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Database: UniProt
Entry: A0A1S3FYB6_DIPOR
LinkDB: A0A1S3FYB6_DIPOR
Original site: A0A1S3FYB6_DIPOR 
ID   A0A1S3FYB6_DIPOR        Unreviewed;       730 AA.
AC   A0A1S3FYB6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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|RefSeq:XP_012881548.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012881548.1};
RN   [1] {ECO:0000313|RefSeq:XP_012881548.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012881548.1};
RG   RefSeq;
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   RefSeq; XP_012881548.1; XM_013026094.1.
DR   AlphaFoldDB; A0A1S3FYB6; -.
DR   STRING; 10020.ENSDORP00000018895; -.
DR   GeneID; 105992969; -.
DR   KEGG; dord:105992969; -.
DR   CTD; 3082; -.
DR   OrthoDB; 211181at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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:UP000081671};
KW   Serine protease homolog {ECO:0000256|ARBA:ARBA00022542,
KW   ECO:0000256|PIRNR:PIRNR001152}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..730
FT                   /note="Hepatocyte growth factor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010193388"
FT   DOMAIN          37..123
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          127..206
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          210..288
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          304..383
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          390..469
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          495..723
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        211..288
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        232..271
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        260..283
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        326..365
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        354..377
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   730 AA;  82957 MW;  0F2F878B12DF8630 CRC64;
     MWVTKLLPVL LLQPVLLHLL LLPTAIPSAA GQKKRRNTLH EFKKSAKTTL IKEDPLLRIK
     TKKMNTADQC ANRCIRNKGL PFTCKAFVFD KARKRCLWFP FNSMSSGVKK GFGHEFDLYE
     NKDYIRNCII GKGGSYKGTV SITKSGIKCQ HWNSMIPHEH SFLPSSYRGK DLQENYCRNP
     RGEEGGPWCF TSNPEVRYEV CDIPQCSEVE CMTCNGESYR GPMDHTESGK ICQRWDHQTP
     HRHKFLPERY PDKGFDDNYC RNPDGKPRPW CYTLDPDTPW EYCAIKMCAH STINDTHVPM
     ETTECIQGQG EGYRGTVNTI WNGIPCQRWD SQYPHEHDVT PENFKCKDLR ENYCRNPDGA
     ESPWCFTTDP NIRVGYCSQI PKCDVSSGQD CYRGNGKNYM GNLSKTRSGL TCSMWDKNME
     DLHRHIFWEP DASKLNKNYC RNPDDDAHGP WCYTGNPLIP WDYCPISRCE GDTTPTIVNL
     DHPVISCAKT KQLRVVNGIP TQTNVGWMVS LKYRNKHICG GSLIKESWVL TARQCFPARN
     KDLKDYEAWL GVHDVHGRGE EKRKQVLNIS QLVYGPEGSD LVLLKLARPA ILDSFVSTID
     LPNYGCTIPE KTTCSVYGWG YTGLINSDGL LRVAHLYIMG NEKCNQHHQG KVTLSESELC
     AGAENIGSGP CEGDYGGPLV CEQHKMRMLL GVIVPGRGCA IPNRPGIFIR VAYYAKWMHK
     VILTYKAQQS
//
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