AVR2B_XENLA
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 03-AUG-2022, entry version 124.
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}.
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DR EMBL; M88594; AAB00480.1; -; mRNA.
DR RefSeq; NP_001084049.1; NM_001090580.1.
DR AlphaFoldDB; P27041; -.
DR SMR; P27041; -.
DR GeneID; 399277; -.
DR KEGG; xla:399277; -.
DR CTD; 399277; -.
DR Xenbase; XB-GENE-484252; acvr2b.L.
DR OrthoDB; 390511at2759; -.
DR BRENDA; 2.7.10.2; 6725.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 399277; Expressed in blastula and 12 other tissues.
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:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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 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; 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
