GenomeNet

Database: UniProt
Entry: F7A9J8_MACMU
LinkDB: F7A9J8_MACMU
Original site: F7A9J8_MACMU 
ID   F7A9J8_MACMU            Unreviewed;       509 AA.
AC   F7A9J8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   31-JUL-2019, entry version 63.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   Name=ACVR1 {ECO:0000313|EMBL:AFE63706.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000024342, ECO:0000313|VGNC:VGNC:69438};
GN   ORFNames=EGK_04456 {ECO:0000313|EMBL:EHH21400.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000024342, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000024342, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000024342,
RC   ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C.,
RA   Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W.,
RA   Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E.,
RA   Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y.,
RA   Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T.,
RA   Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J.,
RA   Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A.,
RA   Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M.,
RA   Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D.,
RA   Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J.,
RA   Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E.,
RA   Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S.,
RA   Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X.,
RA   Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E.,
RA   Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M.,
RA   Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M.,
RA   Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y.,
RA   Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J.,
RA   Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A.,
RA   Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B.,
RA   Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S.,
RA   Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V.,
RA   Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A.,
RA   Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C.,
RA   Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P.,
RA   Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E.,
RA   Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque
RT   genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:EHH21400.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-5 {ECO:0000313|EMBL:EHH21400.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N.,
RA   Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P.,
RA   Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T.,
RA   Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D.,
RA   Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X.,
RA   Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J.,
RA   Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal
RT   models, the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
RN   [3] {ECO:0000313|Ensembl:ENSMMUP00000024342}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000024342};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:AFE63706.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE63706.1}, Testis
RC   {ECO:0000313|EMBL:AFI33568.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH29502.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X.,
RA   Pandey S., Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P.,
RA   Tharp G.K., Marcais G., Roberts M., Ferguson B., Fox H.S.,
RA   Treangen T., Salzberg S.L., Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
CC         phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
CC         COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|SAAS:SAAS01128400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-threonine + ATP = [receptor-
CC         protein]-O-phospho-L-threonine + ADP + H(+);
CC         Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-
CC         COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30; Evidence={ECO:0000256|RuleBase:RU361271,
CC         ECO:0000256|SAAS:SAAS01128404};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU361271};
CC       Single-pass type I membrane protein
CC       {ECO:0000256|RuleBase:RU361271}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00595019}.
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DR   EMBL; JSUE03008937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JSUE03008938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JU319950; AFE63706.1; -; mRNA.
DR   EMBL; JU472698; AFH29502.1; -; mRNA.
DR   EMBL; JV043497; AFI33568.1; -; mRNA.
DR   EMBL; CM001264; EHH21400.1; -; Genomic_DNA.
DR   RefSeq; NP_001247690.1; NM_001260761.1.
DR   RefSeq; XP_014965630.1; XM_015110144.1.
DR   RefSeq; XP_014965631.1; XM_015110145.1.
DR   RefSeq; XP_014965632.1; XM_015110146.1.
DR   STRING; 9544.ENSMMUP00000024342; -.
DR   Ensembl; ENSMMUT00000026013; ENSMMUP00000024342; ENSMMUG00000018497.
DR   GeneID; 697935; -.
DR   KEGG; mcc:697935; -.
DR   CTD; 90; -.
DR   VGNC; VGNC:69438; ACVR1.
DR   eggNOG; KOG2052; Eukaryota.
DR   eggNOG; ENOG410XQT0; LUCA.
DR   GeneTree; ENSGT00940000160160; -.
DR   KO; K04675; -.
DR   OMA; LCNMNIT; -.
DR   OrthoDB; 776697at2759; -.
DR   TreeFam; TF314724; -.
DR   Proteomes; UP000006718; Chromosome 12.
DR   Bgee; ENSMMUG00000018497; Expressed in 14 organ(s), highest expression level in lung.
DR   GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR   GO; GO:0016361; F:activin receptor activity, type I; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0098821; F:BMP receptor activity; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
DR   GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR   GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR   GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
DR   GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IBA:GO_Central.
DR   GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IBA:GO_Central.
DR   GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0003289; P:atrial septum primum morphogenesis; IEA:Ensembl.
DR   GO; GO:0061312; P:BMP signaling pathway involved in heart development; IEA:Ensembl.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR   GO; GO:0060923; P:cardiac muscle cell fate commitment; IEA:Ensembl.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; IEA:Ensembl.
DR   GO; GO:0061445; P:endocardial cushion cell fate commitment; IEA:Ensembl.
DR   GO; GO:0003274; P:endocardial cushion fusion; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR   GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR   GO; GO:0003183; P:mitral valve morphogenesis; IEA:Ensembl.
DR   GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR   GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:2000017; P:positive regulation of determination of dorsal identity; IEA:Ensembl.
DR   GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IEA:Ensembl.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR003605; GS_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006718};
KW   Kinase {ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138139};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|RuleBase:RU361271};
KW   Membrane {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138203};
KW   Metal-binding {ECO:0000256|RuleBase:RU361271};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:AFE63706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138186}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138220};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00488859}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    509       Serine/threonine-protein kinase receptor.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5014090488.
FT   TRANSMEM    124    146       Helical. {ECO:0000256|RuleBase:RU361271}.
FT   DOMAIN      178    207       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      208    502       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   509 AA;  57135 MW;  A3D54196CDEC174E CRC64;
     MVDGVMILPV LIIIALPSPS MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN
     DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF
     HLEVGLIILS VVFAVCLLAC LLGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL
     ADLLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR
     DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL
     DTVSCLRIVL SIASGLAHLH IEIFGTQGKP AIAHRDLKSK NILVKKNGQC CIADLGLAVM
     HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS
     NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ
     NPSARLTALR IKKTLTKIDN SLDKLKTDC
//
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