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
O70494
SP3_MOUSE
MTAPEKPVKQEEMAALDVDGGGGGGGHGEYLQQQQQQQQQHGNGAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDDEEAAVAAAAGVPAAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPGAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQSTDAQQVQIGFTGSSDNGGINQENSQIQIIPGSNQTLLASGTPPANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSP...
null
null
B cell differentiation [GO:0030183]; definitive hemopoiesis [GO:0060216]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic placenta development [GO:0001892]; embryonic process involved in female pregnancy [GO:0060136]; embryonic skeletal system development [GO:0048706]; enucleate erythrocyte differentiat...
cytosol [GO:0005829]; nucleus [GO:0005634]; PML body [GO:0016605]; protein-DNA complex [GO:0032993]; transcription repressor complex [GO:0017053]
chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polyme...
PF00096;
3.30.160.60;
Sp1 C2H2-type zinc-finger protein family
PTM: Acetylated by histone acetyltransferase p300, deacetylated by HDACs. Acetylation/deacetylation states regulate transcriptional activity. Acetylation appears to activate transcription. Alternate sumoylation and acetylation at Lys-553 also control transcriptional activity (By similarity). {ECO:0000250}.; PTM: Sumoyl...
SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body {ECO:0000250}. Note=Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies (By similarity). {ECO:0000250}.
null
null
null
null
null
FUNCTION: Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different proces...
Mus musculus (Mouse)
O70496
CLCN7_MOUSE
MANVSKKVSWSGRDRDDEEGAPLLRRTGQPDEETPLLNGAGPGARQSHSALFRIGQMNNVELDDELLDPEVDPPHTFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKDNIDKFTEKGGLSFSLLLWATLNSAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQF...
null
null
response to pH [GO:0009268]
intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]
antiporter activity [GO:0015297]; ATP binding [GO:0005524]; chloride transmembrane transporter activity [GO:0015108]; voltage-gated chloride channel activity [GO:0005247]
PF00571;PF00654;
3.10.580.10;1.10.3080.10;
Chloride channel (TC 2.A.49) family, ClC-7/CLCN7 subfamily
null
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16525474, ECO:0000269|PubMed:31155284}; Multi-pass membrane protein {ECO:0000269|PubMed:16525474}.
CATALYTIC ACTIVITY: Reaction=2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in); Xref=Rhea:RHEA:29567, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P51798};
null
null
null
null
FUNCTION: Slowly voltage-gated channel mediating the exchange of chloride ions against protons (PubMed:16525474, PubMed:19661288). Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH (PubMed:16525474, PubMed:19661288). The CLC channel family...
Mus musculus (Mouse)
O70497
FCN2_MOUSE
MALGSAALFVLTLTVHAAGTCPELKVLDLEGYKQLTILQGCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGPSQSCATGPRTCKELLTQGHFLTGWYTIYLPDCRPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGSQLGEFWLGNDNIHALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFLGGGAGDSLTPHNNRLFSTKDQDNDGSTSSCAMGYHGAWWYSQCHTSNLNGLYLRGPHKSYANGVNWKSWRGYNYSCKVSEMKVRLI
null
null
cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation, lectin pathway [GO:0001867]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of interleukin-8 production [GO:0032757]; positive ...
collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; serine-type endopeptidase complex [GO:1905370]
antigen binding [GO:0003823]; carbohydrate binding [GO:0030246]; carbohydrate derivative binding [GO:0097367]; G protein-coupled receptor binding [GO:0001664]; metal ion binding [GO:0046872]; pattern recognition receptor activity [GO:0038187]; sialic acid binding [GO:0033691]; signaling receptor binding [GO:0005102]
PF01391;PF00147;
3.90.215.10;
Ficolin lectin family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin (By similarity). {ECO:0000250|UniProtKB:Q15485}.
Mus musculus (Mouse)
O70503
DHB12_MOUSE
MECAPPAAGFLYWVGASTIAYLALRASYSLFRAFQVWCVGNEALVGPRLGEWAVVTGGTDGIGKAYAEELAKRGMKIVLISRSQDKLNQVSNNIKEKFNVETRTIAVDFSLDDIYDKIKTGLSGLEIGVLVNNVGMSYEYPEYFLEIPDLDNTIKKLININVLSVCKVTRLVLPGMVERSKGVILNISSASGMLPVPLLTIYSATKAFVDFFSQCLHEEYKSKGIFVQSVMPYLVATKLAKIQKPTLDKPSAETFVKSAIKTVGLQTRTTGYVIHSLMGSINSIMPRWMYFKIIMGFSKSLRNRYLKKRKKN
1.1.1.330; 1.1.1.62
null
estrogen biosynthetic process [GO:0006703]; extracellular matrix organization [GO:0030198]; fatty acid elongation, saturated fatty acid [GO:0019367]; positive regulation of cell-substrate adhesion [GO:0010811]
endoplasmic reticulum [GO:0005783]; extracellular matrix [GO:0031012]; fatty acid elongase complex [GO:0009923]
collagen binding [GO:0005518]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; fibronectin binding [GO:0001968]; heparin binding [GO:0008201]; oxidoreductase activity [GO:0016491]; very-long-chain 3-oxoacyl-CoA reductase activity [GO:0141040]
PF00106;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family, 17-beta-HSD 3 subfamily
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q53GQ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53GQ0}.
CATALYTIC ACTIVITY: Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330; Evidence={ECO:0000250|UniProtKB:Q53GQ0}; CATALYTIC ACTIVITY...
null
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000250|UniProtKB:Q53GQ0}.; PATHWAY: Steroid biosynthesis; estrogen biosynthesis. {ECO:0000250|UniProtKB:Q53GQ0}.
null
null
FUNCTION: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducin...
Mus musculus (Mouse)
O70507
HCN4_MOUSE
MDKLPPSMRKRLYSLPQQVGAKAWIMDEEEDGEEEGAGGRQDPSRRSIRLRPLPSPSPSVAAGCSESRGAALGATESEGPGRSAGKSSTNGDCRRFRGSLASLGSRGGGSGGAGGGSSLGHLHDSAEERRLIAAEGDASPGEDRTPPGLATEPERPATAAQPAASPPPQQPPQPASASCEQPSADTAIKVEGGAAAIDHILPEAEVRLGQSGFMQRQFGAMLQPGVNKFSLRMFGSQKAVEREQERVKSAGFWIIHPYSDFRFYWDLTMLLLMVGNLIIIPVGITFFKDENTTPWIVFNVVSDTFFLIDLVLNFRTGIVV...
null
null
cellular response to cAMP [GO:0071320]; in utero embryonic development [GO:0001701]; monoatomic cation transport [GO:0006812]; potassium ion transmembrane transport [GO:0071805]; regulation of heart contraction [GO:0008016]; regulation of heart rate [GO:0002027]; regulation of membrane depolarization [GO:0003254]; sodi...
axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; HCN channel complex [GO:0098855]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195]
cAMP binding [GO:0030552]; intracellularly cAMP-activated cation channel activity [GO:0005222]; sodium channel activity [GO:0005272]; voltage-gated potassium channel activity [GO:0005249]
PF00027;PF00520;PF08412;
1.10.287.70;1.10.287.630;2.60.120.10;
Potassium channel HCN family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11675786}; Multi-pass membrane protein {ECO:0000269|PubMed:11675786}.
null
null
null
null
null
FUNCTION: Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) that regulate the rhythm of heart beat. May contribute to the native pacemaker currents in neurons (Ih) (By ...
Mus musculus (Mouse)
O70511
ANK3_RAT
MAHAASQLKKNRDLEINAEEETEKKKKHRKRSRDRKKKSDANASYLRAARAGHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDTNADIESKMVVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSG...
null
null
anterograde axonal transport [GO:0008089]; axon development [GO:0061564]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cellular response to magnesium ion [GO:0071286]; clustering of voltage-gated sodium channels [GO:0045162]; establishment of protein localization [GO:0045184]; establishment or maintenance of ...
axon [GO:0030424]; axon cytoplasm [GO:1904115]; axon initial segment [GO:0043194]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; costamere [GO:0043034]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; intercalated disc [GO:0014704]; lateral plasma membrane [G...
cadherin binding [GO:0045296]; cytoskeletal protein binding [GO:0008092]; phosphorylation-dependent protein binding [GO:0140031]; protein-macromolecule adaptor activity [GO:0030674]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; spectrin binding [GO:0030507]; structural constituent o...
PF00023;PF12796;PF13637;PF00531;PF17809;PF00791;
2.60.220.30;2.60.40.2660;1.25.40.20;1.10.533.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q12955}. Cell projection, axon {ECO:0000269|PubMed:9744885}. Cell membrane {ECO:0000269|PubMed:21223964}. Cell membrane, sarcolemma {ECO:0000269|PubMed:15953600, ECO:0000269|PubMed:21223964}. Postsynaptic cell membrane {ECO:0000269|PubMed:11796721}. L...
null
null
null
null
null
FUNCTION: Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (By similarity). In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Regulates KCNA1 channel activ...
Rattus norvegicus (Rat)
O70514
FGFP1_MOUSE
MRLHSLILLSFLLLATQAFSEKVRKRAKNAPHSTAEEGVEGSAPSLGKAQNKQRSRTSKSLTHGKFVTKDQATCRWAVTEEEQGISLKVQCTQADQEFSCVFAGDPTDCLKHDKDQIYWKQVARTLRKQKNICRNAKSVLKTRVCRKRFPESNLKLVNPNARGNTKPRKEKAEVSAREHNKVQEAVSTEPNRVKEDITLNPAATQTMAIRDPECLEDPDVLNQRKTALEFCGESWSSICTFFLNMLQATSC
null
null
cell-cell signaling [GO:0007267]; fibroblast growth factor receptor signaling pathway [GO:0008543]; myoblast proliferation [GO:0051450]; positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903589]; positive regulation of cell migration involved in sprouting angioge...
cell surface [GO:0009986]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
fibroblast growth factor binding [GO:0017134]; growth factor binding [GO:0019838]
PF06473;
null
Fibroblast growth factor-binding protein family
null
SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:Q14512}. Cell membrane {ECO:0000250|UniProtKB:Q14512}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14512}. Note=Extracellular and plasma membrane-associated. {ECO:0000250|UniProtKB:Q14512}.
null
null
null
null
null
FUNCTION: Acts as a carrier protein that releases fibroblast-binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhances the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O70521
RGS19_RAT
MPTPHEAEKQHTGPEEADRPPSMSSHDAAPSGPPSRNPCCLCWCCCCSCSWNQERQRAWQVSRESKLQPLPSCEVCTPPSPEEVQSWAQSFDKLMHSPTGRSVFRAFLRTEYSEENMLFWLACEELKTEADRHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINRKMQEPSPHTFDDAQLQIYTLMHRDSYPRFLTSPTYRSLLLQGAPQSSEA
null
null
negative regulation of signal transduction [GO:0009968]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; response to ethanol [GO:0045471]
brush border [GO:0005903]; clathrin-coated vesicle [GO:0030136]; Golgi membrane [GO:0000139]
G-protein alpha-subunit binding [GO:0001965]; GTPase activator activity [GO:0005096]
PF00615;
1.10.196.10;1.10.167.10;
null
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity). {ECO:0000250}.; PTM: Phosphorylated, mainly on serine residues. {ECO:0000269|PubMed:10760275}.
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
null
null
null
null
null
FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, predominantly to G(i)-alpha-3. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein (B...
Rattus norvegicus (Rat)
O70523
FXR1_CRIGR
MADVTVEVRGSNGAFYKGFIKDVHEDSLTVVFENNWQPERQVPFNEVRLPPPPDIKKEISEGDEVEVYSRANDQEPCGWWLAKVRMMKGEFYVIEYAACDATYNEIVTFERLRPVNQNKTVKKNTFFKCTVDVPEDLREACANENAHKDFKKAVGACRIFYHPETTQLMILSASEATVKRVNILSDMHLRSIRTKLMLMSRNEEATKHLECTKQLAAAFHEEFVVREDLMGLAIGTHGSNIQQARKVPGVTAIELDEDTGTFRIYGESAEAVKKARGFMEFVEDFIQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEG...
null
null
dentate gyrus development [GO:0021542]; mRNA destabilization [GO:0061157]; muscle organ development [GO:0007517]; negative regulation of inflammatory response [GO:0050728]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of translation [GO:0017148]; negative regulation of tumor ...
cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; dendritic filopodium [GO:1902737]; dendritic spine neck [GO:0044326]; growth cone [GO:0030426]; intracellular non-membrane-bounded organelle [GO:0043232]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nuclear envelope...
molecular condensate scaffold activity [GO:0140693]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA binding [GO:0003729]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA strand annealing activity [GO:0033592]; translation regulator activity [GO:0045182]
PF05641;PF12235;PF16096;PF16097;PF00013;PF17904;PF18336;
2.30.30.140;3.30.1370.10;
FMR1 family
PTM: Phosphorylation at Ser-420 by PAK1 promotes its relocalization to stress granules and activity (By similarity). Phosphorylated by MAPK1/ERK2, promoting subsequent phosphorylation by GSK3B. Phosphorylated by GSK3B, promoting ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P5...
SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q61584}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P51114}. Cytoplasm {ECO:0000250|UniProtKB:Q61584}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61584}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q61...
null
null
null
null
null
FUNCTION: mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for various processes, such as neurogenesis, muscle development and spermatogenesis. Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Promotes formation of some phase-separate...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O70525
PEX5_CAVPO
MAMRELVEGECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGAPASETVSKPLGVASEDELVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFIAEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGAATTDRWYDEYHPEEDLQHTASDFVAKVDDPKLANSEFLKFVRQIGEGQVSLESVAGSGRAQAEQWAAEFIQQQGTSDAWVDQFTRPVNTSALDMEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSAS...
null
null
pexophagy [GO:0000425]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, docking [GO:0016560]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into peroxisome matrix, substrate release [GO:0044721]; protein import into peroxisome matrix, t...
cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]
peroxisome matrix targeting signal-1 binding [GO:0005052]; protein carrier chaperone [GO:0140597]
PF13432;PF13181;
1.25.40.10;
Peroxisomal targeting signal receptor family
PTM: Monoubiquitinated at Cys-11 by PEX2 during PEX5 passage through the retrotranslocation channel (By similarity). Cys-11 monoubiquitination acts as a recognition signal for the PEX1-PEX6 complex and is required for PEX5 extraction and export from peroxisomes. Monoubiquitination at Cys-11 is removed by USP9X in the c...
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P50542}. Peroxisome matrix {ECO:0000250|UniProtKB:P50542}. Note=Cycles between the cytosol and the peroxisome matrix (By similarity). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the dockin...
null
null
null
null
null
FUNCTION: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (PubMed:11085934). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing throu...
Cavia porcellus (Guinea pig)
O70531
S26A2_RAT
MSSENKEQHNLSPRDLPEEAYGFPPELPLGAQRGSSTDLRQFEPSDRRRAFRRIHMELHEKPDTNIRQLVMRKLQKSCQCNATKIRNRIFDFFPVLRWLPKYDLKKNILGDMMSGLIVGILLVPQSIAYSLLAGQEPIYGLYTSFFASIIYFLFGTSRHISVGIFGILCLMIGEVVDRELHKACPDIDTTSSSIAMFSNGCVVVNHTLDGLCDKSCYAIKIGSTVTFMAGVYQVAMGFFQVGFVSVYLSDALLSGFVTGASFTILTSQAKYLLGLSLPRSNGVGSVITTWIHIFRNIHKTNICDLITSLLCLLVLVPTKE...
null
null
chondrocyte differentiation [GO:0002062]; chondrocyte proliferation [GO:0035988]; ossification [GO:0001503]; sulfate transmembrane transport [GO:1902358]; sulfate transport [GO:0008272]
apical plasma membrane [GO:0016324]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886]
bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; oxalate transmembrane transporter activity [GO:0019531]; secondary active sulfate transmembrane transporter activity [GO:0008271]; solute:inorganic anion antiporter activity [GO:0005452]; sulfate trans...
PF01740;PF00916;
3.30.750.24;
SLC26A/SulP transporter (TC 2.A.53) family
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P50443}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9575183}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:20369363}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=oxalate(in) + sulfate(out) = oxalate(out) + sulfate(in); Xref=Rhea:RHEA:72275, ChEBI:CHEBI:16189, ChEBI:CHEBI:30623; Evidence={ECO:0000250|UniProtKB:Q62273}; CATALYTIC ACTIVITY: Reaction=2 chloride(in) + sulfate(out) = 2 chloride(out) + sulfate(in); Xref=Rhea:RHEA:75091, ChEBI:CHEBI:16189, ...
null
null
null
null
FUNCTION: Sulfate transporter which mediates sulfate uptake into chondrocytes in order to maintain adequate sulfation of proteoglycans which is needed for cartilage development (PubMed:9575183). Mediates electroneutral anion exchange of sulfate ions for oxalate ions, sulfate and oxalate ions for chloride and/or hydroxy...
Rattus norvegicus (Rat)
O70534
DLK1_RAT
MIATGALLRVLLLLLAFGHSTYGAECDPACDPQHGFCEADNVCRCEPGWEGPLCEKCVTSPGCVNGLCEEPWQCVCKEGWDGKFCEIDIRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGRASHASCLCPPGFSGNFCEIVTNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCLNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGTSPVQVTHLPSGYGLTYRLTPGVHELPVQQPEHHILKVSMKELNKSAPLLTEGQAICFTILGVLTSLVVLG...
null
null
bone mineralization [GO:0030282]; cell differentiation [GO:0030154]; embryonic skeletal system development [GO:0048706]; multicellular organism growth [GO:0035264]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of vascular ...
cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; membrane [GO:0016020]
calcium ion binding [GO:0005509]
PF21700;PF00008;PF12661;
2.10.25.10;
null
PTM: Glycosylated. {ECO:0000250|UniProtKB:Q09163}.
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein. Cytoplasm {ECO:0000269|PubMed:9645708}.
null
null
null
null
null
FUNCTION: May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation. {ECO:0000250|UniProtKB:Q09163}.
Rattus norvegicus (Rat)
O70535
LIFR_RAT
MGAFSWWRQPSWMADNKRGRMTPSLPWLLSALTLLHLMMHVNGLKRGVQQDLKCTTNNMRVWDCSWPAPLGVSPGTVKDICIKDRPHSCHRLETTNVKIPALSPGDHEVTINYQNGFQSKFTLNEKDVSLVPDTPEILSLSADFSTSTLQLKWNDKGSALPYPSNATWEVKVLQNPRTEPVALVSLNTVLSGKDKGHHWNWTSELPLQCATHSVSIRWHIDYPRFSGYKEWSEWSPLKNISWTRNTETNVFPQDKVVLAGSNMTICCISTTKVLSGQIGNTFRPLIHLYGETVAINILNIPVSENSGSNVIFSTVDDVYG...
null
null
animal organ regeneration [GO:0031100]; ciliary neurotrophic factor-mediated signaling pathway [GO:0070120]; cytokine-mediated signaling pathway [GO:0019221]; leukemia inhibitory factor signaling pathway [GO:0048861]; negative regulation of muscle cell apoptotic process [GO:0010656]; neuron projection morphogenesis [GO...
external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235]
ciliary neurotrophic factor receptor binding [GO:0005127]; cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; growth factor binding [GO:0019838]; leukemia inhibitory factor receptor activity [GO:0004923]; oncostatin-M receptor activity [GO:0004924]
PF00041;PF21177;PF17971;PF18207;
2.60.40.10;
Type I cytokine receptor family, Type 2 subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
O70536
SOAT1_RAT
MVGEETSLRNRLSRSAENPEQDEAQKNLLDTHRNGHITMKQLIAKKRQLAAEAEELKPLFLKEVGCHFDDFVTNLIDKSASLDNGGCALTTFSILEEMKNNHRAKDLRAPPEQGKIFISRRSLLDELFEVDHIRTIYHMFIALLIIFILSTLVVDYIDEGRLVLEFSLLAYAFGQFPIVIWTWWAMFLSTLAIPYFLFQRWAHGYSKSSHPLIYSLIHGAFFLVFQLGILGFIPTYVVLAYTLPPASRFILILEQIRLVMKAHSYVRENVPRVLSAAKEKSSTVPVPTVNQYLYFLFAPTLIYRDSYPRTPTVRWGYVAM...
2.3.1.26
null
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol storage [GO:0010878]; macrophage derived foam cell differentiation [GO:0010742]; positive regulation of amyloid precursor protein biosynthetic process [GO:0042986]; very-low-density lipoprotein...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772]
PF03062;
null
Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35610}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35610}.
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA; Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817; Evidence={ECO:00...
null
null
null
null
FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrateb a higher activity towards an acyl-CoA substrate wit...
Rattus norvegicus (Rat)
O70546
KDM6A_MOUSE
MKSCGVSLATAAAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATILQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASA...
1.14.11.68
COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
cellular response to angiotensin [GO:1904385]; cellular response to endothelin [GO:1990859]; cellular response to hypoxia [GO:0071456]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to vitamin D [GO:0071305]; chromatin remodeling [GO:0006338]; circulatory system developme...
histone methyltransferase complex [GO:0035097]; MLL3/4 complex [GO:0044666]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin DNA binding [GO:0031490]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF02373;PF21322;PF21326;PF13432;PF13181;
1.20.58.1370;2.10.110.20;2.60.120.650;1.25.40.10;
UTX family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:1...
null
null
null
null
FUNCTION: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylati...
Mus musculus (Mouse)
O70551
SRPK1_MOUSE
MERKVLALQARKKRTKAKKDKAQRKPETQHRGSAPHSESDIPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNGEMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVDRPLTEN...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:9446799};
cell differentiation [GO:0030154]; chromosome segregation [GO:0007059]; intracellular signal transduction [GO:0035556]; negative regulation of viral genome replication [GO:0045071]; positive regulation of viral genome replication [GO:0045070]; protein phosphorylation [GO:0006468]; regulation of mRNA processing [GO:0050...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96SB4}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96SB4}. Nucleus matrix {ECO:0000250|UniProtKB:Q96SB4}. Microsome {ECO:0000250|UniProtKB:Q96SB4}. Nucleus speckle {ECO:0000250|UniProtKB:Q96SB4}. Chromosome {ECO:0000250|UniProtKB:Q96SB4}. Note=Shuttles between t...
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:10390541, ECO:000026...
null
null
null
null
FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the ...
Mus musculus (Mouse)
O70552
BTG4_MOUSE
MRDEIATAVFFVTRLVKKHEKLSTQQIETFALKLMTILFEKYRGHWHPDCPSKGQAFRCIRINNNENKDPVLERACAESNVNFFHLGLPKEMTIWVDPYEVCCRYGEKKHPFTIASFKGRWENWELAQHVSCAVNRATGDCSSGTSSDEESCSREAQIIPKVNNPKSVYQVENFKQSLQPWFCLPRRKHLADGRGFLPGAACHPVPKSSKWCRPASRRVDRYHWVNAQLFSGQTAPGEPGEEALSSLKQK
null
null
maternal-to-zygotic transition of gene expression [GO:0160021]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mitotic cell cycle [GO:0045930]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
mRNA 3'-UTR binding [GO:0003730]
PF07742;
3.90.640.90;
BTG family
null
null
null
null
null
null
null
FUNCTION: Adapter protein that bridges CNOT7, a catalytic subunit of the CCR4-NOT complex, to EIF4E, and facilitates maternal mRNAs decay during the maturation of oocytes and in the fertilized egg (PubMed:27065194). It is therefore required for the maternal-zygotic transition (MZT), zygotic cleavage and initiation of e...
Mus musculus (Mouse)
O70566
DIAP2_MOUSE
MEELGAAASGAGGGGGGGEEHGGGRSNKRGAGNRAANEEETRNKPKLRDRITSFRKSATKREKPVIQHSIDYQTAVVEIPPALIVHDDRSLILSEKEVLDLFEKMMEDMNLNEEKKAPLRKKDFSIKREMVVQYISATSKSIVGSKVLGGLKNSKHEFTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSHPVSWVNNFGYEGLGVLLDVLEKLLDKKQQENIDKKNQYKVIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQQNMMTEIVKILSAICIVGEENILDKLLGGITAAAELNNRERFSPIVEGLENNE...
null
null
actin filament polymerization [GO:0030041]; axon midline choice point recognition [GO:0016199]; ephrin receptor signaling pathway [GO:0048013]; multicellular organismal locomotion [GO:0071965]; negative regulation of neuron projection regeneration [GO:0070571]; neuron projection retraction [GO:0106028]; oogenesis [GO:0...
actin filament [GO:0005884]
actin binding [GO:0003779]; small GTPase binding [GO:0031267]
PF06367;PF06371;PF02181;
1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10;
Formin homology family, Diaphanous subfamily
null
null
null
null
null
null
null
FUNCTION: May be involved in oogenesis.
Mus musculus (Mouse)
O70571
PDK4_MOUSE
MKAARFVMRSASSLSSASLVPREVELFSRYSPSPLSMKQLLDFGSENACERTSFAFLRQELPVRLANILKEIDILPDRLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQKALSEFVDTLVKVRNRHHNVVPTMAQGILEYKDTCTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDSKTGNPSHIGSIDPNCDVVAVVQDAFECAKMLCDQYYLTSPELNLTQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRPSLTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMD...
2.7.11.2
null
cellular response to fatty acid [GO:0071398]; cellular response to starvation [GO:0009267]; glucose homeostasis [GO:0042593]; insulin receptor signaling pathway [GO:0008286]; negative regulation of anoikis [GO:2000811]; phosphorylation [GO:0016310]; reactive oxygen species metabolic process [GO:0072593]; regulation of ...
mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
ATP binding [GO:0005524]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; pyruvate dehydrogenase (acetyl-transferring) kinase activity [GO:0004740]
PF10436;PF02518;
1.20.140.20;3.30.565.10;
PDK/BCKDK protein kinase family
null
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit]; Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:45621...
null
null
null
null
FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates ...
Mus musculus (Mouse)
O70572
NSMA_MOUSE
MKLNFSLRLRVFNLNCWDIPYLSKHRADRMKRLGDFLNLENFDLALLEEVWSEQDFQYLRQRLSLTYPDAHYFRSGMIGSGLCVFSKHPIQEIFQHVYSLNGYPYMFHHGDWFCGKSVGLLVLRLSGLVLNAYVTHLHAEYSRQKDIYFAHRVAQAWELAQFIHHTSKNADVVLLCGDLNMHPKDLGCCLLKEWTGLHDAFVETEDFKGSDDGCTMVPKNCYVSQQDLGPFPSGIRIDYVLYKAVSEFHVCCETLKTTTGCDPHSDKPFSDHEALMATLYVKHSPPQEDPCTACGPLERSDLISVLREARTELGLGIAKA...
3.1.4.12
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9520418};
ceramide biosynthetic process [GO:0046513]; ceramide metabolic process [GO:0006672]; intracellular signal transduction [GO:0035556]; positive regulation of apoptotic process [GO:0043065]; response to mechanical stimulus [GO:0009612]; sphingolipid catabolic process [GO:0030149]; sphingomyelin catabolic process [GO:00066...
caveola [GO:0005901]; cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
metal ion binding [GO:0046872]; sphingomyelin phosphodiesterase activity [GO:0004767]
PF03372;
3.60.10.10;
Neutral sphingomyelinase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9520418}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269|PubMed:15764706, ECO:0000269|PubMed:9520418}; PhysiologicalDirect...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 uM for sphingomyelin (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:9520418}; Vmax=10 umol/h/mg enzyme with sphingomyelin as substrate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:9520418};
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:9520418}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:9520418};
null
FUNCTION: Catalyzes, at least in vitro, the hydrolysis of sphingomyelin to form ceramide and phosphocholine (PubMed:9520418). Also hydrolyzes 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine (lyso-platelet-activating factor) in vivo (By similarity). Also acts on 1-acyl-2-lyso-sn-glycero-3-phosphocholine (lyso-PC) and sphin...
Mus musculus (Mouse)
O70576
STAG3_MOUSE
MPTLWSPSTQHHGSSSGSESSPLQKSVRRAQMALSPCSSSILPCDDRDSQGTAEWDSPSTNEDSDFEDSLRRNVKKRAAKQPPKAVPAAKHRKKQSRIVSSGNGKNESVPSTNYLFDAVKAARSCMQSLVDEWLDNYKQDENAGFLELINFFIRACGCKSTVTPEMFKTMSNSEIIQHLTEEFNEDSGDYPLTAPGPSWKKFQGSFCEFVKTLVYQCQYSLLYDGFPMDDLISLLIGLSDSQVRAFRHTSTLAAMKLMTSLVKVALQLSLHKDNNQRQYEAERNKGPEQRAPERLESLLEKRKEFQENQEDIEGMMNAIF...
null
null
establishment of meiotic sister chromatid cohesion [GO:0034089]; female meiosis sister chromatid cohesion [GO:0007066]; homologous chromosome pairing at meiosis [GO:0007129]; male meiosis sister chromatid cohesion [GO:0007065]; protein localization to chromosome [GO:0034502]; sister chromatid cohesion [GO:0007062]
chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; condensed nuclear chromosome [GO:0000794]; lateral element [GO:0000800]; male germ cell nucleus [GO:0001673]; meiotic cohesin complex [GO:0030893]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synaptonemal complex [GO:000079...
chromatin binding [GO:0003682]
PF21581;PF08514;
null
SCC3 family
PTM: Phosphorylated. {ECO:0000269|PubMed:22346761}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750, ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:22346761}. Chromosome, centromere {ECO:0000269|PubMed:22346761}. Note=Associates with chromatin. In prophase I stage of meiosis, it is found along the axial elements of synaptonemal complexe...
null
null
null
null
null
FUNCTION: Meiosis specific 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 ch...
Mus musculus (Mouse)
O70577
S22A2_MOUSE
MPTVDDILEHIGEFHLFQKQTFFLLALLSGAFTPIYVGIVFLGFTPNHHCRSPGVAELSQRCGWSPAEELNYTVPGLGSAGEVSFLSQCMRYEVDWNQSTLDCVDPLSSLAANRSHLPLSPCEHGWVYDTPGSSIVTEFNLVCAHSWMLDLFQSLVNVGFFIGAVGIGYLADRFGRKFCLLVTILINAISGVLMAISPNYAWMLVFRFLQGLVSKAGWLIGYILITEFVGLGYRRTVGICYQIAFTVGLLILAGVAYALPNWRWLQFAVTLPNFCFLLYFWCIPESPRWLISQNKNAKAMKIIKHIAKKNGKSVPVSLQS...
null
null
acetylcholine transport [GO:0015870]; cellular detoxification [GO:1990748]; dopamine transport [GO:0015872]; dopamine uptake [GO:0090494]; epinephrine transport [GO:0048241]; export across plasma membrane [GO:0140115]; histamine transport [GO:0051608]; histamine uptake [GO:0051615]; L-arginine import across plasma memb...
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cholinergic synapse [GO:0098981]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]
acetylcholine transmembrane transporter activity [GO:0005277]; amine transmembrane transporter activity [GO:0005275]; choline transmembrane transporter activity [GO:0015220]; efflux transmembrane transporter activity [GO:0015562]; L-arginine transmembrane transporter activity [GO:0061459]; monoamine transmembrane trans...
PF00083;
1.20.1250.20;
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
PTM: Tyrosine phosphorylated by tyrosine-protein kinase YES1. {ECO:0000269|PubMed:26979622}.
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9R0W2}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:O15244}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O15244}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000250|UniProtKB:Q9R0W2}; CATALYTI...
null
null
null
null
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:23458604). Functions as a Na(+)-independent, bidirectional uniporter (By similarity). Cation cellular uptake or release is driven b...
Mus musculus (Mouse)
O70578
CCG1_MOUSE
MSQTKTAKVRVTLFFILVGGVLAMVAVVTDHWAVLSPHLEHHNETCEAAHFGLWRICTARVAVHNKDKSCEHVTPSGEKNCSYFRHFNPGESSEIFEFTTQKEYSISAAAIAIFSLGFIIVGSICAFLSFGNKRDYLLRPASMFYAFAGLCLIVSVEVMRQSVKRMIDSEDTVWIEHYYSWSFACACAAFILLFLGGLFLLLFSLPRMPQNPWESCMDAEPEH
null
null
calcium ion transmembrane transport [GO:0070588]; establishment of localization in cell [GO:0051649]; positive regulation of muscle contraction [GO:0045933]; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1902514]; sarcoplasmic reticulum calcium ion transport [GO:0070296]
L-type voltage-gated calcium channel complex [GO:1990454]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]
calcium channel regulator activity [GO:0005246]; voltage-gated calcium channel activity [GO:0005245]
PF13903;
1.20.140.150;
PMP-22/EMP/MP20 family, CACNG subfamily
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19518}.
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305|PubMed:10799530, ECO:0000305|PubMed:9504716}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19518}.
null
null
null
null
null
FUNCTION: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics. {ECO:0000269|PubMed:10799530, ECO:0000269|PubMed:12409298}.
Mus musculus (Mouse)
O70579
PM34_MOUSE
MASVLSYESLVHAVAGAVGSVTAMTVFFPLDTARLRLQVDEKRKSKTTHAVLLEIIKEEGLLAPYRGWFPVISSLCCSNFVYFYTFNSLKAVWVKGQRSSTGKDLVVGFVAGVVNVLLTTPLWVVNTRLKLQGAKFRNEDIIPTNYKGIIDAFHQIIRDEGILALWNGTFPSLLLVFNPAIQFMFYEGLKRQLLKKRMKLSSLDVFIIGAIAKAIATTVTYPMQTVQSILRFGRHRLNPENRTLGSLRNVLSLLHQRVKRFGIMGLYKGLEAKLLQTVLTAALMFLVYEKLTAATFTVMGLKSTHKH
null
null
ADP transport [GO:0015866]; AMP transport [GO:0080121]; coenzyme A transmembrane transport [GO:0035349]; FAD transmembrane transport [GO:0035350]; fatty acid beta-oxidation [GO:0006635]; fatty acid transport [GO:0015908]; NAD transport [GO:0043132]
membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]
ADP transmembrane transporter activity [GO:0015217]; AMP transmembrane transporter activity [GO:0080122]; antiporter activity [GO:0015297]; ATP transmembrane transporter activity [GO:0005347]; coenzyme A transmembrane transporter activity [GO:0015228]; FAD transmembrane transporter activity [GO:0015230]; FMN transmembr...
PF00153;
1.50.40.10;
Mitochondrial carrier (TC 2.A.29) family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43808}. Peroxisome membrane {ECO:0000250|UniProtKB:O43808}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=AMP(out) + CoA(in) = AMP(in) + CoA(out); Xref=Rhea:RHEA:73095, ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA(in) + AMP(out) = 3'-dephospho-CoA(out) + AMP(in); Xref=Rhea:RHEA:73099, ChEBI:CHEBI:57328, ChEBI:CHEBI...
null
null
null
null
FUNCTION: Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extent for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate ...
Mus musculus (Mouse)
O70582
LX12B_MOUSE
MATYKVKVATGTDFFSGTLDSISLTIVGTQGESHKQRLNHFGRDFATGAVDDYTVQCQQDLGELIIIRLHKEPHSFLAKDPWYCNYVQICAPDCRVYHFPAYQWMDGYETLALREATGKITADDTLPILLEHRQEEIRAKKDFYHWRVFVPGLPNYVDIPSYHPPPRRCRNPNRPEWDGYIPGFPILINIKATRFLNSNLRFSFVKTASFFYRLGPMALAFKLRGLVDRKRSWKRLKDIKNIFPATKSVVSEYVAEHWTEDSFFGYQYLNGINPGLIRRCTQIPDKFPVTDEMVAPFLGEGTCLQAELERGNIYLADYRI...
1.13.11.-
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726};
arachidonic acid metabolic process [GO:0019369]; ceramide biosynthetic process [GO:0046513]; establishment of skin barrier [GO:0061436]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372]; positive regulation of gene...
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]
arachidonate 12(R)-lipoxygenase activity [GO:0106237]; arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 8(R)-lipoxygenase activity [GO:0047677]; catalytic activity [GO:0003824]; iron ion binding [GO:0005506]; linoleate 9S-lipoxygenase activity [GO:1990136]
PF00305;PF01477;
3.10.450.60;2.60.60.20;
Lipoxygenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl (5Z,8Z,10E,12R,14Z)-hydroperoxyiecosatetraenoate; Xref=Rhea:RHEA:41311, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033, ChEBI:CHEBI:78034; Evidence={ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665}; P...
null
PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis.; PATHWAY: Lipid metabolism; sphingolipid metabolism.
null
null
FUNCTION: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:16129665). Does not convert arachidonic acid to (12R)-hydroperoxy...
Mus musculus (Mouse)
O70583
TRI18_MOUSE
METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMSSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVIRLRKLAQQIANCKQCLERSASLISQAEHSL...
2.3.2.27
null
negative regulation of microtubule depolymerization [GO:0007026]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein localization to microtubule [GO:0035372]; regulation of microtubule cytoskeleton organization [GO:0070507]
centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630]
microtubule binding [GO:0008017]; phosphoprotein binding [GO:0051219]; protein homodimerization activity [GO:0042803]; transferase activity [GO:0016740]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
PF18568;PF00041;PF00622;PF00643;PF13445;
2.60.120.920;4.10.830.40;3.30.160.60;2.60.40.10;3.30.40.10;
TRIM/RBCC family
PTM: Phosphorylated. {ECO:0000269|PubMed:11371618}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15344}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15344}. Note=Microtubule-associated. {ECO:0000250|UniProtKB:O15344}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
null
null
null
FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000250|UniProtKB:O15344}.
Mus musculus (Mouse)
O70584
NKX28_MOUSE
MATSGRLGFTVRSLLNLPEQDAKPRVRREQQTCVPQTAAWLESECSHYLSSDESGLETSPADSSQLASLRRESPGSDPEKRRKRRVLFSKAQTLELERRFRQQRYLSAPEREQLARLLRLTPTQVKIWFQNHRYKLKRGRAPGITEPSDMAASSDLHAAPGLLRRVVVPVLVHDRPPSNNGRGEGTSAVPQDKCSARLATACPVPGYTAFGPGSALGLFPAYQHLAPPALVSWNW
null
null
axonogenesis [GO:0007409]; cell differentiation [GO:0030154]; epithelial cell proliferation [GO:0050673]; lung development [GO:0030324]; negative regulation of epithelial cell proliferation [GO:0050680]; regulation of transcription by RNA polymerase II [GO:0006357]; respiratory tube development [GO:0030323]; transcript...
nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
PF00046;
1.10.10.60;
NK-2 homeobox family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Possible role in the specification of a distinct subset of neurons.
Mus musculus (Mouse)
O70585
DTNB_MOUSE
MIEEGGNKRKTMAEKRQLFIEMRAQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTMMADPPPQCLVWLPLMHRLAHVENVFHPVECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEHSSWKSPAKKLSHAISKSLGCVPSREPPHPVF...
null
null
synaptic signaling [GO:0099536]
basal plasma membrane [GO:0009925]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; inhibitory synapse [GO:0060077]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; synapse [GO:0045202]
DNA binding [GO:0003677]; phosphatase binding [GO:0019902]; zinc ion binding [GO:0008270]
PF09068;PF09069;PF00569;
3.30.60.90;1.10.238.10;
Dystrophin family, Dystrobrevin subfamily
PTM: Phosphorylated by PKA (PubMed:17610895). Phosphorylation at Thr-11 alters the interaction with KIF5A (PubMed:22978324). {ECO:0000269|PubMed:17610895, ECO:0000269|PubMed:22978324}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530487}. Postsynaptic density {ECO:0000250|UniProtKB:P84060}. Cell projection, dendrite {ECO:0000269|PubMed:11585924, ECO:0000269|PubMed:16540561}. Basal cell membrane {ECO:0000269|PubMed:10893187}. Postsynapse {ECO:0000269|PubMed:16540561}. Nucleus {ECO:0000269|Pub...
null
null
null
null
null
FUNCTION: Scaffolding protein that assembles DMD and SNTA1 molecules to the basal membrane of kidney cells and liver sinusoids (PubMed:11585924). May function as a repressor of the SYN1 promoter through the binding of repressor element-1 (RE-1), in turn regulates SYN1 expression and may be involved in cell proliferatio...
Mus musculus (Mouse)
O70589
CSKP_MOUSE
MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSF...
2.7.11.1
COFACTOR: Note=Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity. {ECO:0000250};
calcium ion import [GO:0070509]; establishment of localization in cell [GO:0051649]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cellular response to growth factor stimulus [GO:0090288]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of wound hea...
apical dendrite [GO:0097440]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nuclear lamina [GO:0005652]...
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; neurexin family protein binding [GO:0042043]; PDZ domain binding [GO:0030165]; protein kinase C binding [GO:0005080]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044...
PF00625;PF02828;PF00595;PF00069;PF07653;
2.30.42.10;6.10.140.620;3.30.63.10;1.10.287.650;3.40.50.300;2.30.30.40;1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily; MAGUK family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62915}. Cytoplasm {ECO:0000250|UniProtKB:Q62915}. Cell membrane {ECO:0000250|UniProtKB:Q62915}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62915}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O14936}; Physiolo...
null
null
null
null
FUNCTION: Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking (By similarity). Contributes to neural development and regulation of gene expression via int...
Mus musculus (Mouse)
O70593
SGTA_RAT
MDNRKRLAYAIIQFLHGQLRHGGLSSDAQESLEVAIQCLETAFGVTLEDSDLALPQTLPEIFEAATASKEMPQDPRGPDRTPPSEEDSAEAERLKTEGNEQMKLENFEAAVHLYGKAIELNPANAVYFCNRAAAYSKLGNYVGAVQDCERAIGIDPGYSKAYGRMGLALSSLNKHAEAVAYYKKALELDPDNDTYKSNLKIAELKLREAPSPTGGVGSLDIAGLLNNPHFITMASSLMNSPQLQQLMSGMISGGHNPLGTPGSSPQHSDLASLIQAGQQFAQQMQQQNPEFVEQIRSQVVRSRTPSASHEEQQE
null
null
chaperone-mediated protein folding [GO:0061077]; ERAD pathway [GO:0036503]; negative regulation of ERAD pathway [GO:1904293]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; positive regulation of ERAD pathway [GO:1904294]; positive regulation of ubiquitin-dependent protein catabolic ...
cytosol [GO:0005829]; extrinsic component of synaptic vesicle membrane [GO:0098850]; membrane [GO:0016020]; nucleus [GO:0005634]; presynapse [GO:0098793]; TRC complex [GO:0072380]
BAT3 complex binding [GO:1904288]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; protein self-association [GO:0043621]
PF16546;PF00515;PF13181;
1.20.5.420;1.25.40.10;
SGT family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43765}. Nucleus {ECO:0000250|UniProtKB:O43765}. Note=Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis. {ECO:0000250|UniProtKB:O43765}.
null
null
null
null
null
FUNCTION: Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion const...
Rattus norvegicus (Rat)
O70594
S22A5_RAT
MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFNGMSIVFLAGTPEHRCLVPHTVNLSSAWRNHSIPLETKDGRQVPQSCRRYRLATIANFSALGLEPGRDVDLEQLEQENCLDGWEYNKDVFLSTIVTEWDLVCKDDWKAPLTTSLFFVGVLMGSFISGQLSDRFGRKNVLFLTMGMQTGFSFLQLFSVNFEMFTVLFVLVGMGQISNYVAAFVLGTEILSKSIRIIFATLGVCIFYAFGFMVLPLFAYFIRDWRMLLLALTVPGVLCGALWWFIPESPRWLISQGRVKEAEVIIRKAAKFNGIVAPSTIFDPSELQD...
null
null
(R)-carnitine transmembrane transport [GO:1902270]; (R)-carnitine transport [GO:1900749]; adult heart development [GO:0007512]; carnitine metabolic process [GO:0009437]; carnitine transport [GO:0015879]; establishment of localization in cell [GO:0051649]; locomotory behavior [GO:0007626]; mitochondrion organization [GO...
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
(R)-carnitine transmembrane transporter activity [GO:1901235]; amino-acid betaine transmembrane transporter activity [GO:0015199]; ATP binding [GO:0005524]; carnitine transmembrane transporter activity [GO:0015226]; PDZ domain binding [GO:0030165]; quaternary ammonium group transmembrane transporter activity [GO:001565...
PF00083;
1.20.1250.20;
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76082}. Apical cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + Na(+)(out) = (R)-carnitine(in) + Na(+)(in); Xref=Rhea:RHEA:72091, ChEBI:CHEBI:16347, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10454528}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-acetyl-(R)-carnitine(out) = Na(+)(in) + O-acetyl-(R)-carnitine(in); Xref=Rhea:RHEA...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=63 uM for tetraethylammonium (at pH 7.5) {ECO:0000269|PubMed:10454528}; KM=14.8 uM for carnitine (at pH 7.5 adn 140 mM NaCl) {ECO:0000269|PubMed:10454528};
null
null
null
FUNCTION: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of c...
Rattus norvegicus (Rat)
O70595
ABCB6_RAT
MVTVGNYCEAEGPAGPAWTQNGLSPCFFYTLVPSTLMTLGVLALVLVLPCRRREVPAGTEELSWAAGPRVAPYALQLSLAILQMALPLASLAGRVGTARGVRLPGYLLLASVLESLASACGLWLLVVERSQARQSLAMGVWMKFRHSLGLLLLWTVTFAAENLVLVSWNSPQWWWSRADLGQQVQFGLWVLRYMTSGGLFILGLWAPGLRPQSYTLHVNEEDQDGGRNQGRSTDPRSTWRDLGRKLRLLSGYLWPRGSPSLQLTVLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGT...
7.6.2.5
null
brain development [GO:0007420]; cellular detoxification of cadmium ion [GO:0098849]; heme metabolic process [GO:0042168]; heme transmembrane transport [GO:0035351]; heme transport [GO:0015886]; intracellular copper ion homeostasis [GO:0006878]; melanosome assembly [GO:1903232]; porphyrin-containing compound biosyntheti...
cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [G...
ABC-type heme transporter activity [GO:0015439]; ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; efflux transmembrane transporter activity [GO:0015562]; heme binding [GO:0020037]; tetrapyrrole binding [GO:0046906]
PF00664;PF00005;PF16185;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily
PTM: N-glycosylated. {ECO:0000269|PubMed:18160489}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}....
CATALYTIC ACTIVITY: Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate; Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344, ChEBI:CHEBI:456216; EC=7.6.2.5; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; ...
null
null
null
null
FUNCTION: ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen (By similarity). May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, i...
Rattus norvegicus (Rat)
O70597
PX11A_RAT
MDAFIRVANQSQGRDRLFRATQHACMLLRYLLESKAGKEAVVTKLKNLETSVSTGRKWFRLGNVLHAIQATEQSIQATDLVPRLCLTLANLNRVVYYICDTVLWAKSVGLTSGINREKWQMRAARHYYYFLLLSLVRDLYEVLLHMGQVARDRAKREKSSGDPPKYSVANEESEWLQSFLLLLFQSLKRNPPLFLDTVKNFCDILIPLNQLGIYKSNLGVVGFGGLVSSVAGLITVVYPQLKLKAR
null
null
brown fat cell differentiation [GO:0050873]; peroxisome fission [GO:0016559]; peroxisome membrane biogenesis [GO:0016557]; peroxisome organization [GO:0007031]; regulation of peroxisome size [GO:0044375]; signal transduction [GO:0007165]
peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]
protein homodimerization activity [GO:0042803]
PF05648;
null
Peroxin-11 family
null
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:9548716}; Multi-pass membrane protein {ECO:0000269|PubMed:9548716}.
null
null
null
null
null
FUNCTION: May be involved in peroxisomal proliferation and may regulate peroxisomes division. May mediate binding of coatomer proteins to the peroxisomal membrane (PubMed:9548716). Promotes membrane protrusion and elongation on the peroxisomal surface. {ECO:0000250|UniProtKB:O75192, ECO:0000269|PubMed:9548716}.
Rattus norvegicus (Rat)
O70600
RSAD2_RAT
MLVPTALAARLLSLFQQQLGSLWSGLAMLFCWLRIALGWPDPGKGQPRVRGEPKETQETHEDPGSAQPTTPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGDYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFLISNEEFEAFLQRHKDVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPS...
4.2.-.-
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q8WXG1}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q8WXG1};
CD4-positive, alpha-beta T cell activation [GO:0035710]; CD4-positive, alpha-beta T cell differentiation [GO:0043367]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; negative regulation of protein secretion [GO:0050709]; negative regulation of viral genome replication [GO:0045071]; ossific...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; lipid droplet [GO:0005811]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
4 iron, 4 sulfur cluster binding [GO:0051539]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; protein self-association [GO:0043621]
PF13353;PF04055;
3.20.20.70;
Radical SAM superfamily, RSAD2 family
PTM: Acetylated by HAT1. HAT1-mediated acetylation of Lys-196 in turn recruits UBE4A that stimulates RSAD2 polyubiquitination leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q8WXG1}.; PTM: 'Lys-6'-linked polyubiquitination at Lys-205 leads to RSAD2 protein degradation. {ECO:0000250|UniProtKB:Q8WXG1}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WXG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8WXG1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8WXG1}. Golgi apparatus {ECO:0000250|UniProtKB:Q8WXG1}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8WXG1}. Lipid droplet {ECO:00002...
CATALYTIC ACTIVITY: Reaction=AH2 + CTP + S-adenosyl-L-methionine = 3'-deoxy-3',4'-didehydro-CTP + 5'-deoxyadenosine + A + H(+) + H2O + L-methionine; Xref=Rhea:RHEA:65944, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499, ChEBI:CHEBI:37563, ChEBI:CHEBI:57844, ChEBI:CHEBI:5978...
null
null
null
null
FUNCTION: Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism. In turn, ddhCTP acts as a chain terminat...
Rattus norvegicus (Rat)
O70601
LAT_RAT
MEADALSPVELGLLLLPFVVMLLAALCVRCRELPASYDSASTESLYPRSILIKPPQITVPRTPATSYPLVTSFPPLRQPDLLPIPRSPQPLGGSHRMPSSRQNSDDANSVASYENQEPARKNVDEDEDEDDYPEGYLVVLPDSSPAAVPVVSSAPVPSNPDLGDSAFSMESCEDYVNVPESEESAEASLDGSREYVNVSQDAQPVIRAELASVTSQEVEDEEEEDVDGEEAPDYENLQELN
null
null
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; gene expression [GO:0010467]; homeostasis of number of cells [GO:0048872]; immune response [GO:0006955]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; l...
cell-cell junction [GO:0005911]; COP9 signalosome [GO:0008180]; immunological synapse [GO:0001772]; membrane [GO:0016020]; plasma membrane [GO:0005886]
protein kinase binding [GO:0019901]; signaling receptor complex adaptor activity [GO:0030159]
PF15234;
null
null
PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ (By similarit...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Present in lipid rafts. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-med...
Rattus norvegicus (Rat)
O70608
SYCP2_RAT
MPVRPDPQQLEKCIDDALRKNDFKPLVTLLQIDICEDVKIKCSKQFLRKLDDLICRELHKKDIQTISNILISIGRCSKNIFILGQTGLQTMIKQGLVQKMVSWFENSKEIILSQRQSKDEAVMNMIEDLFDLLMVVYDVNDEGKNQVLESFIPHICALVIDSRVNFCIQQEALKKMNLMLDRIPQDANKILCNQEILTLMSNMGERILDVGDYELQVGIVEALCRMTTEKRRQELAYEWFSMDFIANAFKKIKDCEFETDCRIFLNLVNGMLGDRRRVFTFPCLSAFLGKYELQIPSDEKLEEFWIDFNLGSHTLSFYIA...
null
null
animal organ morphogenesis [GO:0009887]; apoptotic process [GO:0006915]; cell division [GO:0051301]; ectopic germ cell programmed cell death [GO:0035234]; female meiotic nuclear division [GO:0007143]; fertilization [GO:0009566]; male genitalia morphogenesis [GO:0048808]; male meiotic nuclear division [GO:0007140]; nega...
lateral element [GO:0000800]; synaptonemal complex [GO:0000795]
DNA binding [GO:0003677]
PF18581;PF18584;
null
SYCP2 family
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9CUU3}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9933407}. Chromosome {ECO:0000269|PubMed:9592139, ECO:0000269|PubMed:9933407}. Note=In axial/lateral elements of the tripartite segments of synaptonemal complexes. {ECO:0000269|PubMed:9933407}.
null
null
null
null
null
FUNCTION: Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase (PubMed:9592139, PubMed:9933407). Plays a role in the assembly of synaptonemal complexes. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and fem...
Rattus norvegicus (Rat)
O70622
RTN2_MOUSE
MGQVLPVFAHCKEAPSTASSTPDSTEGGNDDSDFRELHTAREFSEDEEEETTSQDWGTPRELTFSYIAFDGVVGSGGRRDSVVRRPRPQGRSVSEPRDPPQQSGLGDSLESIPSLSQSPEPGRRGDPDPVPPAERPLEELRLRLDQLGWVVRSAGSGEDSATSSSTPLENEEPDGLEASEAGEETNLELRLAQSLHLQLEVLTPQLSPSSGTPQAHTPSPQRSQDSNSGPDDEPLLNVVEEHWRLLEQEPITAQCLDSTDQSEFMLEPLLLVADLLYWKDTRTSGAVFTGLMASLLCLLHFSIVSVAAHLALLGLCATIS...
null
null
gene expression [GO:0010467]; intracellular protein transmembrane transport [GO:0065002]; negative regulation of amyloid-beta formation [GO:1902430]; protein transport [GO:0015031]; regulation of glucose import [GO:0046324]
cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intermediate filament [GO:0005882]; sarcoplasmic reticulum membrane [GO:0033017]; T-tubule [GO:0030315]; terminal cisterna [GO:0014802]; Z disc [GO:0030018]
null
PF02453;
1.20.5.2480;
null
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75298}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:19720795}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q6WN19}; Multi-pass membrane protein {ECO:0000255...
null
null
null
null
null
FUNCTION: Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity (By similarity). Enhances trafficking of the glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to the cell surface (By similarity). Plays a role in the translocation of SLC2A4/GLUT4 from intracellular membranes ...
Mus musculus (Mouse)
O70624
MYOC_MOUSE
MPALHLLFLACLVWGMGARTAQFRKANDRSGRCQYTFTVASPNESSCPREDQAMSAIQDLQRDSSIQHADLESTKARVRSLESLLHQMTLGRVTGTQEAQEGLQGQLGALRRERDQLETQTRDLEAAYNNLLRDKSALEEEKRQLEQENEDLARRLESSSEEVTRLRRGQCPSTQYPSQDMLPGSREVSQWNLDTLAFQELKSELTEVPASQILKENPSGRPRSKEGDKGCGALVWVGEPVTLRTAETIAGKYGVWMRDPKPTHPYTQESTWRIDTVGTEIRQVFEYSQISQFEQGYPSKVHVLPRALESTGAVVYAGSL...
null
null
bone development [GO:0060348]; clustering of voltage-gated sodium channels [GO:0045162]; ERBB2-ERBB3 signaling pathway [GO:0038133]; myelination in peripheral nervous system [GO:0022011]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of Rho protein signal transduction [GO:0035024]; negat...
cilium [GO:0005929]; collagen-containing extracellular matrix [GO:0062023]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; mesaxon [GO:0097453]; mitochondrial inner membrane [GO:0005743]; mitochond...
fibronectin binding [GO:0001968]; frizzled binding [GO:0005109]; metal ion binding [GO:0046872]; myosin light chain binding [GO:0032027]; receptor tyrosine kinase binding [GO:0030971]
PF02191;
null
null
PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q2PT31}.; PTM: Undergoes a calcium-dependent proteolytic cleavage at Gln-212 by CAPN2 in the endoplasmic reticulum. The result is the production of two fragments, one of 35 kDa containing the C-terminal olfactomedin-like domain, and another of 20 kDa containing the N-terminal ...
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16392033}. Golgi apparatus {ECO:0000269|PubMed:23629661}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q99972}. Secreted, ext...
null
null
null
null
null
FUNCTION: Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regul...
Mus musculus (Mouse)
O70628
PDE9A_MOUSE
MGAGSSSYRPKAIYLDIDGRIQKVVFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAVKQVSEREELIQGVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARNSRTNCPCKYSFLDNKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPITLRRWLLCVHDNYRNNPFHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPL...
3.1.4.35
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O76083}; Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc. {ECO:0000250|UniProtKB:O76083}; COFACTOR: Name=Mg(2+...
cAMP-mediated signaling [GO:0019933]; cGMP catabolic process [GO:0046069]; negative regulation of neural precursor cell proliferation [GO:2000178]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of long-term synaptic potentiation [GO:1900273]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; ruffle membrane [GO:0032587]; sarcolemma [GO:0042383]
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872]
PF00233;
1.10.1300.10;
Cyclic nucleotide phosphodiesterase family, PDE9 subfamily
null
SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}.
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000269|PubMed:9624145};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for cGMP {ECO:0000269|PubMed:9624145};
PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
null
null
FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes (PubMed:9624145). Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriu...
Mus musculus (Mouse)
O70631
EST2C_RAT
MARKQPHSWLNAVLFGLLLILIHVWGQDSPESSSIRTTHTGQVRGKLDHVRDTKAGVHTFLGIPFAKAPVGPLRFAPPEDPEPWSGVRDGTSHPAMCLQNIDMLDEVGLTDMKMILSSIPMSEDCLYLNIYTPAHAHEGSNLPVMVCIHGGALVIGMASMCDGSLLAVNEDLVVVAIQYRLGVLGFFSTGDEHARGNWGYLDQVAALRWVQQNIAHFGGNPNRVTIFGVSAGGTSVSSHVISPMSQGLFHGAIMESGVALLPDLISETSETVSTTVAKLSGCEATDSETLVRCLRAKSGAEILVINKVFKMIPAVVDGEF...
3.1.1.-; 3.1.1.28
null
retinoid metabolic process [GO:0001523]
endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]
acylcarnitine hydrolase activity [GO:0047619]; all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; carboxylic ester hydrolase activity [GO:0052689]; retinyl-palmitate esterase activity [GO:0050253]
PF00135;
3.40.50.1820;
Type-B carboxylesterase/lipase family
null
SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12230550}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q91WG0}.
CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000305|PubMed:12230550}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:...
null
null
null
null
FUNCTION: Hydrolase with high activity towards palmitoylcarnitine. Is also active with p-nitrophenylacetate and alpha-naphthylacetate (By similarity). May also hydrolyze retinyl esters (PubMed:12230550). {ECO:0000250|UniProtKB:Q91WG0, ECO:0000269|PubMed:12230550}.
Rattus norvegicus (Rat)
O70632
M2_I97A1
MSLLTEVETLTRNGWGCRCSDSSDPLVVAASIIGILHLILWILDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYRQEQQNAVDVDDGHFVNIELE
null
null
protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
identical protein binding [GO:0042802]; monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078]
PF00599;
6.10.250.1640;
Influenza viruses matrix protein M2 family
null
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit...
null
null
null
null
null
FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is...
Influenza A virus (strain A/Hong Kong/156/1997 H5N1 genotype Gs/Gd)
O70889
TAT_HV193
MELVDPNLDPWNHPGSQPTTPCTRCYCKWCCFHCYWCFTTKGLGISYGRKKRRQRPRTPQSSQIHQDFVPKQPISQARGNPTGPKESKKEVESKAKTDP
null
null
DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s...
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970]
PF00539;
4.10.20.10;
Lentiviruses Tat family
PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of...
SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ...
null
null
null
null
null
FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE...
Human immunodeficiency virus type 1 group M subtype F1 (isolate 93BR020) (HIV-1)
O70899
TAT_HV190
MDPVDPKLEPWNHPGSQPQTACNNCYCKKCCYHCQMCFLKKGLGISYGRKKRSQRHRTPASLQDHQNSISKQPLSRTHGDPTGPKEQKKEVASKTETDP
null
null
DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s...
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970]
PF00539;
4.10.20.10;
Lentiviruses Tat family
PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of...
SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ...
null
null
null
null
null
FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE...
Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056) (HIV-1)
O70902
ENV_HV190
METQRNYPSLWRWGTLILGMLLICSAAQNLWVTVYYGVPVWKEAKTTLFCASDAKAYETEKHNVWATHACVPTDPNPQEMVMENVTESFNMWENNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCTNVRNNTSNSTSSMEAGGELTNCSFNVTTVLRDKQQKVHALFYRLDVVPIDNNSTQYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGLCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEQIIIRTKNISDNTKNIIVQLKTPVNITCTRPNNNTRTSIHLGPGRAFYATGDIIGDIRQ...
null
null
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz...
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
structural molecule activity [GO:0005198]
PF00516;PF00517;
1.10.287.210;2.170.40.20;1.20.5.490;
HIV-1 env protein family
PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ...
SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-...
null
null
null
null
null
FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like...
Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056) (HIV-1)
O70903
NEF_HV190
MGGKWSKSRMGGWSTIRERMRRAEPVAEGVGAVSRDLDRRGAVTINNTASTNRDAAWLEAQEDGEEVGFPVRPQVPLRPMTYKGAFDLSHFLKEKGGLDGLIYSKQRQDILDLWVYNTQGYFPDWQNYTPGPGERFPLTFGWCFKLVPVNPQEVEQANEGENNSLLHPMSLHGMEDDGREVLMWKFDSRLALTHLARVKHPEYKDC
null
null
suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu...
extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
GTP binding [GO:0005525]; SH3 domain binding [GO:0017124]
PF00469;
4.10.890.10;3.30.62.10;
Lentivirus primate group Nef protein family
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM...
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0...
null
null
null
null
null
FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells...
Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056) (HIV-1)
O71189
R1AB_GLRV3
MDYIRPLRVFSFPHVNNTLEYVRYNKANGDVGAFLTTMKFIGNVKLSDFTPRCAAMIYIGKLTKGVKRTFVPPPVKGFARQYAVVSGSVSALRGDGKKVLMEARTSTSATSDVSDFDVVFEAVSNALLVVHYHRVVPYAPVKREQPKPAVKQDEQKPKRQASHWAVKPTAVGVHVPLPKKQEALEPAQSVPQQSLEEKAALTFGLFFSKGGGDESDAVILRKGKLFNRALNVPIDVKNTFVWAKIWDEASRRRGYFYVKDRAVKFFPIVRGRATIEDFIVNTAPGCDVALPRIELWSMRERAFVCTTKGWCWFNNERLRG...
2.1.1.-; 2.7.7.48; 3.4.22.-; 3.6.4.13
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805};
DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694]
null
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activ...
PF03171;PF00978;PF01443;PF01660;
2.60.120.590;3.40.50.300;
SsRNA positive-strand viruses RNA-directed RNA polymerase family
null
null
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2...
null
null
null
null
FUNCTION: RNA-dependent RNA polymerase replicates the viral genome. {ECO:0000305}.
Grapevine leafroll-associated virus 3 (isolate United States/NY1) (GLRaV-3) (Grapevine leafroll-associated closterovirus (isolate 109))
O71305
HBSAG_WMHBV
MGLNQSTFNPLGFFPSHQLDPLFKANAGSADWDKNPNKDPWPQAHDTAVGAFGPGLVPPHGGLLGWSSQAQGLSVTVPDTPPPPSTNRDKGRKPTPATPPLRDTHPQAMTWNTSSFQSYLQNPKVRGLYFPAGGSTSSIVNPVPTTASTTSSSFSTTGVPVSTMDITSSGFLGPLLALQAVFFLLTKILTMPQSLDSLWTSLNFLGGTPACPGLNSQSPTSSHSPTCCPPTCPGYRWMCLRRSIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPTVTGTTTTTGPCRTCTPIVPGISSYPSCCCTKPTDGNCTCIPIPSS...
null
null
caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
null
PF00695;
null
Orthohepadnavirus major surface antigen family
PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}.
null
null
null
null
null
FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici...
Woolly monkey hepatitis B virus (isolate Louisville) (WMHBV)
O72157
RDRP_SBMVA
MYHPGRSPSFLITLANVICAAILFDIHTGGYQPGSLIPIVAWMTPFVTLLWLSASFATYLYKYVRTRLLPEEKVARVYYTAQSAPYFDPALGVMMQFAPSHGGASIEVQVNPSWISLLGGSLKINGDDASNESAVLGSFYSSVKPGDEPASLVAIKSGPQTIGFGCRTKIDGDDCLFTANHVWNNSMRPTALAKRGKQVAIEDWETPLSCDHKMLDFVVVRVPKHVWSKLGVKATQLVCPSDKDAVTCYGGSSSDNLLSGTGVCSKVDFSWKLTHSCPTAAGWSGTPIYSSRGVVGMHVGFEDIGKLNRGVNAFYVSNYL...
2.7.7.48; 3.4.21.-
null
DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral process [GO:0016032]
host cell membrane [GO:0033644]; membrane [GO:0016020]
nucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]
PF02122;PF02123;
2.40.10.10;
null
PTM: The polyprotein is proteolytically cleaved into several chains by the viral protease.
SUBCELLULAR LOCATION: [N-terminal protein]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Replicase polyprotein P2AB]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48;
null
null
null
null
FUNCTION: [Serine protease]: Responsible for cleavages of polyprotein P2A and replicase polyprotein P2AB.; FUNCTION: [VPg]: Covalently attached to the 5' extremity of the genomic and subgenomic RNAs. It may serve as a primer for the replicase.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:...
Southern bean mosaic virus (isolate Bean/United States/Arkansas) (SBMV)
O73556
POLG_HPE2W
METIKSIADMATGVTKTIDATINSVNEIITNTDNASGGDILTKVADDASNILGPNCYATTSEPENKDVVQATTTVNTTNLTQHPSAPTLPFTPDFSNVDTFHSMAYDTTTGSKNPNKLVRLTTHAWASTLQRGHQIDHVNLPVDFWDEQRKPAYGHAKYFAAVRCGFHFQVQVNVNQGTAGSALVVYEPKPVVDYDKDLEFGAFTNLPHVLMNLAETTQADLCIPYVADTNYVKTDSSDLGQLKVYVWTPLSIPSGSSNQVDVTILGSLLQLDFQNPRVYGQNVDIYDTAPSKPIPLRKTKYLTMSTKYKWTRNKVDIAE...
2.7.7.48; 3.4.22.28; 3.6.1.15
COFACTOR: [RNA-directed RNA polymerase 3D-POL]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center. The magnesium ions are not prebound but only present for catalysis. {ECO:0000250|UniProtKB:P03300};
DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]
host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [G...
PF06344;PF00548;PF06363;PF00680;PF00073;PF00910;
2.60.120.20;3.30.70.270;3.40.50.300;2.40.10.10;
Picornaviruses polyprotein family
PTM: VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}.; PTM: Specific enzymatic cleavages yield mature proteins (By similarity). All cleavages are catalyzed by P3C (By...
SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:Q66578}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2A H-NC]: Host cytoplasm {ECO:0000250|UniProtKB:Q66578}. Host nucleus, host nu...
CATALYTIC ACTIVITY: [RNA-directed RNA polymerase 3D-POL]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};...
null
null
null
null
FUNCTION: [Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid proteins interact...
Human parechovirus 2 (strain Williamson) (HPeV-2) (Echovirus 23)
O73557
Z_LASSJ
MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAAPTAPPTGAADSIRPPPYSP
null
null
viral budding from plasma membrane [GO:0046761]; viral budding via host ESCRT complex [GO:0039702]
host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
RNA binding [GO:0003723]; zinc ion binding [GO:0008270]
PF03854;
3.30.160.310;
Arenaviridae Z protein family
null
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04087}. Note=Mainly perinuclear. Du...
null
null
null
null
null
FUNCTION: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction...
Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
O73673
GCR_PAROL
MDQGGLKRNCNRDDSLTFGETAVGVGSDTGDTAGSLLQPAAMHLPSPSSLPQLTVAPNGGAGTKDQGEFGGLFESPRGQCEGSEMKEGKIIRLQKRKHHLDIGMFNMEDNLSLLNQNISDLNRTSTSVISTSDTSVLGKLPLPNLFPQHIKQEGGFSLEKELGTYGGHTGGGPCDLDGNSGHLIEDTEIWQDLDLPNSLPEISDFELDSEVAHLDNILHDSSGGCGPDGSLLKETKVLVGNGGNCTDVNGTDQQHPLQHHQHQQQQHRHLLQHQQHQLHHQHQQPPSLLSSVMIKEEKDHDNSFIHIRTPGVVKQEKQEN...
null
null
cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to steroid hormone stimulus [GO:0071383]; chromatin organization [GO:0006325]; positive regulation of transcription by RNA polymerase II [GO:0045944]
centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle [GO:0005819]
DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear glucocorticoid receptor activity [GO:0004883]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270]
PF02155;PF00104;PF00105;
3.30.50.10;1.10.565.10;
Nuclear hormone receptor family, NR3 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=A...
null
null
null
null
null
FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in...
Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
O73682
VGFAA_DANRE
MNLVVYLIQLFLAALLHLSAVKAAHIPKEGGKSKNDVIPFMDVYKKSACKTRELLVDIIQEYPDEIEHTYIPSCVVLMRCAGCCNDEALECVPTETRNVTMEVLRVKQRVSQHNFQLSFTEHTKCECRPKAEVKAKKENHCEPCSERRKRLYVQDPLTCKCSCKFTQMQCKSRQLELNERTCRCEKPR
null
null
angioblast cell migration from lateral mesoderm to midline [GO:0035479]; angiogenesis [GO:0001525]; artery morphogenesis [GO:0048844]; blood vessel development [GO:0001568]; blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; branching involved in blood vessel morphogenesis [GO:...
extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]
chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; vascular endothelial growth factor receptor 1 binding [GO:0043183]; vascular endothelial growth factor receptor 2 binding [GO:0043184]; vascular endothelial growth factor receptor binding [GO:0005172]
PF00341;PF14554;
2.10.90.10;2.10.160.10;
PDGF/VEGF growth factor family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17698971}.
null
null
null
null
null
FUNCTION: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis, and induces permeabilization of blood vessels. Required for intersegmental vessel development in the tail during embryogenesis (PubMed:15305301...
Danio rerio (Zebrafish) (Brachydanio rerio)
O73683
A4_TETFL
MGHSVAWLLLVAAASTLAAEVPTDVSMGLLAEPQVAMFCGKINMHINVQSGKWEPDPSGTKSCIGTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHMHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRAMNLHDYGMLLPCGIDRFRGVEFVCCPAEAERDMDSTEKDADDSDVWWGGADNDYSDNSMVREPEPAEQQEETRPSVVEEEEEGEVAQEDDEEEEEVLDTDQDGDGEEDHEAADDEEEEEDVDEIDAFGESDDVDADEPTTNVAMTTTTTTTTTESVE...
null
null
axonogenesis [GO:0007409]; central nervous system development [GO:0007417]
cell surface [GO:0009986]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]
heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor activator activity [GO:0030546]; signaling receptor binding [GO:0005102]; transition metal ion binding [GO:0046914]
PF10515;PF12924;PF12925;PF02177;PF03494;PF00014;
6.10.250.1670;1.20.120.770;3.30.1490.140;3.90.570.10;4.10.410.10;2.30.29.30;
APP family
null
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Functional neuronal receptor which couples to intracellular signaling pathway through the GTP-binding protein G(O). {ECO:0000250}.
Tetraodon fluviatilis (Green pufferfish) (Chelonodon fluviatilis)
O73689
ZIC1_XENLA
MLLDAGAQYPAIGVTTFGSSRHHSAGDVTDREVALGINPFADGMGAFKLNPSSHDLASGQTAFTSQAPGYAAAALGHHHHPGHVSSYSSAAFNSTRDFLFRNRGFGEAASAQHSLFASAAGGFPGPHGPHADTTGHLIFPGLHEQAASHASPNVVNGQMRLGFSGDMYGRPDQYGQVTSPRSEHYASSQLHGYGPMNMNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLANPKKSCNKTFSTMHELVTHVTVEHVGGPEQSNHICVWEECPREGKPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKR...
null
null
dorsal/ventral neural tube patterning [GO:0021904]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell differentiation [GO:0014033]; neural crest cell fate commitment [GO:0014034]; neural crest formation [GO:0014029]; neural plate development [GO:0001840]; neurogenesis [GO:0022008...
cytoplasm [GO:0005737]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00096;PF18366;
3.30.160.60;
GLI C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9655809}. Cytoplasm {ECO:0000250}.
null
null
null
null
null
FUNCTION: Transcriptional activator that induces expression of multiple genes including pax3, en2, snai2/slug, feb and a subset of wnt genes. Has multiple key roles in the regulation of neural induction and neurogenesis: acts as a neural competence factor, sensitizing the presumptive neuroectoderm to respond to subsequ...
Xenopus laevis (African clawed frog)
O73693
EGR1_TAEGU
CDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKVEKAAPASTASPIPAYSSSVTTSYPSSITTTYPSPVRTAYSSPAPSSYPSPVHTTFPSPSIATTYPSGTATFQTQVATSFSSPGVANNFSSQVTSALSDINSAFSPRTIEIC
null
null
cellular response to interleukin-8 [GO:0098759]; circadian regulation of gene expression [GO:0032922]; interleukin-1-mediated signaling pathway [GO:0070498]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein sum...
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded methylated DNA binding [GO:0010385]; hemi-methylated DNA-binding [GO:0044729]; histone acetyltransferase binding [GO:0035035]; promoter-sp...
PF11914;PF00096;
3.30.160.60;
EGR C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18146}. Cytoplasm {ECO:0000250|UniProtKB:P18146}.
null
null
null
null
null
FUNCTION: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (By similarity). Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerous target genes, and...
Taeniopygia guttata (Zebra finch) (Poephila guttata)
O73700
CAC1D_CHICK
MQHHQQQQPEQHPEEANYASSTRIPLPGDGPTTQSNSSAPSKQTVLSWQAAIDAARQAKAAQNMNTTTAQPVGSLSQRKRQQYAKSKKQGNTSNSRPPRALFCLSLNNPIRRACISLVEWKPFDIFILLSIFANCVALAVYIPFPEDDSNSTNHNLEKVEYAFLIIFTVETFLKIIAYGLLLHPNAYVRNGWNLLDFVIVVVGLFSVILEQLTKETEGGSHSGGKPGGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFIGKMHKSCFLIDSDILVEEDPAPCAFSGNGRQ...
null
null
calcium ion import across plasma membrane [GO:0098703]
voltage-gated calcium channel complex [GO:0005891]
high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]
PF08763;PF16885;PF16905;PF00520;
1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350;
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1D subfamily
null
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group.
Gallus gallus (Chicken)
O73707
CAC1C_CHICK
ALIVVGSIVDIAITEVNNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPDKKCDPDSEPANSTEADHSCGSSFAVFYFISFYMLCAFLIIDLFVAVI
null
null
calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transmembrane transport via high voltage-gated calcium channel [GO:0061577]; calcium ion transport into cytosol [GO:0060402]; cardiac conduction [GO:0061337]; regulation of cardiac muscle contraction by...
dendrite [GO:0030425]; L-type voltage-gated calcium channel complex [GO:1990454]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]
calmodulin binding [GO:0005516]; high voltage-gated calcium channel activity [GO:0008331]; voltage-gated calcium channel activity [GO:0005245]
PF00520;
1.10.287.70;1.20.120.350;
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1C subfamily
PTM: Phosphorylation by PKA activates the channel. {ECO:0000250|UniProtKB:P15381}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22002}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P22002}. Perikaryon {ECO:0000250|UniProtKB:P22002}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-...
null
null
null
null
null
FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm. Plays an important role in excitation-contraction coupling in the heart. Required for no...
Gallus gallus (Chicken)
O73727
INS_DANRE
MAVWLQAGALLVLLVVSSVSTNPGTPQHLCGSHLVDALYLVCGPTGFFYNPKRDVEPLLGFLPPKSAQETEVADFAFKDHAELIRKRGIVEQCCHKPCSIFELQNYCN
null
null
glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; negative regulation of feeding behavior [GO:2000252]; positive regulation of pancreatic A cell differentiation [GO:2000228]; positive regulation of protein secretion [GO:0050714]; response to glucose [GO:0009749]; response to nutrient levels [GO:...
extracellular space [GO:0005615]
hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]
PF00049;
1.10.100.10;
Insulin family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Danio rerio (Zebrafish) (Brachydanio rerio)
O73754
GREM1_XENLA
MNCLVYALGSLFLLSGLLLPSSEGKKKVSGSQGAIPPPDKGQPNDSEQGQAQPGDRVRGKGKGQALAAEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEDGCNSRTIINRFCYGQCNSFYIPRHIRREEGSFQSCSFCKPKKFTTMVVTLNCPELQPPTKKKRITRVKQCRCISIDLD
null
null
animal organ morphogenesis [GO:0009887]; determination of dorsal identity [GO:0048263]; nervous system development [GO:0007399]; neural crest cell development [GO:0014032]; neural crest formation [GO:0014029]; pronephric duct development [GO:0039022]; sequestering of BMP from receptor via BMP binding [GO:0038098]; sequ...
extracellular space [GO:0005615]
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; morphogen activity [GO:0016015]
PF03045;
2.10.90.10;
DAN family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: Cytokine that has an axial patterning activity. Acts like BMP antagonist in embryonic explants. Blocks the BMP2 activity. {ECO:0000269|PubMed:9660951}.
Xenopus laevis (African clawed frog)
O73755
GREM1_CHICK
MVRTLYAIGAVFLLTGFLLPTAEGRKRNRGSQGAIPPPDKDQPNDSEQMQTQQQSGSRHRERGKGTSMPAEEVLESSQEALHITERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHVRKEEGSFQSCSFCKPKKFTTMTVTLNCPELQPPRKKKRITRVKECRCISIDLD
null
null
animal organ morphogenesis [GO:0009887]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [GO:0060379]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell morphogenesis [GO:0000902]; cell-cell signaling [GO:0007267]; collagen fibril organization [GO:003019...
cell surface [GO:0009986]; extracellular space [GO:0005615]
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; protein homodimerization activity [GO:0042803]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; vascular endothelial growth factor receptor 2 binding [GO:0043184]
PF03045;
2.10.90.10;
DAN family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: Cytokine that may play a role in the development of the medial pallium and during optic nerve and pecten development by modulating BMP signaling. {ECO:0000269|PubMed:14991724}.
Gallus gallus (Chicken)
O73790
SPB10_CHICK
MEQVSASIGNFTVDLFNKLNETNRDKNIFFSPWSISSALALTYLAAKGSTAREMAEVLHFTEAVRAESSSVARPSRGRPKRRRMDPEHEQAENIHSGFKELLTAFNKPRNNYSLRSANRIYVEKTYALLPTYLQLSKKYYKAEPQKVNFKTAPEQSRKEINTWVEKQTESKIKNLLSSDDVKATTRLILVNAIYFKAEWEVKFQAEKTSIQPFRLSKNKSKPVKMMYMRDTFPVLIMEKMNFKMIELPYVKRELSMFILLPDDIKDGTTGLEQLERELTYERLSEWADSKMMTETLVDLHLPKFSLEDRIDLRDTLRNMG...
null
null
chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; nucleate erythrocyte maturation [GO:0043362]
chromatin [GO:0000785]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]
chromatin DNA binding [GO:0031490]; serine-type endopeptidase inhibitor activity [GO:0004867]
PF00079;
2.30.39.10;3.30.497.10;
Serpin family, Ov-serpin subfamily
null
SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with chromatin.
null
null
null
null
null
FUNCTION: DNA-binding protein that promotes DNA condensation into transcriptionally inactive heterochromatin in terminally differentiated avian blood cells. Promotes tight packing of nucleosomes into spherical clusters by binding to linker DNA and subsequent oligomerization. Acts as a cysteine protease inhibitor toward...
Gallus gallus (Chicken)
O73791
TIE2_DANRE
MCLLDSCTALLLLGCWMSGSAVRISDVTLVNPDPVVSPLTAPSLLCVSSDWSSGGSVLALGQEFPRPQGSVLALGQEFPHTEPRPHPAAATVTWSSRSHAFGAFYCQIRNSTGRKIYTYKMLQEAAFLPESLTITVNQGENINISYSRRLYSPEDTVIHKNGHFEHSSPKEDISDIIHYPVTNAKAESHAGIYAIRYISAAPSSAAITRLIVRSCRAGFWGPNCTESCPRCANGGVCDDTTGECVCPPGFRGHTCDIVCGEGRFGAGCKERCVDGVCRALVFCLRDPYGCSCASGWRGLSCNDACPDGYYGAGCTQKCVC...
2.7.10.1
null
angiogenesis [GO:0001525]; endothelial cell proliferation [GO:0001935]; heart development [GO:0007507]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of...
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
PF00041;PF00047;PF10430;PF07714;
2.60.40.10;2.170.300.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Tie subfamily
PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner, where Tyr-984 in the kinase activation loop is phosphorylate...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q02763}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000250|UniProtKB:Q02763}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q02763}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Recruited to cell-cell contacts in quiescent endo...
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:PRU100...
null
null
null
null
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for angiopoietins and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Can activate or inhibit angiogenes...
Danio rerio (Zebrafish) (Brachydanio rerio)
O73792
TIE1_DANRE
QLLQFAADVATGMHYLSDKQFIHRDLAARNVLVGDNLVAKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEQPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLNRMQEARKAYVNMALFENFTYAGIDATAEEA
2.7.10.1
null
angiogenesis [GO:0001525]; blood vessel development [GO:0001568]; endothelial cell-cell adhesion [GO:0071603]; heart development [GO:0007507]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vasculature develo...
plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
PF07714;
1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Tie subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
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:PRU100...
null
null
null
null
FUNCTION: Transmembrane tyrosine-protein kinase (Probable). Required for the formation of facial lymphatic structures and brain lymphatic endothelial cells (PubMed:37097004). Also required for embryonic ventral and dorsal migration of parachordal lymphoblasts along the arterial intersegmental vessel (PubMed:37097004). ...
Danio rerio (Zebrafish) (Brachydanio rerio)
O73798
IGF1R_XENLA
MKAELVPVCTAWILGLLLCLGPAAAKVCGPNMDIRNDVSELKQLRDCVVIEGYLQILLISNAKAEDFRNLRFPNLTVITDYLLLFRVSGLVSLSNLFPNLTVIRGRVLFYNYALVIFEMTDLKEIGLYNLRNITRGAVRIEKNSELCYVSTVDWSLVLDAVYNNYIVGNKPPKECVDLCPGAREKMQICEKSSINNEFADRCWSDEHCQKVCPSVCGKRACSDNNECCHPECLGSCTAPDNDTACVACHHYFYEGRCVPTCPSNTYKFEGWRCITREVCAKMHIWIHSTIPFIIHKGECVYECPSGYMLNKSQSMTCSPC...
2.7.10.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
cellular response to glucose stimulus [GO:0071333]; insulin-like growth factor receptor signaling pathway [GO:0048009]; oocyte maturation [GO:0001556]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; protein autoph...
axon [GO:0030424]; insulin receptor complex [GO:0005899]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor binding [GO:0005520]; insulin-like growth factor receptor activity [GO:0005010]; metal ion binding [GO:0046872]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein tyros...
PF00757;PF07714;PF01030;
2.60.40.10;3.80.20.20;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
PTM: The cytoplasmic domain of the beta subunit is autophosphorylated on Tyr residues in response to low concentrations of insulin-like growth factor (IGF 1) and higher concentrations of insulin.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1847619}; Single-pass type I membrane protein {ECO:0000269|PubMed:1847619}. Note=Expressed at the oocyte surface.
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:PRU100...
null
null
null
null
FUNCTION: This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade. Plays a role in oocyte maturation. Promotes head development by inh...
Xenopus laevis (African clawed frog)
O73810
DRD2_MELGA
MDPLNLSWYNTGDRNWSEPVNESSADQKPQYNYYAVLLTLLIFVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWRFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAAAMPMLYNTRYSSKRRVTVMIACVWVLSFAISSPILFGLNKADERECIIANPAFVVYSSVVSFYVPFIVTLLVYVQIYMVLRRRRKRHTKRSSHGLDSDTHAPLKDKCTHPENVKLGTVIVKSNGSFQVNKRKCEAESHIKMEMEMMSSTSPPERTIVKAAAPSNHQLVVPVASSRSTLDSPGKVEKN...
null
null
adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-inhibiting dopamine receptor signaling pathway [GO:0007195]; hyaloid vascular plexus regression [GO:1990384]; negative regulation of calcium ion transport into cytosol [GO:0010523]; negative regulation of peptide hormone ...
glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]
dopamine binding [GO:0035240]; dopamine neurotransmitter receptor activity, coupled via Gi/Go [GO:0001591]; G protein-coupled receptor activity [GO:0004930]; signaling receptor activity [GO:0038023]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Palmitoylated. Palmitoylation which is required for proper localization to the plasma membrane and stability of the receptor could be carried on by ZDHHC4, ZDHHC3 and ZDHHC8. {ECO:0000250|UniProtKB:P14416}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (By similarity). {ECO:0000250|UniProtKB:P14416, ECO:0000250|UniProtKB:P6116...
Meleagris gallopavo (Wild turkey)
O73864
WNT11_DANRE
MTEYRNFLLLFITSLSVIYPCTGISWLGLTINGSSVGWNQTHHCKLLDGLVPDQQQLCKRNLELMHSIVRAARLTKSACTSSFSDMRWNWSSIESAPHFTPDLAKGTREAAFVVSLAAAVVSHAIARACASGDLPSCSCAAMPSEQAAPDFRWGGCGDNLRYYGLQMGSAFSDAPMRNRRSGPQDFRLMQLHNNAVGRQVLMDSLEMKCKCHGVSGSCSVKTCWKGLQDISTISADLKSKYLSATKVIPRQIGTRRQLVPREMEVRPVGENELVYLVSSPDYCTQNAKQGSLGTTDRQCNKTASGSESCGLMCCGRGYNA...
null
null
camera-type eye development [GO:0043010]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cell migration [GO:0016477]; cell migration involved in gastrulation [GO:0042074]; cell-cell adhesion [GO:0098609]; central nervous system development [GO:0007417]; convergent extension [GO:0060026...
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; GTPase activator activity [GO:0005096]; protein heterodimerization activity [GO:0046982]; 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. May play a role in the formation of dermal structure in limb buds. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.
Danio rerio (Zebrafish) (Brachydanio rerio)
O73872
SODC_DANRE
MVNKAVCVLKGTGEVTGTVYFNQEGEKKPVKVTGEITGLTPGKHGFHVHAFGDNTNGCISAGPHFNPHDKTHGGPTDSVRHVGDLGNVTADASGVAKIEIEDAMLTLSGQHSIIGRTMVIHEKEDDLGKGGNEESLKTGNAGGRLACGVIGITQ
1.15.1.1
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
neuron cellular homeostasis [GO:0070050]; removal of superoxide radicals [GO:0019430]; response to metal ion [GO:0010038]; response to methylmercury [GO:0051597]; response to xenobiotic stimulus [GO:0009410]
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777]
copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784]
PF00080;
2.60.40.200;
Cu-Zn superoxide dismutase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1;
null
null
null
null
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Danio rerio (Zebrafish) (Brachydanio rerio)
O73874
EFNB2_DANRE
MGDSLWRYYFGVLVIACKVNLSRALILDSIYWNTTNTKFVPGQGLVLYPQIGDKMDIVCPRVEGGSMEGVEYYKLYMVPLEQLKSCQVTKADTPLLNCVKPDQDVKFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKVGQNPSDPISPKDYPTSYPPKHPDLGGKDSKSNEVLKPDASPHGEDKGDGNKSSSVIGSEVALFACIASASVIVIIIIIMLVFLLLKYRRRHRKHSPQHATTLSLSTLATPKRGGSGGNNNGSEPSDIIIPLRTADSVFCPHYEKVSGDYGHPVYIVQEM...
null
null
angioblast cell migration involved in selective angioblast sprouting [GO:0035475]; anterior/posterior pattern specification [GO:0009952]; axon guidance [GO:0007411]; axon target recognition [GO:0007412]; blood vessel development [GO:0001568]; blood vessel morphogenesis [GO:0048514]; cell adhesion [GO:0007155]; cell mig...
glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
ephrin receptor binding [GO:0046875]
PF00812;
2.60.40.420;
Ephrin family
PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P52799}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional sign...
Danio rerio (Zebrafish) (Brachydanio rerio)
O73875
EPB4A_DANRE
MELFSRNVAAFWIILLEFLLGSVAEEEVLMNTKTETSDLKWTTHSRSKPEWEEVSGLDEENNSVRTYQICQADGSSSHWLRSKLIERRGASQVYVELFFTMVECSSRNTHHRSCKETFNLYYYQSDTDDATATHPAWMENPYTKVDTVAADFLLRKGGEKKVNVKTLRLGPLSKRGFYLAFQAQGACMALLSVRVFFKKCPALTRSLSVFPETVPRSLVQEAVGQCVANAAQPGPSPRPPKMFCGEDGQWVDQPTTTCTCLPGFEASHGELECRACPVGLFKMGSGTGPCSVCPENSQTGETGSAACVCRSGFYRALSDS...
2.7.10.1
null
angioblast cell migration involved in selective angioblast sprouting [GO:0035475]; angiogenesis [GO:0001525]; axon guidance [GO:0007411]; blood vessel development [GO:0001568]; convergent extension [GO:0060026]; ephrin receptor signaling pathway [GO:0048013]; lymph vessel development [GO:0001945]; phosphorylation [GO:0...
dendrite [GO:0030425]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005]
PF14575;PF01404;PF00041;PF07714;PF00536;
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54760}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54760}.
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:PRU001...
null
null
null
null
FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway dow...
Danio rerio (Zebrafish) (Brachydanio rerio)
O73878
EPB4B_DANRE
MDRVCWIMALSWFWMVSTGLVSAEEEVLMNTKLETSDLRWTIYPSGDPEWEEMSGLDEEGNSVRTFQVCPMDSSVSHWLRTRFIPRHGASQVYVEIRFTMMECSAMPASFRTCKETFNLYYYQSDEDTASATHPAWMENPYSKVDTVAADFLLRRGGERKSNVKTVRVGPLSKKGFYLAFQTQGACMALLSVRVFFKKCPAVSRAFSSFPETLPHSLVQQAEGVCVDNSAPTGQSTAPPTMFCGEDGQWVGPPSSTCACKPGYEPVDSDRCRACGLGQYKASVGGSLCRVCPDNSNTHFAGSSLCVCRPGYHRATSDLPD...
2.7.10.1
null
angiogenesis [GO:0001525]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; Kupffer's vesicle development [GO:0070121]; phosphorylation [GO:0016310]; somitogenesis [GO:0001756]
dendrite [GO:0030425]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005]
PF14575;PF01404;PF00041;PF07714;PF00536;
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54760}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54760}.
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:PRU001...
null
null
null
null
FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway dow...
Danio rerio (Zebrafish) (Brachydanio rerio)
O73885
HSP7C_CHICK
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDSVVQSDMKHWPFTVVNDAGRPKVQVEYKGETKSFYPEEISSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQGTKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNLLIFDLGGGTFDVSILTIENGIFEVKSTAGDTHLGGEDFDNRLVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEKLNADLFRGTLDPVEKA...
null
null
chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated autophagy translocation complex disassembly [GO:1904764]; clathrin coat disassembly [GO:0072318]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic organ development [GO:0048568]; gastrulation [GO:0007369]; late end...
autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; lysosomal membrane [GO:0005765]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic cytosol [GO:0099524]; presynaptic cytosol [GO:0099523]; ribonucleoprotein complex [GO:1990904]; termi...
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; clathrin-uncoating ATPase activity [GO:1990833]; heat shock protein binding [GO:0031072]; phosphoprotein binding [GO:0051219]; protein folding chaperone [GO:0044183]; protein-macromolecule adaptor activ...
PF00012;
1.20.1270.10;3.30.30.30;3.30.420.40;
Heat shock protein 70 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11142}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11142}. Cell membrane {ECO:0000250|UniProtKB:P11142}. Lysosome membrane {ECO:0000250|UniProtKB:P11142}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11142}; Cytoplasmic side {ECO:0000250|UniProtKB:P11142}. ...
null
null
null
null
null
FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complex...
Gallus gallus (Chicken)
O73888
HPGDS_CHICK
MPNYKLTYFNLRGRAEICRYLFAYAGIKYEDHRLEGADWPKIKPTIPFGKVPILEVDGVIIHQSLAIARYLARESGLAGQTPVEQALADAIVDTIDDFMMLFPWAEKNQDVKEKAFNDILTNKAPELLKDLDTFLGDKKWFVGKSVTWADFYWDVCSTTLLSYKADLADKYPRLLALRDRVEALPAIAAWIQKRPKTAI
2.5.1.18; 5.3.99.2
COFACTOR: Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000269|PubMed:9657971}; Note=Glutathione is required for the prostaglandin D synthase activity. {ECO:0000269|PubMed:9657971};
glutathione metabolic process [GO:0006749]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin metabolic process [GO:0006693]
cytoplasm [GO:0005737]
calcium ion binding [GO:0005509]; glutathione transferase activity [GO:0004364]; magnesium ion binding [GO:0000287]; prostaglandin-D synthase activity [GO:0004667]
PF14497;PF02798;
1.20.1050.10;3.40.30.10;
GST superfamily, Sigma family
null
SUBCELLULAR LOCATION: Cytoplasm.
CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000269|PubMed:9657971}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10601; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide a...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=128 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=97 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=410 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene a...
null
null
null
FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides, organic isothiocyanates and alpha,beta-unsaturated car...
Gallus gallus (Chicken)
O73916
SIX3_ORYLA
MVFRAPLDFISASRLLLPHFADAPPVLSRSRSPEHPPAGFLSLALPGLCFSATQIASVCETLEETGDIERLARFLWSLPVNTDGRDSISEHESVQRARAVVAFHTGCYRELYRILETHRFTRASHSKLQAMWLEAHYREAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRGLLREWYLQDPYPNPGKKRELAHATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHHRICPDSACTLSGGDSSERADGDTFLSVTDSDSDLDV
null
null
apoptotic process involved in development [GO:1902742]; cell proliferation in forebrain [GO:0021846]; epithelial cell maturation [GO:0002070]; eye development [GO:0001654]; forebrain dorsal/ventral pattern formation [GO:0021798]; lens development in camera-type eye [GO:0002088]; lens fiber cell apoptotic process [GO:19...
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription corepressor binding [GO:0001222]
PF00046;PF16878;
1.10.10.60;
SIX/Sine oculis homeobox family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62233, ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-po...
Oryzias latipes (Japanese rice fish) (Japanese killifish)
O73925
KCNQ1_SQUAC
MSSEVKSRWSGSGSQKSGTARKPTMLEMAENAASRHYEPVPLPLQRSNSPDSSTDKNPESRAADSRAEVIINPDIPPKAIALPLSRYRGRNPFFSKVNIQGRTYNFLERPTGWKCFIYHFTVFLIVLVCLIFSVMSTIEQYHYFANRALVWMEIVLVVFFGTEYIVRLWSAGCRSKYVGFWGRLRFARKPISIIDLIVVVASVIVLCVGSNGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVDDSGSQQFGSYADALWWGVVTVTTIGYGDKVPQTWIGRT...
null
null
inner ear development [GO:0048839]; intestinal absorption [GO:0050892]; membrane repolarization [GO:0086009]; regulation of gastric acid secretion [GO:0060453]; renal absorption [GO:0070293]
basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; 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]
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
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51787}. Membrane raft {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane {ECO:...
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-selectiv...
Squalus acanthias (Spiny dogfish)
O73932
IF23A_XENLA
MNKLYIGNLSENVSPTDLESLFKESKIPFTGQFLVKSGYAFVDCPDETWAMKAIDTLSGKVELHGKVIEVEHSVPKRQRSRKLQIRNIPPHLQWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYANKEHARQGLEKLNGYQLENYSLKVTYIPDEMATPQAPSQQLQQQPQQQHPQGRRGFGQRGPARQGSPGAAARPKPQTEVPLRMLVPTQFVGAIIGKEGATIRNITKQTQSKIDIHRKENAGAAEKPITIHSTPEGCSAACKIIMEIMQKEAQDTKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKI...
null
null
mRNA transport [GO:0051028]; nervous system development [GO:0007399]; regulation of translation [GO:0006417]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
DNA binding [GO:0003677]; mRNA 3'-UTR binding [GO:0003730]
PF00013;PF00076;
3.30.310.210;3.30.70.330;3.30.1370.10;
RRM IMP/VICKZ family
null
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum. Note=Accumulates along the vegetal cortex in oocytes as oogenesis progresses ('late pathway' for RNA localization). Colocalizes with Vg1 RNA along the vegetal cortex.
null
null
null
null
null
FUNCTION: RNA-binding protein that acts as a regulator of mRNA transport and localization. Binds to the RNA sequence motif 5'-UUCAC-3'. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Mediates the specific association of Vg1 RNA to microtubules. Binds spe...
Xenopus laevis (African clawed frog)
O73946
HELS_PYRFU
MRVDELRVDERIKSTLKERGIESFYPPQAEALKSGILEGKNALISIPTASGKTLIAEIAMVHRILTQGGKAVYIVPLKALAEEKFQEFQDWEKIGLRVAMATGDYDSKDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKILVADEIHLIGSRDRGATLEVILAHMLGKAQIIGLSATIGNPEELAEWLNAELIVSDWRPVKLRRGVFYQGFVTWEDGSIDRFSSWEELVYDAIRKKKGALIFVNMRRKAERVALELSKKVKSLLTKPEIRALNELADSLEENPTNEKLAKAIRGGVAFHHAGLGRDERVLVEENFRKGI...
5.6.2.4
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15677450}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15677450}; Note=Divalent cations, Mg(2+) and Zn(2+) are best. {ECO:0000269|PubMed:15677450};
DNA repair [GO:0006281]
null
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; isomerase activity [GO:0016853]
PF00270;PF00271;PF21280;PF14520;
1.10.3380.30;1.10.150.20;3.40.50.300;
Helicase family, Hel308 subfamily
null
null
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:16436047}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, Ch...
null
null
null
null
FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Unwinds the lagging strand from forked DNA structures in a 3'-5' direction. PCNA, the DNA polymerase sliding clamp subunit, stimulates the helicase activity, and may alter substrate specificity. Unwinds br...
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
O74113
CDC45_SCHPO
MFIKRSDYASAYLKIKEASVSGGCTVQLFVALDPDALCACKLLSTLLKGDFISHKIRPVSGYRDLEQANKTLLEQNEDIKFIILLNCGTMVDLNNYLVSMEDVSIYVIDSHRPHNLNNIYIENNIFVFDDGDIEEDMNKIHDAWYAFNSHELSDEENSDSSNEREEEVEDDNRSVESYSSSDYQARSRRRFSEETTQRRAEIKEKRKKRKEFASILSEYYEKGSWYGESITNILFAVASMLGREDNDMLWLAIVGLTCLEIHCQSSKKYFNRSYSLLKDEVNRLNPSPLENQIVGRAHGKTPHDQSIRLEDEFRFMLVRH...
null
null
DNA replication initiation [GO:0006270]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA replication initiation [GO:1902975]; mitotic DNA replication preinitiation complex assembly [GO:1902977]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]
chromatin [GO:0000785]; cytosol [GO:0005829]; DNA replication preinitiation complex [GO:0031261]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; single-stranded DNA binding [GO:0003697]
PF02724;
null
CDC45 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9619628}.
null
null
null
null
null
FUNCTION: Required for initiation of chromosomal DNA replication. May have a role in regulating the MCM proteins nda1 and nda4. {ECO:0000269|PubMed:9619628}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74135
CKI3_SCHPO
MSTTSSHSNVVGVHYRVGKKIGEGSFGMLFQGVNLINNQPIALKFESRKSEVPQLRDEYLTYKLLMGLPGIPSVYYYGQEGMYNLLVMDLLGPSLEDLFDYCGRRFSPKTVAMIAKQMITRIQSVHERHFIYRDIKPDNFLIGFPGSKTENVIYAVDFGMAKQYRDPKTHVHRPYNEHKSLSGTARYMSINTHLGREQSRRDDLESMGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQVTPLKELCEGYPKEFLQYMIYARNLGYEEAPDYDYLRSLFDSLLLRINETDDGKYDWTLLNNGKGWQYSAAKQHVVQRR...
2.7.11.1
null
endocytosis [GO:0006897]; negative regulation of establishment of bipolar cell polarity [GO:1904846]; negative regulation of protein localization to cell tip [GO:1903067]; phosphorylation [GO:0016310]; regulation of endocytosis [GO:0030100]; signal transduction [GO:0007165]
cell division site [GO:0032153]; cell periphery [GO:0071944]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily
null
SUBCELLULAR LOCATION: Cytoplasm.
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-[pr...
null
null
null
null
FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74184
WAT1_SCHPO
MSVQYPPQHSVLLVSSGYDHTIRFWEALSGICSRTIQHADSQVNRLCISPDKKFLAAAGNPHVRLYDINTSSQMPLMTFEGHTNNVTAIAFHCDGKWLATSSEDGTVKVWDMRAPSVQRNYDHKSPVNDLLIHPNQGELLSCDQSGRVRAWDLGENSCTHELIPEEDVPMSSITVGSDGSMLIAGNNKGNCYVWRMLNHQGASLLQPVVKFQAHQRYITRCVLSPDVKHLATCSADATVNIWSTEDMSFMLERRLQGHQRWVWDCAFSADSTYLVTASSDHVARLWELSSGETIRQYSGHHKAAVCVALNDYQI
null
null
meiotic cell cycle [GO:0051321]; regulation of actin cytoskeleton organization [GO:0032956]; sporulation resulting in formation of a cellular spore [GO:0030435]; TOR signaling [GO:0031929]; TORC1 signaling [GO:0038202]; TORC2 signaling [GO:0038203]
cytosol [GO:0005829]; fungal-type vacuole membrane [GO:0000329]; nucleus [GO:0005634]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932]
null
PF00400;
2.130.10.10;
WD repeat LST8 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: component of both TORC1 and TORC2, which regulate multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls cell growth and ribosome biogenesis by regulating riboso...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74189
PMT1_CANAL
MAKKPVTPASKVAAKQAAVRSRHQEDVFTLDPLIDPIFQKGELRSYLVTEPSPSVLKKRSIHTKEYWMLSSLLLIAFYVRMYNLSNPNSVVFDEVHFGGFARKYILGTFFMDVHPPLAKMLFGAVGAIGGFKGDFEFKSIGDKFPDSTPYIFMRQFPALLGVGTVILCYLTLRQSGVRPIIAYITTFLLIIENSNVTISRYILLDSPLIFFIAAAIYAWKKFEIQIPFTFGWYRSLLATGIALGLALSSKWVGLFTVAWVGFLCIYQLWFLIGDLSVSTKKIWGHFFARGIILLGVPIALYLGFFAIHFQLLNKEGDGGA...
2.4.1.109
null
biological process involved in interaction with host [GO:0051701]; cell-substrate adhesion [GO:0031589]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; fungal-type cell wall organization [...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
dolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]; mannosyltransferase activity [GO:0000030]
PF02815;PF02366;PF16192;
2.80.10.50;
Glycosyltransferase 39 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33775}.
CATALYTIC ACTIVITY: Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:576...
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
null
null
FUNCTION: Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of tar...
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
O74198
ERG6_CANAL
MSPVQLAEKNYERDEQFTKALHGESYKKTGLSALIAKSKDAASVAAEGYFKHWDGGISKDDEEKRLNDYSQLTHHYYNLVTDFYEYGWGSSFHFSRYYKGEAFRQATARHEHFLAHKMNLNENMKVLDVGCGVGGPGREITRFTDCEIVGLNNNDYQIERANHYAKKYHLDHKLSYVKGDFMQMDFEPESFDAVYAIEATVHAPVLEGVYSEIYKVLKPGGVFGVYEWVMTDKYDETNEEHRKIAYGIEVGDGIPKMYSRKVAEQALKNVGFEIEYQKDLADVDDEIPWYYPLSGDLKFCQTFGDYLTVFRTSRIGRFIT...
2.1.1.41
null
ergosterol biosynthetic process [GO:0006696]; methylation [GO:0032259]; zymosterol biosynthetic process [GO:0036197]
endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
sterol 24-C-methyltransferase activity [GO:0003838]
PF08241;PF08498;
3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, Erg6/SMT family
null
null
CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + zymosterol = fecosterol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21128, ChEBI:CHEBI:15378, ChEBI:CHEBI:17038, ChEBI:CHEBI:18252, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.41; Evidence={ECO:0000269|PubMed:20946868}; PhysiologicalDirection=left-to-righ...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55 uM for zymosterol {ECO:0000269|PubMed:20946868};
PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from zymosterol: step 1/5. {ECO:0000269|PubMed:20946868}.
null
null
FUNCTION: Sterol 24-C-methyltransferase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:20946868, PubMed:9593144). ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol (PubMed:20946868, PubMed:9593144)...
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
O74201
UBC2_CANAL
MSTPARRRLMRDFKRMQQDPPSGVSASPLPDNVMKWNAVIIGPSDTPFEDGTFRLLLSFDEQYPNKPPQVKFISEMFHPNVYASGELCLDILQNRWSPTYDVSSILTSVQSLLNDPNISSPANVEAANLYKDHRSLYVKRVRETVENSWNDDDDEEEEEEDEDEAEDEDDDDDDNIDED
2.3.2.23
null
cellular response to UV [GO:0034644]; cytoplasm protein quality control by the ubiquitin-proteasome system [GO:0071629]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA-templated transcription termination [GO:0006353]; double-strand break repair via homologous recombination [GO:0000724]; ERAD pathway [GO...
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; fungal biofilm matrix [GO:0062040]; HULC complex [GO:0033503]; MUB1-RAD6-UBR2 ubiquitin ligase complex [GO:1990304]; nucleus [GO:0005634]; Rad6-Rad18 complex [GO:0097505]; RAD6-UBR2 ubiquitin ligase complex [GO:1990305]; UBR1-RAD6 ubiquitin ligase compl...
ATP binding [GO:0005524]; proteasome binding [GO:0070628]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842]
PF00179;
3.10.110.10;
Ubiquitin-conjugating enzyme family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVX9}. Nucleus {ECO:0000250|UniProtKB:Q5VVX9}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROS...
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}.
null
null
FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formati...
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
O74205
TOXE_COCCA
MGTTSPNSEKRQITDINERRKLQNRVAQRKYRTRQKTRMKLAEAVLNDYTYIHPTLGTIQSKKKSPLTMECDRSSASYPDLSSYAEICSETRSETQATRARQLTSQRTCFRESVDNNQADSHAQLSRCLNRQEMFYGISGETEFSEGDTRDRVECIDPNLTRGWLDMDLRSGTPNSSTVVDCGLCTVGANSQPPTRTNVQEAIETLELFEPNDQRKTENLPREPCGSCPSSSHGYSPTSGNPSTLLLTPSESLMNSVIVTSDSPLLAADDKSPGDLVISEANTHGPKEDQFSPLMTAISLGRLDIARILLQSGAPLDIPD...
null
null
negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of JNK cascade [GO:0046330]; protein targeting to chloroplast [GO:0045036]; regulation of DNA-templated transcription [GO:0006355]; toxin biosynthetic process [GO:000...
cytoplasm [GO:0005737]; nucleus [GO:0005634]
chloroplast targeting sequence binding [GO:0030941]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]
PF00023;PF12796;
1.20.5.170;1.25.40.20;
BZIP family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11698648}.
null
null
null
null
null
FUNCTION: Transcription factor, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid (PubMed:11698648, PubMed:9894916). HC-toxin is a determinant of specificity an...
Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola)
O74208
PDH1_CANGA
MNTPDDSSVSSVDSHQPYMGFDDNVEKRIRELARSLTQQSLTSSNRSVNKEAPADGSAPLDRVSTRASSIFSADFKGVNPVFSDEEEDDYDARLDPNSDEFSSKAWVQNMAKITTGDPEFYKPYSIGCCWKDLSASGESADVSYQSTFLNLPVKLLNAVWRKARPARESDTFRILKPMDGLLKPGELLVVLGRPGSGCTTLLKSISSTTHGFQISKDSVISYNGLTPNEIKKHYRGEVVYNAEADIHLPHLTVYQTLVTVARLKTPQNRVKGVTREDFANHVTDVAMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAE...
null
null
response to xenobiotic stimulus [GO:0009410]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961]
plasma membrane [GO:0005886]
ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]
PF01061;PF19055;PF00005;PF14510;PF06422;
3.40.50.300;
ABC transporter superfamily, ABCG family, PDR (TC 3.A.1.205) subfamily
PTM: Phosphorylated by PKA. Dephosphorylated on glucose depletion and independently rephosphorylated during glucose exposure or under stress. {ECO:0000269|PubMed:12244114}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12244114}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Pleiotropic ABC efflux transporter that confers resistance to structurally and functionally unrelated compounds including caspofungin or azoles such as fluconazole, itraconazole, posaconazole, voriconazole, and isavuconazole (PubMed:11257032, PubMed:12244114, PubMed:12557277, PubMed:15105134, PubMed:15388433,...
Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
O74213
PGLR1_ASPAC
MHLNTTLLVSLALGAASVLASPAPPAITAPPTAEEIAKRATTCTFSGSNGASSASKSKTSCSTIVLSNVAVPSGTTLDLTKLNDGTHVIFSGETTFGYKEWSGPLISVSGSDLTITGASGHSINGDGSRWWDGEGGNGGKTKPKFFAAHSLTNSVISGLKIVNSPVQVFSVAGSDYLTLKDITIDNSDGDDNGGHNTDAFDIGTSTYVTISGATVYNQDDCVAVNSGENIYFSGGYCSGGHGLSIGSVGGRSDNTVKNVTFVDSTIINSDNGVRIKTNIDTTGSVSDVTYKDITLTSIAKYGIVVQQNYGDTSSTPTTGV...
3.2.1.15
null
cell wall organization [GO:0071555]; pectin catabolic process [GO:0045490]
extracellular region [GO:0005576]
polygalacturonase activity [GO:0004650]
PF00295;
2.160.20.10;
Glycosyl hydrolase 28 family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
null
null
null
null
FUNCTION: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Aspergillus aculeatus
O74237
XYL1_CANTE
MSASIPDIKLSSGHLMPSIGFGCWKLANATAGEQVYQAIKAGYRLFDGAEDYGNEKEVGDGVKRAIDEGLVKREEIFLTSKLWNNYHDPKNVETALNKTLADLKVDYVDLFLIHFPIAFKFVPIEEKYPPGFYCGDGNNFVYEDVPILETWKALEKLVAAGKIKSIGVSNFPGALLLDLLRGATIKPAVLQVEHHPYLQQPKLIEFAQKAGVTITAYSSFGPQSFVEMNQGRALNTPTLFAHDTIKAIAAKYNKTPAEVLLRWAAQRGIAVIPKSNLPERLVQNRSFNTFDLTKEDFEEIAKLDIGLRFNDPWDWDNIPI...
1.1.1.307
null
D-xylose catabolic process [GO:0042843]
cytosol [GO:0005829]
D-xylose:NADP reductase activity [GO:0032866]
PF00248;
3.20.20.100;
Aldo/keto reductase family
null
null
CATALYTIC ACTIVITY: Reaction=NAD(+) + xylitol = D-xylose + H(+) + NADH; Xref=Rhea:RHEA:27441, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151, ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.307; CATALYTIC ACTIVITY: Reaction=NADP(+) + xylitol = D-xylose + H(+) + NADPH; Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, Ch...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=142 mM for xylose {ECO:0000269|PubMed:15320875, ECO:0000269|PubMed:16336198}; KM=38 uM for NADH {ECO:0000269|PubMed:15320875, ECO:0000269|PubMed:16336198}; KM=3 uM for NADPH {ECO:0000269|PubMed:15320875, ECO:0000269|PubMed:16336198};
PATHWAY: Carbohydrate metabolism; D-xylose degradation.
null
null
FUNCTION: Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.
Candida tenuis (Yeast) (Yamadazyma tenuis)
O74288
ABFB_EMENI
MTMSRSSRSSVLALALATGSLVAAGPCDIYSSGGTPCIAAHSTTRALYSSYNGPLYQVQRASDGTTTTITPLSAGGVADASAQDAFCENTTCLITIIYDQSGNGNDLTQAPPGGFNGPDVGGYDNLAGAIGAPVTLNGKKAYGVFVSPGTGYRNNEAIGTATGDEPEGMYAVLDGTHYNDGCCFDYGNAETSSLDTGNGHMEAIYYGTNTAWGYGAGNGPWIMADLENGLFSGQSSDYNAGDPSISYRFVTAILKGGPNLWALRGGNAASGSLSTYYNGIRPTDASGYNPMSKEGAIILGIGGDNSVSAQGTFYEGAMTD...
3.2.1.55
null
arabinan catabolic process [GO:0031222]; arabinose metabolic process [GO:0019566]; L-arabinose metabolic process [GO:0046373]; pectin catabolic process [GO:0045490]; xylan catabolic process [GO:0045493]
extracellular region [GO:0005576]
alpha-L-arabinofuranosidase activity [GO:0046556]
PF05270;PF09206;
2.60.120.200;2.80.10.50;
Glycosyl hydrolase 54 family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10217508}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.2.1.55;
null
PATHWAY: Glycan metabolism; L-arabinan degradation.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.8. {ECO:0000269|PubMed:16844780};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:16844780};
FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains...
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
O74304
WIN1_SCHPO
MENILDPSVVNSHILENGSRRSSINPILDSELRDKTFEKAHRRSLTLLSSFTSSMLELPNNGKEENHRRPSVARSSSDRSKASAKEDLFSEAFRMAEQPPAEALTISTPVDPINIDELDRAYAVSPSDTSNLLHPPTSSSSIPIPIKNAGHSNLDHPIRPSLQSSISSNRIIKSPGIKEDDYMHRGRSISSPMIDVEHINSTAVPSKTKNLPEKPKRSHKLRNSITFAKIEDHPERKSQLRRLSSSLKCFDPEYDYNDPSLSIRRDSSTYYFSNVNETYDEEDSDLDSETSTVNWVQSVLNLPSLLSDDLMANPKNKERF...
2.7.11.25
null
p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; stress-activated MAPK cascade [GO:0051403]
cytoplasm [GO:0005737]; Mcs4 RR-MAPKKK complex [GO:1990315]
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]
PF00069;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
null
null
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=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Activates the wis1 MAP kinase kinase by phosphorylation. {ECO:0000269|PubMed:9693384}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74309
SLM9_SCHPO
MHIFVPKLLENHQFSSISSSKDFVAVSAETNVYILSKDFFYPKSSEKRIIQSLNGHKTTHLSFDSPISCIRFTYDGSCLAVATEAGTFLYHSEKWDKAFQVLSGPAYEVCWSQQGHILATSWKQISIYVKDEGLRTETIVKKTEHADSNHQPAVSIEESKEAVESTSQSSEISFKLIKVIEGHHTFVGGLAFDPMGQFLASQSFDHTLKVWKLSTFGVEKSIAKPFEQMPTGNRFLRLSWSPDGAHIASVNAVNEGAYVIAIVQRDTWTYDINLVGHQGPLECATFNPYLYEDPFQKSIIASAAHDGCVSIWNTACARPM...
null
null
chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; regulation of DNA-templated transcription [GO:0006355]; transcription elongation-coupled chromatin remodeling [GO:0140673]; transcription initiation-coupled chromatin remodeling [GO:0045815]
chromatin [GO:0000785]; cytosol [GO:0005829]; HIR complex [GO:0000417]; nucleus [GO:0005634]
ATP-dependent H3-H4 histone complex chaperone activity [GO:0140665]; nucleosome binding [GO:0031491]
PF07569;PF00400;
2.130.10.10;
WD repeat HIR1 family
null
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
null
null
null
null
null
FUNCTION: Probably required for replication-independent chromatin assembly (By similarity). Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. May play an indirect role in the regulation of cdc2 and/or wee1 at the G2/M stage of mitosis...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74312
ATG9_SCHPO
MFYQPAQNKKQYDDLADIEAQNNVPNTQEVLEAWQESLDSDEDESSPLEESNGFTISEHDDFVKSVPRKNNPTDLLYSGKLLDSDEPPSVHGNSSKVPSKHPSPSFPETTSLRNLQNGSKQKPALPNFNDPHFYNEDVTRSGHPNRSIYTQLPRNEFSNARVLWNRLSARDRVLWRWANVENLDSFLQQVYTYYTGKGLSCIIVHRLFQILTVSFVIGFTTFITSCIDWPAVTPHGSLAGVTKSQCIAQMSPITYLVLWLFLSFLLALWIYYLTDIPRLWQMREFYIHALKIATADMPTVSWQRVLYRLLKLKNVNALTA...
null
null
autophagosome assembly [GO:0000045]; macroautophagy [GO:0016236]; piecemeal microautophagy of the nucleus [GO:0034727]; protein localization to phagophore assembly site [GO:0034497]; reticulophagy [GO:0061709]
autophagosome [GO:0005776]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; fungal-type vacuole membrane [GO:0000329]; Golgi membrane [GO:0000139]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]
phospholipid scramblase activity [GO:0017128]
PF04109;
null
ATG9 family
PTM: Phosphorylated by atg1. Atg1 phosphorylation is required for preautophagosome elongation. {ECO:0000250|UniProtKB:Q12142}.
SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:23950735}; Multi-pass membrane protein {ECO:0000269|PubMed:23950735}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q1...
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-s...
null
null
null
null
FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation (PubMed:23950735). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (By similarity). Lipid ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74327
AVT5_SCHPO
MSGYSPLSSGPADVHIGKAGFFSSVINLANTILGAGILSLPNAFTKTGLLFGCLTIVFSAFASFLGLYFVSQCAARLPRGKASFAAVAKHTFPSLAVVFDASIAVKCFGVAVSYLVIVGDLMPQIAPSLGLSSPMFLRRQTWIVFALFVLTPLSFLKRLDSLRHTSVISLIALCYLVFIVLYHFIIGDTVKGEIRYFVPESGFGYLSVLPVFVFGFTCHQNAFSVINEVRNFSQGFVNFTMFTAIISSTLLYLLVAITGYLSFGSLASGNIIAMYDNTSIWIIGGKLAIVVLVLFSYPLQCHPCRNSVYQAIRRSYSAHD...
null
null
amino acid transmembrane import into vacuole [GO:0032975]; amino acid transmembrane transport [GO:0003333]; L-arginine transmembrane import into vacuole [GO:0090518]; L-glutamate import involved in cellular response to nitrogen starvation [GO:1901481]; L-glutamate transmembrane import into vacuole [GO:0090515]; L-histi...
fungal-type vacuole membrane [GO:0000329]
L-arginine transmembrane transporter activity [GO:0061459]; L-glutamate transmembrane transporter activity [GO:0005313]; L-histidine transmembrane transporter activity [GO:0005290]; L-lysine transmembrane transporter activity [GO:0015189]; L-serine transmembrane transporter activity [GO:0015194]; L-tyrosine transmembra...
PF01490;
null
Amino acid/polyamine transporter 2 family
null
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:20388511}; Multi-pass membrane protein {ECO:0000269|PubMed:20388511}.
null
null
null
null
null
FUNCTION: Vacuolar amino acid transporter involved in the vacuolar uptake of histidine, glutamate, tyrosine, arginine, lysine, and serine. Required for sporulation. {ECO:0000269|PubMed:19778961, ECO:0000269|PubMed:20388511}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74352
HOB1_SCHPO
MSWKGFTKALARTPQTLRSKFNVGEITKDPIYEDAGRRFKSLETEAKKLAEDAKKYTDAINGLLNHQIGFADACIEIYKPISGRASDPESYEQEGNAEGIEAAEAYKEIVYDLQKNLASEMDVINTRIVNPTGELLKIVKDVDKLLLKRDHKQLDYDRHRSSFKKLQEKKDKSLKDEKKLYEAETAFEQSSQEYEYYNEMLKEELPKLFALAQSFIAPLFQGFYYMQLNVYYVLYEKMSHCEIQYFDFNTDILESYERRRGDVKDRAEALTITKFKTAKPTYKRPGMGPGGKDATASSSSSFSSKREEAAAEPSSSTATD...
null
null
actin cortical patch localization [GO:0051666]; DNA damage response [GO:0006974]; endocytosis [GO:0006897]; establishment or maintenance of cell polarity [GO:0007163]; plasma membrane tubulation [GO:0097320]
actin cortical patch [GO:0030479]; mating projection tip [GO:0043332]; medial cortex [GO:0031097]; mitotic actomyosin contractile ring [GO:0110085]; Rvs161p-Rvs167p complex [GO:1990528]
lipid binding [GO:0008289]; protein-membrane adaptor activity [GO:0043495]
PF03114;PF00018;
1.20.1270.60;2.30.30.40;
null
null
null
null
null
null
null
null
FUNCTION: Has a role in DNA damage signaling as a part of stress response processes. {ECO:0000269|PubMed:12569356}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74354
DNT1_SCHPO
MRTTLRLHIIKDGEQDNQFMILFDPSSSISLLKEKVQETYKSLYPFESNINIRNIKNEESYDIPNEYLVGEIFPTNSKVIVESFSSPLKKLDGTMINFKEKNIQHDLDGVENDFATVQSASNGVHAINGKRTHPDESENPRKLPKKNFVEAIDANSPGFVYRPTSIRDRAYSISSNHDNESTLTEGIALKEIESPDKDRKADGIVNLSVTQEEDDNHQSFNSSLTPSQPTTYNRANFFSINDASSDSSSDAPLRTLSSPSRLRMKDNDRKYLVEHSPAALIKESETIDGIDDKSLRSSTREVSVESPNEDSVNDDSSSDV...
null
null
deactivation of mitotic spindle assembly checkpoint [GO:1902426]; division septum assembly [GO:0000917]; negative regulation of protein localization to mitotic spindle pole body [GO:1902543]; negative regulation of septation initiation signaling [GO:0031030]; positive regulation of G2/M transition of mitotic cell cycle...
cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]
phosphatase activator activity [GO:0019211]; rDNA binding [GO:0000182]
PF10407;
null
null
PTM: Phosphorylated by clp1. {ECO:0000269|PubMed:17538026, ECO:0000269|PubMed:18257517}.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Note=In late anaphase, localizes to the ends of the mitotic spindle.
null
null
null
null
null
FUNCTION: Negatively regulates the septation initiation network (SIN) pathway, independently of the cdc14 phosphatase clp1. May also have a role in silencing rDNA transcription. Required for maintaining the exclusive nucleolus localization of nuc1. {ECO:0000269|PubMed:17538026}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74360
RGA4_SCHPO
MNSGTTLHLDRLSLETPSERTCFCIKCWESVPSTSQVWFGGKCWHSDCFKCVNCNKKLDPSSEDFSQDDQKQIFCKLCVDICNGCSTPICEFNAVSNSQANHPCCSNCRAFINSNAFGKFKGQHYCLPCLRKQDEENQKAVMESASGFIPLRNIAQTAENTSLTGQNQGFQNPHFIASDSPSSVLSGRMQNTSSPTNSLRPQLKVQTNGYETPGDINSAKSYKDIQKDFLLKPKNSFVKTSPSPLANGPSFRSANASPFDSCDSFHSGSSIPIEPVSSRQSSVVNNNSVQQPVAYHAFVQSPTENGTLPQLPKNESVVNP...
null
null
establishment or maintenance of bipolar cell polarity [GO:0061245]; negative regulation of cell wall integrity MAPK cascade [GO:1903138]; positive regulation of establishment of bipolar cell polarity [GO:0061173]; positive regulation of establishment of cell polarity regulating cell shape [GO:2000784]; regulation of ac...
cell periphery [GO:0071944]; cytoplasm [GO:0005737]; lateral cell cortex [GO:0097575]; lateral plasma membrane [GO:0016328]; medial cortex [GO:0031097]
GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267]
PF00412;PF00620;
2.10.110.10;1.10.555.10;
null
null
null
null
null
null
null
null
FUNCTION: GTPase-activating protein for Rho-type proteins. {ECO:0000305}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74365
SOL1_SCHPO
MNNQGFVPASDYPTAVSYPTQGQSYNTQEEQPAYPQRFSTSQGMYAAEYGNANMMNTSENEPNNLAHSQPFRQSPSTQRNLPNQSFDFASNGAWNGSGSVKYSSPMMPSSRIPFQQEKEAAMQQQQQQQQQQQLYQRQMQSREALLSQQIPPNQIGINAHPAVRQTPQPAPSPNTPSGNANQLTPAYAASFDKFMVSLISFMEKRGTPIKSYPQINNTPINLMMLYALVMRAGGSRQVSAHNFWPKISASLGFPSPDAISLLIQYYNSYLLPYEEAWLAAQQQQKSLQQAKANHSANVQSRPKNYPQKPVQTTPEAVHAN...
null
null
chromatin remodeling [GO:0006338]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815]
chromatin [GO:0000785]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]
transcription cis-regulatory region binding [GO:0000976]
PF01388;
1.10.150.60;
SWI1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome po...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74369
CSS1_SCHPO
MSVEKAPELRVLSFNCWGLRFVSKYRTERLKAVGEKLAKCDYDIVLLQEVWSIYDFQEIRNLVSCNLVYSRFFHSAAMGAGLAMFSKFPIIESSMNKYPLNGRPQAFWRGDWYVGKGVATASLQHPSGRIISLFNTHLHAPYGKGADTYLCHRLSQAWYISKLLRAAVQRGHIVIAAGDFNIQPLSVPHEIITSYGLVNDAWLSVYPDQVEHPPNRFSMNDKELVEIAGTTCDSRLNTWRENISSKDMDDFVAKRLDYVFHSPSTCEAKNAKVVFLERVPKLDCSYSDHFAIETVLSIKLQPIPVQETRVSYSIIDDTLG...
3.1.4.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
cell wall organization [GO:0071555]; ceramide biosynthetic process [GO:0046513]; sphingoid catabolic process [GO:0046521]; sphingolipid catabolic process [GO:0030149]
cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; fungal-type vacuole [GO:0000324]; membrane [GO:0016020]; plasma membrane [GO:0005886]
inositol phosphosphingolipid phospholipase activity [GO:0052712]; mannosyl-inositol phosphorylceramide phospholipase activity [GO:0052714]; metal ion binding [GO:0046872]; sphingomyelin phosphodiesterase activity [GO:0004767]
PF03372;
3.60.10.10;
Neutral sphingomyelinase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11514435}; Multi-pass membrane protein {ECO:0000269|PubMed:11514435}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11514435}; Multi-pass membrane protein {ECO:0000269|PubMed:11514435}.
null
null
PATHWAY: Lipid metabolism; sphingolipid metabolism.
null
null
FUNCTION: Inositol phosphosphingolipids phospholipase essential for the coordination of cell wall formation. Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C). {ECO:0000269|...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74372
DUO1_SCHPO
MTSELQQELQILRSFNYTIEKLTDGLSASKEKIKSFETSINNSNRLIQLWSSVLSQTEHTQNLILNSDWKGLSFDNEELERLQHQKMLQIQAEEQRKIELQQEQERLEQERRQKEEAIALQKQQQQRLLRSKDPKVRPARRAASSYVPSRPSHVPRSSSMNVRSRVSMATTSNPNSLRTPSSSFASHRQSAIPKSATSSAPTIPTSNLPSVASSIPNNGLNSSNRKSIISKTSSRLRPPSRVSNVPSVPQHPSTRSRTSTRETTQPPFTTNPSNRSKRTTLR
null
null
attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; mitotic sister chromatid biorientation [GO:1990758]; protein transport along microtubule to mitotic spindle pole body [GO:1990976]; spindle attachment to meiosis I kinetochore [GO:0051455]
cytoplasm [GO:0005737]; DASH complex [GO:0042729]; microtubule [GO:0005874]; mitotic spindle [GO:0072686]
null
PF08651;
null
DASH complex DUO1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53168}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53168}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P53168}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20624975}. Note=Associates with the mitotic spindle and the kinetochore (By simil...
null
null
null
null
null
FUNCTION: Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74374
PGM_SCHPO
MIETIPTKPYEGQRPGTSGLRKKVTVFEQPNYVENFVQATMDVVEPSAKGAHLVVGGDGRYFNFHAIQVIAAIAAGNGVEKIIVGTNGYLSTPAASHIIRKYKLTGGIILTASHNAGGPKNDFGIKYNLGNGGPAPESVTEKIYSITKTISEYKMVKIPPLDLTTTGVRRYGPLTVEVIDPVKDYVQLMKEIFDFDLIRSFLSKNPDFTFVFDALHGITGPYGEALFCKELGMPSSVCQNCKPLPDFGGGHPDPNLTYAKSLVARVDRDNIVMGAASDGDGDRNMIYGANAFVTPSDSVAIIAHHAELIPYFRDGGVHGF...
5.4.2.2
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00949}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949};
carbohydrate metabolic process [GO:0005975]; galactose catabolic process [GO:0019388]; glucose 1-phosphate metabolic process [GO:0019255]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; trehalose biosynthetic process [GO:0005992]; ...
cytosol [GO:0005829]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; phosphoglucomutase activity [GO:0004614]
PF02878;PF02879;PF02880;
3.40.120.10;3.30.310.50;
Phosphohexose mutase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:P37012}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + O-phospho-L-seryl-[protein] = alpha-D-glucose 1,6-bisphospha...
null
null
null
null
FUNCTION: Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (By similarity). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (By similarity). Key enzyme in hexose metabolism (By similarity). The reverse reaction is an essential ste...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74384
ERFB_SCHPO
MSYEKHSDAKASRYAWNQPWNPFEVTLSDPTYPMNLEEKNQIPYRFQSVPDDVPEVPHIESRYKNLPGNNIYLCCGRLQMSSQYKAFLISLFALILPGVLFFIFSAFWLWHHVSPAVPITFAYLYALAVVSMFKCSTADPGILPRNAYSLTYNPAHPWSVIPEDRKVLVGSTRSDSVFVNTVYCHTCHLYRPPRASHCHLCDNCVEYLDHHCIWLNTCIGRRNYRYYFIFLLSVVLSALYLTGLGFYTSIGSFHESTDTNFAAHLRRPWAGVSFFLGIYGALGAILPGILFCYQCYLISVGQNVHEYLRAKSTETEDVHP...
2.3.1.225
null
protein targeting to membrane [GO:0006612]; sporulation resulting in formation of a cellular spore [GO:0030435]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum palmitoyltransferase complex [GO:0031211]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]
protein-cysteine S-palmitoyltransferase activity [GO:0019706]
PF01529;
null
DHHC palmitoyltransferase family, ERF2/ZDHHC9 subfamily
PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q06551}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q06551}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000305|PubMed:23843742};
null
null
null
null
FUNCTION: The erf2-erf4 complex is a palmitoyltransferase with a major role in driving sexual development (PubMed:16303567, PubMed:23843742). Palmitoylates ras1 (PubMed:23843742). Palmitoylates isp3 (PubMed:23843742). Palmitoylates rho3 (PubMed:23843742). {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:23843742}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74420
WTF13_SCHPO
MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIAIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAISLAQCVKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEME...
null
null
meiotic drive [GO:0110134]
ascus epiplasm [GO:0072324]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; vacuolar membrane [GO:0005774]
null
PF03303;
null
WTF family
null
SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000255, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the i...
null
null
null
null
null
FUNCTION: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-s...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)