AVR2A_BOVIN
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 03-AUG-2022, entry version 162.
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 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 -!- 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 (By similarity). Interacts with BMP7 (By similarity).
CC {ECO:0000250|UniProtKB:P27037, ECO:0000250|UniProtKB:P27038}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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 PaxDb; Q28043; -.
DR Ensembl; ENSBTAT00000024108; ENSBTAP00000024108; ENSBTAG00000018114.
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; 390511at2759; -.
DR TreeFam; TF352876; -.
DR BRENDA; 2.7.10.2; 908.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000018114; Expressed in spiral colon and 107 other tissues.
DR ExpressionAtlas; Q28043; baseline.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; IEA:Ensembl.
DR GO; GO:0005886; C: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:0017002; F:activin receptor activity; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; 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:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Magnesium; Manganese;
KW Membrane; Metal-binding; 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_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
