ID HGFL_HUMAN Reviewed; 711 AA. AC P26927; A6NLA3; A8MSX3; Q13350; Q14870; Q6GTN4; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 2. DT 08-NOV-2023, entry version 209. DE RecName: Full=Hepatocyte growth factor-like protein; DE AltName: Full=Macrophage stimulatory protein; DE AltName: Full=Macrophage-stimulating protein; DE Short=MSP; DE Contains: DE RecName: Full=Hepatocyte growth factor-like protein alpha chain; DE Contains: DE RecName: Full=Hepatocyte growth factor-like protein beta chain; DE Flags: Precursor; GN Name=MST1; Synonyms=D3F15S2, DNF15S2, HGFL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TYR-13. RC TISSUE=Liver; RX PubMed=1655021; DOI=10.1021/bi00104a029; RA Han S., Stuart L.A., Friezner Degen S.J.; RT "Characterization of the DNF15S2 locus on human chromosome 3: RT identification of a gene coding for four kringle domains with homology to RT hepatocyte growth factor."; RL Biochemistry 30:9768-9780(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=8393443; DOI=10.1016/s0021-9258(18)82279-7; RA Yoshimura T., Yuhki N., Wang M.H., Skeel A., Leonard E.J.; RT "Cloning, sequencing, and expression of human macrophage stimulating RT protein (MSP, MST1) confirms MSP as a member of the family of kringle RT proteins and locates the MSP gene on chromosome 3."; RL J. Biol. Chem. 268:15461-15468(1993). RN [3] 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., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., 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., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 230-247; 288-310; 326-341; 484-501; 530-552; 574-596 RP AND 602-611, AND SUBUNIT. RC TISSUE=Plasma; RX PubMed=1827141; DOI=10.1084/jem.173.5.1227; RA Skeel A., Yoshimura T., Showalter S.D., Tanaka S., Appella E., RA Leonard E.J.; RT "Macrophage stimulating protein: purification, partial amino acid sequence, RT and cellular activity."; RL J. Exp. Med. 173:1227-1234(1991). RN [6] RP INTERACTION WITH MST1R. RX PubMed=9202013; DOI=10.1074/jbc.272.27.16999; RA Wang M.H., Julian F.M., Breathnach R., Godowski P.J., Takehara T., RA Yoshikawa W., Hagiya M., Leonard E.J.; RT "Macrophage stimulating protein (MSP) binds to its receptor via the MSP RT beta chain."; RL J. Biol. Chem. 272:16999-17004(1997). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [8] RP POSSIBLE INVOLVEMENT IN INFLAMMATORY BOWEL DISEASE, AND VARIANT CYS-689. RX PubMed=19079170; DOI=10.1038/mi.2007.15; RA Goyette P., Lefebvre C., Ng A., Brant S.R., Cho J.H., Duerr R.H., RA Silverberg M.S., Taylor K.D., Latiano A., Aumais G., Deslandres C., RA Jobin G., Annese V., Daly M.J., Xavier R.J., Rioux J.D.; RT "Gene-centric association mapping of chromosome 3p implicates MST1 in IBD RT pathogenesis."; RL Mucosal Immunol. 1:131-138(2008). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-615. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP POSSIBLE INVOLVEMENT IN INFLAMMATORY BOWEL DISEASE, AND VARIANT CYS-689. RX PubMed=20228799; DOI=10.1038/ng.549; RA McGovern D.P., Gardet A., Torkvist L., Goyette P., Essers J., Taylor K.D., RA Neale B.M., Ong R.T., Lagace C., Li C., Green T., Stevens C.R., RA Beauchamp C., Fleshner P.R., Carlson M., D'Amato M., Halfvarson J., RA Hibberd M.L., Lordal M., Padyukov L., Andriulli A., Colombo E., Latiano A., RA Palmieri O., Bernard E.J., Deslandres C., Hommes D.W., de Jong D.J., RA Stokkers P.C., Weersma R.K., Sharma Y., Silverberg M.S., Cho J.H., Wu J., RA Roeder K., Brant S.R., Schumm L.P., Duerr R.H., Dubinsky M.C., Glazer N.L., RA Haritunians T., Ippoliti A., Melmed G.Y., Siscovick D.S., RA Vasiliauskas E.A., Targan S.R., Annese V., Wijmenga C., Pettersson S., RA Rotter J.I., Xavier R.J., Daly M.J., Rioux J.D., Seielstad M.; RT "Genome-wide association identifies multiple ulcerative colitis RT susceptibility loci."; RL Nat. Genet. 42:332-337(2010). RN [11] RP PROTEOLYTIC CLEAVAGE. RX PubMed=21875933; DOI=10.1158/1541-7786.mcr-11-0004; RA Ganesan R., Kolumam G.A., Lin S.J., Xie M.H., Santell L., Wu T.D., RA Lazarus R.A., Chaudhuri A., Kirchhofer D.; RT "Proteolytic activation of pro-macrophage-stimulating protein by hepsin."; RL Mol. Cancer Res. 9:1175-1186(2011). RN [12] RP INTERACTION WITH MST1R, AND CHARACTERIZATION OF VARIANT CYS-689. RX PubMed=22087277; DOI=10.1371/journal.pone.0027269; RA Gorlatova N., Chao K., Pal L.R., Araj R.H., Galkin A., Turko I., Moult J., RA Herzberg O.; RT "Protein characterization of a candidate mechanism SNP for Crohn's disease: RT the macrophage stimulating protein R689C substitution."; RL PLoS ONE 6:E27269-E27269(2011). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 465-711, AND INTERCHAIN DISULFIDE RP BOND. RX PubMed=16279944; DOI=10.1111/j.1742-4658.2005.04968.x; RA Carafoli F., Chirgadze D.Y., Blundell T.L., Gherardi E.; RT "Crystal structure of the beta-chain of human hepatocyte growth factor- RT like/macrophage stimulating protein."; RL FEBS J. 272:5799-5807(2005). CC -!- SUBUNIT: Dimer of an alpha chain and a beta chain linked by a disulfide CC bond. Interacts (via beta chain) with MST1R (via SEMA domain). CC {ECO:0000269|PubMed:1827141, ECO:0000269|PubMed:22087277, CC ECO:0000269|PubMed:9202013}. CC -!- INTERACTION: CC P26927; Q04912: MST1R; NbExp=5; IntAct=EBI-6929133, EBI-2637518; CC P26927; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-6929133, EBI-2854842; CC P26927; Q15831: STK11; NbExp=2; IntAct=EBI-6929133, EBI-306838; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: Cleaved after Arg-483, probably by HPN/Hepsin, to yield the active CC form consisting of two disulfide-linked chains. CC -!- DISEASE: Note=MST1 variant Cys-689 may be associated with inflammatory CC bowel disease (IBD), a chronic, relapsing inflammation of the CC gastrointestinal tract with a complex etiology. It is unsure whether CC Cys-689 itself or a variation in linkage disequilibrium with Cys-689 is CC responsible for the association with IBD. {ECO:0000269|PubMed:19079170, CC ECO:0000269|PubMed:20228799}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- CAUTION: Although related to peptidase S1 family, the active site CC residues characteristic of serine proteases appear to be absent from CC this protein, which may therefore lack protease activity. CC {ECO:0000305}. 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; M74178; AAA50165.1; -; mRNA. DR EMBL; U37055; AAC50471.1; -; Genomic_DNA. DR EMBL; L11924; AAA59872.1; -; mRNA. DR EMBL; AC099668; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC048330; AAH48330.1; -; mRNA. DR PIR; A40331; A47136. DR RefSeq; NP_066278.3; NM_020998.3. DR PDB; 2ASU; X-ray; 1.85 A; A=465-483, B=484-711. DR PDB; 4QT8; X-ray; 3.00 A; C/D=465-711. DR PDBsum; 2ASU; -. DR PDBsum; 4QT8; -. DR AlphaFoldDB; P26927; -. DR SMR; P26927; -. DR BioGRID; 110591; 16. DR DIP; DIP-6028N; -. DR IntAct; P26927; 9. DR MINT; P26927; -. DR STRING; 9606.ENSP00000414287; -. DR BindingDB; P26927; -. DR ChEMBL; CHEMBL6042; -. DR MEROPS; S01.975; -. DR GlyConnect; 1310; 5 N-Linked glycans (5 sites). DR GlyCosmos; P26927; 6 sites, 7 glycans. DR GlyGen; P26927; 6 sites, 6 N-linked glycans (5 sites), 1 O-linked glycan (1 site). DR iPTMnet; P26927; -. DR PhosphoSitePlus; P26927; -. DR BioMuta; MST1; -. DR DMDM; 147744563; -. DR CPTAC; non-CPTAC-2672; -. DR jPOST; P26927; -. DR MassIVE; P26927; -. DR MaxQB; P26927; -. DR PaxDb; 9606-ENSP00000414287; -. DR PeptideAtlas; P26927; -. DR ProteomicsDB; 54368; -. DR CPTC; P26927; 1 antibody. DR DNASU; 4485; -. DR GeneID; 4485; -. DR KEGG; hsa:4485; -. DR AGR; HGNC:7380; -. DR CTD; 4485; -. DR DisGeNET; 4485; -. DR GeneCards; MST1; -. DR HGNC; HGNC:7380; MST1. DR MalaCards; MST1; -. DR MIM; 142408; gene. DR neXtProt; NX_P26927; -. DR Orphanet; 171; Primary sclerosing cholangitis. DR PharmGKB; PA31185; -. DR eggNOG; ENOG502QRJ0; Eukaryota. DR InParanoid; P26927; -. DR OrthoDB; 211181at2759; -. DR PhylomeDB; P26927; -. DR PathwayCommons; P26927; -. DR Reactome; R-HSA-8852405; Signaling by MST1. DR SignaLink; P26927; -. DR SIGNOR; P26927; -. DR BioGRID-ORCS; 4485; 323 hits in 1111 CRISPR screens. DR ChiTaRS; MST1; human. DR EvolutionaryTrace; P26927; -. DR GeneWiki; MST1; -. DR GenomeRNAi; 4485; -. DR Pharos; P26927; Tchem. DR PRO; PR:P26927; -. DR Proteomes; UP000005640; Unplaced. DR RNAct; P26927; Protein. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IDA:UniProtKB. DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; IDA:UniProtKB. DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central. DR CDD; cd00108; KR; 4. DR CDD; cd01099; PAN_AP_HGF; 1. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1. DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR024174; HGF/MST1. DR InterPro; IPR000001; Kringle. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR018056; Kringle_CS. DR InterPro; IPR038178; Kringle_sf. DR InterPro; IPR043575; MSP_HGFL. DR InterPro; IPR003609; Pan_app. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR PANTHER; PTHR24261:SF12; HEPATOCYTE GROWTH FACTOR-LIKE PROTEIN-RELATED; 1. DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1. DR Pfam; PF00051; Kringle; 4. DR Pfam; PF00024; PAN_1; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001152; HGF_MST1; 1. DR PIRSF; PIRSF500185; MSP_HGFL; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00018; KRINGLE. DR SMART; SM00130; KR; 4. DR SMART; SM00473; PAN_AP; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1. DR SUPFAM; SSF57440; Kringle-like; 4. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS00021; KRINGLE_1; 4. DR PROSITE; PS50070; KRINGLE_2; 4. DR PROSITE; PS50948; PAN; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Kringle; Reference proteome; Repeat; Secreted; Serine protease homolog; KW Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..711 FT /note="Hepatocyte growth factor-like protein" FT /id="PRO_0000028085" FT CHAIN 19..483 FT /note="Hepatocyte growth factor-like protein alpha chain" FT /evidence="ECO:0000305" FT /id="PRO_0000028086" FT CHAIN 484..711 FT /note="Hepatocyte growth factor-like protein beta chain" FT /evidence="ECO:0000305" FT /id="PRO_0000028087" FT DOMAIN 21..105 FT /note="PAN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315" FT DOMAIN 110..186 FT /note="Kringle 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 191..268 FT /note="Kringle 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 283..361 FT /note="Kringle 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 370..448 FT /note="Kringle 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 484..709 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT CARBOHYD 72 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 296 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 615 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 56..78 FT /evidence="ECO:0000250" FT DISULFID 60..66 FT /evidence="ECO:0000250" FT DISULFID 110..186 FT /evidence="ECO:0000250" FT DISULFID 131..169 FT /evidence="ECO:0000250" FT DISULFID 157..181 FT /evidence="ECO:0000250" FT DISULFID 191..268 FT /evidence="ECO:0000250" FT DISULFID 194..324 FT /evidence="ECO:0000250" FT DISULFID 212..251 FT /evidence="ECO:0000250" FT DISULFID 240..263 FT /evidence="ECO:0000250" FT DISULFID 283..361 FT /evidence="ECO:0000250" FT DISULFID 304..343 FT /evidence="ECO:0000250" FT DISULFID 332..355 FT /evidence="ECO:0000250" FT DISULFID 370..448 FT /evidence="ECO:0000250" FT DISULFID 391..431 FT /evidence="ECO:0000250" FT DISULFID 419..443 FT /evidence="ECO:0000250" FT DISULFID 468..588 FT /note="Interchain (between alpha and beta chains)" FT DISULFID 507..523 FT /evidence="ECO:0000250" FT DISULFID 602..667 FT /evidence="ECO:0000250" FT DISULFID 632..646 FT /evidence="ECO:0000250" FT DISULFID 657..685 FT /evidence="ECO:0000250" FT VARIANT 13 FT /note="C -> Y" FT /evidence="ECO:0000269|PubMed:1655021" FT /id="VAR_006631" FT VARIANT 212 FT /note="C -> F" FT /id="VAR_006632" FT VARIANT 551 FT /note="S -> G (in dbSNP:rs6791037)" FT /id="VAR_059787" FT VARIANT 689 FT /note="R -> C (may be associated with inflammatory bowel FT disease; results in reduced binding affinity to MST1R; FT dbSNP:rs3197999)" FT /evidence="ECO:0000269|PubMed:19079170, FT ECO:0000269|PubMed:20228799, ECO:0000269|PubMed:22087277" FT /id="VAR_070224" FT CONFLICT 292 FT /note="R -> G (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 304 FT /note="C -> E (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 306 FT /note="R -> E (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 550 FT /note="Missing (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 593 FT /note="W -> E (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="L -> F (in Ref. 2; AAA59872)" FT /evidence="ECO:0000305" FT TURN 475..479 FT /evidence="ECO:0007829|PDB:4QT8" FT STRAND 495..499 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 505..513 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 516..520 FT /evidence="ECO:0007829|PDB:2ASU" FT HELIX 521..523 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 535..539 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 541..544 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 553..562 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 569..576 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 581..584 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 601..608 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 620..627 FT /evidence="ECO:0007829|PDB:2ASU" FT HELIX 629..635 FT /evidence="ECO:0007829|PDB:2ASU" FT TURN 636..638 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 644..647 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 651..653 FT /evidence="ECO:0007829|PDB:4QT8" FT STRAND 664..669 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 672..679 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 683..686 FT /evidence="ECO:0007829|PDB:2ASU" FT STRAND 692..696 FT /evidence="ECO:0007829|PDB:2ASU" FT HELIX 697..699 FT /evidence="ECO:0007829|PDB:2ASU" FT HELIX 701..707 FT /evidence="ECO:0007829|PDB:2ASU" SQ SEQUENCE 711 AA; 80320 MW; 2E4B3C7D4AA9B566 CRC64; MGWLPLLLLL TQCLGVPGQR SPLNDFQVLR GTELQHLLHA VVPGPWQEDV ADAEECAGRC GPLMDCRAFH YNVSSHGCQL LPWTQHSPHT RLRRSGRCDL FQKKDYVRTC IMNNGVGYRG TMATTVGGLP CQAWSHKFPN DHKYTPTLRN GLEENFCRNP DGDPGGPWCY TTDPAVRFQS CGIKSCREAA CVWCNGEEYR GAVDRTESGR ECQRWDLQHP HQHPFEPGKF LDQGLDDNYC RNPDGSERPW CYTTDPQIER EFCDLPRCGS EAQPRQEATT VSCFRGKGEG YRGTANTTTA GVPCQRWDAQ IPHQHRFTPE KYACKDLREN FCRNPDGSEA PWCFTLRPGM RAAFCYQIRR CTDDVRPQDC YHGAGEQYRG TVSKTRKGVQ CQRWSAETPH KPQFTFTSEP HAQLEENFCR NPDGDSHGPW CYTMDPRTPF DYCALRRCAD DQPPSILDPP DQVQFEKCGK RVDRLDQRRS KLRVVGGHPG NSPWTVSLRN RQGQHFCGGS LVKEQWILTA RQCFSSCHMP LTGYEVWLGT LFQNPQHGEP SLQRVPVAKM VCGPSGSQLV LLKLERSVTL NQRVALICLP PEWYVVPPGT KCEIAGWGET KGTGNDTVLN VALLNVISNQ ECNIKHRGRV RESEMCTEGL LAPVGACEGD YGGPLACFTH NCWVLEGIII PNRVCARSRW PAVFTRVSVF VDWIHKVMRL G //