CTR2_VESOR
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 03-AUG-2022, entry version 101.
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:0005615; C:extracellular space; 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; -; 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 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
