ID   CTR2_VESOR              Reviewed;         216 AA.
AC   P00768;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Chymotrypsin-2;
DE            EC=3.4.21.1;
DE   AltName: Full=Chymotrypsin II;
OS   Vespa orientalis (Oriental hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=7447;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX   PubMed=6340663; DOI=10.1016/0006-291x(83)91251-2;
RA   Jany K.-D., Bekelar K., Pfleiderer G., Ishay J.;
RT   "Amino acid sequence of an insect chymotrypsin from the larvae of the
RT   hornet, Vespa orientalis.";
RL   Biochem. Biophys. Res. Commun. 110:1-7(1983).
RN   [2]
RP   ACTIVE SITE.
RX   PubMed=6786354; DOI=10.1016/0005-2795(81)90164-1;
RA   Jany K.-D., Bekelar K., Ishay J.;
RT   "The amino acid sequences around the reactive serine and histidine residues
RT   of the chymotrypsin-like protease from the hornet, Vespa orientalis.";
RL   Biochim. Biophys. Acta 668:197-200(1981).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-
CC         Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078,
CC         ECO:0000255|PROSITE-ProRule:PRU10079};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   PIR; A00954; KYVH2O.
DR   AlphaFoldDB; P00768; -.
DR   SMR; P00768; -.
DR   MEROPS; S01.438; -.
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:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
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; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24250:SF65; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW   Serine protease.
FT   CHAIN           1..216
FT                   /note="Chymotrypsin-2"
FT                   /id="PRO_0000088677"
FT   DOMAIN          1..216
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        39
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:6786354"
FT   ACT_SITE        82
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:6786354"
FT   ACT_SITE        173
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:6786354"
FT   DISULFID        25..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:6340663"
FT   DISULFID        146..159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:6340663"
FT   DISULFID        169..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:6340663"
SQ   SEQUENCE   216 AA;  23471 MW;  F235BF992AEFEDE1 CRC64;
     IVGGTNAPRG KYPYQVSLRA PKHFCGGSIS KRYVLTAAHC LVGKSEHQVT VGSVLLNKEE
     AVYNAKELIV NKNYNSIRLI NDIGLIRVSK DISFTQLVQP VKLPVSNTIK AGDPVVLTGW
     GRIYVNGPIP NNLQQITLSI VNQQTCKSKH WGLTDSQICT FTKRGEGACH GDSGGPLVAN
     GVQIGIVSYG HPCAIGSPNV FTRVYSFLDW IQKNQL
//