ID AVR2A_XENLA Reviewed; 514 AA.
AC P27039; Q5D043;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Activin receptor type-2A {ECO:0000250|UniProtKB:P27038};
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=acvr2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1661587; DOI=10.1016/0006-291x(91)91245-8;
RA Kondo M., Tashiro K., Fujii G., Asano M., Miyoshi R., Yamada R.,
RA Muramatsu M., Shiokawa K.;
RT "Activin receptor mRNA is expressed early in Xenopus embryogenesis and the
RT level of the expression affects the body axis formation.";
RL Biochem. Biophys. Res. Commun. 181:684-690(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for activin A, activin B and inhibin A. Involved in
CC transmembrane signaling.
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 -!- 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; S70930; AAB20638.1; -; mRNA.
DR EMBL; BC066770; AAH66770.1; -; mRNA.
DR PIR; JQ1317; JQ1317.
DR RefSeq; NP_001084061.1; NM_001090592.1.
DR AlphaFoldDB; P27039; -.
DR SMR; P27039; -.
DR GlyCosmos; P27039; 3 sites, No reported glycans.
DR DNASU; 399283; -.
DR GeneID; 399283; -.
DR KEGG; xla:399283; -.
DR AGR; Xenbase:XB-GENE-865037; -.
DR CTD; 399283; -.
DR Xenbase; XB-GENE-865037; acvr2a.L.
DR OMA; HCYVLWQ; -.
DR OrthoDB; 3900892at2759; -.
DR BRENDA; 2.7.10.2; 6725.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 399283; Expressed in lung and 19 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0017002; F:activin receptor activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..514
FT /note="Activin receptor type-2A"
FT /id="PRO_0000024402"
FT TOPO_DOM 21..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 193..486
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 199..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..61
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 51..79
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 86..105
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 92..104
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 106..111
FT /evidence="ECO:0000250|UniProtKB:P38445"
SQ SEQUENCE 514 AA; 57904 MW; 9FA4B4D7F9756C26 CRC64;
MGAATKLAFA VFLISCSSAG SILGRSETKE CIYYNANWEK DKTNSNGTEI CYGDNDKRKH
CFATWKNISG SIEIVKQGCW LDDINCYNKS KCTEKKDSPD VFFCCCEGNY CNEKFYHSPE
MEVTQPTSNP VTTKPPLFNT LLYSLVPIMV VAVIVLFSFW MYRHHKLAYP PVLVPTQDPG
PPPPSPLLGL KPLQLLEVKA RGRFGCVWKA QLLNETVAVK IFPVQDKLSW QNEYEIYSLP
GMKHENILYF IGAEKRGTNL DTDLWLITAF HEKGSLTDYL KANVVSWNEL CLIAETMARG
LSHLHEDIPG LKDGHKPAVA HRDIKSKNVL LKNNLTACIA DFGLALKFEA GKSAGDTHGQ
VGTRRYMAPE VLEGAINFQR DAFLRIDMYA FGLVLWELAS RCTASDGPVD EYMLPFEEEV
GQHPSLEDMQ EVVVHKKKRP ILRECWQKHA GMAMLCETIE ECWDHDAEAR LSAGCVEERI
IQMQKLTNII TTEDIVTVVT MVTNVDFPPK ESSL
//
