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 02-JUN-2021, entry version 184. 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 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; P38444; -. DR MINT; P38444; -. DR STRING; 10116.ENSRNOP00000007404; -. DR GlyGen; P38444; 2 sites. DR PhosphoSitePlus; P38444; -. DR PaxDb; P38444; -. DR PRIDE; P38444; -. DR GeneID; 29263; -. DR KEGG; rno:29263; -. DR UCSC; RGD:70911; rat. DR CTD; 92; -. DR RGD; 70911; Acvr2a. DR eggNOG; KOG3653; Eukaryota. DR InParanoid; P38444; -. DR OrthoDB; 390511at2759; -. 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; IBA:GO_Central. DR GO; GO:0043235; C:receptor complex; ISO:RGD. DR GO; GO:0048185; F:activin binding; IDA:RGD. DR GO; GO:0017002; F:activin-activated 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; 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: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: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:0043084; P:penile erection; ISO:RGD. 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:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:RGD. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central. DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; 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:0042713; P:sperm ejaculation; ISO:RGD. DR GO; GO:0007283; P:spermatogenesis; ISO:RGD. 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; 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 PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Disulfide bond; Glycoprotein; Kinase; Magnesium; KW Manganese; Membrane; Metal-binding; Nucleotide-binding; Receptor; KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase; KW 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 NP_BIND 198..206 FT /note="ATP" 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 219 FT /note="ATP" 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 //