown, but it seems to preclude pro-apoptotic activity, possibly by lowering affinity for APAF1. {ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:2822698}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:9866716}.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase. Cytochrome c then transfers this electron to the dinuclear copper A center (CU(A)) of the COX2 subunit of cytochrome oxidase, the final protein carrier in the mitochondrial electron-transport chain. Isoform 1 (CYC1) is the predominant cytochrome c during aerobic/normoxic growth. {ECO:0000269|PubMed:7814361, ECO:0000269|PubMed:7851399, ECO:0000269|PubMed:9169434}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00045
|
CYC7_YEAST
|
MAKESTGFKPGSAKKGATLFKTRCQQCHTIEEGGPNKVGPNLHGIFGRHSGQVKGYSYTDANINKNVKWDEDSMSEYLTNPKKYIPGTKMAFAGLKKEKDRNDLITYMTKAAK
| null |
COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:18390544}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:18390544};
|
mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; respirasome [GO:0070469]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00034;
|
1.10.760.10;
|
Cytochrome c family
| null |
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:8636074}.
| null | null | null | null | null |
FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase. Cytochrome c then transfers this electron to the dinuclear copper A center (CU(A)) of the COX2 subunit of cytochrome oxidase, the final protein carrier in the mitochondrial electron-transport chain. Isoform 2 (CYC7) is the predominant cytochrome c under anaerobic/hypoxic conditions. {ECO:0000269|PubMed:7814361, ECO:0000269|PubMed:9169434}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00125
|
CY1_BOVIN
|
MAAAAATLRGAMVGPRGAGLPGARARGLLCGARPGQLPLRTPQAVSLSSKSGLSRGRKVILSALGMLAAGGAGLAVALHSAVSASDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCSSCHSMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEMFMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIGMAPPIYNEVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDHRKRMGLKMLLMMGLLLPLVYAMKRHKWSVLKSRKLAYRPPK
|
7.1.1.8
|
COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:9651245}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:9651245};
|
mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]
|
PF02167;
|
1.10.760.10;1.20.5.100;
|
Cytochrome c family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein {ECO:0000250|UniProtKB:P07143}.
|
CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000250|UniProtKB:P07143};
| null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c. {ECO:0000250|UniProtKB:P07143}.
|
Bos taurus (Bovine)
|
P00127
|
QCR6_YEAST
|
MGMLELVGEYWEQLKITVVPVVAAAEDDDNEQHEEKAAEGEEKEEENGDEDEDEDEDEDDDDDDDEDEEEEEEVTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK
| null | null |
aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; proton transmembrane transport [GO:1902600]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]; nuclear periphery [GO:0034399]
| null |
PF02320;
|
1.10.287.20;
|
UQCRH/QCR6 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Intermembrane side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
| null | null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. {ECO:0000250|UniProtKB:P07919, ECO:0000305|PubMed:11880631}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00128
|
QCR7_YEAST
|
MPQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDNIEVSK
| null | null |
aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; mitochondrial respiratory chain complex III assembly [GO:0034551]; proton transmembrane transport [GO:1902600]
|
matrix side of mitochondrial inner membrane [GO:0099617]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]
| null |
PF02271;
|
1.10.1090.10;
|
UQCRB/QCR7 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
| null | null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. {ECO:0000305|PubMed:11880631}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00156
|
CYB_HUMAN
|
MTPMRKTNPLMKLINHSFIDLPTPSNISAWWNFGSLLGACLILQITTGLFLAMHYSPDASTAFSSIAHITRDVNYGWIIRYLHANGASMFFICLFLHIGRGLYYGSFLYSETWNIGIILLLATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGYSVDSPTLTRFFTFHFILPFIIAALATLHLLFLHETGSNNPLGITSHSDKITFHPYYTIKDALGLLLFLLSLMTLTLFSPDLLGDPDNYTLANPLNTPPHIKPEWYFLFAYTILRSVPNKLGGVLALLLSILILAMIPILHMSKQQSMMFRPLSQSLYWLLAADLLILTWIGGQPVSYPFTIIGQVASVLYFTTILILMPTISLIENKMLKWA
| null |
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P00157}; Note=Binds 2 heme b groups non-covalently. {ECO:0000250|UniProtKB:P00157};
|
animal organ regeneration [GO:0031100]; cellular respiration [GO:0045333]; electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; response to cadmium ion [GO:0046686]; response to calcium ion [GO:0051592]; response to cobalamin [GO:0033590]; response to copper ion [GO:0046688]; response to ethanol [GO:0045471]; response to glucagon [GO:0033762]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to mercury ion [GO:0046689]; response to toxic substance [GO:0009636]; response to xenobiotic stimulus [GO:0009410]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]
|
metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; ubiquinol-cytochrome-c reductase activity [GO:0008121]
|
PF00032;PF00033;
| null |
Cytochrome b family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00157}.
| null | null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. {ECO:0000250|UniProtKB:P00157}.
|
Homo sapiens (Human)
|
P00157
|
CYB_BOVIN
|
MTNIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILLLTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIMAIAMVHLLFLHETGSNNPTGISSDVDKIPFHPYYTIKDILGALLLILALMLLVLFAPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAFSILILALIPLLHTSKQRSMMFRPLSQCLFWALVADLLTLTWIGGQPVEHPYITIGQLASVLYFLLILVLMPTAGTIENKLLKW
| null |
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245}; Note=Binds 2 heme b groups non-covalently. {ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245};
|
mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; respiratory electron transport chain [GO:0022904]
|
membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex III [GO:0005750]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]; ubiquinone binding [GO:0048039]
|
PF00032;PF00033;
| null |
Cytochrome b family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:1225597, ECO:0000305|PubMed:1327781, ECO:0000305|PubMed:189810}; Multi-pass membrane protein {ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245}.
| null | null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. {ECO:0000269|PubMed:1327781, ECO:0000269|PubMed:20025846, ECO:0000269|PubMed:9485330, ECO:0000305|PubMed:189810}.
|
Bos taurus (Bovine)
|
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