ID AVR2A_RAT STANDARD; PRT; 513 AA. AC P38444; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-JUN-2006, entry version 67. DE Activin receptor type 2A precursor (EC 2.7.11.30) (Activin receptor DE type IIA) (ACTR-IIA). GN Name=Acvr2a; Synonyms=Actrii, Acvr2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX MEDLINE=93050162; PubMed=1385212; DOI=10.1016/0014-5793(92)81408-E; RA Shinozaki H., Ito I., Hasegawa Y., Nakamura K., Igarashi S., RA Nakamura M., 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 MEDLINE=93279247; PubMed=7916681; DOI=10.1210/en.132.6.2593; 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 CC of two type II and two type I transmembrane serine/threonine CC kinases. Type II receptors phosphorylate and activate type I CC receptors which autophosphorylate, then bind and activate SMAD CC transcriptional regulators. Receptor for activin A, activin B and CC inhibin A. CC -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor- CC protein] phosphate. CC -!- COFACTOR: Magnesium or manganese (By similarity). CC -!- SUBUNIT: Interacts with AIP1. Part of a complex consisting of CC AIP1, ACVR2A, ACVR1B and SMAD3 (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. TGFB CC receptor subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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; S27258; S27258. DR PDB; 1NYS; X-ray; A/C=34-114. DR PDB; 1NYU; X-ray; A/C=34-114. DR Ensembl; ENSRNOG00000005334; Rattus norvegicus. DR RGD; 70911; Acvr2a. DR GO; GO:0048179; C:activin receptor complex; TAS. DR GO; GO:0048185; F:activin binding; TAS. DR GO; GO:0016362; F:activin receptor activity, type II; IDA. DR GO; GO:0004675; F:transmembrane receptor protein serine/threo...; TAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS. DR InterPro; IPR000472; Activin_rcpt. DR InterPro; IPR000333; Activin_rcpt_II. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF01064; Activin_recp; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00653; ACTIVIN2R. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW 3D-structure; ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; KW Membrane; Metal-binding; Nucleotide-binding; Receptor; KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane. FT SIGNAL 1 19 Potential. FT CHAIN 20 513 Activin receptor type 2A. FT /FTId=PRO_0000024401. FT TOPO_DOM 20 135 Extracellular (Potential). FT TRANSMEM 136 161 Potential. FT TOPO_DOM 162 513 Cytoplasmic (Potential). FT DOMAIN 192 485 Protein kinase. FT NP_BIND 198 206 ATP (By similarity). FT ACT_SITE 322 322 Proton acceptor (By similarity). FT BINDING 219 219 ATP (By similarity). FT CARBOHYD 43 43 N-linked (GlcNAc...) (Potential). FT CARBOHYD 66 66 N-linked (GlcNAc...) (Potential). FT DISULFID 30 60 By similarity. FT DISULFID 50 78 By similarity. FT DISULFID 85 104 By similarity. FT DISULFID 91 103 By similarity. FT DISULFID 105 110 By similarity. FT CONFLICT 165 165 M -> K (in Ref. 2). FT CONFLICT 218 218 V -> I (in Ref. 2). FT CONFLICT 353 353 G -> A (in Ref. 2). FT CONFLICT 475 475 L -> V (in Ref. 2). FT STRAND 29 34 FT TURN 35 41 FT STRAND 44 49 FT STRAND 58 66 FT STRAND 68 69 FT STRAND 71 80 FT HELIX 83 85 FT TURN 86 87 FT STRAND 90 93 FT STRAND 96 97 FT STRAND 99 105 FT STRAND 107 107 FT TURN 108 109 FT HELIX 110 112 FT STRAND 113 116 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 //