ID   CTR2_CANLF              Reviewed;         263 AA.
AC   P04813;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   02-SEP-2026, entry version 155.
DE   RecName: Full=Chymotrypsinogen 2;
DE            EC=3.4.21.1;
DE   Contains:
DE     RecName: Full=Chymotrypsin 2 chain A;
DE   Contains:
DE     RecName: Full=Chymotrypsin 2 chain B;
DE   Contains:
DE     RecName: Full=Chymotrypsin 2 chain C;
DE   Flags: Precursor;
GN   Name=CTRB1; Synonyms=CTRB;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6584866; DOI=10.1073/pnas.80.24.7486;
RA   Pinsky S.D., Laforge K.S., Luc V., Scheele G.;
RT   "Identification of cDNA clones encoding secretory isoenzyme forms: sequence
RT   determination of canine pancreatic prechymotrypsinogen 2 mRNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:7486-7490(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   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; K01173; AAA30841.1; -; mRNA.
DR   PIR; A21195; A21195.
DR   RefSeq; NP_001183984.1; NM_001197055.1.
DR   AlphaFoldDB; P04813; -.
DR   SMR; P04813; -.
DR   FunCoup; P04813; 41.
DR   STRING; 9615.ENSCAFP00000029763; -.
DR   MEROPS; S01.152; -.
DR   PaxDb; 9615-ENSCAFP00000029763; -.
DR   Ensembl; ENSCAFT00000036999; ENSCAFP00000032437; ENSCAFG00000020084.
DR   Ensembl; ENSCAFT00030004451; ENSCAFP00030003946; ENSCAFG00030002402.
DR   Ensembl; ENSCAFT00040022821; ENSCAFP00040019772; ENSCAFG00040012242.
DR   Ensembl; ENSCAFT00805017184; ENSCAFP00805013491; ENSCAFG00805009369.
DR   Ensembl; ENSCAFT00845043296.1; ENSCAFP00845033932.1; ENSCAFG00845024500.1.
DR   GeneID; 479649; -.
DR   KEGG; cfa:479649; -.
DR   VEuPathDB; HostDB:ENSCAFG00845024500; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000153216; -.
DR   HOGENOM; CLU_006842_7_6_1; -.
DR   InParanoid; P04813; -.
DR   OMA; WLLSYCA; -.
DR   OrthoDB; 5918597at2759; -.
DR   Reactome; R-CFA-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-CFA-9758881; Uptake of dietary cobalamins into enterocytes.
DR   Proteomes; UP000805418; Chromosome 5.
DR   Bgee; ENSCAFG00000020084; Expressed in pancreas and 45 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000118; Chymotrypsinogen A; 1.
DR   FunFam; 2.40.10.10:FF:000176; Chymotrypsinogen A; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24250:SF65; CHYMOTRYPSINOGEN B; 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   2: Evidence at transcript level;
KW   Digestion; Disulfide bond; Hydrolase; Phosphoprotein; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT   CHAIN           19..263
FT                   /note="Chymotrypsinogen 2"
FT                   /id="PRO_0000027634"
FT   CHAIN           19..31
FT                   /note="Chymotrypsin 2 chain A"
FT                   /id="PRO_0000027635"
FT   CHAIN           34..164
FT                   /note="Chymotrypsin 2 chain B"
FT                   /id="PRO_0000027636"
FT   CHAIN           167..263
FT                   /note="Chymotrypsin 2 chain C"
FT                   /id="PRO_0000027637"
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   ACT_SITE        120
FT                   /note="Charge relay system"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CR35"
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"
SQ   SEQUENCE   263 AA;  27787 MW;  2A2F449D813B3961 CRC64;
     MAFLWLLSCF ALLGTAFGCG VPAIQPVLSG LSRIVNGEDA VPGSWPWQVS LQDSTGFHFC
     GGSLISEDWV VTAAHCGVRT THQVVAGEFD QGSDAESIQV LKIAKVFKNP KFNMFTINND
     ITLLKLATPA RFSKTVSAVC LPQATDDFPA GTLCVTTGWG LTKHTNANTP DKLQQAALPL
     LSNAECKKFW GSKITDLMVC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSGTCST
     STPGVYARVT KLIPWVQQIL QAN
//