ID   PGDS_HUMAN     STANDARD;      PRT;  1089 AA.
AC   P16234; Q96KZ7;
DT   01-APR-1990 (Rel. 14, Created)
DT   01-APR-1990 (Rel. 14, Last sequence update)
DT   29-MAR-2004 (Rel. 43, Last annotation update)
DE   Alpha platelet-derived growth factor receptor precursor (EC 2.7.1.112)
DE   (PDGF-R-alpha) (CD140a antigen).
GN   PDGFRA.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A. (ISOFORM 1).
RX   MEDLINE=89130149; PubMed=2536956;
RA   Matsui T., Heidaran M., Miki T., Popescu N., la Rochelle W.,
RA   Kraus M., 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   SEQUENCE FROM N.A. (ISOFORM 1).
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
RT   the B-type PDGF receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:4917-4921(1989).
RN   [3]
RP   SEQUENCE FROM N.A. (ISOFORM 1).
RC   TISSUE=Blood;
RX   MEDLINE=96163874; PubMed=8586421;
RA   Kawagishi J., Ku T.;
RT   "Structure, organization, and transcription units of the human
RT   alpha-platelet-derived growth factor receptor gene, PDGFRA.";
RL   Genomics 30:224-232(1995).
RN   [4]
RP   SEQUENCE FROM N.A. (ISOFORM 2).
RC   TISSUE=Placenta;
RX   MEDLINE=22388257; PubMed=12477932;
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   DISEASE.
RX   MEDLINE=22547205; PubMed=12660384;
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1185-1189 IN COMPLEX WITH
RP   SLC9A3R1 AND PDGFRB.
RX   MEDLINE=22013966; PubMed=11882663;
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 + protein
CC       tyrosine phosphate.
CC   -!- SUBUNIT: Homodimer, and heterodimer with PDGFRB.
CC   -!- SUBCELLULAR LOCATION: Type I membrane 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], a rare hematologic
CC       disorder characterized by sustained overproduction of eosinophils
CC       in the bone marrow, eosinophilia, tissue infiltration and organ
CC       damage.
CC   -!- SIMILARITY: Belongs to the Tyr family of protein kinases.
CC       CSF-1/PDGF receptor subfamily.
CC   -!- SIMILARITY: Contains 5 immunoglobulin-like C2-type domains.
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DR   EMBL; M21574; AAA96715.1; -.
DR   EMBL; M22734; AAA60048.1; -.
DR   EMBL; D50017; BAA08742.1; -.
DR   EMBL; D50002; BAA08742.1; JOINED.
DR   EMBL; D50003; BAA08742.1; JOINED.
DR   EMBL; D50004; BAA08742.1; JOINED.
DR   EMBL; D50005; BAA08742.1; JOINED.
DR   EMBL; D50006; BAA08742.1; JOINED.
DR   EMBL; D50007; BAA08742.1; JOINED.
DR   EMBL; D50008; BAA08742.1; JOINED.
DR   EMBL; D50009; BAA08742.1; JOINED.
DR   EMBL; D50010; BAA08742.1; JOINED.
DR   EMBL; D50011; BAA08742.1; JOINED.
DR   EMBL; D50012; BAA08742.1; JOINED.
DR   EMBL; D50013; BAA08742.1; JOINED.
DR   EMBL; D50014; BAA08742.1; JOINED.
DR   EMBL; D50015; BAA08742.1; JOINED.
DR   EMBL; D50016; BAA08742.1; JOINED.
DR   EMBL; BC015186; AAH15186.1; -.
DR   PIR; A40162; PFHUGA.
DR   PDB; 1GQ5; 14-NOV-02.
DR   Genew; HGNC:8803; PDGFRA.
DR   MIM; 173490; -.
DR   MIM; 607685; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS.
DR   GO; GO:0005018; F:platelet-derived growth factor, alpha-recep...; TAS.
DR   GO; GO:0008283; P:cell proliferation; TAS.
DR   GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR003598; Ig_c2.
DR   InterPro; IPR000719; Prot_kinase.
DR   InterPro; IPR001824; RecepttyrkinsIII.
DR   InterPro; IPR001245; Tyr_pkinase.
DR   InterPro; IPR008266; Tyr_pkinase_AS.
DR   Pfam; PF00047; ig; 3.
DR   Pfam; PF00069; pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 2.
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   Tyrosine-protein kinase; Receptor; Transmembrane; Glycoprotein;
KW   Transferase; Phosphorylation; ATP-binding; Immunoglobulin domain;
KW   Signal; Repeat; Alternative splicing; 3D-structure.
FT   SIGNAL        1     23
FT   CHAIN        24   1089       Alpha platelet-derived growth factor
FT                                receptor.
FT   DOMAIN       24    524       Extracellular (Potential).
FT   TRANSMEM    525    549       Potential.
FT   DOMAIN      550   1089       Cytoplasmic (Potential).
FT   DOMAIN       24    113       Ig-like C2-type 1.
FT   DOMAIN      202    306       Ig-like C2-type 3.
FT   DOMAIN      319    410       Ig-like C2-type 4.
FT   DOMAIN      593    954       Protein kinase.
FT   DOMAIN     1041   1087       Ser-rich.
FT   NP_BIND     599    607       ATP (By similarity).
FT   BINDING     627    627       ATP (By similarity).
FT   ACT_SITE    818    818       By similarity.
FT   MOD_RES     849    849       PHOSPHORYLATION (AUTO-) (BY 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;  122669 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
//