CTRC_MOUSE
ID CTRC_MOUSE Reviewed; 268 AA.
AC Q3SYP2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Chymotrypsin-C;
DE EC=3.4.21.2;
DE Flags: Precursor;
GN Name=Ctrc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has chymotrypsin-type protease activity and hypocalcemic
CC activity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, Phe-|-Xaa, Met-|-
CC Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa.; EC=3.4.21.2;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-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; BC103715; AAI03716.1; -; mRNA.
DR EMBL; BC115516; AAI15517.1; -; mRNA.
DR EMBL; BC115517; AAI15518.1; -; mRNA.
DR RefSeq; NP_001029047.1; NM_001033875.2.
DR AlphaFoldDB; Q3SYP2; -.
DR SMR; Q3SYP2; -.
DR STRING; 10090.ENSMUSP00000039879; -.
DR MEROPS; S01.157; -.
DR GlyGen; Q3SYP2; 4 sites.
DR PaxDb; Q3SYP2; -.
DR PRIDE; Q3SYP2; -.
DR ProteomicsDB; 285419; -.
DR DNASU; 76701; -.
DR GeneID; 76701; -.
DR KEGG; mmu:76701; -.
DR UCSC; uc008vpk.1; mouse.
DR CTD; 11330; -.
DR MGI; MGI:1923951; Ctrc.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q3SYP2; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q3SYP2; -.
DR BioGRID-ORCS; 76701; 1 hit in 66 CRISPR screens.
DR ChiTaRS; Ctrc; mouse.
DR PRO; PR:Q3SYP2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3SYP2; protein.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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 Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..29
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000288616"
FT CHAIN 30..268
FT /note="Chymotrypsin-C"
FT /id="PRO_0000288617"
FT DOMAIN 30..267
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 121
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 17..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 59..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 155..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 186..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 212..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 268 AA; 29470 MW; F5B813882E5F93C4 CRC64;
MLGITVLAAI LACASSCGDP TFPPNLSARV VGGEDAVPNS WPWQVSLQYL RDDTWRHTCG
GSLITTSHVL TAAHCINTNL TYRVGLGKYN LTVEDEEGSV YAEVDTIYVH EKWNRLLLWN
DIAIIKLAEP VELSDTIQVA CIPEQDSLLP GDYPCYVTGW GRLWTNGPIA EVLQQGLQPI
VNHTTCSRLD WWFIKVRETM VCAGGDGVIS ACNGDSGGPL NCPVEDGLWQ VHGIVSFGSS
RGCNTYKKPV VFTRVSAYID WIKEKIQL
