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   27-MAR-2024, entry version 141.
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   GlyCosmos; Q90670; 2 sites, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000009931; -.
DR   Ensembl; ENSGALT00010065687.1; ENSGALP00010039953.1; ENSGALG00010027103.1.
DR   Ensembl; ENSGALT00015056593; ENSGALP00015034226; ENSGALG00015023131.
DR   GeneID; 374213; -.
DR   KEGG; gga:374213; -.
DR   CTD; 93; -.
DR   VEuPathDB; HostDB:geneid_374213; -.
DR   eggNOG; KOG3653; Eukaryota.
DR   GeneTree; ENSGT00940000156210; -.
DR   InParanoid; Q90670; -.
DR   OMA; SWNDLCH; -.
DR   OrthoDB; 3900892at2759; -.
DR   PhylomeDB; Q90670; -.
DR   PRO; PR:Q90670; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR   GO; GO:0045178; C:basal part of cell; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0048185; F:activin binding; IDA:AgBase.
DR   GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:AgBase.
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; 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
//