LOCUS       NP_775150                247 aa            linear   ROD 20-OCT-2018
DEFINITION  cationic trypsin-3 precursor [Rattus norvegicus].
ACCESSION   NP_775150
VERSION     NP_775150.1
DBSOURCE    REFSEQ: accession NM_173127.1
KEYWORDS    RefSeq.
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  (residues 1 to 247)
  AUTHORS   Jiang C, Zheng H, Liu S and Fang K.
  TITLE     Relationship between carbachol hyperstimulation-induced pancreatic
            intracellular trypsinogen and NF-kappa B activation in rats in
            vitro
  JOURNAL   J. Huazhong Univ. Sci. Technol. Med. Sci. 28 (1), 69-72 (2008)
   PUBMED   18278461
  REMARK    GeneRIF: NF-kappa B activation is likely not necessary for high
            concentrations of carbachol-induced trypsinogen activation in
            pancreatic acinar cells in vitro
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Gaiser S, Ahler A, Gundling F, Kruse ML, Savkovic V, Selig L, Teich
            N, Tomasini R, Dagorn JC, Mossner J, Keim V and Bodeker H.
  TITLE     Expression of mutated cationic trypsinogen reduces cellular
            viability in AR4-2J cells
  JOURNAL   Biochem. Biophys. Res. Commun. 334 (2), 721-728 (2005)
   PUBMED   16036133
  REMARK    GeneRIF: Expression of trypsin and R122H trypsinogen induced
            caspase-3 activity. Acinar cells might react to intracellular
            trypsin activity by triggering apoptosis.
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Wang S, He R and Anderson R.
  TITLE     PrM- and cell-binding domains of the dengue virus E protein
  JOURNAL   J. Virol. 73 (3), 2547-2551 (1999)
   PUBMED   9971841
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Roach JC, Wang K, Gan L and Hood L.
  TITLE     The molecular evolution of the vertebrate trypsinogens
  JOURNAL   J. Mol. Evol. 45 (6), 640-652 (1997)
   PUBMED   9419241
  REMARK    GeneRIF: This trypsinogen is typical of non-human gnathostomata
            trypinsogens; it has 6 predicted cystine bridges and an acidic
            activation peptide. It clusters with group II ('cationic')
            trypsins.
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Fletcher,T.S., Alhadeff,M., Craik,C.S. and Largman,C.
  TITLE     Isolation and characterization of a cDNA encoding rat cationic
            trypsinogen
  JOURNAL   Biochemistry 26 (11), 3081-3086 (1987)
   PUBMED   3607011
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M16624.1.
            
            Summary: serine protease; involved in protein cleavage [RGD, Feb
            2006].
            
            ##Evidence-Data-START##
            Transcript exon combination :: M16624.1, FQ226997.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMN01906358, SAMN02642598
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..247
                     /product="cationic trypsin-3 precursor"
                     /EC_number="3.4.21.4"
                     /note="cationic trypsin-3; pretrypsinogen III; cationic
                     trypsin III; cationic trypsinogen"
                     /calculated_mol_wt=24751
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:4.0"
                     /calculated_mol_wt=1536
     mat_peptide     24..247
                     /product="cationic trypsin-3"
                     /calculated_mol_wt=23852
     Region          24..240
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; smart00020"
                     /db_xref="CDD:214473"
     Region          25..243
                     /region_name="Tryp_SPc"
                     /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...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            25
                     /site_type="cleavage"
                     /db_xref="CDD:238113"
     Site            order(64,108,201)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(195,216,218)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     Site            195
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Required for specificity. {ECO:0000250}; propagated
                     from UniProtKB/Swiss-Prot (P08426.1)"
     CDS             1..247
                     /gene="Prss3"
                     /gene_synonym="Try3"
                     /coded_by="NM_173127.1:1..744"
                     /db_xref="GeneID:286911"
                     /db_xref="RGD:708437"
ORIGIN      
        1 mkaliflafl gaavalpldd dddkivggyt cqknslpyqv slnagyhfcg gslinsqwvv
       61 saahcyksri qvrlgehnid vveggeqfid aakiirhpsy nantfdndim liklnspatl
      121 nsrvstvslp rscgssgtkc lvsgwgntls sgtnypsllq cldapvlsds sckssypgki
      181 tsnmfclgfl eggkdscqgd sggpvvcngq lqgvvswgyg caqkgkpgvy tkvcnyvnwi
      241 qqtvaan
//