ID H2UB48_TAKRU Unreviewed; 756 AA.
AC H2UB48;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Hepatocyte growth factor {ECO:0000256|ARBA:ARBA00021784};
DE AltName: Full=Hepatopoietin-A {ECO:0000256|ARBA:ARBA00033078};
DE AltName: Full=Scatter factor {ECO:0000256|ARBA:ARBA00031997};
GN Name=HGF {ECO:0000313|Ensembl:ENSTRUP00000034166.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000034166.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000034166.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000034166.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR AlphaFoldDB; H2UB48; -.
DR STRING; 31033.ENSTRUP00000034166; -.
DR MEROPS; S01.976; -.
DR Ensembl; ENSTRUT00000034292.3; ENSTRUP00000034166.3; ENSTRUG00000013402.3.
DR GeneTree; ENSGT00940000156019; -.
DR InParanoid; H2UB48; -.
DR OMA; CNIKVCE; -.
DR OrthoDB; 211181at2759; -.
DR Proteomes; UP000005226; Chromosome 9.
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; 3.
DR CDD; cd01099; PAN_AP_HGF; 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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Growth factor {ECO:0000256|ARBA:ARBA00023030};
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:UP000005226};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..756
FT /note="Hepatocyte growth factor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025510710"
FT DOMAIN 15..106
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 110..191
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 195..273
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 286..365
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 373..448
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 473..693
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 196..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 217..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 245..268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 308..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 336..359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 756 AA; 86196 MW; 0B2D8A04808E6963 CRC64;
MWIYALFLVL VVISCSESKR NALQDYQKTD GVRLVPSDSS HLTKSKKVSM AKCAKACSRN
RRLPFTCRAF LYDHKNRKCQ WLSFDRNSLG VRSLEDFNYQ LYQKKDYVRE CIVGTGQSYR
GRRSVTVTGI LCQAWSSPIP HEHNFMSKRF RKKDLRKNYC RNPDNATAGP WCFTTDPRPH
LRHQECGVPQ CSQVECVNCN GEDYRGPMDH TESGKECQRW DLNEPHKHLY HPKRYPDSGL
SDNYCRNPDG RQRPWCFTTD PDTPWEYCNI RVCDTPPKRS VVETSECYEG RGRGYRGTVD
VTPTGLTCQR WDSQYPHNHT FTPQAYTCKD LRENYCRNPD GQEFPWCFTT DPRIRTMLCT
NIPQCGTQSK ADDCYTGFGE NYQGKQARTR SNLPCAPWRD HRSSGERGLM VANLEGSYCR
NPDNDKHGPW CHTNKSGIPW DYCHVKPCDA SQNTIPLGEL SSVGCFIHKT TRIVGGGPVG
ISDGSWMVSI QKGAMHWCGG SLIREEWVLT DRQCFSSCVP DLRDYRVWLG DSFNRQEISI
AHVICGPEGS SLALMRLSQP ARPADNVHTV QLPVAGCSIP EGKFCKMYGW GETKGTGHED
VLKAVDLPIV SNERCREMHR GYLDITNTRI CAGGRRNEGV CERDYGGPLV CQDGEIRVIV
GVSVHGRGCA RANQPGIFIN VPFYTHWIHK VFKYYPDPEA WHSSISHPWR TLMSQSLSLR
TLPCVVCNGF FTEMTEWPLK RITACLFAMS AIEVLF
//
