LOCUS       NP_579829                565 aa            linear   ROD 27-MAR-2025
DEFINITION  carboxylesterase 1D precursor [Rattus norvegicus].
ACCESSION   NP_579829 XP_346520
VERSION     NP_579829.3
DBSOURCE    REFSEQ: accession NM_133295.3
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 565)
  AUTHORS   Capece,D., D'Andrea,D., Begalli,F., Goracci,L., Tornatore,L.,
            Alexander,J.L., Di Veroli,A., Leow,S.C., Vaiyapuri,T.S.,
            Ellis,J.K., Verzella,D., Bennett,J., Savino,L., Ma,Y.,
            McKenzie,J.S., Doria,M.L., Mason,S.E., Chng,K.R., Keun,H.C.,
            Frost,G., Tergaonkar,V., Broniowska,K., Stunkel,W., Takats,Z.,
            Kinross,J.M., Cruciani,G. and Franzoso,G.
  TITLE     Enhanced triacylglycerol catabolism by carboxylesterase 1 promotes
            aggressive colorectal carcinoma
  JOURNAL   J Clin Invest 131 (11) (2021)
   PUBMED   33878036
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Liu,D., Li,X., Li,X., Wang,H. and Dong,M.
  TITLE     Carboxylesterase 1 polymorphisms are associated with clinical
            outcomes in gastroenteric cancer patients treated with capecitabine
  JOURNAL   Cancer Chemother Pharmacol 87 (5), 681-687 (2021)
   PUBMED   33586000
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Hou,J.Y., Wang,Y.G., Ma,S.J., Yang,B.Y. and Li,Q.P.
  TITLE     Identification of a prognostic 5-Gene expression signature for
            gastric cancer
  JOURNAL   J Cancer Res Clin Oncol 143 (4), 619-629 (2017)
   PUBMED   28035468
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Quiroga,A.D., Ceballos,M.P., Parody,J.P., Comanzo,C.G.,
            Lorenzetti,F., Pisani,G.B., Ronco,M.T., Alvarez,M.L. and
            Carrillo,M.C.
  TITLE     Hepatic carboxylesterase 3 (Ces3/Tgh) is downregulated in the early
            stages of liver cancer development in the rat
  JOURNAL   Biochim Biophys Acta 1862 (11), 2043-2053 (2016)
   PUBMED   27523631
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Wallace,T.J., Kodsi,E.M., Langston,T.B., Gergis,M.R. and
            Grogan,W.M.
  TITLE     Mutation of residues 423 (Met/Ile), 444 (Thr/Met), and 506
            (Asn/Ser) confer cholesteryl esterase activity on rat lung
            carboxylesterase. Ser-506 is required for activation by
            cAMP-dependent protein kinase
  JOURNAL   J Biol Chem 276 (35), 33165-33174 (2001)
   PUBMED   11429416
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Ghosh,S.
  TITLE     Cholesteryl ester hydrolase in human monocyte/macrophage: cloning,
            sequencing, and expression of full-length cDNA
  JOURNAL   Physiol Genomics 2 (1), 1-8 (2000)
   PUBMED   11015575
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Ghosh,S., Mallonee,D.H., Hylemon,P.B. and Grogan,W.M.
  TITLE     Molecular cloning and expression of rat hepatic neutral cholesteryl
            ester hydrolase
  JOURNAL   Biochim Biophys Acta 1259 (3), 305-312 (1995)
   PUBMED   8541339
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Medda,S. and Proia,R.L.
  TITLE     The carboxylesterase family exhibits C-terminal sequence diversity
            reflecting the presence or absence of
            endoplasmic-reticulum-retention sequences
  JOURNAL   Eur J Biochem 206 (3), 801-806 (1992)
   PUBMED   1606962
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Robbi,M., Beaufay,H. and Octave,J.N.
  TITLE     Nucleotide sequence of cDNA coding for rat liver pI 6.1 esterase
            (ES-10), a carboxylesterase located in the lumen of the endoplasmic
            reticulum
  JOURNAL   Biochem J 269 (2), 451-458 (1990)
   PUBMED   2386485
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC061789.1, CO574231.1 and CF111142.1.
            
            On Apr 5, 2007 this sequence version replaced NP_579829.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061789.1, L81144.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [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..565
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..565
                     /product="carboxylesterase 1D precursor"
                     /EC_number="3.1.1.1"
                     /EC_number="3.1.1.67"
                     /note="ES-HVEL; FAEE synthase; pI 6.1 esterase;
                     carboxyesterase ES-10; liver carboxylesterase 10; fatty
                     acid ethyl ester synthase; carboxylesterase 3"
                     /calculated_mol_wt=60057
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2112
     mat_peptide     19..565
                     /product="Carboxylesterase 1D. /id=PRO_0000008584"
                     /note="propagated from UniProtKB/Swiss-Prot (P16303.2)"
                     /calculated_mol_wt=60057
     Region          22..545
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P16303.2)"
     Site            order(141..143,220..222,225,382,386..387,419,467,470)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(221,353,466)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            489
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16303.2)"
     Region          562..565
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P16303.2)"
     CDS             1..565
                     /gene="Ces1d"
                     /gene_synonym="Ces3"
                     /coded_by="NM_133295.3:52..1749"
                     /db_xref="GeneID:113902"
                     /db_xref="RGD:70896"
ORIGIN      
        1 mrlyplvwlf laactawgyp ssppvvntvk gkvlgkyvnl egfaqpvavf lgipfakppl
       61 gslrfappqp aepwnfvknt tsyppmcsqd avggqvlsel ftnrkenipl qfsedclyln
      121 vytpadltkn srlpvmvwih ggglvvggas tydgqvlsah envvvvtiqy rlgiwgffst
      181 gdehsqgnwg hldqvaalhw vqdnianfgg npgsvtifge saggfsvsal vlsplaknlf
      241 hraisesgvv ltsalittds kpianliatl sgcktttsav mvhclrqkte delletslkl
      301 nlfkldllgn pkesypflpt vidgvvlpkt peeilteksf ntvpyivgin kqefgwiipt
      361 lmgyplsegk ldqktaksll wksyptlkis ekmipvvaek yfggtddpak rkdlfqdlva
      421 dvmfgvpsvm vsrshrdaga ptfmyefeyr psfvsamrpk tvigdhgdel fsvfgspflk
      481 dgaseeetnl skmvmkywan farngspngg glphwpeydq kegylkigas tqaaqrlkdk
      541 evafwselra keaaeepshw khvel
//
