ID PGFRA_HUMAN STANDARD; PRT; 1089 AA. AC P16234; Q96KZ7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 07-MAR-2006, entry version 69. DE Alpha platelet-derived growth factor receptor precursor (EC 2.7.1.112) DE (PDGF-R-alpha) (CD140a antigen). GN Name=PDGFRA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX MEDLINE=89130149; PubMed=2536956; RA Matsui T., Heidaran M., Miki T., Popescu N., la Rochelle W., Kraus M., RA Pierce J., Aaronson S.; RT "Isolation of a novel receptor cDNA establishes the existence of two RT PDGF receptor genes."; RL Science 243:800-804(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Foreskin; RX MEDLINE=89296915; PubMed=2544881; RA Claesson-Welsh L., Eriksson A., Westermark B., Heldin C.H.; RT "cDNA cloning and expression of the human A-type platelet-derived RT growth factor (PDGF) receptor establishes structural similarity to the RT B-type PDGF receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4917-4921(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Blood; RX MEDLINE=96163874; PubMed=8586421; RA Kawagishi J., Ku T.; RT "Structure, organization, and transcription units of the human alpha- RT platelet-derived growth factor receptor gene, PDGFRA."; RL Genomics 30:224-232(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 579-1089, DISEASE, AND IDENTIFICATION BY RP MASS SPECTROMETRY OF FIP1L1-PDGFRA FUSION PROTEIN. RC TISSUE=Eosinophil; RX PubMed=12808148; DOI=10.1073/pnas.0932698100; RA Griffin J.H., Leung J., Bruner R.J., Caligiuri M.A., Briesewitz R.; RT "Discovery of a fusion kinase in EOL-1 cells and idiopathic RT hypereosinophilic syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7830-7835(2003). RN [6] RP DISEASE. RX MEDLINE=22547205; PubMed=12660384; DOI=10.1056/NEJMoa025217; RA Cools J., DeAngelo D.J., Gotlib J., Stover E.H., Legare R.D., RA Cortes J., Kutok J., Clark J., Galinsky I., Griffin J.D., Cross N.C., RA Tefferi A., Malone J., Alam R., Schrier S.L., Schmid J., Rose M., RA Vandenberghe P., Verhoef G., Boogaerts M., Wlodarska I., RA Kantarjian H., Marynen P., Coutre S.E., Stone R., Gilliland D.G.; RT "A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as RT a therapeutic target of imatinib in idiopathic hypereosinophilic RT syndrome."; RL N. Engl. J. Med. 348:1201-1214(2003). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1185-1189 IN COMPLEX WITH RP SLC9A3R1 AND PDGFRB. RX MEDLINE=22013966; PubMed=11882663; DOI=10.1074/jbc.M201507200; RA Karthikeyan S., Leung T., Ladias J.A.A.; RT "Structural determinants of the Na+/H+ exchanger regulatory factor RT interaction with the beta 2 adrenergic and platelet-derived growth RT factor receptors."; RL J. Biol. Chem. 277:18973-18978(2002). CC -!- FUNCTION: Receptor that binds both PDGFA and PDGFB and has a CC tyrosine-protein kinase activity. CC -!- CATALYTIC ACTIVITY: ATP + a protein tyrosine = ADP + a protein CC tyrosine phosphate. CC -!- SUBUNIT: Homodimer, and heterodimer with PDGFRB. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P16234-1; Sequence=Displayed; CC Name=2; CC IsoId=P16234-2; Sequence=VSP_007833, VSP_007834; CC Note=No experimental confirmation available; CC -!- DISEASE: A fusion of PDGFRA and FIP1L1 (FIP1L1-PDGFRA), due to an CC interstitial chromosomal deletion, is the cause of some cases of CC hypereosinophilic syndrome (HES) [MIM:607685]. HES is a rare CC hematologic disorder characterized by sustained overproduction of CC eosinophils in the bone marrow, eosinophilia, tissue infiltration CC and organ damage. CC -!- SIMILARITY: Belongs to the Tyr protein kinase family. CSF-1/PDGF CC receptor subfamily. CC -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like) CC domains. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M21574; AAA96715.1; -; mRNA. DR EMBL; M22734; AAA60048.1; -; mRNA. DR EMBL; D50017; BAA08742.1; -; Genomic_DNA. DR EMBL; BC015186; AAH15186.1; -; mRNA. DR EMBL; AY229892; AAP69563.1; ALT_INIT; mRNA. DR PIR; A40162; PFHUGA. DR PDB; 1GQ5; X-ray; -. DR Ensembl; ENSG00000134853; Homo sapiens. DR HGNC; HGNC:8803; PDGFRA. DR MIM; 173490; gene. DR MIM; 607685; phenotype. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0005018; F:platelet-derived growth factor alpha-recept...; TAS. DR GO; GO:0008283; P:cell proliferation; TAS. DR GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS. DR InterPro; IPR013098; I-set. DR InterPro; IPR003599; Ig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR003598; Ig_c2. DR InterPro; IPR013151; Immunoglobulin. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001824; RecepttyrkinsIII. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR InterPro; IPR009134; VEGFR. DR Pfam; PF07679; I-set; 1. DR Pfam; PF00047; ig; 2. DR Pfam; PF07714; Pkinase_Tyr; 1. DR PRINTS; PR01832; VEGFRECEPTOR. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1. KW 3D-structure; Alternative splicing; ATP-binding; Glycoprotein; KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; KW Phosphorylation; Receptor; Repeat; Signal; Transferase; Transmembrane; KW Tyrosine-protein kinase. FT SIGNAL 1 23 FT CHAIN 24 1089 Alpha platelet-derived growth factor FT receptor. FT /FTId=PRO_0000016760. FT TOPO_DOM 24 524 Extracellular (Potential). FT TRANSMEM 525 549 Potential. FT TOPO_DOM 550 1089 Cytoplasmic (Potential). FT DOMAIN 24 113 Ig-like C2-type 1. FT DOMAIN 202 306 Ig-like C2-type 2. FT DOMAIN 319 410 Ig-like C2-type 3. FT DOMAIN 593 954 Protein kinase. FT NP_BIND 599 607 ATP (By similarity). FT COMPBIAS 1041 1087 Ser-rich. FT ACT_SITE 818 818 By similarity. FT BINDING 627 627 ATP (By similarity). FT SITE 578 579 Breakpoint for interstitial deletion to FT form the FIP1L1-PDGFRA fusion protein. FT MOD_RES 849 849 Phosphotyrosine (by autocatalysis) (By FT similarity). FT CARBOHYD 42 42 N-linked (GlcNAc...) (Potential). FT CARBOHYD 76 76 N-linked (GlcNAc...) (Potential). FT CARBOHYD 103 103 N-linked (GlcNAc...) (Potential). FT CARBOHYD 179 179 N-linked (GlcNAc...) (Potential). FT CARBOHYD 353 353 N-linked (GlcNAc...) (Potential). FT CARBOHYD 359 359 N-linked (GlcNAc...) (Potential). FT CARBOHYD 458 458 N-linked (GlcNAc...) (Potential). FT CARBOHYD 468 468 N-linked (GlcNAc...) (Potential). FT VARSPLIC 210 218 ATSELDLEM -> GTCIISFLL (in isoform 2). FT /FTId=VSP_007833. FT VARSPLIC 219 1089 Missing (in isoform 2). FT /FTId=VSP_007834. SQ SEQUENCE 1089 AA; 122670 MW; 5E3FB9940ACD1BE8 CRC64; MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG TFTVGPYICE ATVKGKKFQT IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL KNNLTLIENL TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED AVKSYTFELL TQVPSSILDL VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC KDIKKCNNET SWTILANNVS NIITEIHSRD RSTVEGRVTF AKVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK PKKELDIFGL NPADESTRSY VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN LLSDDNSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV ENLLPGQYKK SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL //