ID   CTR_PHACE               Reviewed;         276 AA.
AC   O97398; P81521;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Chymotrypsin;
DE            EC=3.4.21.1;
DE   Flags: Precursor;
OS   Phaedon cochleariae (Mustard beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX   NCBI_TaxID=80249;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAA76928.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Larval gut {ECO:0000269|PubMed:10612046};
RX   PubMed=10612046; DOI=10.1016/s0965-1748(99)00104-6;
RA   Girard C., Jouanin L.;
RT   "Molecular cloning of cDNAs encoding a range of digestive enzymes from a
RT   phytophagous beetle, Phaedon cochleariae.";
RL   Insect Biochem. Mol. Biol. 29:1129-1142(1999).
CC   -!- FUNCTION: Serine protease with chymotryptic and collagenolytic
CC       activities. {ECO:0000250|UniProtKB:Q00871}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-
CC         Xaa.; EC=3.4.21.1; Evidence={ECO:0000250|UniProtKB:Q00871,
CC         ECO:0000255|PROSITE-ProRule:PRU10078, ECO:0000255|PROSITE-
CC         ProRule:PRU10079};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:Q00871}.
CC   -!- TISSUE SPECIFICITY: Expressed in larval carcasses and gut, and adult
CC       gut. {ECO:0000269|PubMed:10612046}.
CC   -!- DEVELOPMENTAL STAGE: Ovarial and mature eggs, larvae and adult.
CC       {ECO:0000269|PubMed:10612046}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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; Y17904; CAA76928.1; -; mRNA.
DR   AlphaFoldDB; O97398; -.
DR   SMR; O97398; -.
DR   MEROPS; S01.082; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 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   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Collagen degradation; Digestion; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..45
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q00871"
FT                   /id="PRO_0000314680"
FT   CHAIN           46..276
FT                   /note="Chymotrypsin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000147324"
FT   DOMAIN          46..272
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        89
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P00771"
FT   ACT_SITE        135
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P00771"
FT   ACT_SITE        229
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P00771"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..90
FT                   /evidence="ECO:0000250|UniProtKB:P00771,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        202..215
FT                   /evidence="ECO:0000250|UniProtKB:P00771,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        225..250
FT                   /evidence="ECO:0000250|UniProtKB:P00771,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   276 AA;  29868 MW;  FC5FD05DB882A1DE CRC64;
     MKVALVVLAL FGVSLAASID NIEIPPSKNI YVEPINQPEV DPSLEIVNGQ EVVPHSIPYQ
     IFLVASAGET SWTCGGSLIT KRYVLTAAHC IQGAKSVHVT LGAHNLAKHE ASKVTVNGRS
     WVIHEKYDST NIDNDIGVIQ LERNLTLTRS IQLARLPSLR DVGINLEGRT ATVSGWGLTN
     GIFQTTTDVL RANNTIISNK ECNDVFKIVQ PTEVCLSIAG GRSACSGDSG GPLVIDNVQH
     GIVSYGSSYC RSTPSVFTRV SSYLNWLQTH SEWRAQ