ID PGFRA_HUMAN Reviewed; 1089 AA. AC P16234; B2RE69; Q96KZ7; Q9UD28; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-MAY-2011, entry version 133. DE RecName: Full=Alpha-type platelet-derived growth factor receptor; DE Short=PDGF-R-alpha; DE EC=2.7.10.1; DE AltName: Full=CD140 antigen-like family member A; DE AltName: Full=CD140a antigen; DE AltName: CD_antigen=CD140a; DE Flags: Precursor; GN Name=PDGFRA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Foreskin; RX MEDLINE=89296915; PubMed=2544881; DOI=10.1073/pnas.86.13.4917; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX MEDLINE=89130149; PubMed=2536956; DOI=10.1126/science.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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Blood; RX MEDLINE=96163874; PubMed=8586421; DOI=10.1006/geno.1995.9883; 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 1), AND VARIANT RP PRO-478. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 823-876, AND TISSUE SPECIFICITY. RC TISSUE=Colon tumor; RX MEDLINE=95204052; PubMed=7896447; DOI=10.1002/ijc.2910600611; RA Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., RA Srivastava S., Varnum B., Liu E.T., Cance W.G.; RT "Receptor tyrosine kinases expressed in metastatic colon cancer."; RL Int. J. Cancer 60:791-797(1995). RN [8] RP INTERACTION WITH SHF, AND PROBABLE PHOSPHORYLATION AT TYR-720. RX MEDLINE=20548990; PubMed=11095946; DOI=10.1006/bbrc.2000.3847; RA Lindholm C.K., Frantz J.D., Shoelson S.E., Welsh M.; RT "Shf, a Shb-like adapter protein, is involved in PDGF-alpha-receptor RT regulation of apoptosis."; RL Biochem. Biophys. Res. Commun. 278:537-543(2000). RN [9] RP INVOLVEMENT IN HES. 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-762; TYR-768; TYR-849 RP AND TYR-1018, AND MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [11] 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). RN [12] RP VARIANTS [LARGE SCALE ANALYSIS] ASP-79; ASP-426; PRO-478; CYS-764; RP ARG-829; LYS-996 AND ASN-1071. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Receptor that binds both PDGFA and PDGFB and has a CC tyrosine-protein kinase activity. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- SUBUNIT: Homodimer, and heterodimer with PDGFRB. Interacts with CC the SH2 domain of SHB via phosphorylated Tyr-720 (By similarity). CC Interacts with the SH2 domain of SHF via phosphorylated Tyr-720. 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 -!- TISSUE SPECIFICITY: Expressed in primary and metastatic colon CC tumors and in normal colon tissue. Tumors may express a different CC isoform to that found in normal tissue. CC -!- DISEASE: Note=A chromosomal aberration involving PDGFRA is found CC in some cases of hypereosinophilic syndrome. Interstitial CC chromosomal deletion del(4)(q12q12) causes the fusion of FIP1L1 CC and PDGFRA (FIP1L1-PDGFRA). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. CSF-1/PDGF receptor subfamily. CC -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like) CC domains. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAP69563.1; Type=Erroneous initiation; 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; M22734; AAA60048.1; -; mRNA. DR EMBL; M21574; AAA96715.1; -; mRNA. DR EMBL; D50017; BAA08742.1; -; Genomic_DNA. DR EMBL; AK316578; BAG38166.1; -; mRNA. DR EMBL; BC015186; AAH15186.1; -; mRNA. DR EMBL; AY229892; AAP69563.1; ALT_INIT; mRNA. DR IPI; IPI00027721; -. DR IPI; IPI00336178; -. DR PIR; A40162; PFHUGA. DR RefSeq; NP_006197.1; NM_006206.4. DR UniGene; Hs.74615; -. DR PDB; 1GQ5; X-ray; 2.20 A; -. DR PDBsum; 1GQ5; -. DR ProteinModelPortal; P16234; -. DR SMR; P16234; 25-516, 547-956. DR DIP; DIP-5736N; -. DR IntAct; P16234; 1. DR STRING; P16234; -. DR PhosphoSite; P16234; -. DR PRIDE; P16234; -. DR Ensembl; ENST00000257290; ENSP00000257290; ENSG00000134853. DR GeneID; 5156; -. DR KEGG; hsa:5156; -. DR UCSC; uc003hal.2; human. DR UCSC; uc003han.2; human. DR CTD; 5156; -. DR GeneCards; GC04P051043; -. DR H-InvDB; HIX0004218; -. DR HGNC; HGNC:8803; PDGFRA. DR HPA; CAB018143; -. DR MIM; 173490; gene. DR MIM; 607685; phenotype. DR neXtProt; NX_P16234; -. DR Orphanet; 513; Acute lymphoblastic leukemia. DR Orphanet; 44890; Gastrointestinal stromal tumor. DR Orphanet; 168956; Hypereosinophilic syndromes. DR Orphanet; 168947; Myeloid neoplasm associated with PDGFRA rearrangement. DR PharmGKB; PA33147; -. DR eggNOG; prNOG04413; -. DR GeneTree; ENSGT00600000084056; -. DR HOGENOM; HBG445154; -. DR HOVERGEN; HBG004335; -. DR InParanoid; P16234; -. DR OMA; YIGVTYK; -. DR OrthoDB; EOG4XWFX0; -. DR PhylomeDB; P16234; -. DR BRENDA; 2.7.10.1; 2681. DR Pathway_Interaction_DB; pdgfrapathway; PDGFR-alpha signaling pathway. DR Reactome; REACT_16888; Signaling by PDGF. DR DrugBank; DB00102; Becaplermin. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB01268; Sunitinib. DR NextBio; 19946; -. DR ArrayExpress; P16234; -. DR Bgee; P16234; -. DR CleanEx; HS_PDGFRA; -. DR Genevestigator; P16234; -. DR GermOnline; ENSG00000134853; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005887; C:integral to plasma membrane; IDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:BHF-UCL. DR GO; GO:0048407; F:platelet-derived growth factor binding; IPI:BHF-UCL. DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IDA:BHF-UCL. DR GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB. DR GO; GO:0001775; P:cell activation; TAS:BHF-UCL. DR GO; GO:0001553; P:luteinization; ISS:UniProtKB. DR GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:BHF-UCL. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL. DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL. DR GO; GO:0046777; P:protein autophosphorylation; IDA:BHF-UCL. DR GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr-Pkinase. DR InterPro; IPR020635; Tyr_Pkinase_cat_dom. DR InterPro; IPR008266; Tyr_prot_kinase_AS. DR InterPro; IPR016243; Tyr_prot_kinase_CSF1/PDGF_rcpt. DR InterPro; IPR001824; Tyr_prot_kinase_rcpt_3_CS. DR InterPro; IPR009134; Tyr_prot_kinase_VEGFR_rcpt_N. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 5. DR Pfam; PF07679; I-set; 2. DR Pfam; PF07714; Pkinase_Tyr; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1. DR PRINTS; PR01832; VEGFRECEPTOR. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF56112; Kinase_like; 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. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome; KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Membrane; KW Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Repeat; KW Signal; Transferase; Transmembrane; Transmembrane helix; KW Tyrosine-protein kinase. FT SIGNAL 1 23 FT CHAIN 24 1089 Alpha-type platelet-derived growth factor FT receptor. FT /FTId=PRO_0000016760. FT TOPO_DOM 24 524 Extracellular (Potential). FT TRANSMEM 525 549 Helical; (Potential). FT TOPO_DOM 550 1089 Cytoplasmic (Potential). FT DOMAIN 24 113 Ig-like C2-type 1. FT DOMAIN 117 201 Ig-like C2-type 2. FT DOMAIN 202 306 Ig-like C2-type 3. FT DOMAIN 319 410 Ig-like C2-type 4. FT DOMAIN 414 517 Ig-like C2-type 5. 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 Proton acceptor (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 720 720 Phosphotyrosine (Probable). FT MOD_RES 762 762 Phosphotyrosine. FT MOD_RES 768 768 Phosphotyrosine. FT MOD_RES 849 849 Phosphotyrosine; by autocatalysis (By FT similarity). FT MOD_RES 1018 1018 Phosphotyrosine. 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 DISULFID 49 100 By similarity. FT DISULFID 150 189 By similarity. FT DISULFID 235 290 By similarity. FT DISULFID 435 501 By similarity. FT VAR_SEQ 210 218 ATSELDLEM -> GTCIISFLL (in isoform 2). FT /FTId=VSP_007833. FT VAR_SEQ 219 1089 Missing (in isoform 2). FT /FTId=VSP_007834. FT VARIANT 79 79 G -> D (in dbSNP:rs36035373). FT /FTId=VAR_042032. FT VARIANT 426 426 G -> D (in dbSNP:rs55865821). FT /FTId=VAR_042033. FT VARIANT 478 478 S -> P (in dbSNP:rs35597368). FT /FTId=VAR_034378. FT VARIANT 764 764 R -> C (in dbSNP:rs34392012). FT /FTId=VAR_042034. FT VARIANT 829 829 G -> R (in a glioblastoma multiforme FT sample; somatic mutation). FT /FTId=VAR_042035. FT VARIANT 996 996 E -> K (in a metastatic melanoma sample; FT somatic mutation). FT /FTId=VAR_042036. FT VARIANT 1071 1071 D -> N (in a lung neuroendocrine FT carcinoma sample; somatic mutation). FT /FTId=VAR_042037. 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 //