LOCUS       NP_031980                554 aa            linear   ROD 07-MAY-2024
DEFINITION  carboxylesterase 1C precursor [Mus musculus].
ACCESSION   NP_031980
VERSION     NP_031980.2
DBSOURCE    REFSEQ: accession NM_007954.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Feng,Y., Lee,J., Yang,L., Hilton,M.B., Morris,K., Seaman,S.,
            Edupuganti,V.V.S.R., Hsu,K.S., Dower,C., Yu,G., So,D., Bajgain,P.,
            Zhu,Z., Dimitrov,D.S., Patel,N.L., Robinson,C.M.,
            Difilippantonio,S., Dyba,M., Corbel,A., Basuli,F., Swenson,R.E.,
            Kalen,J.D., Suthe,S.R., Hussain,M., Italia,J.S., Souders,C.A.,
            Gao,L., Schnermann,M.J. and St Croix,B.
  TITLE     Engineering CD276/B7-H3-targeted antibody-drug conjugates with
            enhanced cancer-eradicating capability
  JOURNAL   Cell Rep 42 (12), 113503 (2023)
   PUBMED   38019654
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Gan,C., Wang,J., Wang,Y., Martinez-Chavez,A., Hillebrand,M., de
            Vries,N., Beukers,J., Lebre,M.C., Wagenaar,E., Rosing,H.,
            Klarenbeek,S., Bleijerveld,O.B., Song,J.Y., Altelaar,M.,
            Beijnen,J.H. and Schinkel,A.H.
  TITLE     Natural deletion of mouse carboxylesterases Ces1c/d/e impacts drug
            metabolism and metabolic syndrome development
  JOURNAL   Biomed Pharmacother 164, 114956 (2023)
   PUBMED   37267638
  REMARK    GeneRIF: Natural deletion of mouse carboxylesterases Ces1c/d/e
            impacts drug metabolism and metabolic syndrome development.
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Rais,R., Lemberg,K.M., Tenora,L., Arwood,M.L., Pal,A., Alt,J.,
            Wu,Y., Lam,J., Aguilar,J.M.H., Zhao,L., Peters,D.E., Tallon,C.,
            Pandey,R., Thomas,A.G., Dash,R.P., Seiwert,T., Majer,P.,
            Leone,R.D., Powell,J.D. and Slusher,B.S.
  TITLE     Discovery of DRP-104, a tumor-targeted metabolic inhibitor prodrug
  JOURNAL   Sci Adv 8 (46), eabq5925 (2022)
   PUBMED   36383674
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Li,H., Perino,A., Huang,Q., Von Alvensleben,G.V.G.,
            Banaei-Esfahani,A., Velazquez-Villegas,L.A., Gariani,K.,
            Korbelius,M., Bou Sleiman,M., Imbach,J., Sun,Y., Li,X.,
            Bachmann,A., Goeminne,L.J.E., Gallart-Ayala,H., Williams,E.G.,
            Ivanisevic,J., Auwerx,J. and Schoonjans,K.
  TITLE     Integrative systems analysis identifies genetic and dietary
            modulators of bile acid homeostasis
  JOURNAL   Cell Metab 34 (10), 1594-1610 (2022)
   PUBMED   36099916
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Zhu,C., Lee,J.Y., Woo,J.Z., Xu,L., Nguyenla,X., Yamashiro,L.H.,
            Ji,F., Biering,S.B., Van Dis,E., Gonzalez,F., Fox,D., Wehri,E.,
            Rustagi,A., Pinsky,B.A., Schaletzky,J., Blish,C.A., Chiu,C.,
            Harris,E., Sadreyev,R.I., Stanley,S., Kauppinen,S., Rouskin,S. and
            Naar,A.M.
  TITLE     An intranasal ASO therapeutic targeting SARS-CoV-2
  JOURNAL   Nat Commun 13 (1), 4503 (2022)
   PUBMED   35922434
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Genetta,T.L., D'Eustachio,P., Kadner,S.S. and Finlay,T.H.
  TITLE     cDNA cloning of esterase 1, the major esterase activity in mouse
            plasma
  JOURNAL   Biochem Biophys Res Commun 151 (3), 1364-1370 (1988)
   PUBMED   2895647
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Fox,R.R. and van Zutphen,L.F.
  TITLE     Chromosomal homology of rabbit (Oryctolagus cuniculus) linkage
            group VI with rodent species
  JOURNAL   Genetics 93 (1), 183-188 (1979)
   PUBMED   297012
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Soares,E.R.
  TITLE     Identification of a new allele of Es-I segregating in an inbred
            strain of mice
  JOURNAL   Biochem Genet 17 (7-8), 577-583 (1979)
   PUBMED   540008
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Peters,J. and Nash,H.R.
  TITLE     Esterases of Mus musculus: substrate and inhibition
            characteristics, new isozymes, and homologies with man
  JOURNAL   Biochem Genet 16 (5-6), 553-569 (1978)
   PUBMED   216346
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Womack,J.E.
  TITLE     Esterase-6 (Es-6) in laboratory mice: hormone-influenced expression
            and linkage relationship to oligosyndactylism (Os), esterase-1
            (Es-1), and esterase-2 (Es-2) in chromosome 8
  JOURNAL   Biochem Genet 13 (5-6), 311-322 (1975)
   PUBMED   170908
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI116924.1, AI527022.1, AC121985.3, AA286207.1 and AI047526.1.
            
            On Jul 2, 2009 this sequence version replaced NP_031980.1.
            
            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 :: M57960.1, BC028907.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849386, SAMN01164135
                                           [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..554
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 44.99 cM"
     Protein         1..554
                     /product="carboxylesterase 1C precursor"
                     /EC_number="3.1.1.1"
                     /note="liver carboxylesterase N; lung surfactant
                     convertase; PES-N; esterase 1"
                     /calculated_mol_wt=59094
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1980
     mat_peptide     19..554
                     /product="Carboxylesterase 1C. /id=PRO_0000008574"
                     /note="propagated from UniProtKB/Swiss-Prot (P23953.4)"
                     /calculated_mol_wt=59094
     Region          25..525
                     /region_name="Esterase_lipase"
                     /note="Esterases and lipases (includes fungal lipases,
                     cholinesterases, etc.) These enzymes act on carboxylic
                     esters (EC: 3.1.1.-). The catalytic apparatus involves
                     three residues (catalytic triad): a serine, a glutamate or
                     aspartate and a histidine.These...; cd00312"
                     /db_xref="CDD:238191"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17330941; propagated from
                     UniProtKB/Swiss-Prot (P23953.4)"
     Site            order(141..143,220..222,225,371,375..376,408,456,459)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(221,342,455)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17330941; propagated from
                     UniProtKB/Swiss-Prot (P23953.4)"
     Site            304
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16944957,
                     ECO:0000269|PubMed:17330941; propagated from
                     UniProtKB/Swiss-Prot (P23953.4)"
     Site            377
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16944957,
                     ECO:0000269|PubMed:17330941; propagated from
                     UniProtKB/Swiss-Prot (P23953.4)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10959; propagated from
                     UniProtKB/Swiss-Prot (P23953.4)"
     Site            478
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23953.4)"
     Region          551..554
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P23953.4)"
     CDS             1..554
                     /gene="Ces1c"
                     /gene_synonym="Ces-N; Ee-1; Ee1; Es-4; Es-N; Es1; Es4;
                     EsN; PESN"
                     /coded_by="NM_007954.4:26..1690"
                     /db_xref="CCDS:CCDS22527.1"
                     /db_xref="GeneID:13884"
                     /db_xref="MGI:MGI:95420"
ORIGIN      
        1 mwlhalvwas lavcpilghs llppvvdttq gkvlgkyisl egfeqpvavf lgvpfakppl
       61 gslrfappqp aepwsfvkna tsyppmcsqd agwakilsdm fstekeilpl kisedclyln
      121 iyspadltks sqlpvmvwih ggglviggas pynglalsah envvvvtiqy rlgiwglfst
      181 gdehspgnwa hldqlaalrw vqdnianfgg npdsvtifge ssggisvsvl vlsplgkdlf
      241 hraisesgvv intnvgkkni qavneiiatl sqcndtssaa mvqclrqkte selleisgkl
      301 vqynislstm idgvvlpkap eeilaeksfn tvpyivgfnk qefgwiipmm lqnllpegkm
      361 neetaslllr rfhselnise smipavieqy lrgvddpakk selildmfgd iffgipavll
      421 srslrdagvs tymyefryrp sfvsdkrpqt vegdhgdeif fvfgapllke gaseeetnls
      481 kmvmkfwanf arngnpngeg lphwpeydeq egylqigatt qqaqrlkaee vafwtellak
      541 nppetdpteh tehk
//
