ID   CTR2_VESCR              Reviewed;         218 AA.
AC   P00769;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Chymotrypsin-2;
DE            EC=3.4.21.1;
DE   AltName: Full=Chymotrypsin II;
OS   Vespa crabro (European hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=7445;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Jany K.-D., Haug H.;
RT   "Amino acid sequence of the chymotryptic protease II from the larvae of the
RT   nornet, Vespa crabro.";
RL   FEBS Lett. 158:98-102(1983).
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   -!- MISCELLANEOUS: An additional Arg at the carboxyl end was found in some
CC       of the molecules.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   PIR; A00955; KYVH2C.
DR   AlphaFoldDB; P00769; -.
DR   SMR; P00769; -.
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..218
FT                   /note="Chymotrypsin-2"
FT                   /id="PRO_0000088676"
FT   DOMAIN          1..218
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        39
FT                   /note="Charge relay system"
FT   ACT_SITE        84
FT                   /note="Charge relay system"
FT   ACT_SITE        175
FT                   /note="Charge relay system"
FT   DISULFID        25..40
FT   DISULFID        148..161
FT   DISULFID        171..195
SQ   SEQUENCE   218 AA;  23677 MW;  509AB50DE190EB39 CRC64;
     IVGGTDAPRG KYPYQVSLRA PKHFCGGSIS KRYVLTAAHC LVGKSKHQVT VHAGSVLLNK
     EEAVYNAEEL IVNKNYNSIR LINDIGLIRV SKDISYTQLV QPVKLPVSNT IKAGDPVVLT
     GWGRIYVNGP IPNNLQQITL SIVNQQTCKF KHWGLTDSQI CTFTKLGEGA CDGDSGGPLV
     ANGVQIGIVS YGHPCAVGSP NVFTRVYSFL DWIQKNQL
//