ID M3ZQC7_XIPMA Unreviewed; 719 AA.
AC M3ZQC7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
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:ENSXMAP00000004420.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000004420.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000004420.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000004420.1};
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 RefSeq; XP_014325357.1; XM_014469871.1.
DR AlphaFoldDB; M3ZQC7; -.
DR STRING; 8083.ENSXMAP00000004420; -.
DR Ensembl; ENSXMAT00000004425.2; ENSXMAP00000004420.1; ENSXMAG00000004388.2.
DR GeneID; 102226489; -.
DR KEGG; xma:102226489; -.
DR CTD; 100334116; -.
DR eggNOG; ENOG502QR40; Eukaryota.
DR GeneTree; ENSGT00940000156019; -.
DR HOGENOM; CLU_017565_0_0_1; -.
DR InParanoid; M3ZQC7; -.
DR OMA; CNIKVCE; -.
DR OrthoDB; 211181at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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:UP000002852};
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_5004046450"
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; 81602 MW; 6A316A54F8FFCF79 CRC64;
MKAMWIYRLV VGLAVVSCCE SRRNALQDYQ KSEGTRLAIV SPDSSHLTKS RKLSLTKCAK
TCSRGKRLPF NCRAFLYDHR NRKCQWLSFD RNSAGAQSHQ NIDYDLYQKK DYIRECIVGT
GQSYRGRRSV TVSGILCQAW ASPIPHEHKF MSKRYRKKDL IENYCRNPDN STVGPWCFTT
DPRPDLRHQE CGIPQCSQVE CITCNGEDYR GPMDYTESGK ECQRWDLNEP HKHTYHPSRY
PDKGLHDNYC RNPDGRHRPW CFTTDPNTHW EYCNIKVCET PPKSPEAETT ECYEGRGEGY
RGTADTTPIG LACQRWDSQY PHNHTFLPEA YPCKDLKENY CRNPDGQEFP WCFTTDPRVR
TMFCTQIPQC GIQNSPVSDC FSGFGENYQG EQSRTRSNLP CAPWRDHSNR GERGMLMAGL
EGNFCRNPDK DKHGPWCFAN NSAISWDYCN VKPCDALQNS IPPVFVPEPT PVRCFIHKRT
RIVGGAPVGI SDGSWMVSIQ KGSVHWCGGS LVREEWVLTD RQCFSSCVPD LSEYRVWLGV
SDLREGSPDR PKRQEVRIAQ VICGPNGSSL ALLRLSKPAR PADNVHTIQL PVAGCSIPEG
TMCKMYGWGE TKGTGHDDVL KAVDLPIVGN DRCREMHRGN FHITNTKICA GGKRNEGVCE
RDYGGPLVCQ DGDLKVIVGI SVHGRGCARA NQPGIFINVP FYTQWIYKVF RYNPNSETA
//
