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Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)

 F1N870_CHICK            Unreviewed;      1087 AA.
F1N870;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
26-JUN-2013, sequence version 2.
28-MAR-2018, entry version 66.
RecName: Full=Platelet-derived growth factor receptor alpha {ECO:0000256|PIRNR:PIRNR500950};
Short=PDGF-R-alpha {ECO:0000256|PIRNR:PIRNR500950};
Short=PDGFR-alpha {ECO:0000256|PIRNR:PIRNR500950};
EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500950};
AltName: Full=Alpha platelet-derived growth factor receptor {ECO:0000256|PIRNR:PIRNR500950};
AltName: Full=Alpha-type platelet-derived growth factor receptor {ECO:0000256|PIRNR:PIRNR500950};
Name=PDGFRA {ECO:0000313|Ensembl:ENSGALP00000009175};
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000009175, ECO:0000313|Proteomes:UP000000539};
[1] {ECO:0000313|Ensembl:ENSGALP00000009175, ECO:0000313|Proteomes:UP000000539}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000009175,
ECO:0000313|Proteomes:UP000000539};
PubMed=15592404; DOI=10.1038/nature03154;
International Chicken Genome Sequencing Consortium;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[2] {ECO:0000313|Ensembl:ENSGALP00000009175}
IDENTIFICATION.
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000009175};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface
receptor for PDGFA, PDGFB and PDGFC and plays an essential role in
the regulation of embryonic development, cell proliferation,
survival and chemotaxis. Depending on the context, promotes or
inhibits cell proliferation and cell migration. Plays an important
role in the differentiation of bone marrow-derived mesenchymal
stem cells. Required for normal skeleton development.
{ECO:0000256|PIRNR:PIRNR500950}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00701269}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. Binding of PDGFA and/or PDGFB leads to
dimerization and activation by autophosphorylation on tyrosine
residues. {ECO:0000256|PIRNR:PIRNR500950}.
-!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and
with heterodimers formed by PDGFA and PDGFB. Monomer in the
absence of bound ligand. {ECO:0000256|PIRNR:PIRNR500950}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000256|PIRNR:PIRNR500950}; Single-pass type I membrane
protein {ECO:0000256|PIRNR:PIRNR500950}. Membrane
{ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
protein {ECO:0000256|RuleBase:RU000311}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000256|PIRNR:PIRNR500950, ECO:0000256|RuleBase:RU000311}.
-----------------------------------------------------------------------
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EMBL; AADN04000076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_990080.2; NM_204749.2.
RefSeq; XP_015140900.1; XM_015285414.1.
UniGene; Gga.274; -.
Ensembl; ENSGALT00000009189; ENSGALP00000009175; ENSGALG00000013929.
GeneID; 395509; -.
KEGG; gga:395509; -.
CTD; 5156; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
KO; K04363; -.
OMA; CKDIKKC; -.
OrthoDB; EOG091G01TL; -.
TreeFam; TF325768; -.
Reactome; R-GGA-1257604; PIP3 activates AKT signaling.
Reactome; R-GGA-186763; Downstream signal transduction.
Reactome; R-GGA-186797; Signaling by PDGF.
Reactome; R-GGA-5673001; RAF/MAP kinase cascade.
Reactome; R-GGA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Proteomes; UP000000539; Chromosome 4.
Bgee; ENSGALG00000013929; -.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IEA:Ensembl.
GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0001553; P:luteinization; IEA:Ensembl.
GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
GO; GO:0072277; P:metanephric glomerular capillary formation; IEA:Ensembl.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IEA:Ensembl.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027290; PDGFRA.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF07679; I-set; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00708816};
Cell membrane {ECO:0000256|PIRNR:PIRNR500950};
Chemotaxis {ECO:0000256|PIRNR:PIRNR500950};
Complete proteome {ECO:0000313|Proteomes:UP000000539};
Developmental protein {ECO:0000256|PIRNR:PIRNR500950};
Disulfide bond {ECO:0000256|SAAS:SAAS00916669};
Immunoglobulin domain {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00941986};
Kinase {ECO:0000256|PIRNR:PIRNR500950, ECO:0000256|SAAS:SAAS00582553};
Membrane {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00708816};
Receptor {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|RuleBase:RU000311, ECO:0000256|SAAS:SAAS00600436};
Reference proteome {ECO:0000313|Proteomes:UP000000539};
Repeat {ECO:0000256|SAAS:SAAS00457685};
Signal {ECO:0000256|SAM:SignalP};
Transferase {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00582553};
Transmembrane {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00582553}.
SIGNAL 1 23 {ECO:0000256|SAM:SignalP}.
CHAIN 24 1087 Platelet-derived growth factor receptor
alpha. {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5003270323.
TRANSMEM 525 549 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 215 306 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 414 517 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 593 954 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
SEQUENCE 1087 AA; 122817 MW; 91A5DCF5EBD9DC87 CRC64;
MGTPPRTFLI LGCFLTGPLL TLCQLPLPTI VPNRNEMVVQ LNSNFTLKCS GDSEVSWQYP
VTEGSHRIDI RHEENNSGLF MTVLEVGNAS AAHTGMYVCY YNHTQVEDGE VEGKDIYIYV
PDPDMPFVPS LPEDQFILVE EGDPTVIPCR TSDPSAEVTL VNSLDKPVYA FYDSKQGFVG
NFLAGPYTCK TMVKGVEFKS DEFLIYILRA TSQLPVEIEA LKTVYKTGET IVVTCVVFDN
EVVNLQWNYP GKVKEKGLIK LDDIKVPSQK LVYTLTIPDA SVKDTGDYEC TARHATKEVK
ENKKVVITVH DKGFIHLEPQ FSPLEAVNLH EVKNFVVDVQ AYPAPKMYWL KDNVTLIENL
TEIVTSSNRV QETRFQSVLK LIRAKEEDSG YYTLVAENED EIKRYTFSLL IQVPALILDL
MDDHQGSAGR QTVRCLAEGT PLPDVEWLVC KDIKKCSNDT SWTLLTNNIS DIHMEAHLDE
RNMVESQVTF QKVEETLAVR CVARNDLGAV TRELKLVAPT LRSELTVAAA VLVLLVIVII
SLIVLVIIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL
LGACTKSGPI YIITEYCFYG DLVNYLHKNR DNFLSRHPEK PKKDLDIFGM NPADESTRSY
VILSFENTGE YMDMKQADTT QYVPMLERKE GSKYSDIQRS VYDRPASYKK KSLSESEVKN
LLSDDGSEGL SLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM
VDSTFYNKIK SGYRMAKPDH ATNEVYEIMV KCWNSEPEKR PSFYHLSEIV ESLLPGEYKK
SYEKIHLDFL KSDHPAVTRM RGDCDNAYIG VTYKNEDKIK DRESGFDEQR LSADSGYIIP
LPDIDPVSED ELGKRNRHSS QTSEESAIET GSSSSTFIKR EDETIEDIDM MDDIGIDSSD
LVEDSFL


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