ID U4U680_DENPD Unreviewed; 484 AA.
AC U4U680;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=trypsin {ECO:0000256|ARBA:ARBA00038868};
DE EC=3.4.21.4 {ECO:0000256|ARBA:ARBA00038868};
GN ORFNames=D910_06745 {ECO:0000313|EMBL:ERL89374.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL89374.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL89374.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036320};
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DR EMBL; KB632168; ERL89374.1; -; Genomic_DNA.
DR AlphaFoldDB; U4U680; -.
DR STRING; 77166.U4U680; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..484
FT /note="trypsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004655939"
FT DOMAIN 35..266
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 227..483
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 484 AA; 52235 MW; 701B8E046AA95620 CRC64;
MKLKILALLY VIQVCQSKTL PGIFSPLFKQ QDSRIVGGSP VNIDNYPYQV SLEYIYSHMC
GGAIISNRWV LTAAHCTQLF LAYTPPSLFT IRLGTSFVES EGERFTVNQV IEHPGYGNSA
HFFDYDMCLI QVSREIVFSN SVQPVALPAP HAPLIPGSRC LVSGWGTLTE GGSSPSQLHA
VEVPLISIES CNEYYQNGLG VTETMMCAGS PYGGRDACQG DSGGPLVVGN ILIGIVSWGA
GCARPNFPGV YANVPFVREW ITEVAVNIEN YPYQVSLEYV YRHICGGAII SNRWVLSAAH
CTQLWRDYTP PSLFTIRMGT SFLQSEGERF TVTRVIEHPG YGNTATPFDY DMCLIQVSRE
IVSSNSLQPV ALPAPHAPLI PGSRCVISGW GALTEGGSSP SQLHAVAVPL ISIESADVTE
TMMCAGSPYG GRDACQGDSG GPLIVDNVLI GIVSWGAGCA RPNFPGVYAN VPFMREWITE
VSGV
//
