AVR2A_HUMAN
ID AVR2A_HUMAN Reviewed; 513 AA.
AC P27037; B2RAB8; B4DWQ2; D3DP85; Q53TH4; Q6NWV2; Q92474;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Activin receptor type-2A;
DE EC=2.7.11.30;
DE AltName: Full=Activin receptor type IIA;
DE Short=ACTR-IIA;
DE Short=ACTRIIA;
DE Flags: Precursor;
GN Name=ACVR2A; Synonyms=ACVR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=1311955; DOI=10.1016/0167-4781(92)90472-c;
RA Matzuk M.M., Bradley A.;
RT "Cloning of the human activin receptor cDNA reveals high evolutionary
RT conservation.";
RL Biochim. Biophys. Acta 1130:105-108(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=1314589; DOI=10.1016/0006-291x(92)91194-u;
RA Donaldson C.J., Mathews L.S., Vale W.W.;
RT "Molecular cloning and binding properties of the human type II activin
RT receptor.";
RL Biochem. Biophys. Res. Commun. 184:310-316(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RA Geiser A.G.;
RL Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Iimura T., Oida S.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH BMP7.
RX PubMed=12667445; DOI=10.1016/s1097-2765(03)00094-7;
RA Greenwald J., Groppe J., Gray P., Wiater E., Kwiatkowski W., Vale W.,
RA Choe S.;
RT "The BMP7/ActRII extracellular domain complex provides new insights into
RT the cooperative nature of receptor assembly.";
RL Mol. Cell 11:605-617(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH ACVR1.
RX PubMed=17911401; DOI=10.1677/joe-07-0281;
RA Renlund N., O'Neill F.H., Zhang L., Sidis Y., Teixeira J.;
RT "Activin receptor-like kinase-2 inhibits activin signaling by blocking the
RT binding of activin to its type II receptor.";
RL J. Endocrinol. 195:95-103(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 191-488 IN COMPLEX WITH
RP DORSOMORPHIN.
RG Structural genomics consortium (SGC);
RT "Crystal structure of activin receptor type-IIa (ACVR2A) kinase domain in
RT complex with dorsomorphin.";
RL Submitted (FEB-2011) to the PDB data bank.
RN [12]
RP VARIANTS ARG-258 AND ASN-306.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [13]
RP VARIANT THR-367.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: On ligand binding, forms a receptor complex consisting of two
CC type II and two type I transmembrane serine/threonine kinases. Type II
CC receptors phosphorylate and activate type I receptors which
CC autophosphorylate, then bind and activate SMAD transcriptional
CC regulators. Receptor for activin A, activin B and inhibin A
CC (PubMed:17911401). Mediates induction of adipogenesis by GDF6 (By
CC similarity). {ECO:0000250|UniProtKB:P27038, ECO:0000269|PubMed:1314589,
CC ECO:0000269|PubMed:17911401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with AIP1. Part of a complex consisting of AIP1,
CC ACVR2A, ACVR1B and SMAD3 (By similarity). Interacts with type I
CC receptor ACVR1 (PubMed:17911401). Interacts with BMP7
CC (PubMed:12667445). {ECO:0000250|UniProtKB:P27038,
CC ECO:0000269|PubMed:12667445, ECO:0000269|PubMed:17911401}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P27037-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27037-2; Sequence=VSP_054689;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ACVR2ID567ch2q22.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X63128; CAA44839.1; -; mRNA.
DR EMBL; M93415; AAA35504.1; -; mRNA.
DR EMBL; X62381; CAA44245.1; -; mRNA.
DR EMBL; D31770; BAA06548.1; -; mRNA.
DR EMBL; AK301629; BAG63114.1; -; mRNA.
DR EMBL; AK314124; BAG36815.1; -; mRNA.
DR EMBL; AC009480; AAX93050.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11561.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11562.1; -; Genomic_DNA.
DR EMBL; BC067418; AAH67418.1; -; mRNA.
DR EMBL; BC067417; AAH67417.1; -; mRNA.
DR EMBL; BC069707; AAH69707.1; -; mRNA.
DR CCDS; CCDS33301.1; -. [P27037-1]
DR CCDS; CCDS63030.1; -. [P27037-2]
DR PIR; JQ1486; JQ1486.
DR RefSeq; NP_001265508.1; NM_001278579.1. [P27037-1]
DR RefSeq; NP_001265509.1; NM_001278580.1. [P27037-2]
DR RefSeq; NP_001607.1; NM_001616.4. [P27037-1]
DR PDB; 3Q4T; X-ray; 1.96 A; A/B=191-488.
DR PDB; 3SOC; X-ray; 1.95 A; A/B=191-488.
DR PDB; 4ASX; X-ray; 2.05 A; A/B=191-488.
DR PDB; 5NH3; X-ray; 2.35 A; A/B=20-135.
DR PDBsum; 3Q4T; -.
DR PDBsum; 3SOC; -.
DR PDBsum; 4ASX; -.
DR PDBsum; 5NH3; -.
DR AlphaFoldDB; P27037; -.
DR SMR; P27037; -.
DR BioGRID; 106607; 126.
DR DIP; DIP-520N; -.
DR IntAct; P27037; 21.
DR MINT; P27037; -.
DR STRING; 9606.ENSP00000241416; -.
DR BindingDB; P27037; -.
DR ChEMBL; CHEMBL5616; -.
DR DrugBank; DB12118; Sotatercept.
DR DrugCentral; P27037; -.
DR GuidetoPHARMACOLOGY; 1791; -.
DR GlyGen; P27037; 2 sites.
DR iPTMnet; P27037; -.
DR PhosphoSitePlus; P27037; -.
DR BioMuta; ACVR2A; -.
DR DMDM; 114722; -.
DR EPD; P27037; -.
DR jPOST; P27037; -.
DR MassIVE; P27037; -.
DR MaxQB; P27037; -.
DR PaxDb; P27037; -.
DR PeptideAtlas; P27037; -.
DR PRIDE; P27037; -.
DR ProteomicsDB; 5369; -.
DR ProteomicsDB; 54373; -. [P27037-1]
DR ABCD; P27037; 1 sequenced antibody.
DR Antibodypedia; 18817; 478 antibodies from 38 providers.
DR DNASU; 92; -.
DR Ensembl; ENST00000241416.12; ENSP00000241416.7; ENSG00000121989.15. [P27037-1]
DR Ensembl; ENST00000404590.1; ENSP00000384338.1; ENSG00000121989.15. [P27037-1]
DR Ensembl; ENST00000535787.5; ENSP00000439988.1; ENSG00000121989.15. [P27037-2]
DR GeneID; 92; -.
DR KEGG; hsa:92; -.
DR MANE-Select; ENST00000241416.12; ENSP00000241416.7; NM_001616.5; NP_001607.1.
DR UCSC; uc002twg.5; human. [P27037-1]
DR CTD; 92; -.
DR DisGeNET; 92; -.
DR GeneCards; ACVR2A; -.
DR HGNC; HGNC:173; ACVR2A.
DR HPA; ENSG00000121989; Low tissue specificity.
DR MalaCards; ACVR2A; -.
DR MIM; 102581; gene.
DR neXtProt; NX_P27037; -.
DR OpenTargets; ENSG00000121989; -.
DR PharmGKB; PA24494; -.
DR VEuPathDB; HostDB:ENSG00000121989; -.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000157233; -.
DR HOGENOM; CLU_000288_8_4_1; -.
DR InParanoid; P27037; -.
DR OMA; IICAFWV; -.
DR OrthoDB; 390511at2759; -.
DR PhylomeDB; P27037; -.
DR TreeFam; TF352876; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; P27037; -.
DR Reactome; R-HSA-1181150; Signaling by NODAL.
DR Reactome; R-HSA-1433617; Regulation of signaling by NODAL.
DR Reactome; R-HSA-1502540; Signaling by Activin.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR SignaLink; P27037; -.
DR SIGNOR; P27037; -.
DR BioGRID-ORCS; 92; 40 hits in 1098 CRISPR screens.
DR ChiTaRS; ACVR2A; human.
DR EvolutionaryTrace; P27037; -.
DR GeneWiki; ACVR2A; -.
DR GenomeRNAi; 92; -.
DR Pharos; P27037; Tchem.
DR PRO; PR:P27037; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P27037; protein.
DR Bgee; ENSG00000121989; Expressed in buccal mucosa cell and 201 other tissues.
DR Genevisible; P27037; HS.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IPI:BHF-UCL.
DR GO; GO:0048185; F:activin binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0098821; F:BMP receptor activity; ISS:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; IDA:BHF-UCL.
DR GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR GO; GO:0034711; F:inhibin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; EXP:Reactome.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0032924; P:activin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0007498; P:mesoderm development; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0043084; P:penile erection; IEA:Ensembl.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:HGNC-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
DR GO; GO:0042713; P:sperm ejaculation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; TAS:ProtInc.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Disulfide bond;
KW Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..513
FT /note="Activin receptor type-2A"
FT /id="PRO_0000024398"
FT TOPO_DOM 20..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 192..485
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 322
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 198..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..60
FT /evidence="ECO:0000250|UniProtKB:P27038"
FT DISULFID 50..78
FT /evidence="ECO:0000250|UniProtKB:P27038"
FT DISULFID 85..104
FT /evidence="ECO:0000250|UniProtKB:P27038"
FT DISULFID 91..103
FT /evidence="ECO:0000250|UniProtKB:P27038"
FT DISULFID 105..110
FT /evidence="ECO:0000250|UniProtKB:P27038"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054689"
FT VARIANT 258
FT /note="S -> R (in dbSNP:rs34917571)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032809"
FT VARIANT 306
FT /note="D -> N (in a gastric adenocarcinoma sample; somatic
FT mutation; dbSNP:rs764255410)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032810"
FT VARIANT 367
FT /note="A -> T (found in a clear cell renal carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064692"
FT CONFLICT 13
FT /note="L -> V (in Ref. 4; BAA06548)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..206
FT /note="GCV -> PSL (in Ref. 4; BAA06548)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="E -> V (in Ref. 4; BAA06548)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="P -> L (in Ref. 8; AAH67417)"
FT /evidence="ECO:0000305"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:5NH3"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:5NH3"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:5NH3"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:5NH3"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:5NH3"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5NH3"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:5NH3"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5NH3"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 286..303
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 379..398
FT /evidence="ECO:0007829|PDB:3SOC"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 425..432
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 449..461
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:3SOC"
FT HELIX 472..485
FT /evidence="ECO:0007829|PDB:3SOC"
SQ SEQUENCE 513 AA; 57848 MW; A89822E880979618 CRC64;
MGAAAKLAFA VFLISCSSGA ILGRSETQEC LFFNANWEKD RTNQTGVEPC YGDKDKRRHC
FATWKNISGS IEIVKQGCWL DDINCYDRTD CVEKKDSPEV YFCCCEGNMC NEKFSYFPEM
EVTQPTSNPV TPKPPYYNIL LYSLVPLMLI AGIVICAFWV YRHHKMAYPP VLVPTQDPGP
PPPSPLLGLK PLQLLEVKAR GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG
MKHENILQFI GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL
AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG KSAGDTHGQV
GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR CTAADGPVDE YMLPFEEEIG
QHPSLEDMQE VVVHKKKRPV LRDYWQKHAG MAMLCETIEE CWDHDAEARL SAGCVGERIT
QMQRLTNIIT TEDIVTVVTM VTNVDFPPKE SSL
