HGF_BOVIN
ID HGF_BOVIN Reviewed; 730 AA.
AC Q76BS1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16207523; DOI=10.1016/j.domaniend.2005.08.005;
RA Yamaji D., Kimura K., Watanabe A., Kon Y., Iwanaga T., Soliman M.M.,
RA Ahmed M.M., Saito M.;
RT "Bovine hepatocyte growth factor and its receptor c-Met: cDNA cloning and
RT expression analysis in the mammary gland.";
RL Domest. Anim. Endocrinol. 30:239-246(2006).
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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}.
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DR EMBL; AB110822; BAD02475.1; -; mRNA.
DR RefSeq; NP_001026921.1; NM_001031751.2.
DR AlphaFoldDB; Q76BS1; -.
DR SMR; Q76BS1; -.
DR STRING; 9913.ENSBTAP00000023490; -.
DR MEROPS; S01.976; -.
DR PaxDb; Q76BS1; -.
DR PRIDE; Q76BS1; -.
DR GeneID; 282879; -.
DR KEGG; bta:282879; -.
DR CTD; 3082; -.
DR eggNOG; ENOG502QR40; Eukaryota.
DR InParanoid; Q76BS1; -.
DR Proteomes; UP000009136; 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; 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Growth factor; Kringle;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat;
KW Serine protease homolog; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..494
FT /note="Hepatocyte growth factor alpha chain"
FT /id="PRO_0000274197"
FT CHAIN 495..730
FT /note="Hepatocyte growth factor beta chain"
FT /id="PRO_0000274198"
FT DOMAIN 37..123
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 128..206
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 211..288
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 305..383
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 391..469
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 495..723
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOD_RES 32
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P14210"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..96
FT /evidence="ECO:0000250"
FT DISULFID 74..84
FT /evidence="ECO:0000250"
FT DISULFID 128..206
FT /evidence="ECO:0000250"
FT DISULFID 149..189
FT /evidence="ECO:0000250"
FT DISULFID 177..201
FT /evidence="ECO:0000250"
FT DISULFID 211..288
FT /evidence="ECO:0000250"
FT DISULFID 232..271
FT /evidence="ECO:0000250"
FT DISULFID 260..283
FT /evidence="ECO:0000250"
FT DISULFID 305..383
FT /evidence="ECO:0000250"
FT DISULFID 326..365
FT /evidence="ECO:0000250"
FT DISULFID 354..377
FT /evidence="ECO:0000250"
FT DISULFID 391..469
FT /evidence="ECO:0000250"
FT DISULFID 412..452
FT /evidence="ECO:0000250"
FT DISULFID 440..464
FT /evidence="ECO:0000250"
FT DISULFID 487..606
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 519..535
FT /evidence="ECO:0000250"
FT DISULFID 614..681
FT /evidence="ECO:0000250"
FT DISULFID 644..660
FT /evidence="ECO:0000250"
FT DISULFID 671..699
FT /evidence="ECO:0000250"
SQ SEQUENCE 730 AA; 83357 MW; E39D653B0A85F49B CRC64;
MWVTRLLPVL LLQHVLLHLL LLPIAIPYAE GQKKRRNTLH EFKRSAKTTL IKEDPLLKIK
TKKMNTADQC ANRCIRNKGL PFTCKAFVFD KARKRCLWFP FNSMSSGVKK EFGHEFDLYE
NKDYIRNCII GKGGSYKGTV SITKSGIKCQ PWNSMIPHEH SFLPSSYRGK DLQENYCRNP
RGEEGGPWCF TSNPEVRYEV CDIPQCSEVE CMTCNGESYR GPMDHTETGK ICQRWDHQTP
HRHKFLPERY PDKGFDDNYC RNPDGKPRPW CYTLDPDTPW EYCAIKMCAH STMNDTDLPM
QTTECIQGQG EGYRGTINTI WNGIPCQRWD SQYPHQHDIT PENFKCKDLR ENYCRNPDGA
ESPWCFTTDP NIRVGYCSQI PKCDVSSGQD CYRGNGKNYM GSLSKTRSGL TCSMWDKNME
DLHRHIFWEP DATKLNKNYC RNPDDDAHGP WCYTGNPLIP WDYCPISRCE GDTTPTIVNL
DHPVISCAKT KQLRVVNGIP TRTNVGWMVS LKYRNKHICG GSLIKESWIL TARQCFPSRN
KDLKDYEAWL GIHDVHGRGD EKRKQVLNVT QLVYGPEGSD LVLLKLARPA ILDDFVSTID
LPNYGCTIPE KTTCSVYGWG YTGLINSDGL LRVAHLYIMG NEKCSQYHQG KVTLNESEIC
AGAENIVSGP CEGDYGGPLV CEQHKMRMVL GVIVPGRGCA IPNRPGIFVR VAYYAKWIHK
IILTYKAPQL
