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Database: UniProt
Entry: A0A3P8T1W7_AMPPE
LinkDB: A0A3P8T1W7_AMPPE
Original site: A0A3P8T1W7_AMPPE 
ID   A0A3P8T1W7_AMPPE        Unreviewed;       713 AA.
AC   A0A3P8T1W7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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:ENSAPEP00000018233.1};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000018233.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000018233.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000018233.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3P8T1W7; -.
DR   STRING; 161767.ENSAPEP00000018233; -.
DR   Ensembl; ENSAPET00000018740.1; ENSAPEP00000018233.1; ENSAPEG00000013054.1.
DR   GeneTree; ENSGT00940000156019; -.
DR   OMA; CNIKVCE; -.
DR   Proteomes; UP000265080; Chromosome 4.
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   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:UP000265080};
KW   Serine protease homolog {ECO:0000256|ARBA:ARBA00022542,
KW   ECO:0000256|PIRNR:PIRNR001152}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..713
FT                   /note="Hepatocyte growth factor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017946075"
FT   DOMAIN          15..108
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          112..193
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          197..275
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          288..367
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          376..451
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          476..705
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        198..275
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        219..258
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        247..270
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        310..349
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        338..361
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   713 AA;  81029 MW;  2117D075F872E1C2 CRC64;
     MWIYKLVFGL FLLSCSEGRR NALQDYQKTD GVQLVVTSPD SSHLTKSRKL SLSRCAKSCS
     RGRRLPFACR AFVYDHKNRK CQWLSFDRNS PGTQSHQNIN YQLYQKKDYV RECIVGTGQS
     YRGRRSVTVS GILCQAWASP IPHEHKFMSK RFRKKDLREN YCRNPDNSTV GPWCFTTDPR
     PHLRHQECGI PQCSQVECMN CNGEDYRGPM DHTESGKECQ RWDLDEPHKH LYHPRRYPDK
     GLDDNYCRNP DGRHRPWCFT TDPNTPWEYC NIKVCETPQK SNVLETTECY QGRGEGYRGT
     VDVTPTGLTC QRWDSQYPHN HTFTPQAYPC KDLRENYCRN PDGQEFPWCF TTDPRVRTIF
     CTNIPQCGTQ NKPVSDCYES FGENYQGQQS RTRSNLPCAP WRDHSNSGER GMLTASLEGN
     YCRNPDKDKH GPWCHTNNSA ILWDYCNVKP CDTSLNNIPL GGLSSVSCFI HKSPRIVGGG
     RVGISDGSWM VSIQRGSVHW CGGSLIREEW VLTDRQCFSS CVPDLSEYRV WLGVSDIRED
     APDWSKRQEV SIAHVICGPE GSSLALLKLS KPASPADNVH TIQLPVAGCS IPEGTICKMY
     GWGETKGTGH DDVLKSVDLP IVSSGRCREM HRGNLHITNT KICAGGRRNE GVCERDYGGP
     LVCQDGEIRV IVGVSVPGRG CARANQPGIF INVPFYTQWI YKVFKYYPNP EIV
//
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