ID   AVR2A_CHICK             Reviewed;         513 AA.
AC   Q90669; Q90745;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Activin receptor type-2A {ECO:0000305|PubMed:1318847};
DE            EC=2.7.11.30 {ECO:0000250|UniProtKB:P27038};
DE   AltName: Full=Activin receptor type IIA;
DE            Short=ACTR-IIA;
DE            Short=ACTRIIA;
DE   Flags: Precursor;
GN   Name=ACVR2A;
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], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=1318847; DOI=10.1016/0014-5793(92)80515-i;
RA   Ohuchi H., Noji S., Koyama E., Myokai F., Nishikawa K., Nohno T.,
RA   Tashiro K., Shiokawa K., Matsuo N., Taniguchi S.;
RT   "Expression pattern of the activin receptor type IIA gene during
RT   differentiation of chick neural tissues, muscle and skin.";
RL   FEBS Lett. 303:185-189(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION.
RC   TISSUE=Embryo;
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   [3]
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   [4]
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   [5]
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   [6]
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         Evidence={ECO:0000250|UniProtKB:P27038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881;
CC         Evidence={ECO:0000250|UniProtKB:P27038};
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; Evidence={ECO:0000250|UniProtKB:P27038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674;
CC         Evidence={ECO:0000250|UniProtKB:P27038};
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: Cell membrane {ECO:0000250|UniProtKB:P27038};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in hen anterior pituitary during the
CC       ovulatory cycle and 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:1318847,
CC       ECO:0000269|PubMed:16039645, 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; D31899; BAA06697.1; -; mRNA.
DR   EMBL; U31222; AAA87841.1; -; mRNA.
DR   PIR; S23089; S23089.
DR   RefSeq; NP_990698.1; NM_205367.1.
DR   AlphaFoldDB; Q90669; -.
DR   SMR; Q90669; -.
DR   STRING; 9031.ENSGALP00000037012; -.
DR   GlyCosmos; Q90669; 2 sites, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000037012; -.
DR   Ensembl; ENSGALT00010022658.1; ENSGALP00010013077.1; ENSGALG00010009474.1.
DR   GeneID; 396324; -.
DR   KEGG; gga:396324; -.
DR   CTD; 92; -.
DR   VEuPathDB; HostDB:geneid_396324; -.
DR   eggNOG; KOG3653; Eukaryota.
DR   GeneTree; ENSGT00940000157233; -.
DR   HOGENOM; CLU_000288_8_4_1; -.
DR   InParanoid; Q90669; -.
DR   PhylomeDB; Q90669; -.
DR   TreeFam; TF352876; -.
DR   Reactome; R-GGA-1502540; Signaling by Activin.
DR   Reactome; R-GGA-201451; Signaling by BMP.
DR   PRO; PR:Q90669; -.
DR   Proteomes; UP000000539; Chromosome 7.
DR   Bgee; ENSGALG00000012444; Expressed in kidney and 14 other cell types or tissues.
DR   GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0016020; C:membrane; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0048185; F:activin binding; IDA:AgBase.
DR   GO; GO:0017002; F:activin receptor activity; ISS:UniProtKB.
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:0048333; P:mesodermal cell differentiation; IMP:AgBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14141; STKc_ACVR2a; 1.
DR   Gene3D; 2.10.60.10; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF64; ACTIVIN RECEPTOR TYPE-2A; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00220; S_TKc; 1.
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; Cell membrane; Disulfide bond; Glycoprotein; Kinase;
KW   Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..513
FT                   /note="Activin receptor type-2A"
FT                   /id="PRO_0000269545"
FT   TOPO_DOM        20..139
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..513
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          192..485
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         198..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         219
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        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..60
FT                   /evidence="ECO:0000250|UniProtKB:P27038"
FT   DISULFID        50..78
FT                   /evidence="ECO:0000250|UniProtKB:P27038"
FT   DISULFID        85..104
FT                   /evidence="ECO:0000250|UniProtKB:P27038"
FT   DISULFID        91..103
FT                   /evidence="ECO:0000250|UniProtKB:P27038"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000250|UniProtKB:P27038"
FT   CONFLICT        9
FT                   /note="F -> L (in Ref. 1; BAA06697)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43..45
FT                   /note="NRS -> IAV (in Ref. 1; BAA06697)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="F -> S (in Ref. 1; BAA06697)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  58092 MW;  03128AB7FF732552 CRC64;
     MGAATKLAFA VFLISCSSGA ILGRSETQEC IYYNANWEKD KTNRSGIEPC YGDKDKRRHC
     FATWKNISGS IEIVKQGCWL DDINCYDRND CIEKKDSPEV FFCCCEGNMC NERFFYFPEM
     EVTQPTSNPV TPKPPLFNTL LYSLVPIMGI AVIVLFSFWM YRHHKLAYPP VLVPTQDPGP
     PPPSPLMGLK PLQLLEIKAR GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEIYSLPG
     MKHDNILQFI GAEKRGTSID VDLWLITAFH EKGSLTDFLK ANVVSWNELC HIAQTMARGL
     AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG KSAGDTHGQV
     GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR CTASDGPVDE YMLPFEEEIG
     QHPSLEDMQE VVVHKKKRPV LRECWQKHSG MAMLCETIEE CWDHDAEARL SAGCVEERII
     QMQKLTNIIT TEDIVTVVTM VTNVDFPPKE SSL
//