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 03-MAR-2009, entry version 30. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Has chymotrypsin-type protease activity and hypocalcemic CC activity (By similarity). CC -!- CATALYTIC ACTIVITY: Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, CC Phe-|-Xaa, Met-|-Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase CC subfamily. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC103715; AAI03716.1; -; mRNA. DR EMBL; BC115516; AAI15517.1; -; mRNA. DR EMBL; BC115517; AAI15518.1; -; mRNA. DR IPI; IPI00378682; -. DR RefSeq; NP_001029047.1; -. DR UniGene; Mm.440471; -. DR SMR; Q3SYP2; 17-268. DR MEROPS; S01.157; -. DR Ensembl; ENSMUSG00000062478; Mus musculus. DR GeneID; 76701; -. DR KEGG; mmu:76701; -. DR MGI; MGI:1923951; Ctrc. DR HOGENOM; Q3SYP2; -. DR HOVERGEN; Q3SYP2; -. DR BRENDA; 3.4.21.2; 244. DR NextBio; 345647; -. DR ArrayExpress; Q3SYP2; -. DR Bgee; Q3SYP2; -. DR CleanEx; MM_CTRC; -. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR018114; Peptidase_S1/S6_AS. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 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 Disulfide bond; Glycoprotein; Hydrolase; Protease; Serine protease; KW Signal; Zymogen. FT SIGNAL 1 16 Potential. FT PROPEP 17 29 Activation peptide (By similarity). FT /FTId=PRO_0000288616. FT CHAIN 30 268 Chymotrypsin-C. FT /FTId=PRO_0000288617. FT DOMAIN 30 267 Peptidase S1. FT ACT_SITE 74 74 Charge relay system (By similarity). FT ACT_SITE 121 121 Charge relay system (By similarity). FT ACT_SITE 216 216 Charge relay system (By similarity). FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential). FT CARBOHYD 79 79 N-linked (GlcNAc...) (Potential). FT CARBOHYD 90 90 N-linked (GlcNAc...) (Potential). FT CARBOHYD 182 182 N-linked (GlcNAc...) (Potential). FT DISULFID 17 141 By similarity. FT DISULFID 59 75 By similarity. FT DISULFID 155 222 By similarity. FT DISULFID 186 202 By similarity. FT DISULFID 212 243 By similarity. 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 //