HGF_MOUSE
ID HGF_MOUSE Reviewed; 728 AA.
AC Q08048; O55027; Q53WS5; Q61662; Q64007; Q6LBE6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Hepatocyte growth factor;
DE AltName: Full=Hepatopoietin-A;
DE AltName: Full=Scatter factor;
DE Short=SF;
DE Contains:
DE RecName: Full=Hepatocyte growth factor alpha chain;
DE Contains:
DE RecName: Full=Hepatocyte growth factor beta chain;
DE Flags: Precursor;
GN Name=Hgf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PROTEIN SEQUENCE
RP OF 496-504.
RC TISSUE=Mammary fibroblast;
RX PubMed=8135822; DOI=10.1006/bbrc.1994.1296;
RA Sasaki M., Nishio M., Sasaki T., Enami J.;
RT "Identification of mouse mammary fibroblast-derived mammary growth factor
RT as hepatocyte growth factor.";
RL Biochem. Biophys. Res. Commun. 199:772-779(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8081873; DOI=10.3109/15419069309095686;
RA Lee C.C., Kozak C.A., Yamada K.M.;
RT "Structure, genetic mapping, and expression of the mouse Hgf/scatter factor
RT gene.";
RL Cell Adhes. Commun. 1:101-111(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8241272; DOI=10.1016/0167-4781(93)90159-b;
RA Liu Y., Michalopoulos G.K., Zarnegar R.;
RT "Molecular cloning and characterization of cDNA encoding mouse hepatocyte
RT growth factor.";
RL Biochim. Biophys. Acta 1216:299-303(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NK1).
RC TISSUE=Lung;
RX PubMed=9488442; DOI=10.1128/mcb.18.3.1275;
RA Jakubczak J.L., LaRochelle W.J., Merlino G.;
RT "NK1, a natural splice variant of hepatocyte growth factor/scatter factor,
RT is a partial agonist in vivo.";
RL Mol. Cell. Biol. 18:1275-1283(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=SWR/J; TISSUE=Fibroblast;
RA Sharpe M.J.S., Lane K., Gherardi E.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC STRAIN=129;
RX PubMed=7822318; DOI=10.1074/jbc.270.2.830;
RA Plaschke-Schluetter A., Behrens J., Gherardi E., Birchmeier W.;
RT "Characterisation of the scatter factor/hepatocyte growth factor gene
RT promoter: positive and negative regulatory elements direct gene expression
RT to mesenchymal cells.";
RL J. Biol. Chem. 270:830-836(1995).
RN [9]
RP PROTEIN SEQUENCE OF 184-197; 357-367; 375-383 AND 653-666.
RX PubMed=2144630; DOI=10.3181/00379727-195-43115;
RA Rosen E.M., Meromsky L., Setter E., Vinter D.W., Goldberg I.D.;
RT "Purified scatter factor stimulates epithelial and vascular endothelial
RT cell migration.";
RL Proc. Soc. Exp. Biol. Med. 195:34-43(1990).
RN [10]
RP PROTEIN SEQUENCE OF 496-519.
RX PubMed=2142751; DOI=10.1038/346228b0;
RA Gherardi E., Stoker M.;
RT "Hepatocytes and scatter factor.";
RL Nature 346:228-228(1990).
RN [11]
RP PROTEIN SEQUENCE OF 496-519.
RX PubMed=1831975; DOI=10.1042/bj2780035;
RA Coffer A., Fellows J., Young S., Pappin D., Rahman D.;
RT "Purification and characterization of biologically active scatter factor
RT from ras-transformed NIH 3T3 conditioned medium.";
RL Biochem. J. 278:35-41(1991).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 29-210, AND DISULFIDE BONDS.
RX PubMed=17804794; DOI=10.1073/pnas.0704290104;
RA Tolbert W.D., Daugherty J., Gao C., Xie Q., Miranti C., Gherardi E.,
RA Woude G.V., Xu H.E.;
RT "A mechanistic basis for converting a receptor tyrosine kinase agonist to
RT an antagonist.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14592-14597(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-127, DISULFIDE BONDS, AND
RP FUNCTION.
RX PubMed=20624990; DOI=10.1073/pnas.1005183107;
RA Tolbert W.D., Daugherty-Holtrop J., Gherardi E., Vande Woude G., Xu H.E.;
RT "Structural basis for agonism and antagonism of hepatocyte growth factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13264-13269(2010).
CC -!- FUNCTION: Potent mitogen for mature parenchymal hepatocyte cells, seems
CC to be a hepatotrophic factor, and acts as a growth factor for a broad
CC spectrum of tissues and cell types. Activating ligand for the receptor
CC tyrosine kinase MET by binding to it and promoting its dimerization.
CC {ECO:0000269|PubMed:20624990}.
CC -!- SUBUNIT: Dimer of an alpha chain and a beta chain linked by a disulfide
CC bond. Interacts with SRPX2; the interaction increases HGF mitogenic
CC activity.
CC -!- INTERACTION:
CC Q08048; P08581: MET; Xeno; NbExp=3; IntAct=EBI-15655650, EBI-1039152;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Long;
CC IsoId=Q08048-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q08048-2; Sequence=VSP_005408;
CC Name=NK1;
CC IsoId=Q08048-3; Sequence=VSP_044345, VSP_044346;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Has lost two of the three essential catalytic residues and so
CC probably has no enzymatic activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA51054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D10212; BAA01064.1; -; mRNA.
DR EMBL; D10213; BAA01065.1; -; mRNA.
DR EMBL; S71816; AAB31855.1; -; mRNA.
DR EMBL; X72307; CAA51054.1; ALT_INIT; mRNA.
DR EMBL; AF042856; AAC40051.1; -; mRNA.
DR EMBL; X84046; CAA58865.1; -; mRNA.
DR EMBL; CH466586; EDL03238.1; -; Genomic_DNA.
DR EMBL; BC119228; AAI19229.1; -; mRNA.
DR EMBL; X81630; CAA57286.1; -; Genomic_DNA.
DR CCDS; CCDS19097.1; -. [Q08048-1]
DR CCDS; CCDS80213.1; -. [Q08048-2]
DR PIR; JC2117; A60185.
DR RefSeq; NP_001276387.1; NM_001289458.1. [Q08048-1]
DR RefSeq; NP_001276388.1; NM_001289459.1. [Q08048-1]
DR RefSeq; NP_001276389.1; NM_001289460.2. [Q08048-3]
DR RefSeq; NP_001276390.1; NM_001289461.1. [Q08048-2]
DR RefSeq; NP_034557.3; NM_010427.5. [Q08048-1]
DR PDB; 2QJ4; X-ray; 2.50 A; A/B=29-210.
DR PDB; 3HMR; X-ray; 2.00 A; A=31-127.
DR PDB; 4IUA; X-ray; 3.05 A; A/B/C/D/E/F/G/H=31-290.
DR PDBsum; 2QJ4; -.
DR PDBsum; 3HMR; -.
DR PDBsum; 4IUA; -.
DR AlphaFoldDB; Q08048; -.
DR SASBDB; Q08048; -.
DR SMR; Q08048; -.
DR BioGRID; 200294; 1.
DR DIP; DIP-46456N; -.
DR IntAct; Q08048; 1.
DR STRING; 10090.ENSMUSP00000030683; -.
DR MEROPS; S01.982; -.
DR GlyGen; Q08048; 4 sites.
DR iPTMnet; Q08048; -.
DR PhosphoSitePlus; Q08048; -.
DR MaxQB; Q08048; -.
DR PaxDb; Q08048; -.
DR PRIDE; Q08048; -.
DR ProteomicsDB; 269786; -. [Q08048-1]
DR ProteomicsDB; 269787; -. [Q08048-2]
DR ProteomicsDB; 269788; -. [Q08048-3]
DR Antibodypedia; 4150; 1068 antibodies from 43 providers.
DR DNASU; 15234; -.
DR Ensembl; ENSMUST00000030683; ENSMUSP00000030683; ENSMUSG00000028864. [Q08048-1]
DR Ensembl; ENSMUST00000196645; ENSMUSP00000142517; ENSMUSG00000028864. [Q08048-2]
DR Ensembl; ENSMUST00000199581; ENSMUSP00000143424; ENSMUSG00000028864. [Q08048-1]
DR GeneID; 15234; -.
DR KEGG; mmu:15234; -.
DR UCSC; uc008wne.2; mouse. [Q08048-3]
DR UCSC; uc008wnf.2; mouse. [Q08048-1]
DR UCSC; uc008wnj.1; mouse. [Q08048-2]
DR CTD; 3082; -.
DR MGI; MGI:96079; Hgf.
DR VEuPathDB; HostDB:ENSMUSG00000028864; -.
DR eggNOG; ENOG502QR40; Eukaryota.
DR GeneTree; ENSGT00940000156019; -.
DR InParanoid; Q08048; -.
DR OMA; CNIKVCE; -.
DR PhylomeDB; Q08048; -.
DR TreeFam; TF329901; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6806942; MET Receptor Activation.
DR Reactome; R-MMU-6807004; Negative regulation of MET activity.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-8851805; MET activates RAS signaling.
DR Reactome; R-MMU-8851907; MET activates PI3K/AKT signaling.
DR Reactome; R-MMU-8865999; MET activates PTPN11.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8875513; MET interacts with TNS proteins.
DR Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-MMU-8875656; MET receptor recycling.
DR Reactome; R-MMU-8875791; MET activates STAT3.
DR Reactome; R-MMU-9734091; Drug-mediated inhibition of MET activation.
DR BioGRID-ORCS; 15234; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Met; mouse.
DR EvolutionaryTrace; Q08048; -.
DR PRO; PR:Q08048; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q08048; protein.
DR Bgee; ENSMUSG00000028864; Expressed in lumbar dorsal root ganglion and 124 other tissues.
DR Genevisible; Q08048; MM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IDA:MGI.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0001889; P:liver development; IDA:MGI.
DR GO; GO:0051450; P:myoblast proliferation; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0031643; P:positive regulation of myelination; ISO:MGI.
DR GO; GO:0070572; P:positive regulation of neuron projection regeneration; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IMP:MGI.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; IDA:MGI.
DR GO; GO:1902947; P:regulation of tau-protein kinase activity; IDA:MGI.
DR GO; GO:0014856; P:skeletal muscle cell proliferation; IDA:MGI.
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; IPR027284; Hepatocyte_GF.
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; 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; PIRSF500183; Hepatocyte_GF; 1.
DR PIRSF; PIRSF001152; HGF_MST1; 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; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Kringle;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat;
KW Serine protease homolog; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT CHAIN 33..495
FT /note="Hepatocyte growth factor alpha chain"
FT /id="PRO_0000028093"
FT CHAIN 496..728
FT /note="Hepatocyte growth factor beta chain"
FT /id="PRO_0000028094"
FT DOMAIN 38..124
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 129..207
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 212..289
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 306..384
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 392..470
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 496..724
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOD_RES 33
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P14210"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..97
FT DISULFID 75..85
FT DISULFID 129..207
FT DISULFID 150..190
FT DISULFID 178..202
FT DISULFID 212..289
FT /evidence="ECO:0000250"
FT DISULFID 233..272
FT /evidence="ECO:0000250"
FT DISULFID 261..284
FT /evidence="ECO:0000250"
FT DISULFID 306..384
FT /evidence="ECO:0000250"
FT DISULFID 327..366
FT /evidence="ECO:0000250"
FT DISULFID 355..378
FT /evidence="ECO:0000250"
FT DISULFID 392..470
FT /evidence="ECO:0000250"
FT DISULFID 413..453
FT /evidence="ECO:0000250"
FT DISULFID 441..465
FT /evidence="ECO:0000250"
FT DISULFID 488..607
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00315"
FT DISULFID 520..536
FT /evidence="ECO:0000250"
FT DISULFID 615..682
FT /evidence="ECO:0000250"
FT DISULFID 645..661
FT /evidence="ECO:0000250"
FT DISULFID 672..700
FT /evidence="ECO:0000250"
FT VAR_SEQ 163..167
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8135822"
FT /id="VSP_005408"
FT VAR_SEQ 210..211
FT /note="VE -> GK (in isoform NK1)"
FT /evidence="ECO:0000303|PubMed:9488442"
FT /id="VSP_044345"
FT VAR_SEQ 212..728
FT /note="Missing (in isoform NK1)"
FT /evidence="ECO:0000303|PubMed:9488442"
FT /id="VSP_044346"
FT CONFLICT 189
FT /note="W -> K (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="N -> K (in Ref. 2; AAB31855)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="C -> E (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="Q -> E (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="V -> L (in Ref. 2; AAB31855)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="K -> L (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="H -> T (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="R -> H (in Ref. 3; CAA51054)"
FT /evidence="ECO:0000305"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3HMR"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:3HMR"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4IUA"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3HMR"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:3HMR"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3HMR"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3HMR"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:3HMR"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3HMR"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2QJ4"
FT STRAND 110..122
FT /evidence="ECO:0007829|PDB:3HMR"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3HMR"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2QJ4"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2QJ4"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2QJ4"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2QJ4"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:2QJ4"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2QJ4"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4IUA"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4IUA"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:4IUA"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:4IUA"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:4IUA"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:4IUA"
SQ SEQUENCE 728 AA; 82945 MW; A0381FC497534328 CRC64;
MMWGTKLLPV LLLQHVLLHL LLLHVAIPYA EGQKKRRNTL HEFKKSAKTT LTKEDPLLKI
KTKKVNSADE CANRCIRNRG FTFTCKAFVF DKSRKRCYWY PFNSMSSGVK KGFGHEFDLY
ENKDYIRNCI IGKGGSYKGT VSITKSGIKC QPWNSMIPHE HSFLPSSYRG KDLQENYCRN
PRGEEGGPWC FTSNPEVRYE VCDIPQCSEV ECMTCNGESY RGPMDHTESG KTCQRWDQQT
PHRHKFLPER YPDKGFDDNY CRNPDGKPRP WCYTLDPDTP WEYCAIKTCA HSAVNETDVP
METTECIQGQ GEGYRGTSNT IWNGIPCQRW DSQYPHKHDI TPENFKCKDL RENYCRNPDG
AESPWCFTTD PNIRVGYCSQ IPKCDVSSGQ DCYRGNGKNY MGNLSKTRSG LTCSMWDKNM
EDLHRHIFWE PDASKLNKNY CRNPDDDAHG PWCYTGNPLI PWDYCPISRC EGDTTPTIVN
LDHPVISCAK TKQLRVVNGI PTQTTVGWMV SLKYRNKHIC GGSLIKESWV LTARQCFPAR
NKDLKDYEAW LGIHDVHERG EEKRKQILNI SQLVYGPEGS DLVLLKLARP AILDNFVSTI
DLPSYGCTIP EKTTCSIYGW GYTGLINADG LLRVAHLYIM GNEKCSQHHQ GKVTLNESEL
CAGAEKIGSG PCEGDYGGPL ICEQHKMRMV LGVIVPGRGC AIPNRPGIFV RVAYYAKWIH
KVILTYKL
