CTRC_RAT
ID CTRC_RAT Reviewed; 268 AA.
AC P55091; Q63188;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chymotrypsin-C;
DE EC=3.4.21.2;
DE AltName: Full=Caldecrin;
DE AltName: Full=Serum calcium-decreasing factor;
DE Flags: Precursor;
GN Name=Ctrc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Pancreas;
RX PubMed=8530454; DOI=10.1074/jbc.270.51.30315;
RA Tomomura A., Tomomura M., Fukushige T., Akiyama M., Kubota N., Kumaki K.,
RA Nishii Y., Noikura T., Saheki T.;
RT "Molecular cloning and expression of serum calcium-decreasing factor
RT (caldecrin).";
RL J. Biol. Chem. 270:30315-30321(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=1537555; DOI=10.1016/0378-1119(92)90646-7;
RA Kang J., Wiegand U., Mueller-Hill B.;
RT "Identification of cDNAs encoding two novel rat pancreatic serine
RT proteases.";
RL Gene 110:181-187(1992).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9538241; DOI=10.1093/oxfordjournals.jbchem.a021971;
RA Yoshino-Yasuda I., Kobayashi K., Akiyama M., Itoh H., Tomomura A.,
RA Saheki T.;
RT "Caldecrin is a novel-type serine protease expressed in pancreas, but its
RT homologue, elastase IV, is an artifact during cloning derived from
RT caldecrin gene.";
RL J. Biochem. 123:546-554(1998).
CC -!- FUNCTION: Has chymotrypsin-type protease activity and hypocalcemic
CC activity.
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 -!- TISSUE SPECIFICITY: Pancreas.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Was originally thought to be elastase IV.
CC {ECO:0000305|PubMed:1537555}.
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DR EMBL; S80379; AAB35830.1; -; mRNA.
DR EMBL; X59014; CAA41753.1; -; mRNA.
DR PIR; JQ1473; JQ1473.
DR RefSeq; NP_001071117.1; NM_001077649.2.
DR AlphaFoldDB; P55091; -.
DR SMR; P55091; -.
DR STRING; 10116.ENSRNOP00000018393; -.
DR MEROPS; S01.157; -.
DR GlyGen; P55091; 2 sites.
DR PaxDb; P55091; -.
DR GeneID; 362653; -.
DR KEGG; rno:362653; -.
DR UCSC; RGD:1308379; rat.
DR CTD; 11330; -.
DR RGD; 1308379; Ctrc.
DR VEuPathDB; HostDB:ENSRNOG00000013745; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P55091; -.
DR OMA; PDWWGSQ; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P55091; -.
DR TreeFam; TF330455; -.
DR PRO; PR:P55091; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013745; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; P55091; baseline and differential.
DR Genevisible; P55091; RN.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..29
FT /note="Activation peptide"
FT /id="PRO_0000027715"
FT CHAIN 30..268
FT /note="Chymotrypsin-C"
FT /id="PRO_0000027716"
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 90
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"
FT CONFLICT 42
FT /note="P -> A (in Ref. 2; CAA41753)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..120
FT /note="EEGSVYAEVDTIYVHEKWNRLFLWN -> AEAPCTLRWTPSTSMRSGTDSSC
FT GT (in Ref. 2; CAA41753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 29374 MW; 33B67AF34D0F8583 CRC64;
MLGITVLAAI LACASCCGNP AFPPNLSTRV VGGEDAVPNS WPWQVSLQYL KDDTWRHTCG
GSLITTSHVL TAAHCINKDF TYRVGLGKYN LTVEDEEGSV YAEVDTIYVH EKWNRLFLWN
DIAIIKLAEP VELSNTIQVA CIPEEGSLLP QDYPCYVTGW GRLWTNGPIA EVLQQGLQPI
VSHATCSRLD WWFIKVRKTM VCAGGDGVIS ACNGDSGGPL NCQAEDGSWQ VHGIVSFGSS
SGCNVHKKPV VFTRVSAYND WINEKIQL
