CTRB1_PENVA
ID CTRB1_PENVA Reviewed; 271 AA.
AC Q00871;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chymotrypsin BI;
DE EC=3.4.21.1;
DE Flags: Precursor;
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 EMBL; X66415; CAA47046.1; -; mRNA.
DR PIR; S29239; S29239.
DR AlphaFoldDB; Q00871; -.
DR SMR; Q00871; -.
DR MEROPS; S01.122; -.
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:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
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 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_0000027650"
FT CHAIN 46..271
FT /note="Chymotrypsin BI"
FT /id="PRO_0000027651"
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; 28685 MW; 0967398D5401E5B7 CRC64;
MIGKLSLLLV CVAVASGNPA AGKPWHWKSP KPLVDPRIHV NATPRIVGGV EATPHSWPHQ
AALFIDDMYF CGGSLISSEW VLTAAHCMDG AGFVEVVLGA HNIRQNEASQ VSITSTDFFT
HENWNSWLLT NDIALIRLPS PVSLNSNIKT VKLPSSDVSV GTTVTPTGWG RPSDSASGIS
DVLRQVNVPV MTNADCDSVY GIVGDGVVCI DGTGGKSTCN GDSGGPLNLN GMTYGITSFG
SSAGCEKGYP AAFTRVYYYL DWIQQKTGVT P