ID   CTRB2_PENVA             Reviewed;         271 AA.
AC   P36178;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-SEP-2026, entry version 101.
DE   RecName: Full=Chymotrypsin BII;
DE            EC=3.4.21.1;
DE   Flags: Precursor;
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Communostraca;
OC   Malacostraca; Eumalacostraca; Stomatocarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hepatopancreas;
RX   PubMed=1516690; DOI=10.1016/0014-5793(92)80777-e;
RA   Sellos D., van Wormhoudt A.;
RT   "Molecular cloning of a cDNA that encodes a serine protease with
RT   chymotryptic and collagenolytic activities in the hepatopancreas of the
RT   shrimp Penaeus vanameii (Crustacea, Decapoda).";
RL   FEBS Lett. 309:219-224(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-65, AND CHARACTERIZATION.
RC   TISSUE=Hepatopancreas;
RX   PubMed=1458841; DOI=10.1016/0305-0491(92)90389-9;
RA   van Wormhoudt A., le Chevalier P., Sellos D.;
RT   "Purification, biochemical characterization and N-terminal sequence of a
RT   serine-protease with chymotrypsic and collagenolytic activities in a
RT   tropical shrimp, Penaeus vannamei (Crustacea, Decapoda).";
RL   Comp. Biochem. Physiol. 103B:675-680(1992).
CC   -!- FUNCTION: Serine protease with chymotryptic and collagenolytic
CC       activities.
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   AlphaFoldDB; P36178; -.
DR   SMR; P36178; -.
DR   MEROPS; S01.122; -.
DR   EnsemblMetazoa; XM_027356789.1; XP_027212590.1; LOC113805736.
DR   OrthoDB; 5565075at2759; -.
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:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000034; Eupolytin; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR050430; Peptidase_S1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 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   Collagen degradation; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..45
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:1458841"
FT                   /id="PRO_0000027652"
FT   CHAIN           46..271
FT                   /note="Chymotrypsin BII"
FT                   /id="PRO_0000027653"
FT   DOMAIN          46..268
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        86
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        132
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        223
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        196..209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        219..245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   271 AA;  28723 MW;  2254D7C7E63FA2E1 CRC64;
     MIGKLSLLLV CVAVASGNPA AGKPWHWKSP KPLVDPRIHV NATPRIVGGV EATPHSWPHQ
     AALFIDDMYF CGGSLISSEW VLTAAHCMDG AGFVEVVLGA HNIRQNEASQ VSITSTDFFT
     HENWNSWLLT NDIALIKLPS PVSLNSNIKT VKLPSSDVAV GTTVTPTGWG RPLDSAGGIS
     DVLRQVDVPI MTNDDCDAVY GIVGNGVVCI DSEGGKGTCN GDSGGPLNLN GMTYGITSFG
     SSAGCEVGYP DAFTRVYYYL DWIEQKTGVT P
//