HGF_FELCA
ID HGF_FELCA Reviewed; 728 AA.
AC Q9BH09;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=11258464; DOI=10.1292/jvms.63.211;
RA Kobayashi Y., Nakamura N., Ishizaka T., Masuda K., Ohno K., Tsujimoto H.;
RT "Molecular cloning of feline hepatocyte growth factor (HGF) cDNA.";
RL J. Vet. Med. Sci. 63:211-214(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14960804; DOI=10.1292/jvms.66.9;
RA Miyake M., Yaguchi T., Saze K., Wang J., Ogawa T., Endo Y., Suzuta Y.,
RA Okazaki M., Haga Y., Waki T., Takahashi S.Y., Yamamoto Y., Iwabuchi S.;
RT "Isolation and expression of five-amino-acid-deleted variant of feline
RT hepatocyte growth factor (HGF) cDNA.";
RL J. Vet. Med. Sci. 66:9-14(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BH09-1; Sequence=Displayed;
CC Name=2; Synonyms=dHGF;
CC IsoId=Q9BH09-2; Sequence=VSP_022678;
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; AB046610; BAB21499.1; -; mRNA.
DR EMBL; AB080187; BAC10545.1; -; mRNA.
DR RefSeq; NP_001009830.1; NM_001009830.1. [Q9BH09-1]
DR RefSeq; XP_006929205.1; XM_006929143.2. [Q9BH09-2]
DR RefSeq; XP_019670471.1; XM_019814912.1. [Q9BH09-1]
DR AlphaFoldDB; Q9BH09; -.
DR SMR; Q9BH09; -.
DR STRING; 9685.ENSFCAP00000007930; -.
DR MEROPS; S01.976; -.
DR Ensembl; ENSFCAT00000048140; ENSFCAP00000033735; ENSFCAG00000008554. [Q9BH09-1]
DR GeneID; 493705; -.
DR KEGG; fca:493705; -.
DR CTD; 3082; -.
DR eggNOG; ENOG502QR40; Eukaryota.
DR GeneTree; ENSGT00940000156019; -.
DR HOGENOM; CLU_017565_1_0_1; -.
DR InParanoid; Q9BH09; -.
DR OMA; CNIKVCE; -.
DR OrthoDB; 164039at2759; -.
DR Proteomes; UP000011712; Chromosome A2.
DR Bgee; ENSFCAG00000008554; Expressed in liver and 9 other 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:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; 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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; 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:1902947; P:regulation of tau-protein kinase activity; IEA:Ensembl.
DR GO; GO:0014856; P:skeletal muscle cell proliferation; IEA:Ensembl.
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 Alternative splicing; Disulfide bond; Glycoprotein; Growth factor; Kringle;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat;
KW Serine protease homolog; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..492
FT /note="Hepatocyte growth factor alpha chain"
FT /id="PRO_0000274201"
FT CHAIN 493..728
FT /note="Hepatocyte growth factor beta chain"
FT /id="PRO_0000274202"
FT DOMAIN 35..121
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 126..204
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 209..286
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 303..381
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 389..467
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 493..721
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOTIF 556..558
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P14210"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..94
FT /evidence="ECO:0000250"
FT DISULFID 72..82
FT /evidence="ECO:0000250"
FT DISULFID 126..204
FT /evidence="ECO:0000250"
FT DISULFID 147..187
FT /evidence="ECO:0000250"
FT DISULFID 175..199
FT /evidence="ECO:0000250"
FT DISULFID 209..286
FT /evidence="ECO:0000250"
FT DISULFID 230..269
FT /evidence="ECO:0000250"
FT DISULFID 258..281
FT /evidence="ECO:0000250"
FT DISULFID 303..381
FT /evidence="ECO:0000250"
FT DISULFID 324..363
FT /evidence="ECO:0000250"
FT DISULFID 352..375
FT /evidence="ECO:0000250"
FT DISULFID 389..467
FT /evidence="ECO:0000250"
FT DISULFID 410..450
FT /evidence="ECO:0000250"
FT DISULFID 438..462
FT /evidence="ECO:0000250"
FT DISULFID 485..604
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 517..533
FT /evidence="ECO:0000250"
FT DISULFID 612..679
FT /evidence="ECO:0000250"
FT DISULFID 642..658
FT /evidence="ECO:0000250"
FT DISULFID 669..697
FT /evidence="ECO:0000250"
FT VAR_SEQ 160..164
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14960804"
FT /id="VSP_022678"
SQ SEQUENCE 728 AA; 83068 MW; 8D7F4A333D1E190A CRC64;
MWVTKLLPVL LLQHVLLHLL LLPIPYAEGQ KKRRNTLHEF KKSAKTTLIK EDPLLKIKTK
KMNTADQCAN RCIRNKGLPF TCKAFVFDKA RKRCLWFPFN SMTSGVKKEF GHEFDLYENK
DYIRNCIIGK GGSYKGTVSI TKSGIKCQPW NSMIPHEHSF LPSSYRGKDL QENYCRNPRG
EEGGPWCFTS NPEVRYEVCD IPQCSEVECM TCNGESYRGP MDHTESGKIC QRWDRQTPHR
HKFLPERYPD KGFDDNYCRN PDGKPRPWCY TLDPDTPWEY CAIKMCAHST MNDTDVPMET
TECIQGQGEG YRGTINSIWN GVPCQRWDSQ YPHQHDITPE NFKCKDLREN FCRNPDGAES
PWCFTTDPNI RVGYCSQIPK CDVSSGQDCY RGNGKNYMGN LSKTRSGLTC SMWEKNMEDL
HRHIFWEPDA SKLNKNYCRN PDDDAHGPWC YTGNPLIPWD YCPISRCEGD TTPTIVNLDH
PVISCAKTKQ LRVVNGIPTR TNVGWMVSLK YRNKHICGGS LIKESWILTA RQCFPSRNKD
LKDYEAWLGI HDVHGRGDEK RKQVLNVSQL VYGPEGSDLV LLKLARPAVL DDFVSTIDLP
NYGCTIPEKT TCSVYGWGYT GSINSDGLLR VAHLYIMGNE KCSQYHQGKV TLNESEICAG
AENIVSGPCE GDYGGPLVCE QHKMRMVLGV IVPGRGCAIP NRPGIFVRVA YYAKWIHKII
LTYKIPQS
