ID   CTRA_GADMO              Reviewed;         263 AA.
AC   P47796;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Chymotrypsin A;
DE            EC=3.4.21.1;
DE   Flags: Precursor;
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pyloric caecum;
RX   PubMed=8086467; DOI=10.1016/0167-4781(94)90274-7;
RA   Gudmundsdottir A., Oskarsson S., Eakin A.E., Craik C.S., Bjarnason J.B.;
RT   "Atlantic cod cDNA encoding a psychrophilic chymotrypsinogen.";
RL   Biochim. Biophys. Acta 1219:211-214(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-30 AND 34-49.
RC   TISSUE=Pyloric caecum;
RX   PubMed=1764912; DOI=10.1016/0305-0491(91)90050-n;
RA   Asgeirsson B., Bjarnason J.B.;
RT   "Structural and kinetic properties of chymotrypsin from Atlantic cod (Gadus
RT   morhua). Comparison with bovine chymotrypsin.";
RL   Comp. Biochem. Physiol. 99B:327-335(1991).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X78490; CAA55242.1; -; mRNA.
DR   PIR; S47537; S47537.
DR   AlphaFoldDB; P47796; -.
DR   SMR; P47796; -.
DR   STRING; 8049.ENSGMOP00000010152; -.
DR   MEROPS; S01.437; -.
DR   Proteomes; UP000694546; Unplaced.
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:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 3.
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   Digestion; Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:1764912"
FT   CHAIN           19..263
FT                   /note="Chymotrypsin A"
FT                   /id="PRO_0000027646"
FT   DOMAIN          34..261
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        60..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        154..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        186..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        209..238
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        21
FT                   /note="R -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="S -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        29
FT                   /note="T -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="S -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="S -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   263 AA;  28294 MW;  47AAC699A0A64FBB CRC64;
     MGHEVDSVLP GLFRRTYGCG RPAISPVITG YSRIVNGEEA VPHSWSWQVS LQDQTGFHFC
     GGSLINENWV VTAAHCNVKN YHRVVLGEHD RSSNSEGVQV MTVGQVFKHP RYNGFTINND
     ILLVKLATPA TLNMRVSPVC LAETDDVFEG GMKCVTSGWG LTRYNAADTP ALLQQAALPL
     LTNEQCKKFW GNKISDLMIC AGAAGASSCM GDSGGPLVCQ KAGSWTLVGI VSWGSGTCTP
     TMPGVYARVT ELRAWVDQTI AAN