AVR2A_SHEEP
ID AVR2A_SHEEP Reviewed; 513 AA.
AC Q28560;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Romney; TISSUE=Ovarian follicle;
RA Tisdall D.J.;
RL Submitted (MAR-1996) 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). {ECO:0000250|UniProtKB:P27037,
CC 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; L19442; AAA91903.1; -; mRNA.
DR RefSeq; NP_001009293.1; NM_001009293.1.
DR AlphaFoldDB; Q28560; -.
DR SMR; Q28560; -.
DR STRING; 9940.ENSOARP00000010557; -.
DR GeneID; 443304; -.
DR KEGG; oas:443304; -.
DR CTD; 92; -.
DR eggNOG; KOG3653; Eukaryota.
DR OrthoDB; 390511at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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_0000024400"
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:P38445"
FT DISULFID 85..104
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 91..103
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 105..110
FT /evidence="ECO:0000250|UniProtKB:P38445"
SQ SEQUENCE 513 AA; 57768 MW; 7231BF9E85CA57E3 CRC64;
MGAAAKLAFA VFLISCSSGA ILGRSETQEC IFYNANWERD RTNRTGVESC YGDKDKRRHC
FATWKNISSS IDIVKQGCWL DDINCYDRTD CIEKKDSPEV YFCCCEGNMC NERFSYFPEM
EVTQPTSNPV TPKPPYYNIL LYSLVPLMLV AGIVICAFWV YRHHKMAYPP VLVPTQDPGP
PPPSPLLGLK PLQLLEVKAR GGFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG
MKHENILQFI GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL
AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG KSAGDTHGQV
GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR CTAADGPVDE YMLPFVEEIG
QHPSLEDMQE VVVHKKKRPV LRDYWQKLAG MAMLCETIEE CWDHDAEARL SAGCVGERIT
QMQRLTNIIT TEDIVTVVTV VTNVDFPPKE SSL
