ID   AVR2A_RAT               Reviewed;         513 AA.
AC   P38444;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Activin receptor type-2A {ECO:0000305|PubMed:1385212};
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 {ECO:0000312|RGD:70911}; Synonyms=Actrii, Acvr2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=1385212; DOI=10.1016/0014-5793(92)81408-e;
RA   Shinozaki H., Ito I., Hasegawa Y., Nakamura K., Igarashi S., Nakamura M.,
RA   Miyamoto K., Eto Y., Ibuki Y., Minegishi T.;
RT   "Cloning and sequencing of a rat type II activin receptor.";
RL   FEBS Lett. 312:53-56(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=7916681; DOI=10.1210/endo.132.6.7916681;
RA   Feng Z.M., Madigan M.B., Chen C.L.C.;
RT   "Expression of type II activin receptor genes in the male and female
RT   reproductive tissues of the rat.";
RL   Endocrinology 132:2593-2600(1993).
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; S48190; AAB23958.1; -; mRNA.
DR   EMBL; L10639; AAA40674.1; -; mRNA.
DR   PIR; A49193; A49193.
DR   PIR; S27258; S27258.
DR   RefSeq; NP_113759.1; NM_031571.2.
DR   PDB; 1NYS; X-ray; 3.05 A; A/C=34-112.
DR   PDB; 1NYU; X-ray; 3.10 A; A/C=34-112.
DR   PDBsum; 1NYS; -.
DR   PDBsum; 1NYU; -.
DR   AlphaFoldDB; P38444; -.
DR   SMR; P38444; -.
DR   MINT; P38444; -.
DR   STRING; 10116.ENSRNOP00000007404; -.
DR   GlyCosmos; P38444; 2 sites, No reported glycans.
DR   GlyGen; P38444; 2 sites.
DR   PhosphoSitePlus; P38444; -.
DR   PaxDb; 10116-ENSRNOP00000007404; -.
DR   GeneID; 29263; -.
DR   KEGG; rno:29263; -.
DR   UCSC; RGD:70911; rat.
DR   AGR; RGD:70911; -.
DR   CTD; 92; -.
DR   RGD; 70911; Acvr2a.
DR   eggNOG; KOG3653; Eukaryota.
DR   InParanoid; P38444; -.
DR   OrthoDB; 3900892at2759; -.
DR   PhylomeDB; P38444; -.
DR   BRENDA; 2.7.10.2; 5301.
DR   Reactome; R-RNO-1502540; Signaling by Activin.
DR   Reactome; R-RNO-201451; Signaling by BMP.
DR   EvolutionaryTrace; P38444; -.
DR   PRO; PR:P38444; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0048185; F:activin binding; IDA:RGD.
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:0015026; F:coreceptor activity; ISO:RGD.
DR   GO; GO:0019838; F:growth factor binding; ISO:RGD.
DR   GO; GO:0034711; F:inhibin binding; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR   GO; GO:0043621; F:protein self-association; ISO:RGD.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; TAS:RGD.
DR   GO; GO:0032924; P:activin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0030325; P:adrenal gland development; IEP:RGD.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR   GO; GO:0006914; P:autophagy; IMP:RGD.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IMP:RGD.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR   GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; ISO:RGD.
DR   GO; GO:0008584; P:male gonad development; ISO:RGD.
DR   GO; GO:0007498; P:mesoderm development; ISO:RGD.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR   GO; GO:0043084; P:penile erection; ISO:RGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; ISO:RGD.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:RGD.
DR   GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IMP:RGD.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISO:RGD.
DR   GO; GO:0009966; P:regulation of signal transduction; ISO:RGD.
DR   GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR   GO; GO:0060011; P:Sertoli cell proliferation; ISO:RGD.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IMP:RGD.
DR   GO; GO:0042713; P:sperm ejaculation; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW   Kinase; 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_0000024401"
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   CONFLICT        165
FT                   /note="M -> K (in Ref. 2; AAB23958)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="V -> I (in Ref. 2; AAB23958)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        353
FT                   /note="G -> A (in Ref. 2; AAB23958)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        475
FT                   /note="L -> V (in Ref. 2; AAB23958)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  57893 MW;  CE3A8742EF91DD7D CRC64;
     MGAAAKLAFA VFLISCSSGA ILGRSETQEC LFFNANWERD RTNQTGVEPC YGDKDKRRHC
     FATWKNISGS IEIVKQGCWL DDINCYDRTD CIEKKDSPEV YFCCCEGNMC NEKFSYFPEM
     EVTQPTSNPV TPKPPYYNIL LYSLVPLMLI AGIVICAFWV YRHHMMAYPP VLVPTQDPGP
     PPPSPLLGLK PLQLLEVKAR GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG
     MKHENILQFI GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL
     AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG KSGGDTHGQV
     GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR CTAADGPVDE YMLPFEEEIG
     QHPSLEDMQE VVVHKKKRPV LRDYWQKHAG MAMLCETIEE CWDHDAEARL SAGCLGERIT
     QMQRLTNIIT TEDIVTVVTM VTNVDFPPKE SSL
//