ID A0A3B3XRS1_9TELE Unreviewed; 719 AA.
AC A0A3B3XRS1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000017625.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000017625.1}
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 RefSeq; XP_014824940.1; XM_014969454.1.
DR AlphaFoldDB; A0A3B3XRS1; -.
DR STRING; 48701.ENSPMEP00000017625; -.
DR Ensembl; ENSPMET00000026526.1; ENSPMEP00000017625.1; ENSPMEG00000020459.1.
DR GeneID; 106904919; -.
DR KEGG; pmei:106904919; -.
DR CTD; 100334116; -.
DR OrthoDB; 211181at2759; -.
DR Proteomes; UP000261480; 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; 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 Serine protease homolog {ECO:0000256|ARBA:ARBA00022542,
KW ECO:0000256|PIRNR:PIRNR001152}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..719
FT /note="Hepatocyte growth factor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017400718"
FT DOMAIN 19..111
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 115..196
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 200..278
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 291..370
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 379..454
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 482..711
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 201..278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 222..261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 250..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 313..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 341..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 719 AA; 81616 MW; 0C4B3002FCF06FD1 CRC64;
MKAMWIYRLV VGLAVVSCCE GRRNALQDYQ KSEGTRLTVV SPDSSHLTKS RKLSLTKCAK
TCSRGKRLPF NCRAFLYDHR NRKCQWLSFD RNSPGAQSHQ NVYYDLYQKK DYIRECIVGT
GQSYRGRRSV TVSGILCQAW ASPIPHEHKF MSKRYRKTDL IENYCRNPDN STVGPWCFTT
DPRPHLRHQE CGIPQCSQVE CITCNGEDYR GPMDYTESGK ECQRWDLNEP HKHSYHPSRY
PDKGLHDNYC RNPDGRHRPW CFTTDPNTHW EYCNIKVCET PPKSPEAETT ECYEGRGEGY
RGTADTTPSG LACQRWDSQY PHNHTFLPEA YPCKDLKENY CRNPDGQEFP WCFTTDPRVR
TMFCTHIPQC GVQNSPVSDC FLGFGENYQG EQSRTRSNLP CAPWRDHSNR GERGMLMAGL
EGNFCRNPDK DKHGPWCFTN NSAISWDYCN VKPCDALQNS IPPVFVAEPT PVRCFVHKRT
RIVGGAPVGI SDGSWMVSIQ KGSVHWCGGS LVREEWVLTD RQCFSSCVPD LSEYRVWLGV
SDLREGSPDR LKRQEVRIAQ VICGPNGSSL ALLRLSKPAR PADNVHTIQL PVAGCSIPEG
TMCKMYGWGE TKGTGHDDVL KAVDLPIVGN DRCREMHRGN FHITNTKICA GGKRNEGVCE
RDYGGPLVCQ DGDLKVIVGI SVHGRGCARA NQPGIFINVP FYTQWIYKVF RYNPNSDTA
//
