ID A0A2Y9KI03_ENHLU Unreviewed; 730 AA.
AC A0A2Y9KI03;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=LOC111155271 {ECO:0000313|RefSeq:XP_022371104.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022371104.1};
RN [1] {ECO:0000313|RefSeq:XP_022371104.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022371104.1};
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_022371104.1; XM_022515396.1.
DR AlphaFoldDB; A0A2Y9KI03; -.
DR STRING; 391180.A0A2Y9KI03; -.
DR KEGG; elk:111155271; -.
DR OrthoDB; 211181at2759; -.
DR Proteomes; UP000248482; 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:UP000248482};
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_5015970656"
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; 83155 MW; 6E1514D5E18D2CC1 CRC64;
MWGTKLLPVL LLQHVLLHLL LLPIAIPYAE GQKKRRNTLH EFKKSAKTTL IKEDPLLKIK
TKKMNTADQC ANRCIRNKGL PFTCKAFVFD KARKRCLWFP FNSMTSGVKK EFGHEFDLYE
NKDYIRNCII GKGGSYKGTV SITKSGIKCQ PWNSMIPHEH SFLPSSYRGK DLQENYCRNP
RGEEGGPWCF TSNPEVRYEV CDIPQCSEVE CMTCNGESYR GPMDHTESGK ICQRWDHQTP
HRHKFLPERY PDKGFDDNYC RNPDGKPRPW CYTLDPDTPW EYCAIKMCAH GTMNDTDVPM
ETTECIQGQG EGYRGTISTI WNGIPCQRWD SQYPHQHDIT PENFKCKDLR ENYCRNPDGA
ESPWCFTTDP NIRVGYCSQI PKCDVSSGQD CYRGNGKNYM GNLSKTRSGL TCSMWEKNME
DLHRHIFWEP DASKLNKNYC RNPDDDAHGP WCYTGNPLIP WDYCPISRCE GDTTPTIVNL
DHPVISCAKT KQLRVVNGIP TRTNVGWMVS LKYRNKHICG GSLIKESWIL TARQCFPSRN
KDLKDYEAWL GIHDVHGKGD EKRKQVLNVS QLVYGPEGSD LVLLKLARPA VLDDFVSTID
LPNYGCTIPE KTTCSVYGWG YTGSISFDGL LRVAHLYIMG NEKCSQYHQG KVTLNESEIC
AGAENIASGP CEGDYGGPLV CEQHKMRMVL GVIVPGRGCA IPNRPGIFVR VAYYAKWIHK
IILTYKIPQS
//
