LOCUS       NM_001077649             898 bp    mRNA    linear   ROD 11-NOV-2023
DEFINITION  Rattus norvegicus chymotrypsin C (Ctrc), mRNA.
ACCESSION   NM_001077649 XM_001073208 XM_001076330
VERSION     NM_001077649.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (bases 1 to 898)
  AUTHORS   Lacruz RS, Smith CE, Smith SM, Hu P, Bringas P Jr, Sahin-Toth M,
            Moradian-Oldak J and Paine ML.
  TITLE     Chymotrypsin C (caldecrin) is associated with enamel development
  JOURNAL   J Dent Res 90 (10), 1228-1233 (2011)
   PUBMED   21828354
  REMARK    GeneRIF: possibly involved in enamel development
REFERENCE   2  (bases 1 to 898)
  AUTHORS   Yoshino-Yasuda I, Kobayashi K, Akiyama M, Itoh H, Tomomura A and
            Saheki T.
  TITLE     Caldecrin is a novel-type serine protease expressed in pancreas,
            but its homologue, elastase IV, is an artifact during cloning
            derived from caldecrin gene
  JOURNAL   J Biochem 123 (3), 546-554 (1998)
   PUBMED   9538241
REFERENCE   3  (bases 1 to 898)
  AUTHORS   Tomomura A, Akiyama M, Itoh H, Yoshino I, Tomomura M, Nishii Y,
            Noikura T and Saheki T.
  TITLE     Molecular cloning and expression of human caldecrin
  JOURNAL   FEBS Lett 386 (1), 26-28 (1996)
   PUBMED   8635596
REFERENCE   4  (bases 1 to 898)
  AUTHORS   Tomomura A, Tomomura M, Fukushige T, Akiyama M, Kubota N, Kumaki K,
            Nishii Y, Noikura T and Saheki T.
  TITLE     Molecular cloning and expression of serum calcium-decreasing factor
            (caldecrin)
  JOURNAL   J Biol Chem 270 (51), 30315-30321 (1995)
   PUBMED   8530454
REFERENCE   5  (bases 1 to 898)
  AUTHORS   Kang J, Wiegand U and Muller-Hill B.
  TITLE     Identification of cDNAs encoding two novel rat pancreatic serine
            proteases
  JOURNAL   Gene 110 (2), 181-187 (1992)
   PUBMED   1537555
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from S80379.1.
            
            On Aug 31, 2012 this sequence version replaced NM_001077649.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: S80379.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-898               S80379.1           2-899
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Rattus norvegicus"
                     /mol_type="mRNA"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     gene            1..898
                     /gene="Ctrc"
                     /note="chymotrypsin C"
                     /db_xref="GeneID:362653"
                     /db_xref="RGD:1308379"
     exon            1..52
                     /gene="Ctrc"
                     /inference="alignment:Splign:2.1.0"
     misc_feature    7..9
                     /gene="Ctrc"
                     /note="upstream in-frame stop codon"
     CDS             13..819
                     /gene="Ctrc"
                     /EC_number="3.4.21.2"
                     /note="preprocaldecrin; caldecrin; serum
                     calcium-decreasing factor"
                     /codon_start=1
                     /product="chymotrypsin-C precursor"
                     /protein_id="NP_001071117.1"
                     /db_xref="GeneID:362653"
                     /db_xref="RGD:1308379"
                     /translation="

MLGITVLAAILACASCCGNPAFPPNLSTRVVGGEDAVPNSWPWQVSLQYLKDDTWRHTCGGSLITTSHVLTAAHCINKDFTYRVGLGKYNLTVEDEEGSVYAEVDTIYVHEKWNRLFLWNDIAIIKLAEPVELSNTIQVACIPEEGSLLPQDYPCYVTGWGRLWTNGPIAEVLQQGLQPIVSHATCSRLDWWFIKVRKTMVCAGGDGVISACNGDSGGPLNCQAEDGSWQVHGIVSFGSSSGCNVHKKPVVFTRVSAYNDWINEKIQL"

     sig_peptide     13..60
                     /gene="Ctrc"
                     /inference="COORDINATES: ab initio prediction:SignalP:4.0"
     misc_feature    85..87
                     /gene="Ctrc"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55091.1); glycosylation site"
     mat_peptide     100..816
                     /gene="Ctrc"
                     /product="Chymotrypsin-C. /id=PRO_0000027716"
                     /note="propagated from UniProtKB/Swiss-Prot (P55091.1)"
     misc_feature    100..807
                     /gene="Ctrc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...; Region:
                     Tryp_SPc; cd00190"
                     /db_xref="CDD:238113"
     misc_feature    100..102
                     /gene="Ctrc"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     misc_feature    order(232..234,373..375,658..660)
                     /gene="Ctrc"
                     /note="active site"
                     /db_xref="CDD:238113"
     misc_feature    280..282
                     /gene="Ctrc"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55091.1); glycosylation site"
     misc_feature    order(640..642,718..720,724..726)
                     /gene="Ctrc"
                     /note="substrate binding sites [chemical binding]; other
                     site"
                     /db_xref="CDD:238113"
     exon            53..144
                     /gene="Ctrc"
                     /inference="alignment:Splign:2.1.0"
     exon            145..242
                     /gene="Ctrc"
                     /inference="alignment:Splign:2.1.0"
     exon            243..368
                     /gene="Ctrc"
                     /inference="alignment:Splign:2.1.0"
     exon            369..505
                     /gene="Ctrc"
                     /inference="alignment:Splign:2.1.0"
     exon            506..651
                     /gene="Ctrc"
                     /inference="alignment:Splign:2.1.0"
     exon            652..804
                     /gene="Ctrc"
                     /inference="alignment:Splign:2.1.0"
     exon            805..880
                     /gene="Ctrc"
                     /inference="alignment:Splign:2.1.0"
ORIGIN      

aacacctgaaccatgttgggaattacggtcctcgctgccatcctggcctgcgcctcttgctgcgggaaccccgccttcccacctaacctgtcaaccagagtggtaggaggagaggatgctgtccccaacagctggccttggcaggtctctctccagtacctcaaggacgacacatggaggcacacctgtgggggaagtctcatcaccaccagccacgtcctcactgccgcccactgcatcaacaaagacttcacttaccgtgtgggcctggggaagtataatctgacagtggaggatgaggaaggctccgtgtacgctgaggtggacaccatctacgtccatgagaagtggaaccgactcttcctgtggaacgacatcgctatcattaagttggctgagcctgtggaactgagcaacaccatccaggtggcctgcatcccagaggaaggttccctgctgcctcaggactatccctgctatgtcacgggctggggtcgcctctggaccaatggtcccatcgctgaagtgctccagcagggcctgcagcccatcgtgagccatgccacgtgctccaggttggactggtggttcatcaaggtccggaagacgatggtgtgcgctgggggtgatggcgtcatctctgcctgtaacggagattctggcggcccactgaactgccaagcagaagacggctcatggcaggtgcacggcatcgtgagcttcggttccagtagcggctgcaacgtacacaagaaaccggtagtcttcacccgagtgtctgcctacaatgactggatcaacgagaaaatacaactgtgaagaggccgttccagaagtctcgctgcccgtctcccaacagcaataaagcttcttccatgataaaaaaaaaaaaaaaaaa

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