GENTAUR Molecular Products.

 F1N870_CHICK            Unreviewed;      1087 AA.
 F1N870;
 03-MAY-2011, integrated into UniProtKB/TrEMBL.
 26-JUN-2013, sequence version 2.
 10-OCT-2018, entry version 70.
 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}.
 -!- ACTIVITY 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; Expressed in 10 organ(s), highest expression level in colon.
 ExpressionAtlas; F1N870; baseline and differential.
 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:0044877; F:protein-containing 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:0046777; P:protein autophosphorylation; IEA:Ensembl.
 GO; GO:0061298; P:retina vasculature development in camera-type eye; IEA:Ensembl.
 GO; GO:0060021; P:roof of mouth development; 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|PIRSR:PIRSR500950-51, 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|PIRSR:PIRSR500950-52,
 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|PIRSR:PIRSR500950-51, 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}.
 NP_BIND     599    607       ATP. {ECO:0000256|PIRSR:PIRSR500950-51}.
 ACT_SITE    818    818       Proton acceptor.
                              {ECO:0000256|PIRSR:PIRSR500950-50}.
 BINDING     627    627       ATP. {ECO:0000256|PIRSR:PIRSR500950-51}.
 DISULFID     49     99       {ECO:0000256|PIRSR:PIRSR500950-52}.
 DISULFID    149    189       {ECO:0000256|PIRSR:PIRSR500950-52}.
 DISULFID    235    290       {ECO:0000256|PIRSR:PIRSR500950-52}.
 DISULFID    435    501       {ECO:0000256|PIRSR:PIRSR500950-52}.
 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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