ID RON_HUMAN Reviewed; 1400 AA. AC Q04912; B5A944; B5A945; B5A946; B5A947; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 2. DT 21-SEP-2011, entry version 127. DE RecName: Full=Macrophage-stimulating protein receptor; DE Short=MSP receptor; DE EC=2.7.10.1; DE AltName: Full=CDw136; DE AltName: Full=Protein-tyrosine kinase 8; DE AltName: Full=p185-Ron; DE AltName: CD_antigen=CD136; DE Contains: DE RecName: Full=Macrophage-stimulating protein receptor alpha chain; DE Contains: DE RecName: Full=Macrophage-stimulating protein receptor beta chain; DE Flags: Precursor; GN Name=MST1R; Synonyms=PTK8, RON; 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 RON), AND VARIANTS GLN-322; RP ARG-523 AND GLY-1195. RC TISSUE=Keratinocyte; RX MEDLINE=93241719; PubMed=8386824; RA Ronsin C., Muscatelli F., Mattei M.-G., Breathnach R.; RT "A novel putative receptor protein tyrosine kinase of the met RT family."; RL Oncogene 8:1195-1202(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RX MEDLINE=96413302; PubMed=8816464; RA Collesi C., Santoro M.M., Gaudino G., Comoglio P.M.; RT "A splicing variant of the RON transcript induces constitutive RT tyrosine kinase activity and an invasive phenotype."; RL Mol. Cell. Biol. 16:5518-5526(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RON-1; RON-2; RON-3 AND RON-4). RX PubMed=18593464; DOI=10.1186/ar2447; RA Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., RA Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.; RT "Novel splice variants derived from the receptor tyrosine kinase RT superfamily are potential therapeutics for rheumatoid arthritis."; RL Arthritis Res. Ther. 10:R73-R73(2008). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP FUNCTION. RX MEDLINE=95025877; PubMed=7939629; DOI=10.1126/science.7939629; RA Wang M.-H., Ronsin C., Gesnel M.-C., Coupey L., Skeel A., RA Leonard E.J., Breatnach R.; RT "Identification of the ron gene product as the receptor for the human RT macrophage stimulating protein."; RL Science 266:117-119(1994). RN [6] RP INTERACTION WITH HYAL2. RX PubMed=12676986; DOI=10.1073/pnas.0837136100; RA Danilkovitch-Miagkova A., Duh F.-M., Kuzmin I., Angeloni D., RA Liu S.-L., Miller A.D., Lerman M.I.; RT "Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and RT mediates transformation of epithelial cells by jaagsiekte sheep RT retrovirus."; RL Proc. Natl. Acad. Sci. U.S.A. 100:4580-4585(2003). RN [7] RP INTERACTION WITH PLXNB1. RX PubMed=15184888; DOI=10.1038/sj.onc.1207650; RA Conrotto P., Corso S., Gamberini S., Comoglio P.M., Giordano S.; RT "Interplay between scatter factor receptors and B plexins controls RT invasive growth."; RL Oncogene 23:5131-5137(2004). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1060-1357 IN COMPLEX WITH RP AMP-PNP AND MAGNESIUM, ACTIVE SITE, AND PHOSPHORYLATION AT TYR-1238. RX PubMed=20726546; DOI=10.1021/bi100409w; RA Wang J., Steinbacher S., Augustin M., Schreiner P., Epstein D., RA Mulvihill M.J., Crew A.P.; RT "The crystal structure of a constitutively active mutant RON kinase RT suggests an intramolecular autophosphorylation hypothesis."; RL Biochemistry 49:7972-7974(2010). RN [9] RP VARIANTS [LARGE SCALE ANALYSIS] SER-75; THR-95; CYS-185; GLN-322; RP ASP-356; LEU-434; ASP-465; CYS-504; ARG-523; PRO-613; MET-900; RP GLY-1304; GLY-1335 AND CYS-1360. 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 for macrophage stimulating protein (MSP). Has a CC tyrosine-protein kinase activity. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- SUBUNIT: Heterodimer formed of an alpha chain and a beta chain CC which are disulfide linked. Binds PLXNB1. Associates with and is CC negatively regulated by HYAL2. CC -!- INTERACTION: CC O43157:PLXNB1; NbExp=3; IntAct=EBI-2637518, EBI-1111488; CC O15031:PLXNB2; NbExp=2; IntAct=EBI-2637518, EBI-722004; CC Q9ULL4:PLXNB3; NbExp=2; IntAct=EBI-2637518, EBI-311073; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=RON; CC IsoId=Q04912-1; Sequence=Displayed; CC Name=Delta-RON; CC IsoId=Q04912-2; Sequence=VSP_005007; CC Note=Lacks part of the extracellular domain, oligomerizes and is CC constitutively activated; CC Name=RON-1; CC IsoId=Q04912-3; Sequence=VSP_038920, VSP_038921; CC Name=RON-2; CC IsoId=Q04912-4; Sequence=VSP_038919, VSP_038922, VSP_038923; CC Name=RON-3; CC IsoId=Q04912-5; Sequence=VSP_038924, VSP_038925; CC Name=RON-4; CC IsoId=Q04912-6; Sequence=VSP_038922, VSP_038923; CC -!- TISSUE SPECIFICITY: Keratinocytes and lung. CC -!- PTM: Proteolytic processing yields the two subunits. CC -!- PTM: Phosphorylated in response to ligand binding (Probable). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. CC -!- SIMILARITY: Contains 3 IPT/TIG domains. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SIMILARITY: Contains 1 Sema domain. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/RONID287.html"; 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; X70040; CAA49634.1; -; mRNA. DR EMBL; EU826582; ACF47618.1; -; mRNA. DR EMBL; EU826583; ACF47619.1; -; mRNA. DR EMBL; EU826584; ACF47620.1; -; mRNA. DR EMBL; EU826585; ACF47621.1; -; mRNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR IPI; IPI00030273; -. DR IPI; IPI00219706; -. DR IPI; IPI00910383; -. DR IPI; IPI00926020; -. DR IPI; IPI00956299; -. DR IPI; IPI00956695; -. DR PIR; I38185; I38185. DR RefSeq; NP_002438.2; NM_002447.2. DR UniGene; Hs.517973; -. DR PDB; 3PLS; X-ray; 2.24 A; A=1060-1357. DR PDBsum; 3PLS; -. DR ProteinModelPortal; Q04912; -. DR SMR; Q04912; 45-865, 1060-1357. DR DIP; DIP-6029N; -. DR IntAct; Q04912; 5. DR MINT; MINT-6539690; -. DR STRING; Q04912; -. DR PhosphoSite; Q04912; -. DR PRIDE; Q04912; -. DR Ensembl; ENST00000296474; ENSP00000296474; ENSG00000164078. DR Ensembl; ENST00000344206; ENSP00000341325; ENSG00000164078. DR Ensembl; ENST00000411578; ENSP00000407926; ENSG00000164078. DR Ensembl; ENST00000424150; ENSP00000408047; ENSG00000164078. DR GeneID; 4486; -. DR KEGG; hsa:4486; -. DR UCSC; uc003cxy.2; human. DR CTD; 4486; -. DR GeneCards; GC03M049924; -. DR H-InvDB; HIX0030873; -. DR HGNC; HGNC:7381; MST1R. DR HPA; CAB008972; -. DR HPA; HPA007657; -. DR HPA; HPA008180; -. DR MIM; 600168; gene. DR neXtProt; NX_Q04912; -. DR PharmGKB; PA31186; -. DR eggNOG; prNOG05332; -. DR GeneTree; ENSGT00550000074361; -. DR HOGENOM; HBG445765; -. DR HOVERGEN; HBG006348; -. DR InParanoid; Q04912; -. DR OMA; EQKFVHR; -. DR OrthoDB; EOG4M65GR; -. DR BRENDA; 2.7.10.1; 2681. DR Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling. DR Pathway_Interaction_DB; amb2_neutrophils_pathway; amb2 Integrin signaling. DR NextBio; 17355; -. DR ArrayExpress; Q04912; -. DR Bgee; Q04912; -. DR CleanEx; HS_MST1R; -. DR Genevestigator; Q04912; -. DR GermOnline; ENSG00000164078; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc. DR GO; GO:0006952; P:defense response; TAS:ProtInc. DR GO; GO:0007275; P:multicellular organismal development; IEA:InterPro. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc. DR GO; GO:0007338; P:single fertilization; TAS:ProtInc. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_TIG_rcpt. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR003659; Plexin-like. DR InterPro; IPR016201; Plexin-like_fold. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001627; Semaphorin/CD100_Ag. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4. DR Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF01403; Sema; 1. DR Pfam; PF01833; TIG; 2. DR PIRSF; PIRSF000617; TyrPK_HGF-R; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00429; IPT; 3. DR SMART; SM00423; PSI; 1. DR SMART; SM00630; Sema; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF81296; Ig_E-set; 3. DR SUPFAM; SSF56112; Kinase_like; 1. DR SUPFAM; SSF103575; Plexin-like_fold; 1. DR SUPFAM; SSF101912; Sema; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS51004; SEMA; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; KW Polymorphism; Receptor; Reference proteome; Repeat; Signal; KW Transferase; Transmembrane; Transmembrane helix; KW Tyrosine-protein kinase. FT SIGNAL 1 24 Potential. FT CHAIN 25 1400 Macrophage-stimulating protein receptor. FT /FTId=PRO_0000024452. FT CHAIN 25 304 Macrophage-stimulating protein receptor FT alpha chain (Potential). FT /FTId=PRO_0000024453. FT CHAIN 310 1400 Macrophage-stimulating protein receptor FT beta chain (Potential). FT /FTId=PRO_0000024454. FT TOPO_DOM 25 957 Extracellular (Potential). FT TRANSMEM 958 978 Helical; (Potential). FT TOPO_DOM 979 1400 Cytoplasmic (Potential). FT DOMAIN 31 522 Sema. FT DOMAIN 569 671 IPT/TIG 1. FT DOMAIN 684 767 IPT/TIG 2. FT DOMAIN 770 860 IPT/TIG 3. FT DOMAIN 1082 1345 Protein kinase. FT NP_BIND 1088 1096 ATP. FT NP_BIND 1161 1164 ATP. FT COMPBIAS 306 309 Poly-Arg. FT ACT_SITE 1208 1208 Proton acceptor (Probable). FT BINDING 1114 1114 ATP. FT BINDING 1212 1212 ATP. FT MOD_RES 1238 1238 Phosphotyrosine; by autocatalysis FT (Probable). FT MOD_RES 1353 1353 Phosphotyrosine; by autocatalysis (By FT similarity). FT MOD_RES 1360 1360 Phosphotyrosine; by autocatalysis (By FT similarity). FT CARBOHYD 66 66 N-linked (GlcNAc...) (Potential). FT CARBOHYD 419 419 N-linked (GlcNAc...) (Potential). FT CARBOHYD 458 458 N-linked (GlcNAc...) (Potential). FT CARBOHYD 488 488 N-linked (GlcNAc...) (Potential). FT CARBOHYD 654 654 N-linked (GlcNAc...) (Potential). FT CARBOHYD 720 720 N-linked (GlcNAc...) (Potential). FT CARBOHYD 841 841 N-linked (GlcNAc...) (Potential). FT CARBOHYD 897 897 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 411 516 Missing (in isoform RON-2). FT /FTId=VSP_038919. FT VAR_SEQ 475 495 ELVRSLNYLLYVSNFSLGDSG -> GPHPHSPLALGPCLHP FT HFAHI (in isoform RON-1). FT /FTId=VSP_038920. FT VAR_SEQ 496 1400 Missing (in isoform RON-1). FT /FTId=VSP_038921. FT VAR_SEQ 628 647 PVPRKDFVEEFECELEPLGT -> YNLVPPLPFPEGGNQAA FT PSP (in isoform RON-2 and isoform RON-4). FT /FTId=VSP_038922. FT VAR_SEQ 648 1400 Missing (in isoform RON-2 and isoform FT RON-4). FT /FTId=VSP_038923. FT VAR_SEQ 884 932 Missing (in isoform Delta-RON). FT /FTId=VSP_005007. FT VAR_SEQ 884 907 YIGLGAVADCVGINVTVGGESCQH -> VSVRDRGRDSWGS FT ESRGQPTGWSS (in isoform RON-3). FT /FTId=VSP_038924. FT VAR_SEQ 908 1400 Missing (in isoform RON-3). FT /FTId=VSP_038925. FT VARIANT 75 75 R -> S (in dbSNP:rs35887539). FT /FTId=VAR_041768. FT VARIANT 95 95 P -> T (in dbSNP:rs55908300). FT /FTId=VAR_041769. FT VARIANT 185 185 R -> C (in dbSNP:rs55633379). FT /FTId=VAR_041770. FT VARIANT 322 322 R -> Q (in dbSNP:rs2230593). FT /FTId=VAR_006350. FT VARIANT 356 356 G -> D (in dbSNP:rs35924402). FT /FTId=VAR_041771. FT VARIANT 434 434 S -> L (in dbSNP:rs2230591). FT /FTId=VAR_029238. FT VARIANT 440 440 N -> S (in dbSNP:rs2230592). FT /FTId=VAR_029239. FT VARIANT 465 465 G -> D (in dbSNP:rs34564898). FT /FTId=VAR_041772. FT VARIANT 504 504 R -> C (in dbSNP:rs34350470). FT /FTId=VAR_041773. FT VARIANT 523 523 Q -> R (in dbSNP:rs2230590). FT /FTId=VAR_041774. FT VARIANT 613 613 Q -> P (in dbSNP:rs35986685). FT /FTId=VAR_041775. FT VARIANT 900 900 V -> M (in dbSNP:rs56091918). FT /FTId=VAR_041776. FT VARIANT 1195 1195 S -> G (in dbSNP:rs7433231). FT /FTId=VAR_061749. FT VARIANT 1304 1304 R -> G. FT /FTId=VAR_041777. FT VARIANT 1335 1335 R -> G (in dbSNP:rs1062633). FT /FTId=VAR_024577. FT VARIANT 1360 1360 Y -> C (in dbSNP:rs56330223). FT /FTId=VAR_041778. FT CONFLICT 209 209 A -> G (in Ref. 1; CAA49634). FT CONFLICT 813 813 R -> RQ (in Ref. 3; ACF47620). FT HELIX 1064 1069 FT HELIX 1071 1073 FT HELIX 1077 1079 FT STRAND 1104 1106 FT STRAND 1112 1115 FT HELIX 1122 1130 FT STRAND 1158 1161 FT HELIX 1169 1174 FT HELIX 1182 1187 FT TURN 1191 1193 FT HELIX 1197 1201 FT HELIX 1211 1213 FT STRAND 1214 1216 FT STRAND 1222 1224 FT TURN 1232 1235 FT HELIX 1236 1239 FT HELIX 1250 1254 FT HELIX 1256 1259 FT HELIX 1266 1272 FT HELIX 1276 1282 FT TURN 1287 1290 FT HELIX 1293 1295 FT HELIX 1296 1301 FT HELIX 1314 1323 FT HELIX 1328 1330 FT HELIX 1334 1337 FT HELIX 1341 1347 SQ SEQUENCE 1400 AA; 152271 MW; EB5CA79ABC69A882 CRC64; MELLPPLPQS FLLLLLLPAK PAAGEDWQCP RTPYAASRDF DVKYVVPSFS AGGLVQAMVT YEGDRNESAV FVAIRNRLHV LGPDLKSVQS LATGPAGDPG CQTCAACGPG PHGPPGDTDT KVLVLDPALP ALVSCGSSLQ GRCFLHDLEP QGTAVHLAAP ACLFSAHHNR PDDCPDCVAS PLGTRVTVVE QGQASYFYVA SSLDAAVAAS FSPRSVSIRR LKADASGFAP GFVALSVLPK HLVSYSIEYV HSFHTGAFVY FLTVQPASVT DDPSALHTRL ARLSATEPEL GDYRELVLDC RFAPKRRRRG APEGGQPYPV LRVAHSAPVG AQLATELSIA EGQEVLFGVF VTGKDGGPGV GPNSVVCAFP IDLLDTLIDE GVERCCESPV HPGLRRGLDF FQSPSFCPNP PGLEALSPNT SCRHFPLLVS SSFSRVDLFN GLLGPVQVTA LYVTRLDNVT VAHMGTMDGR ILQVELVRSL NYLLYVSNFS LGDSGQPVQR DVSRLGDHLL FASGDQVFQV PIQGPGCRHF LTCGRCLRAW HFMGCGWCGN MCGQQKECPG SWQQDHCPPK LTEFHPHSGP LRGSTRLTLC GSNFYLHPSG LVPEGTHQVT VGQSPCRPLP KDSSKLRPVP RKDFVEEFEC ELEPLGTQAV GPTNVSLTVT NMPPGKHFRV DGTSVLRGFS FMEPVLIAVQ PLFGPRAGGT CLTLEGQSLS VGTSRAVLVN GTECLLARVS EGQLLCATPP GATVASVPLS LQVGGAQVPG SWTFQYREDP VVLSISPNCG YINSHITICG QHLTSAWHLV LSFHDGLRAV ESRCERQLPE QQLCRLPEYV VRDPQGWVAG NLSARGDGAA GFTLPGFRFL PPPHPPSANL VPLKPEEHAI KFEYIGLGAV ADCVGINVTV GGESCQHEFR GDMVVCPLPP SLQLGQDGAP LQVCVDGECH ILGRVVRPGP DGVPQSTLLG ILLPLLLLVA ALATALVFSY WWRRKQLVLP PNLNDLASLD QTAGATPLPI LYSGSDYRSG LALPAIDGLD STTCVHGASF SDSEDESCVP LLRKESIQLR DLDSALLAEV KDVLIPHERV VTHSDRVIGK GHFGVVYHGE YIDQAQNRIQ CAIKSLSRIT EMQQVEAFLR EGLLMRGLNH PNVLALIGIM LPPEGLPHVL LPYMCHGDLL QFIRSPQRNP TVKDLISFGL QVARSMEYLA EQKFVHRDLA ARNCMLDESF TVKVADFGLA RDILDREYYS VQQHRHARLP VKWMALESLQ TYRFTTKSDV WSFGVLLWEL LTRGAPPYRH IDPFDLTHFL AQGRRLPQPE YCPDSLYQVM QQCWEADPAV RPTFRVLVGE VEQIVSALLG DHYVQLPATY MNLGPSTSHE MNVRPEQPQF SPMPGNVRRP RPLSEPPRPT //