ID A0A087X9S0_POEFO Unreviewed; 674 AA.
AC A0A087X9S0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Hepatocyte growth factor a {ECO:0000313|Ensembl:ENSPFOP00000002523.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000002523.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000002523.2}
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 EMBL; AYCK01009975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01009976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087X9S0; -.
DR STRING; 48698.ENSPFOP00000002523; -.
DR Ensembl; ENSPFOT00000002527.2; ENSPFOP00000002523.2; ENSPFOG00000002427.2.
DR eggNOG; ENOG502QR40; Eukaryota.
DR GeneTree; ENSGT00940000156019; -.
DR OMA; NSVTMPM; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IEA:Ensembl.
DR GO; GO:0021603; P:cranial nerve formation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00108; KR; 4.
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; 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; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001152; HGF_MST1; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 4.
DR SMART; SM00020; Tryp_SPc; 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; 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:UP000028760};
KW Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152}.
FT DOMAIN 67..146
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 150..228
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 243..322
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 331..409
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 444..666
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 151..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 172..211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 200..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 265..304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 293..316
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 332..409
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 674 AA; 77079 MW; 0C50803F2CAB1B48 CRC64;
VQNELQNMIG CCQKHRRQFL QNRAFNFQKD NRKCHLLPFD RFTHGAQKQA NINFTLCFFV
LSEYIRECIS GTKDNYRGRR SWTKSNITCQ AWSDNNINEH TFYPDRYPKQ DLRENFCRNP
NNDPGGPWCY TTDPNVRAEE CGIPQCSQDV CMRCNGEDYR GKVDQTESGK ECQRWDSKWP
HEHPFQPKKY RDKDLRDNYC RNPNNRLRPW CHTMDPRTPW EYCNITMCDS DHSEEIDVNT
TTSCIQRDGA NYRGTLNVTP EGVTCQRWDS QFPHNHSFLP VNFKCKDLRE NYCRNPDGAD
YPWCFTTDPN QRIAKCTHIP RCDAEATPKI DCYEDNGEMY QGALSTTRSG IPCADWAPHI
NSGDSHSTIS HVGLERNYCR NPDRDKHGPW CYTSPNNRLV WDYCKLKQCE STIKNYLALL
EGESSVFSVK ASNNDSDVQI NTRIVGGHEV QGADGGWVVS IQREKVHQCG GSLIREDWVL
TTYDQCFTSC VPDLKDYSIQ VGLRHLNESS RRPRLGISRL ICGPEGSNLV MLKLENPAPV
SEGASTIHLP VKECHIAEGT NCTMYGWGET KSTGLDEALN SVTMPMVDNE KCPHTKGDAE
KSRICAGGNK DEGVCERDDG GPLVCQEHHR KVIVGVSTPR AKCASAQPAL FVNVAFYSEW
IYKVFRLYPS LPRN
//
