ID PGDS_HUMAN STANDARD; PRT; 1089 AA. AC P16234; DT 01-APR-1990 (REL. 14, CREATED) DT 01-APR-1990 (REL. 14, LAST SEQUENCE UPDATE) DT 01-FEB-1994 (REL. 28, LAST ANNOTATION UPDATE) DE ALPHA PLATELET-DERIVED GROWTH FACTOR RECEPTOR PRECURSOR DE (EC 2.7.1.112). GN PDGFRA. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RM 89130149 RA MATSUI T., HEIDARAN M., MIKI T., POPESCU N., LA ROCHELLE W., RA KRAUS M., PIERCE J., AARONSON S.; RL SCIENCE 243:800-804(1989). RN [2] RP SEQUENCE FROM N.A. RM 89296915 RA CLAESSON-WELSH L., ERIKSSON A., WESTERMARK B., HELDIN C.H.; RL PROC. NATL. ACAD. SCI. U.S.A. 86:4917-4921(1989). CC -!- FUNCTION: THIS RECEPTOR BINDS PLATELET-DERIVED GROWTH FACTOR AND CC HAS A TYROSINE-PROTEIN KINASE ACTIVITY. THIS RECEPTOR CAN BIND CC EITHER PDGF-A OR PDGF-B. CC -!- SUBUNIT: DIMER OF EITHER ALPHA-ALPHA, BETA-BETA OR ALPHA-BETA CC SUBUNITS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE CSF-1/PDGF RECEPTOR FAMILY OF TYROSINE- CC PROTEIN KINASES. CC -!- SIMILARITY: BELONGS TO THE IMMUNOGLOBULIN SUPERFAMILY. THE CC EXTRACELLULAR DOMAIN CONTAINS FIVE IG-FOLD 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; HSPDGF03. DR EMBL; M22734; HSPDGF02. DR PIR; A40162; PFHUGA. DR MIM; 173490; TENTH EDITION. DR PROSITE; PS00107; PROTEIN_KINASE_ATP. DR PROSITE; PS00109; PROTEIN_KINASE_TYR. DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III. KW TYROSINE-PROTEIN KINASE; RECEPTOR; TRANSMEMBRANE; GLYCOPROTEIN; KW TRANSFERASE; PHOSPHORYLATION; ATP-BINDING; IMMUNOGLOBULIN FOLD; KW SIGNAL. FT SIGNAL 1 23 FT CHAIN 24 1089 ALPHA PDGF RECEPTOR. FT DOMAIN 24 524 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 525 549 POTENTIAL. FT DOMAIN 550 1089 CYTOPLASMIC, CATALYTIC (POTENTIAL). 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 POTENTIAL. FT CARBOHYD 76 76 POTENTIAL. FT CARBOHYD 103 103 POTENTIAL. FT CARBOHYD 179 179 POTENTIAL. FT CARBOHYD 353 353 POTENTIAL. FT CARBOHYD 359 359 POTENTIAL. FT CARBOHYD 458 458 POTENTIAL. FT CARBOHYD 468 468 POTENTIAL. SQ SEQUENCE 1089 AA; 122669 MW; 6396990 CN; 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 //