ID A0A3P8VG89_CYNSE Unreviewed; 685 AA.
AC A0A3P8VG89;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Hepatocyte growth factor-like {ECO:0000313|Ensembl:ENSCSEP00000013352.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000013352.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000013352.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000013352.1}
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; A0A3P8VG89; -.
DR Ensembl; ENSCSET00000013511.1; ENSCSEP00000013352.1; ENSCSEG00000008613.1.
DR GeneTree; ENSGT00940000156019; -.
DR Proteomes; UP000265120; Chromosome 8.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 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; 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; 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 Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542,
KW ECO:0000256|PIRNR:PIRNR001152}.
FT DOMAIN 1..84
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 95..166
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 170..248
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 263..342
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 351..429
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 456..677
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 171..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 192..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 220..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 285..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 313..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 352..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 685 AA; 78867 MW; 965C1F00F0362ED2 CRC64;
MLQRYEKTEK RMLVCTDCPQ SPVVLKSRSQ EHCARKCKVK RNFSCRAFNF HRHNRKCHLL
PFDRFTRGVK KQANVNFTLY EKKDYIRECI SDTLDYRGRR SWTKSNITCQ AWADNNINEH
RYDPERHPTQ DLRENFCRNP DNESGGPWCF TTDPNVRTEK CGIPQCSEEV CMKCNGEDYR
GKVDYTESGK ECQRWDSVRP HKHRFQPKKY RDKDLKDNYC RNPDNRPRPW CYTIDPKTPW
EYCNISLCES TSSEDTDVNV TTSCFQGTGT DYRGTMNVTP EGVTCQRWDS QFPHNHSFLP
QNFRCKDLRE NYCRNPNGED YPWCFTTDPN QRIANCTHIP RCDAEDSQKT ECYEDKGETY
RGTLSITRSG IPCANWSLHI NSEDSHSTVS HVGLEKNYCR NPDRDKHGPW CYTNPNSRLA
WDYCKLKRCE SSTVAQLNQT QPRPKISCFV HISTRIVGGH QVRGADGSWV VSIQRERVHL
CGGSLIREDW VLTDQQCFTS CVPDLRDYSV QVGLKHLNES SNHPRLRISR LICGPEGSNL
VMLKLADAAP VSEGAFTIHL PVKDCHIPEG TNCSMYGWGE TKNTGHDQTL NTVIMPMVDN
NMCSRIKGKA GESRICAGGK RGEGVCDKDN GGPLVCQEHE RRVIVGVSIQ RTKCASSQPA
LFVNVAFYSE WIYKVFRLYP SVESD
//
