GenomeNet

Database: UniProt
Entry: A0A3Q1F1Z0_9TELE
LinkDB: A0A3Q1F1Z0_9TELE
Original site: A0A3Q1F1Z0_9TELE 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system