ID G1Q6A3_MYOLU Unreviewed; 730 AA.
AC G1Q6A3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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:ENSMLUP00000019236.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000019236.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000019236.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000019236.1}
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; AAPE02017835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02017836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02017837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006088747.1; XM_006088685.2.
DR AlphaFoldDB; G1Q6A3; -.
DR STRING; 59463.ENSMLUP00000019236; -.
DR MEROPS; S01.976; -.
DR Ensembl; ENSMLUT00000027287.1; ENSMLUP00000019236.1; ENSMLUG00000023879.1.
DR GeneID; 102441297; -.
DR KEGG; mlf:102441297; -.
DR CTD; 3082; -.
DR eggNOG; ENOG502QR40; Eukaryota.
DR GeneTree; ENSGT00940000156019; -.
DR HOGENOM; CLU_017565_1_0_1; -.
DR InParanoid; G1Q6A3; -.
DR OMA; CNIKVCE; -.
DR OrthoDB; 211181at2759; -.
DR TreeFam; TF329901; -.
DR Proteomes; UP000001074; 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:UP000001074};
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_5003419631"
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; 83221 MW; D9EBF8013B3E0F9D CRC64;
MWVTKLLPAL LLQHVLLHLL LLPIAIPYAE GQKKRRNTLH EFKKSAKTTL FKEDPLLKIK
TKKMNAADQC ANRCIRNKGL PFTCKAFVFD KARKRCLWFP FNSMSTGVKK QFGHEFDLYE
NKDYIRNCII GKGGSYKGTV SITKSGIKCQ PWNSMIPHEH SFLPSSYRGK DLQENYCRNP
RGEEGGPWCF TSNPEVRYEV CDIPQCSEVE CMTCNGESYR GPMDHTESGK TCQRWDHQTP
HRHKFVPERY PDKGFDDNYC RNPDGKPRPW CYTLDPDTPW EYCAIKMCAH STMNDTNVPM
ETTECIQGQG EGYRGTVNTI WNGIPCQRWD SQYPHQHDIT PENFKCKDLR ENYCRNPDGA
ESPWCFTTDP NIRVGYCSQI PKCDVSRGQD CYRGNGKNYM GNLSKTRSGL TCSMWDKNME
DLHRHIFWEP DASKLNKNYC RNPDDDAHGP WCYTGNPLIP WDYCPISRCE GDTTPTIVNL
DHPVISCAKT KQLRVVNGIP TRTNVGWMVS LKYRNKHICG GSLIKESWIL TARQCFPSRN
KDLKDYEVWL GIHDVHGRGD EKRKQVLNVS QVVYGPEGSD LVLLKLARPA VLDNFVSTID
LPNYGCMIPE KTTCSVYGWG YTGLINSDGL LRVAHLFIMG NEKCSQYHQG KVTLNESEIC
AGAENIAAGP CEGDYGGPLV CEQHKMRMVL GVIVPGRGCA IANRPGIFVR VAYYAKWIHK
VILTYKVPQS
//
