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   16-JUN-2009, entry version 52.
DE   RecName: Full=Chymotrypsin;
DE            EC=3.4.21.1;
DE   Flags: Precursor;
OS   Phaedon cochleariae (Mustard beetle).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX   NCBI_TaxID=80249;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Larval gut;
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
RT   a phytophagous beetle, Phaedon cochleariae.";
RL   Insect Biochem. Mol. Biol. 29:1129-1142(1999).
CC   -!- FUNCTION: Serine protease with chymotryptic and collagenolytic
CC       activities (By similarity).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa,
CC       Phe-|-Xaa, Leu-|-Xaa.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in larval carcasses and gut, and
CC       adult gut.
CC   -!- DEVELOPMENTAL STAGE: Ovarial and mature eggs, larvae and adult.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; Y17904; CAA76928.1; -; mRNA.
DR   HSSP; P23946; 1NN6.
DR   BRENDA; 3.4.21.1; 290922.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 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;
KW   Hydrolase; Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     16       Potential.
FT   PROPEP       17     45       Activation peptide (By similarity).
FT                                /FTId=PRO_0000314680.
FT   CHAIN        46    276       Chymotrypsin.
FT                                /FTId=PRO_5000147324.
FT   DOMAIN       46    272       Peptidase S1.
FT   ACT_SITE     89     89       Charge relay system (By similarity).
FT   ACT_SITE    135    135       Charge relay system (By similarity).
FT   ACT_SITE    229    229       Charge relay system (By similarity).
FT   CARBOHYD    144    144       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    193    193       N-linked (GlcNAc...) (Potential).
FT   DISULFID     74     90       By similarity.
FT   DISULFID    202    215       By similarity.
FT   DISULFID    225    250       By similarity.
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
//