ID F1SB93_PIG Unreviewed; 730 AA.
AC F1SB93; A0A480SZ19; A0A4X1SJC0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 94.
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:ENSSSCP00000016330.5,
GN ECO:0000313|VGNC:VGNC:88869};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016330.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000016330.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016330.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB52496.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000016330.5}
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; DQIR01197019; HDB52496.1; -; Transcribed_RNA.
DR RefSeq; XP_003130270.1; XM_003130222.4.
DR RefSeq; XP_013835241.1; XM_013979787.1.
DR STRING; 9823.ENSSSCP00000016330; -.
DR PaxDb; 9823-ENSSSCP00000016330; -.
DR Ensembl; ENSSSCT00000016778.5; ENSSSCP00000016330.5; ENSSSCG00000015403.5.
DR Ensembl; ENSSSCT00005028321.1; ENSSSCP00005017292.1; ENSSSCG00005017589.1.
DR Ensembl; ENSSSCT00005028364.1; ENSSSCP00005017318.1; ENSSSCG00005017589.1.
DR GeneID; 100525120; -.
DR KEGG; ssc:100525120; -.
DR CTD; 3082; -.
DR VGNC; VGNC:88869; HGF.
DR eggNOG; ENOG502QR40; Eukaryota.
DR GeneTree; ENSGT00940000156019; -.
DR HOGENOM; CLU_017565_1_0_1; -.
DR OMA; CNIKVCE; -.
DR OrthoDB; 211181at2759; -.
DR TreeFam; TF329901; -.
DR Reactome; R-SSC-114608; Platelet degranulation.
DR Reactome; R-SSC-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SSC-5673001; RAF/MAP kinase cascade.
DR Reactome; R-SSC-6806942; MET Receptor Activation.
DR Reactome; R-SSC-6807004; Negative regulation of MET activity.
DR Reactome; R-SSC-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-SSC-8851805; MET activates RAS signaling.
DR Reactome; R-SSC-8851907; MET activates PI3K/AKT signaling.
DR Reactome; R-SSC-8865999; MET activates PTPN11.
DR Reactome; R-SSC-8874081; MET activates PTK2 signaling.
DR Reactome; R-SSC-8875513; MET interacts with TNS proteins.
DR Reactome; R-SSC-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-SSC-8875656; MET receptor recycling.
DR Reactome; R-SSC-8875791; MET activates STAT3.
DR Reactome; R-SSC-9734091; Drug-mediated inhibition of MET activation.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000015403; Expressed in omentum and 41 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0005102; F:signaling receptor binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
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:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
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:UP000008227};
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_5014571296"
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; 83264 MW; F11528CC5AE3A2D2 CRC64;
MWVTKLLQVL LLQHVLLHLL LLPIAIPYAE GQKKRRNTLH EFKKSAKTTL INEDPLLKIK
TKKMNTADQC ANRCIRNKGL PFTCKAFVFD KARKRCLWFP FNSMSSGVKK EFGHEFDLYE
NKDYIRNCII GKGGSYKGTV SITKSGIKCQ PWNSMIPHEH SFLPSSYRGK DLQENYCRNP
RGEEGGPWCF TSNPEVRYEV CDIPQCSEVE CLTCNGESYR GPMDHTESGK ICQRWDHQTP
HRHKFLPERY PDKGFDDNYC RNPDGKPRPW CYTLDPDTPW EYCAIKMCAH STMNDTDVPM
ETTECIQGQG EGYRGTINTI WNGIPCQRWD SQYPHQHDIT PENFKCKDLR ENYCRNPDGA
ESPWCFTTDP NIRVGYCSQI PKCDVSSGQD CYRGNGKNYM GNLSKTRSGL TCSMWDKNME
DLHRHIFWEP DASKLNKNYC RNPDDDAHGP WCYTGNPLIP WDYCPISRCE GDTTPTIVNL
DHPVISCAKT KQLRVVNGIP TRTNVGWMVS LKYRNKHICG GSLIKESWIL TARQCFPSRN
KDLKDYEAWL GIHDVHGRGD EKRKQVLNVT QLVYGPEGSD LVLLKLARPA VLDDFVSTID
LPNYGCTIPE KTTCSVYGWG YTGLINSDGL LRVAHLYIMG NEKCSQYHQG KVTLNESEIC
AGAENIVSGP CEGDYGGPLV CEQHKMRMVL GVIVPGRGCA IPNRPGIFVR VAYYAKWIHK
IILTYKVSQS
//
