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Database: UniProt
Entry: W5NER0_LEPOC
LinkDB: W5NER0_LEPOC
Original site: W5NER0_LEPOC 
ID   W5NER0_LEPOC            Unreviewed;       724 AA.
AC   W5NER0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019119.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000019119.1}
RP   IDENTIFICATION.
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   EMBL; AHAT01029105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NER0; -.
DR   STRING; 7918.ENSLOCP00000019119; -.
DR   Ensembl; ENSLOCT00000019151.1; ENSLOCP00000019119.1; ENSLOCG00000015530.1.
DR   eggNOG; ENOG502QR40; Eukaryota.
DR   GeneTree; ENSGT00940000156019; -.
DR   InParanoid; W5NER0; -.
DR   OMA; CNIKVCE; -.
DR   Proteomes; UP000018468; Linkage group LG8.
DR   Bgee; ENSLOCG00000015530; Expressed in ovary and 10 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00108; KR; 4.
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; 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; 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; 3.
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:UP000018468};
KW   Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152}.
FT   DOMAIN          16..116
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          120..199
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          203..281
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          294..373
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          382..462
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          488..719
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        204..281
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        225..264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        253..276
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        316..355
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        344..367
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   724 AA;  82443 MW;  BE362A2594FCD786 CRC64;
     ADKSLPQSFV NLCLICPVVY PVYKSKHPRR NSLHDYRKSD GIHLFKTDSS LLTKSKSLSE
     VKCARRCSRN KGLSFICRAF HFDQKTRKCH WLSFDSNTPG VKKEQDFSFD LYEKKDYTRE
     CIIGEGSSYK GIKSVTKTGL KCQAWASSVP HDHNFLPSRF KRKDLKENYC RNPNNETSGP
     WCYTTDPDIR HQSCEIPQCS EVECMTCNGE NYRGPMDHTE TGKECQRWDL TRPHKHTFHP
     KRYPDKGLND NYCRNPDNRL RPWCFTLDPQ TPWEYCNIKV CDVNAKTDID TTTKCFRGQG
     EQYRGTVAVT PDGVQCQRWD SQFPHNHSYT PENYKCQDLR ENYCRNPDGA ELPWCFTVDT
     KVRTAFCTNI PRCDTEPPAT EECFEGNGEE YRGHLSKTRS GVPCAMWEDN LDRRCITNSA
     TNSEIASLEN NFCRNPDKDK HGPWCYTNNS SVPWDYCMIK PCKPSSNVIP TKSDPSQISC
     FRHKRIRIVG GAPVKIKEAS WMVSIQKGNS HWCGGSLVRE DWVLTDKQCF SSCVPDLAEY
     SVWMGFLHLN DTGREESEKQ VLKISHVVCG PEGSNLALLK LSGNRAALQT ENVRTIPLPV
     TGCAIPEHTN CTMYGWGETK GTGHDGIMKV VQLPIVSNER CNAYHRGSLP ITESRLCAGG
     KRDEGVCEKD YGGSLVCEEG DFKVVVGVSV HGRGCARSNR PAIFVNVPYY AEWIHKVFKY
     YSNL
//
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