HGFL_HUMAN
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 25-MAY-2022, entry version 203.
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}.
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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; 15.
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 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; P26927; -.
DR PeptideAtlas; P26927; -.
DR PRIDE; P26927; -.
DR ProteomicsDB; 54368; -.
DR CPTC; P26927; 1 antibody.
DR DNASU; 4485; -.
DR GeneID; 4485; -.
DR KEGG; hsa:4485; -.
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; 164039at2759; -.
DR PhylomeDB; P26927; -.
DR PathwayCommons; P26927; -.
DR Reactome; R-HSA-8852405; Signaling by MST1.
DR SignaLink; P26927; -.
DR SIGNOR; P26927; -.
DR BioGRID-ORCS; 4485; 301 hits in 1034 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:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0035978; P:histone H2A-S139 phosphorylation; IDA:CACAO.
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; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.20.10; -; 4.
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 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 SMART; SM00130; KR; 4.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 4.
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
