ID AVR2B_XENLA Reviewed; 511 AA. AC P27041; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Activin receptor type-2B; DE EC=2.7.11.30; DE AltName: Full=Activin receptor type IIB; DE Short=ACTR-IIB; DE Flags: Precursor; GN Name=acvr2b; 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=1313188; DOI=10.1126/science.1313188; RA Mathews L.S., Vale W.W., Kintner C.R.; RT "Cloning of a second type of activin receptor and functional RT characterization in Xenopus embryos."; RL Science 255:1702-1705(1992). 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 -!- 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 -!- 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; M88594; AAB00480.1; -; mRNA. DR RefSeq; NP_001084049.1; NM_001090580.1. DR AlphaFoldDB; P27041; -. DR SMR; P27041; -. DR GlyCosmos; P27041; 2 sites, No reported glycans. DR GeneID; 399277; -. DR KEGG; xla:399277; -. DR AGR; Xenbase:XB-GENE-484252; -. DR CTD; 399277; -. DR Xenbase; XB-GENE-484252; acvr2b.L. DR OrthoDB; 3900892at2759; -. DR BRENDA; 2.7.10.2; 6725. DR Proteomes; UP000186698; Chromosome 6L. DR Bgee; 399277; Expressed in blastula and 12 other cell types or tissues. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14140; STKc_ACVR2b; 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:SF70; ACTIVIN RECEPTOR TYPE-2B; 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 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; 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..511 FT /note="Activin receptor type-2B" FT /id="PRO_0000024407" FT TOPO_DOM 21..136 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 137..157 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 158..511 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 189..477 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 320 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 195..203 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 216 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 67 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 30..61 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 511 AA; 57936 MW; A87F1E6BC78C92F0 CRC64; MGASVALTFL LLLATFRAGS GHDEVETREC IYYNANWELE KTNQSGVERL VEGKKDKRLH CYASWRNNSG FIELVKKGCW LDDFNCYDRQ ECIAKEENPQ VFFCCCEGNY CNKKFTHLPE VETFDPKPQP SASVLNILIY SLLPIVGLSM AILLAFWMYR HRKPSYGHVE INEDPGLPPP SPLVGLKPLQ LLDIKARGRF GCVWKARLLN EYVAVKIFPV QDKQSWQCEK EIFTTPGMKH ENLLEFIAAE KRGSNLEMEL WLITAFHDKG SLTDYLKGNL VSWNELCHIT ETMARGLAYL HEDVPRCKGE GHKPAIAHRD FKSKNVLLRN DLTAILADFG LAVRFEPGKP PGDTHGQVGT RRYMAPEVLE GAINFQRDSF LRIDMYAMGL VLWEIVSRCT AADGPVDEYL LPFEEEIGQH PSLEDLQEVV VHKKIRPVFK DHWLKHPGLA QLCVTIEECW DHDAEARLSA GCVEERISQI RKSVNGTTSD CLVSIVTSVT NVDLPPKESS I //