AVR2A_CHICK
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 03-AUG-2022, entry version 153.
DE RecName: Full=Activin receptor type-2A;
DE EC=2.7.11.30;
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 -!- 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: 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 PaxDb; Q90669; -.
DR Ensembl; ENSGALT00000037806; ENSGALP00000037012; ENSGALG00000012444.
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 OMA; IICAFWV; -.
DR OrthoDB; 390511at2759; -.
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 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; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; 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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
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 SMART; SM00220; S_TKc; 1.
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..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
