GenomeNet

Database: UniProt
Entry: A0AAE0RHJ9_9TELE
LinkDB: A0AAE0RHJ9_9TELE
Original site: A0AAE0RHJ9_9TELE 
ID   A0AAE0RHJ9_9TELE        Unreviewed;       401 AA.
AC   A0AAE0RHJ9;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   RecName: Full=trypsin {ECO:0000256|ARBA:ARBA00038868};
DE            EC=3.4.21.4 {ECO:0000256|ARBA:ARBA00038868};
GN   ORFNames=QTP70_019024 {ECO:0000313|EMBL:KAK3553974.1};
OS   Hemibagrus guttatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Bagridae; Hemibagrus.
OX   NCBI_TaxID=175788 {ECO:0000313|EMBL:KAK3553974.1, ECO:0000313|Proteomes:UP001274896};
RN   [1] {ECO:0000313|EMBL:KAK3553974.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Male_cb2023 {ECO:0000313|EMBL:KAK3553974.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAK3553974.1};
RA   Bian C.;
RT   "Male Hemibagrus guttatus genome.";
RL   Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036320};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000256|ARBA:ARBA00004239}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAK3553974.1}.
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   EMBL; JAUCMX010000002; KAK3553974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAE0RHJ9; -.
DR   Proteomes; UP001274896; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031639; P:plasminogen activation; IEA:TreeGrafter.
DR   GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IEA:TreeGrafter.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000003; Transmembrane serine protease 3; 1.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR050127; Serine_Proteases_S1.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24264:SF38; UROKINASE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121}; Plasminogen activation {ECO:0000256|ARBA:ARBA00023202};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP001274896};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..401
FT                   /note="trypsin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041936533"
FT   DOMAIN          51..115
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          141..388
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   401 AA;  45912 MW;  C418DA128BC81DF0 CRC64;
     MWLLITLLMT CSLHEVAESS KHKYWPWITN VLNSGKHGKQ HDVHCLAKGS NGNEYRGTVS
     VTFSGQKCLY WHQILEHKAV GQHNYCRNPD NRSGPWCWVW EDKQKVRRFC DIPRCETKRN
     TPKQDTEMTC GKRIHKPRFK IIGGLRASIE SQPWLASIFK YNTFSCGGTL ISPCWVLTAA
     HCFPDGKRTI KDKYSVYLGK DATNETNLDK EQKFKITKLV LHPEFNSDSE DFNNDIALLQ
     IVDSNGQCAQ KTDSVRIACL PPPQQMMPYG AYCHIAGYGH EKNDDIPDTF RYSRFMKETK
     VEILSNIVCE RKDYYGNRVT ENQFCAASPK WTEDACQGDS GGPLLCKANN RMFLFGIISW
     GEGCAIKKKP GVYTKVTNYN KWIAEQTGLH TYTEGIMYPQ K
//
DBGET integrated database retrieval system