ID   AVR2A_BOVIN             Reviewed;         513 AA.
AC   Q28043; A5D7L7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Activin receptor type-2A {ECO:0000305|PubMed:7534730};
DE            EC=2.7.11.30 {ECO:0000250|UniProtKB:P27038};
DE   AltName: Full=Activin receptor type IIA;
DE            Short=ACTR-IIA;
DE   Flags: Precursor;
GN   Name=ACVR2A; Synonyms=ACTRII, ACVR2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Holstein; TISSUE=Testis;
RX   PubMed=7534730; DOI=10.1016/0303-7207(94)90179-1;
RA   Ethier J.-F., Houde A., Lussier J.G., Silversides D.W.;
RT   "Bovine activin receptor type II cDNA: cloning and tissue expression.";
RL   Mol. Cell. Endocrinol. 106:1-8(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=8875905; DOI=10.1007/s003359900258;
RA   Monteagudo L.V., Heriz A., Flavin N., Rogers M., Ennis S., Arruga M.V.;
RT   "Fluorescent in situ localization of the bovine activin receptor type IIA
RT   locus on chromosome 2 (2q2.3-2.4).";
RL   Mamm. Genome 7:869-869(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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. Mediates
CC       induction of adipogenesis by GDF6. {ECO:0000250|UniProtKB:P27037,
CC       ECO:0000250|UniProtKB:P27038}.
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         Evidence={ECO:0000250|UniProtKB:P27038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881;
CC         Evidence={ECO:0000250|UniProtKB:P27038};
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; Evidence={ECO:0000250|UniProtKB:P27038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674;
CC         Evidence={ECO:0000250|UniProtKB:P27038};
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: Part of a complex consisting of MAGI2/ARIP1, ACVR2A, ACVR1B
CC       and SMAD3 (By similarity). Interacts with MAGI2/ARIP1 (By similarity).
CC       Interacts with type I receptor ACVR1 (By similarity). Interacts with
CC       BMP7 (By similarity). Interacts with TSC22D1/TSC-22 (By similarity).
CC       {ECO:0000250|UniProtKB:P27037, ECO:0000250|UniProtKB:P27038}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P27038};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR   EMBL; L21717; AAA74597.1; -; mRNA.
DR   EMBL; U43208; AAC48694.1; -; mRNA.
DR   EMBL; BC140605; AAI40606.1; -; mRNA.
DR   PIR; I45850; I45850.
DR   RefSeq; NP_776652.1; NM_174227.3.
DR   AlphaFoldDB; Q28043; -.
DR   SMR; Q28043; -.
DR   STRING; 9913.ENSBTAP00000024108; -.
DR   GlyCosmos; Q28043; 2 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000024108; -.
DR   Ensembl; ENSBTAT00000024108.6; ENSBTAP00000024108.5; ENSBTAG00000018114.6.
DR   GeneID; 281598; -.
DR   KEGG; bta:281598; -.
DR   CTD; 92; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018114; -.
DR   VGNC; VGNC:25595; ACVR2A.
DR   eggNOG; KOG3653; Eukaryota.
DR   GeneTree; ENSGT00940000157233; -.
DR   HOGENOM; CLU_000288_8_4_1; -.
DR   InParanoid; Q28043; -.
DR   OrthoDB; 3900892at2759; -.
DR   TreeFam; TF352876; -.
DR   BRENDA; 2.7.10.2; 908.
DR   Reactome; R-BTA-1502540; Signaling by Activin.
DR   Reactome; R-BTA-201451; Signaling by BMP.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000018114; Expressed in spiral colon and 107 other cell types or tissues.
DR   ExpressionAtlas; Q28043; baseline and differential.
DR   GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR   GO; GO:0017002; F:activin receptor activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0098821; F:BMP receptor activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032924; P:activin receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14141; STKc_ACVR2a; 1.
DR   Gene3D; 2.10.60.10; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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:SF64; ACTIVIN RECEPTOR TYPE-2A; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 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; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Kinase;
KW   Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..513
FT                   /note="Activin receptor type-2A"
FT                   /id="PRO_0000024397"
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"
SQ   SEQUENCE   513 AA;  57952 MW;  C2969A54CF00617B CRC64;
     MGAAAKLAFA VFLISCSSGA ILGRSETQEC IFYNANWERD RTNRTGVESC YGDKDKRRHC
     FATWKNISGS IEIVKQGCWL DDINCYDRTD CIEKKDSPEV YFCCCEGNMC NERFSYFPEM
     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
//