AVR2B_CHICK
ID AVR2B_CHICK Reviewed; 512 AA.
AC Q90670;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, FUNCTION, AND INDUCTION.
RX PubMed=7589799; DOI=10.1006/dbio.1995.0015;
RA Stern C.D., Yu R.T., Kakizuka A., Kintner C.R., Mathews L.S., Vale W.W.,
RA Evans R.M., Umesono K.;
RT "Activin and its receptors during gastrulation and the later phases of
RT mesoderm development in the chick embryo.";
RL Dev. Biol. 172:192-205(1995).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11291100; DOI=10.1002/neu.1019;
RA Kos K., Fine L., Coulombe J.N.;
RT "Activin type II receptors in embryonic dorsal root ganglion neurons of the
RT chicken.";
RL J. Neurobiol. 47:93-108(2001).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16039645; DOI=10.1016/j.ydbio.2005.05.039;
RA Timmer J., Chesnutt C., Niswander L.;
RT "The activin signaling pathway promotes differentiation of dI3 interneurons
RT in the spinal neural tube.";
RL Dev. Biol. 285:1-10(2005).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16135664; DOI=10.1677/joe.1.06303;
RA Lovell T.M., Knight P.G., Gladwell R.T.;
RT "Variation in pituitary expression of mRNAs encoding the putative inhibin
RT co-receptor (betaglycan) and type-I and type-II activin receptors during
RT the chicken ovulatory cycle.";
RL J. Endocrinol. 186:447-455(2005).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16461550; DOI=10.1677/joe.1.06525;
RA Lovell T.M., Knight P.G., Gladwell R.T.;
RT "Differential expression of mRNAs encoding the putative inhibin co-receptor
RT (betaglycan) and activin type-I and type-II receptors in preovulatory and
RT prehierarchical follicles of the laying hen ovary.";
RL J. Endocrinol. 188:241-249(2006).
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. May
CC modulate neuropeptide expression in dorsal root ganglia (DRG) neurons
CC and ovarian follicle development. {ECO:0000269|PubMed:11291100,
CC ECO:0000269|PubMed:16039645, ECO:0000269|PubMed:16461550,
CC ECO:0000269|PubMed:7589799}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Not expressed in hen anterior pituitary during the
CC ovulatory cycle but expressed in the ovarian follicle.
CC {ECO:0000269|PubMed:16135664, ECO:0000269|PubMed:16461550}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the differentiation of
CC neuroepithelium, of myotomes to muscle and of surface extoderm.
CC Expressed in the dorsal root ganglia (DRG).
CC {ECO:0000269|PubMed:11291100, ECO:0000269|PubMed:16039645,
CC ECO:0000269|PubMed:7589799}.
CC -!- INDUCTION: By activin. {ECO:0000269|PubMed:7589799}.
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; U31223; AAA87842.1; -; mRNA.
DR RefSeq; NP_989648.1; NM_204317.1.
DR AlphaFoldDB; Q90670; -.
DR SMR; Q90670; -.
DR STRING; 9031.ENSGALP00000009931; -.
DR PaxDb; Q90670; -.
DR GeneID; 374213; -.
DR KEGG; gga:374213; -.
DR CTD; 93; -.
DR VEuPathDB; HostDB:geneid_374213; -.
DR eggNOG; KOG3653; Eukaryota.
DR InParanoid; Q90670; -.
DR OrthoDB; 390511at2759; -.
DR PhylomeDB; Q90670; -.
DR PRO; PR:Q90670; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0045178; C:basal part of cell; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048185; F:activin binding; IDA:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0032924; P:activin receptor signaling pathway; IMP:AgBase.
DR GO; GO:0009798; P:axis specification; IMP:AgBase.
DR GO; GO:0008283; P:cell population proliferation; IMP:AgBase.
DR GO; GO:0061550; P:cranial ganglion development; IMP:AgBase.
DR GO; GO:0048333; P:mesodermal cell differentiation; IMP:AgBase.
DR GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; IMP:AgBase.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:AgBase.
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; Magnesium; Manganese;
KW Membrane; Metal-binding; Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..512
FT /note="Activin receptor type-2B"
FT /id="PRO_0000269546"
FT TOPO_DOM 25..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 190..478
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 196..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..59
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 49..77
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 84..103
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 90..102
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 104..109
FT /evidence="ECO:0000250|UniProtKB:P38445"
SQ SEQUENCE 512 AA; 57776 MW; 6051F0CBE94AE060 CRC64;
MSASWLTLAV LCATLGAGPG HGEAETRECI YYNANWELEK TNQSGVERCE GEKDKRLHCY
ASWRNNSGSI ELVKKGCWLD DFNCYDRQEC VATEENPQVF FCCCEGNYCN EKFTHLPEVT
GPEVIYEPPP PTPSLLNILV YSLLPIAVLS VAILLAFWMY RHRKPPYGHV DINEDPGPPP
PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDYVAVKIFP IQDKQSWQSE REIFNTPGMK
HENLLQFIAA EKRGTNLETE LWLITAFHDK GSLTDYLKGN IISWNELCHV AETMARGLSY
LHEDVPWCKG EGHKPAIAHR DFKSKNVLLK NDLTAVLADF GLAVRFEPGK PPGDTHGQVG
TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC RAVDGPVDEY MLPFEEEIGQ
HPSLEDLQEV VVHKKMRPVF KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERIAQ
IRKSVNGTTS DCLVSIVTSV TNVDLPPKES SI
