LOCUS       NP_445978                457 aa            linear   ROD 03-APR-2024
DEFINITION  carboxypeptidase N catalytic chain precursor [Rattus norvegicus].
ACCESSION   NP_445978 XP_345037
VERSION     NP_445978.1
DBSOURCE    REFSEQ: accession NM_053526.2
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  (residues 1 to 457)
  AUTHORS   Moreau,M.E., Garbacki,N., Molinaro,G., Brown,N.J., Marceau,F. and
            Adam,A.
  TITLE     The kallikrein-kinin system: current and future pharmacological
            targets
  JOURNAL   J Pharmacol Sci 99 (1), 6-38 (2005)
   PUBMED   16177542
  REMARK    Review article
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Dendorfer,A., Wolfrum,S., Wagemann,M., Qadri,F. and Dominiak,P.
  TITLE     Pathways of bradykinin degradation in blood and plasma of
            normotensive and hypertensive rats
  JOURNAL   Am J Physiol Heart Circ Physiol 280 (5), H2182-H2188 (2001)
   PUBMED   11299220
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Sato,T., Miwa,T., Akatsu,H., Matsukawa,N., Obata,K., Okada,N.,
            Campbell,W. and Okada,H.
  TITLE     Pro-carboxypeptidase R is an acute phase protein in the mouse,
            whereas carboxypeptidase N is not
  JOURNAL   J Immunol 165 (2), 1053-1058 (2000)
   PUBMED   10878383
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Kato,T., Akatsu,H., Sato,T., Matsuo,S., Yamamoto,T., Campbell,W.,
            Hotta,N., Okada,N. and Okada,H.
  TITLE     Molecular cloning and partial characterization of rat
            procarboxypeptidase R and carboxypeptidase N
  JOURNAL   Microbiol Immunol 44 (8), 719-728 (2000)
   PUBMED   11021404
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Rajashree,S. and Puvanakrishnan,R.
  TITLE     Dexamethasone induced alterations in the levels of proteases
            involved in blood pressure homeostasis and blood coagulation in
            rats
  JOURNAL   Mol Cell Biochem 197 (1-2), 203-208 (1999)
   PUBMED   10485340
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088124.1.
            
            On Jan 28, 2005 this sequence version replaced XP_345037.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088124.1, AB042599.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..457
                     /product="carboxypeptidase N catalytic chain precursor"
                     /EC_number="3.4.17.3"
                     /note="carboxypeptidase N catalytic chain;
                     carboxypeptidase N, polypeptide 1, 50kD; carboxypeptidase
                     N small subunit; carboxypeptidase N catalytic chain-like"
                     /calculated_mol_wt=49452
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV8.1)"
                     /calculated_mol_wt=2547
     mat_peptide     24..457
                     /product="Carboxypeptidase N catalytic chain.
                     /id=PRO_0000042579"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQV8.1)"
                     /calculated_mol_wt=49452
     Region          25..337
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Site            order(86,89,151,160..161,216..217,223,308)
                     /site_type="active"
                     /db_xref="CDD:349427"
     Region          341..415
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cd11308"
                     /db_xref="CDD:200604"
     Site            400
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV8.1)"
     Site            402
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV8.1)"
     Site            409
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV8.1)"
     Region          418..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQV8.1)"
     CDS             1..457
                     /gene="Cpn1"
                     /gene_synonym="Cpn"
                     /coded_by="NM_053526.2:197..1570"
                     /db_xref="GeneID:365466"
                     /db_xref="RGD:70931"
ORIGIN      
        1 mpdlpsaflp llllskfvtp vtfrhhrydd lvrtlykvhn qcpditrlyn igrsvkgryl
       61 yvlefsdypg theplepevk yvgnmhgnev lgrelllqls eflceefrnr nqrilrliqd
      121 trihilpsmn pdgyevaaaq gpntsgylvg rnnangvdln rnfpdlntyf yynskyggpn
      181 hhlplpdnwk sqvepetrav iqwirslnfv lsanmhggav vanypydksl ehrfrsphrt
      241 snsptpddel fqtlakvysy ahgwmhqgwn cgdyfpdgit ngaswyslsk gmqdfnylht
      301 ncfeitlels cnkfprqeel qrewlgnrea liqfleqvhq gikgmvlden ynnltgavis
      361 vtginhdvts gehgdyfrll lpgtysvtak asgyepktvt vtvgpagptl vdfqlkrstt
      421 qvhpvqkapg rgqgsrakqp rtsrkkdqaa krhrgpa
//
