LOCUS       NP_058700                549 aa            linear   ROD 03-APR-2024
DEFINITION  carboxylesterase 1C precursor [Rattus norvegicus].
ACCESSION   NP_058700 XP_341652
VERSION     NP_058700.1
DBSOURCE    REFSEQ: accession NM_017004.1
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 549)
  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   2  (residues 1 to 549)
  AUTHORS   Furihata,T., Hosokawa,M., Fujii,A., Derbel,M., Satoh,T. and
            Chiba,K.
  TITLE     Dexamethasone-induced methylprednisolone hemisuccinate hydrolase:
            its identification as a member of the rat carboxylesterase 2 family
            and its unique existence in plasma
  JOURNAL   Biochem Pharmacol 69 (8), 1287-1297 (2005)
   PUBMED   15794950
  REMARK    GeneRIF: Es2 was induced by dexamethasone in liver microsomes and
            identified in plasma.
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Sun,G., Alexson,S.E. and Harrison,E.H.
  TITLE     Purification and characterization of a neutral, bile
            salt-independent retinyl ester hydrolase from rat liver microsomes.
            Relationship To rat carboxylesterase ES-2
  JOURNAL   J Biol Chem 272 (39), 24488-24493 (1997)
   PUBMED   9305911
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Alexson,S.E., Finlay,T.H., Hellman,U., Svensson,L.T., Diczfalusy,U.
            and Eggertsen,G.
  TITLE     Molecular cloning and identification of a rat serum
            carboxylesterase expressed in the liver
  JOURNAL   J Biol Chem 269 (25), 17118-17124 (1994)
   PUBMED   8006016
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Takagi,Y., Morohashi,K., Kawabata,S., Go,M. and Omura,T.
  TITLE     Molecular cloning and nucleotide sequence of cDNA of microsomal
            carboxyesterase E1 of rat liver
  JOURNAL   J Biochem 104 (5), 801-806 (1988)
   PUBMED   3235453
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Long,R.M., Satoh,H., Martin,B.M., Kimura,S., Gonzalez,F.J. and
            Pohl,L.R.
  TITLE     Rat liver carboxylesterase: cDNA cloning, sequencing, and evidence
            for a multigene family
  JOURNAL   Biochem Biophys Res Commun 156 (2), 866-873 (1988)
   PUBMED   2973315
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Harano,T., Miyata,T., Lee,S., Aoyagi,H. and Omura,T.
  TITLE     Biosynthesis and localization of rat liver microsomal
            carboxyesterase E1
  JOURNAL   J Biochem 103 (1), 149-155 (1988)
   PUBMED   3360755
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088251.1.
            
            On Jan 13, 2005 this sequence version replaced XP_341652.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088251.1, M20629.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..549
                     /product="carboxylesterase 1C precursor"
                     /EC_number="3.1.1.1"
                     /note="esterase 2, member of carboxylesterase-cluster 1;
                     liver carboxylesterase 1; E1; REH; NREH; ES-THET;
                     esterase-2; carboxyesterase ES-1; retinyl ester hydrolase;
                     neutral retinyl ester hydrolase; Esterase 2 member of
                     carboxylesterase-cluster 1; esterase 1; microsomal
                     carboxyesterase E1-like"
                     /calculated_mol_wt=58224
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2020
     mat_peptide     19..549
                     /product="Carboxylesterase 1C. /id=PRO_0000008579"
                     /note="propagated from UniProtKB/Swiss-Prot (P10959.3)"
                     /calculated_mol_wt=58224
     Region          22..532
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10959.3)"
     Site            order(141..143,220..222,225,369,373..374,406,454,457)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(221,340,453)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10959.3)"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10959.3)"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10959.3)"
     Site            375
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10959.3)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10959.3)"
     Site            476
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10959.3)"
     Region          546..549
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P10959.3)"
     CDS             1..549
                     /gene="Ces1c"
                     /gene_synonym="Es1; Es2"
                     /coded_by="NM_017004.1:41..1690"
                     /db_xref="GeneID:24346"
                     /db_xref="RGD:2571"
ORIGIN      
        1 mwlcvlvwas laacpiwghp ssppvvdttk gkvlgkyvsl egftqpvavf lgvpfakppl
       61 gslrfappep aepwsfvknt ttyppmcsqd gvvgklladm lstgkenipl efsedclyln
      121 iyspadltkn srlpvmvwih gggliiggas pysglalsah envvvvtiqy rlgiwglfst
      181 gdehsrgnwa hldqlaalrw vqdnianfgg npdsvtifge saggvsvsvl vlsplaknlf
      241 hraisesgvv lttnldkknt qavaqmiatl sgcnntssaa mvqclrqkte aelleltvkl
      301 dntsmstvid gvvlpktpee ilteksfntv pyivgfnkqe fgwiiptmmg nllsegrmne
      361 kmassllrrf spnlnisesv ipaiiekylr gtddpakkke llldmfsdvf fgipavlmsr
      421 slrdagapty myefqyrpsf vsdqrpqtvq gdhgdeifsv fgtpflkega seeetnlskl
      481 vmkfwanfar ngnpngeglp hwpeydqkeg ylqigattqq aqklkgeeva fwtellaknp
      541 pqtehteht
//
