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Database: UniProt
Entry: I3M1N9_ICTTR
LinkDB: I3M1N9_ICTTR
Original site: I3M1N9_ICTTR 
ID   I3M1N9_ICTTR            Unreviewed;       730 AA.
AC   I3M1N9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Hepatocyte growth factor {ECO:0000256|ARBA:ARBA00021784, ECO:0000256|PIRNR:PIRNR001152};
DE   AltName: Full=Hepatopoietin-A {ECO:0000256|ARBA:ARBA00033078, ECO:0000256|PIRNR:PIRNR001152};
DE   AltName: Full=Scatter factor {ECO:0000256|ARBA:ARBA00031997, ECO:0000256|PIRNR:PIRNR001152};
GN   Name=HGF {ECO:0000313|Ensembl:ENSSTOP00000002769.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000002769.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000002769.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR001152}.
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. {ECO:0000256|ARBA:ARBA00025867}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC       {ECO:0000256|PIRNR:PIRNR001152}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR   EMBL; AGTP01100858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3M1N9; -.
DR   STRING; 43179.ENSSTOP00000002769; -.
DR   Ensembl; ENSSTOT00000003098.3; ENSSTOP00000002769.3; ENSSTOG00000003087.3.
DR   eggNOG; ENOG502QR40; Eukaryota.
DR   GeneTree; ENSGT00940000156019; -.
DR   HOGENOM; CLU_017565_1_0_1; -.
DR   InParanoid; I3M1N9; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0042056; F:chemoattractant activity; IEA:Ensembl.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:1900744; P:regulation of p38MAPK cascade; IEA:Ensembl.
DR   GO; GO:0014856; P:skeletal muscle cell proliferation; IEA:Ensembl.
DR   CDD; cd00108; KR; 4.
DR   CDD; cd00129; PAN_APPLE; 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; 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   PANTHER; PTHR24261:SF8; HEPATOCYTE GROWTH FACTOR; 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; PIRSF500183; Hepatocyte_GF; 1.
DR   PIRSF; PIRSF001152; HGF_MST1; 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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00121};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW   ECO:0000256|PIRNR:PIRNR001152};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121};
KW   Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Serine protease homolog {ECO:0000256|ARBA:ARBA00022542,
KW   ECO:0000256|PIRNR:PIRNR001152}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..730
FT                   /note="Hepatocyte growth factor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013356878"
FT   DOMAIN          38..124
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          128..207
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          211..289
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          305..384
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          391..470
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          496..723
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        212..289
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        233..272
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        261..284
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        327..366
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        355..378
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   730 AA;  83334 MW;  28127D1EAF34651C CRC64;
     TMWVTKLLPV LLLQHVLLHL LLLPIAIPYA EGQKKRRNTL HEFKKSAKTT LIKEDPLLKI
     KTKKMNTPDQ CANRCIRNKG LPFTCKAFVF DKTRKRCLWL PFNSMSSGVK KEFGHEFDLY
     ENKDYIRNCI IGKGGSYKGT VSITKSGIKC QPWNSMIPHE HSFLPSSYRG KDLQENYCRN
     PRGEEGGPWC FTSNPEVRYE VCDIPQCSEV ECMTCNGESY RGPMDHTESG KICQRWDHQT
     PHRHKFLPER YPDKGFDDNY CRNPDGKPRP WCYTLDPDTP WEYCAIKMCA HSTMNDTDVP
     METTECIQGQ GEGYRGTINT IWNGIPCQRW DSQYPHQHDI TPENFKCKDL RENYCRNPDG
     AESPWCFTTD PNIRVGYCSQ IPKCDVSSGQ DCYRGNGKNY MGNLSKTRFG LTCSMWEKNM
     EDLHRHIFWE PDASKLNKNY CRNPDDDAHG PWCYTGNPLI PWDYCPISRC EGDTTPTIVN
     LDHPVISCAK TKQLRVVNGI PTRTNVGWMV SLKYRNKHIC GGSLIKESWV LTARQCFPAR
     NKDLKEYEAW LGIHDVHGRD EKRKQVLNVS QLVYGPEGSD LVLLKLARPA VLDNFVSTID
     LPNYGCTIPE KTTCSVYGWG YTGLINSDGL LRVAHLYIMG NEKCSQHHQG KVTLNESEIC
     AGAEKIGSGP CEGDYGGPLV CEQHKMRMVL GVIVPGRGCA IPNRPGIFVR VAYYAKWIHK
     IILTYKVTQS
//
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