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   22-JUL-2008, entry version 56.
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   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   MEDLINE=92299088; 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   MEDLINE=96069914; PubMed=7589799; DOI=10.1006/dbio.1995.0015;
RA   Stern C.D., Yu R.T., Kakizuka A., Kintner C.R., Mathews L.S.,
RA   Vale W.W., 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
RT   of the 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
RT   interneurons 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
RT   inhibin co-receptor (betaglycan) and type-I and type-II activin
RT   receptors during 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-
RT   receptor (betaglycan) and activin type-I and type-II receptors in
RT   preovulatory and prehierarchical follicles of the laying hen ovary.";
RL   J. Endocrinol. 188:241-249(2006).
CC   -!- FUNCTION: On ligand binding, forms a receptor complex consisting
CC       of two type II and two type I transmembrane serine/threonine
CC       kinases. Type II receptors phosphorylate and activate type I
CC       receptors which autophosphorylate, then bind and activate SMAD
CC       transcriptional regulators. Receptor for activin A, activin B and
CC       inhibin A. May modulate neuropeptide expression in dorsal root
CC       ganglia (DRG) neurons and ovarian follicle development.
CC   -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC       protein] phosphate.
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in hen anterior pituitary during the
CC       ovulatory cycle and in the ovarian follicle.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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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; -.
DR   UniGene; Gga.2852; -.
DR   HSSP; P27038; 1BTE.
DR   SMR; Q90669; 26-119.
DR   Ensembl; ENSGALG00000012444; Gallus gallus.
DR   GeneID; 396324; -.
DR   KEGG; gga:396324; -.
DR   HOVERGEN; Q90669; -.
DR   InterPro; IPR000333; Activin_II_recpt.
DR   InterPro; IPR015768; Activin_II_recpt_C.
DR   InterPro; IPR000472; Activin_rcpt.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   PANTHER; PTHR23255:SF10; Activin_II_recpt_C; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane;
KW   Metal-binding; Nucleotide-binding; Receptor;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    513       Activin receptor type-2A.
FT                                /FTId=PRO_0000269545.
FT   TOPO_DOM     20    139       Extracellular (Potential).
FT   TRANSMEM    140    160       Potential.
FT   TOPO_DOM    161    513       Cytoplasmic (Potential).
FT   DOMAIN      192    485       Protein kinase.
FT   NP_BIND     198    206       ATP (By similarity).
FT   COMPBIAS    178    185       Poly-Pro.
FT   ACT_SITE    322    322       Proton acceptor (By similarity).
FT   BINDING     219    219       ATP (By similarity).
FT   CARBOHYD     43     43       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     66     66       N-linked (GlcNAc...) (Potential).
FT   CONFLICT      9      9       F -> L (in Ref. 1; BAA06697).
FT   CONFLICT     43     45       NRS -> IAV (in Ref. 1; BAA06697).
FT   CONFLICT    115    115       F -> S (in Ref. 1; BAA06697).
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
//