LOCUS       NP_598421                562 aa            linear   ROD 13-JUN-2024
DEFINITION  carboxylesterase 1E isoform 1 precursor [Mus musculus].
ACCESSION   NP_598421
VERSION     NP_598421.1
DBSOURCE    REFSEQ: accession NM_133660.4
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 562)
  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   2  (residues 1 to 562)
  AUTHORS   Chen,R., Wang,Y., Ning,R., Hu,J., Liu,W., Xiong,J., Wu,L., Liu,J.,
            Hu,G. and Yang,J.
  TITLE     Decreased carboxylesterases expression and hydrolytic activity in
            type 2 diabetic mice through Akt/mTOR/HIF-1alpha/Stra13 pathway
  JOURNAL   Xenobiotica 45 (9), 782-793 (2015)
   PUBMED   25801056
  REMARK    GeneRIF: the carboxylesterase 1d (Ces1d) and carboxylesterase 1e
            (Ces1e) expression and the capacity of hydrolytic activity of liver
            and intestine decreased, whereas the Akt/mTOR/HIF-1alpha/ Stra13
            (DEC1) signaling was activated in type 2 diabetes mice.
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Holmes,R.S., Wright,M.W., Laulederkind,S.J., Cox,L.A., Hosokawa,M.,
            Imai,T., Ishibashi,S., Lehner,R., Miyazaki,M., Perkins,E.J.,
            Potter,P.M., Redinbo,M.R., Robert,J., Satoh,T., Yamashita,T.,
            Yan,B., Yokoi,T., Zechner,R. and Maltais,L.J.
  TITLE     Recommended nomenclature for five mammalian carboxylesterase gene
            families: human, mouse, and rat genes and proteins
  JOURNAL   Mamm Genome 21 (9-10), 427-441 (2010)
   PUBMED   20931200
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Schreiber,R., Taschler,U., Wolinski,H., Seper,A., Tamegger,S.N.,
            Graf,M., Kohlwein,S.D., Haemmerle,G., Zimmermann,R., Zechner,R. and
            Lass,A.
  TITLE     Esterase 22 and beta-glucuronidase hydrolyze retinoids in mouse
            liver
  JOURNAL   J Lipid Res 50 (12), 2514-2523 (2009)
   PUBMED   19723663
  REMARK    GeneRIF: The Es22 plays a role in liver retinoid metabolism.
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Kaput,J., Klein,K.G., Reyes,E.J., Kibbe,W.A., Cooney,C.A.,
            Jovanovic,B., Visek,W.J. and Wolff,G.L.
  TITLE     Identification of genes contributing to the obese yellow Avy
            phenotype: caloric restriction, genotype, diet x genotype
            interactions
  JOURNAL   Physiol Genomics 18 (3), 316-324 (2004)
   PUBMED   15306695
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Ovnic,M., Swank,R.T., Fletcher,C., Zhen,L., Novak,E.K., Baumann,H.,
            Heintz,N. and Ganschow,R.E.
  TITLE     Characterization and functional expression of a cDNA encoding
            egasyn (esterase-22): the endoplasmic reticulum-targeting protein
            of beta-glucuronidase
  JOURNAL   Genomics 11 (4), 956-967 (1991)
   PUBMED   1783403
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Moen,C.J., van der Valk,M.A., Snoek,M., van Zutphen,B.F., von
            Deimling,O., Hart,A.A. and Demant,P.
  TITLE     The recombinant congenic strains--a novel genetic tool applied to
            the study of colon tumor development in the mouse
  JOURNAL   Mamm Genome 1 (4), 217-227 (1991)
   PUBMED   1686571
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Lusis,A.J. and Paigen,K.
  TITLE     Relationships between levels of membrane-bound glucuronidase and
            the associated protein egasyn in mouse tissues
  JOURNAL   J Cell Biol 73 (3), 728-735 (1977)
   PUBMED   873997
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Lusis,A.J., Tomino,S. and Paigen,K.
  TITLE     Inheritance in mice of the membrane anchor protein egasyn: the Eg
            locus determines egasyn levels
  JOURNAL   Biochem Genet 15 (1-2), 115-122 (1977)
   PUBMED   849245
REFERENCE   10 (residues 1 to 562)
  AUTHORS   Lusis,A.J., Tomino,S. and Paigen,K.
  TITLE     Isolation, characterization, and radioimmunoassay of murine egasyn,
            a protein stabilizing glucuronidase membrane binding
  JOURNAL   J Biol Chem 251 (24), 7753-7760 (1976)
   PUBMED   826534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC162949.7.
            
            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 :: BC019208.1, AK144549.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 45.11 cM"
     Protein         1..562
                     /product="carboxylesterase 1E isoform 1 precursor"
                     /EC_number="3.1.1.1"
                     /note="liver carboxylesterase 22; esterase-22"
                     /calculated_mol_wt=59791
     sig_peptide     1..19
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q64176.1)"
                     /calculated_mol_wt=1809
     mat_peptide     20..562
                     /product="Carboxylesterase 1E. /id=PRO_0000008576"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64176.1)"
                     /calculated_mol_wt=59791
     Region          23..546
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64176.1)"
     Site            order(142..144,221..223,226,380,386..387,420,468,471)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(222,354,467)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64176.1)"
     Site            490
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64176.1)"
     Region          559..562
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64176.1)"
     CDS             1..562
                     /gene="Ces1e"
                     /gene_synonym="Eg; egasyn; Es-22; Es22"
                     /coded_by="NM_133660.4:185..1873"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS22529.1"
                     /db_xref="GeneID:13897"
                     /db_xref="MGI:MGI:95432"
ORIGIN      
        1 mclsalilvs laaftagagh pssppmvdtv qgkvlgkyis legftqpvav flgvpfakpp
       61 lgslrfappq paepwssvkn atsyppmcfq dpvtgqivnd lltnrkekip lqfsedclyl
      121 niytpadltk sdrlpvmvwi hggglvlgga stydglvlst henvvvvviq yrlgiwgffs
      181 tgdehsrgnw ghldqvaalh wvqdniakfg gdpgsvtifg esaggesvsv lvlsplaknl
      241 fqraisesgv altaglvkkn trplaekiav isgcknttsa amvhclrqkt eeellgttlk
      301 lnlfkldlhg dsrqshpfvp tvldgvllpk mpeeilaekn fntvpyivgi nkqefgwilp
      361 tmmnyppsdv kldqmtamsl lkkssfllnl pedaiavaie kylrdkdytg rnkdqlleli
      421 gdvvfgvpsv ivsrghrdag aptymyefqy spsfssemkp dtvvgdhgde iysvfgapil
      481 rggtseeein lskmmmkfwa nfarngnpng qglphwpeyd qkegylqiga ttqqaqklke
      541 kevafwtell akkqlpteht el
//
