ID A0A3Q1F1Z0_9TELE Unreviewed; 665 AA.
AC A0A3Q1F1Z0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Hepatocyte growth factor {ECO:0000313|Ensembl:ENSAPOP00000010379.1};
GN Name=HGF {ECO:0000313|Ensembl:ENSAPOP00000010379.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000010379.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000010379.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A3Q1F1Z0; -.
DR STRING; 80966.ENSAPOP00000010379; -.
DR Ensembl; ENSAPOT00000017646.1; ENSAPOP00000010379.1; ENSAPOG00000012803.1.
DR GeneTree; ENSGT00940000156019; -.
DR InParanoid; A0A3Q1F1Z0; -.
DR Proteomes; UP000257200; Unplaced.
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; 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; 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; 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 Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..665
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018654376"
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..665
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 665 AA; 75823 MW; 078AB2CA2D077B4E CRC64;
MWIYKLVFGL FLVSCSEGRR NALQDYQKTD GVQLVVTSPD SSHLTKSRKL SLSRCAKSCS
RSRRLPFACR AFVYDHKNRK CQWLSFDRNS PGTQIHQNIN YQLYQKKDYV RECIVGTGQS
YRGRRSVTVS GILCQAWASP IPHEHKFMSK RFRKKDLREN YCRNPDNSTV GPWCFTTDPR
PHLRHQECGI PQCSQVECMN CNGEDYRGPM DHTESGKECQ RWDLDEPHKH LYHPRRYPDK
GLDDNYCRNP DGRHRPWCFT TDPNTSWEYC NIKVCETPQK SNVLETTECY QGRGEGYRGT
VDVTPTGLTC QRWDSQYPHN HTFTPQAYPC KDLRENYCRN PDGQEFPWCF TTDPRVRTIF
CTNIPQCGTQ NKPVSDCYES FGENYQGQQS RTRSNLPCAP WRDHSNSGER GMLTASLEGN
YCRNPDKDKH GPWCHTNNSA ILWDYCNVKP CDTSLNTIPL GGLSSVSCFI HKRPRIVGGG
RVGISDGSWM VSIQRGSVHW CGGSLIREEW VLTDRQCFSS CVPDLSEYRV WLGVSDIRED
APDWSKRQEV SIAHVICGPE GSSLALLKLS KPASPADNVH TIQLPVAGCS IPEDTICKMY
GWGETKGTGH DDVLKSVDLP IVSSGRCREM HRGNLHITNT KICAGGRKNE GVCEVNCWEQ
FVLLS
//