ID   B0WIS4_CULQU            Unreviewed;       274 AA.
AC   B0WIS4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 103.
DE   RecName: Full=Chymotrypsin {ECO:0000256|PROSITE-ProRule:PRU10078};
DE            EC=3.4.21.1 {ECO:0000256|PROSITE-ProRule:PRU10078};
GN   Name=6038909 {ECO:0000313|EnsemblMetazoa:CPIJ007079-PA};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176 {ECO:0000313|EnsemblMetazoa:CPIJ007079-PA, ECO:0000313|Proteomes:UP000002320};
RN   [1] {ECO:0000313|EnsemblMetazoa:CPIJ007079-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ007079-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- FUNCTION: Major function may be to aid in digestion of the blood meal.
CC       {ECO:0000256|ARBA:ARBA00060213}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036320};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-
CC         Xaa.; EC=3.4.21.1; Evidence={ECO:0000256|PROSITE-ProRule:PRU10078};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC       {ECO:0000256|ARBA:ARBA00024195}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; B0WIS4; -.
DR   STRING; 7176.B0WIS4; -.
DR   MEROPS; S01.130; -.
DR   EnsemblMetazoa; CPIJ007079-RA; CPIJ007079-PA; CPIJ007079.
DR   KEGG; cqu:CpipJ_CPIJ007079; -.
DR   VEuPathDB; VectorBase:CPIJ007079; -.
DR   VEuPathDB; VectorBase:CQUJHB016507; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   OMA; YNANTIT; -.
DR   OrthoDB; 10059102at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000077; Predicted protein; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR050430; Peptidase_S1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF97; GH13245P2-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Digestion {ECO:0000256|ARBA:ARBA00022757};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00274};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00274};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00274}; Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU00274};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..274
FT                   /note="Chymotrypsin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011408100"
FT   DOMAIN          48..273
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   ACT_SITE        88
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        133
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        229
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00274"
FT   DISULFID        73..89
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   274 AA;  28663 MW;  6AFADC713ED8A413 CRC64;
     MFNSLVLCLV LGRSVLLVGA VLGGESDLLP RPHYGTDFGS ILPRGYRIVG GFEISIADAP
     HQVSLQSRGS HICGGSIISP KWILTAAHCT DGASVSNLRI RAGSSKHASG GSVISIKRIV
     QHSSYNRNTI DYDYSLLELK SAISLGSNAA VIPLPAQNET VQDGTLCEVT GWGNTQSVSE
     SRANLRAAYV PAYNQNQCNS AYARYGGVTG RMLCAGYQAG GKDACQGDSG GPLVANGKLV
     GVVSWGLGCA QANYPGVYSR VAAARDWIRS NSGV
//