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RecName: Full=Carboxylesterase 1D; AltName: Full=Carboxyesterase ES-10; AltName: Full=Carboxylesterase 3; AltName: Full=ES-HVEL; AltName: Full=Fatty acid ethyl ester synthase; Short=FAEE synthase; AltName: Full=Liver carboxylesterase 10; AltName: Full=pI 6.1 e...

UniProtKB/Swiss-Prot: P16303.2

Identical Proteins FASTA Graphics 

LOCUS       EST1D_RAT                565 aa            linear   ROD 27-NOV-2024
DEFINITION  RecName: Full=Carboxylesterase 1D; AltName: Full=Carboxyesterase
            ES-10; AltName: Full=Carboxylesterase 3; AltName: Full=ES-HVEL;
            AltName: Full=Fatty acid ethyl ester synthase; Short=FAEE synthase;
            AltName: Full=Liver carboxylesterase 10; AltName: Full=pI 6.1
            esterase; Flags: Precursor.
ACCESSION   P16303
VERSION     P16303.2
DBSOURCE    UniProtKB: locus EST1D_RAT, accession P16303;
            class: standard.
            extra accessions:Q64574,Q6P785,Q91YG2,Q9QUX7,Q9R135
            created: Aug 1, 1990.
            sequence updated: Oct 25, 2004.
            annotation updated: Nov 27, 2024.
            xrefs: X51974.1, CAA36236.1, X65296.1, CAA46391.1, L46791.1,
            AAA88507.1, L81144.1, AAL00849.1, AF171640.1, AAD49369.1,
            BC061789.1, AAH61789.1, A45140, S10367, NP_579829.3
            xrefs (non-sequence databases): AlphaFoldDB:P16303, SMR:P16303,
            STRING:10116.ENSRNOP00000021812, SwissLipids:SLP:000001457,
            ESTHER:ratno-Ces1d, CarbonylDB:P16303, GlyCosmos:P16303,
            GlyGen:P16303, iPTMnet:P16303, PhosphoSitePlus:P16303,
            PaxDb:10116-ENSRNOP00000021812, GeneID:113902, KEGG:rno:113902,
            AGR:RGD:1359640, AGR:RGD:70896, CTD:104158, RGD:70896,
            eggNOG:KOG1516, InParanoid:P16303, OrthoDB:4386at2759,
            PhylomeDB:P16303, BRENDA:3.1.1.1, Reactome:R-RNO-2022377,
            Reactome:R-RNO-211945, Reactome:R-RNO-5578768,
            Reactome:R-RNO-9749641, SABIO-RK:P16303, PRO:PR:P16303,
            Proteomes:UP000002494, GO:0005737, GO:0005829, GO:0005783,
            GO:0005788, GO:0043231, GO:0005811, GO:0047376, GO:0106435,
            GO:0052689, GO:0030339, GO:0050253, GO:0004771, GO:0004806,
            GO:0046464, GO:0071397, GO:0070417, GO:0071404, GO:0006695,
            GO:0042632, GO:0008203, GO:0060086, GO:0106106, GO:0061725,
            GO:0030855, GO:0016042, GO:0051791, GO:0010887, GO:0010875,
            GO:0090205, GO:0045944, GO:0070857, GO:0120188, GO:0001523,
            GO:0043691, GO:0019626, GO:0034379, CDD:cd00312,
            FunFam:3.40.50.1820:FF:000011, Gene3D:3.40.50.1820,
            InterPro:IPR029058, InterPro:IPR002018, InterPro:IPR019826,
            InterPro:IPR019819, InterPro:IPR050309, PANTHER:PTHR11559,
            PANTHER:PTHR11559:SF179, Pfam:PF00135, SUPFAM:SSF53474,
            PROSITE:PS00122, PROSITE:PS00941
KEYWORDS    Cytoplasm; Direct protein sequencing; Disulfide bond; Endoplasmic
            reticulum; Glycoprotein; Hydrolase; Lipid degradation; Lipid
            droplet; Lipid metabolism; Microsome; Reference proteome; Serine
            esterase; Signal.
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   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
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=Sprague-Dawley, and Wistar; TISSUE=Liver
REFERENCE   2  (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
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=Sprague-Dawley; TISSUE=Liver
REFERENCE   3  (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
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=Sprague-Dawley; TISSUE=Liver
REFERENCE   4  (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
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF GLN-186; MET-423;
            SER-491; LYS-492 AND ASN-506.;
            STRAIN=Sprague-Dawley; TISSUE=Lung
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Ryu,J.W., Lee,W. and Jung,C.Y.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-JUL-1999) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=Sprague-Dawley
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Prostate
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Tsujita,T. and Okuda,H.
  TITLE     Fatty acid ethyl ester synthase in rat adipose tissue and its
            relationship to carboxylesterase
  JOURNAL   J Biol Chem 267 (33), 23489-23494 (1992)
   PUBMED   1429692
  REMARK    PROTEIN SEQUENCE OF 19-45, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
            REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.;
            STRAIN=Wistar; TISSUE=Adipose tissue
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Satoh,T. and Hosokawa,M.
  TITLE     Molecular aspects of carboxylesterase isoforms in comparison with
            other esterases
  JOURNAL   Toxicol Lett 82-83, 439-445 (1995)
   PUBMED   8597091
  REMARK    PROTEIN SEQUENCE OF 19-38, NUCLEOTIDE SEQUENCE [MRNA] OF 113-121;
            138-149; 216-224; 350-356 AND 464-469, AND SUBUNIT.;
            TISSUE=Liver
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Sanghani,S.P., Davis,W.I., Dumaual,N.G., Mahrenholz,A. and
            Bosron,W.F.
  TITLE     Identification of microsomal rat liver carboxylesterases and their
            activity with retinyl palmitate
  JOURNAL   Eur J Biochem 269 (18), 4387-4398 (2002)
   PUBMED   12230550
  REMARK    CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE
            SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
COMMENT     On or before Sep 26, 2008 this sequence version replaced
            gi:81916247, gi:81868876, gi:92053, gi:119596.
            [FUNCTION] Major lipase in white adipose tissue (By similarity).
            Involved in the metabolism of xenobiotics and of natural
            substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with
            a preference for monoacylglycerols. The susceptibility of the
            substrate increases with decreasing acyl chain length of the fatty
            acid moiety. Catalyzes the synthesis of fatty acid ethyl esters
            (PubMed:1429692). Hydrolyzes retinyl esters (PubMed:12230550).
            {ECO:0000250|UniProtKB:Q8VCT4, ECO:0000269|PubMed:12230550,
            ECO:0000269|PubMed:1429692}.
            [CATALYTIC ACTIVITY] Reaction=all-trans-retinyl hexadecanoate + H2O
            = all-trans-retinol + hexadecanoate + H(+); Xref=Rhea:RHEA:13933,
            ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:17336, ChEBI:CHEBI:17616;
            Evidence={ECO:0000269|PubMed:12230550};
            PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
            Evidence={ECO:0000305|PubMed:12230550}.
            [CATALYTIC ACTIVITY] Reaction=a carboxylic ester + H2O = an alcohol
            + a carboxylate + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377,
            ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879,
            ChEBI:CHEBI:33308; EC=3.1.1.1;
            Evidence={ECO:0000255|PROSITE-ProRule:PRU10039,
            ECO:0000269|PubMed:1429692}.
            [CATALYTIC ACTIVITY] Reaction=a long-chain fatty acyl ethyl ester +
            H2O = a long-chain fatty acid + ethanol + H(+);
            Xref=Rhea:RHEA:16641, ChEBI:CHEBI:13209, ChEBI:CHEBI:15377,
            ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:57560;
            EC=3.1.1.67; Evidence={ECO:0000269|PubMed:1429692}.
            ACTIVITY REGULATION: FAEE-synthesizing and PNPB-hydrolyzing
            activities are both inhibited by DFP. {ECO:0000269|PubMed:1429692}.
            [BIOPHYSICOCHEMICAL PROPERTIES] Kinetic parameters: KM=0.71 M for
            oleic acid {ECO:0000269|PubMed:1429692}; KM=1.16 uM for retinyl
            palmitate {ECO:0000269|PubMed:12230550}; Vmax=1482 nmol/h/mg enzyme
            toward oleic acid {ECO:0000269|PubMed:1429692}; Note=kcat is 0.22
            min(-1) with retinyl palmitate as substrate.
            {ECO:0000269|PubMed:12230550}; pH dependence: Optimum pH for FAEE
            synthesis is 7.0. Optimum pH for PNPB-hydrolyzing activity is 6-8.
            {ECO:0000269|PubMed:1429692}.
            [SUBUNIT] Homotrimer. {ECO:0000269|PubMed:8597091}.
            [SUBCELLULAR LOCATION] Endoplasmic reticulum lumen
            {ECO:0000250|UniProtKB:Q8VCT4}. Cytoplasm, cytosol
            {ECO:0000250|UniProtKB:Q8VCT4}. Lipid droplet
            {ECO:0000250|UniProtKB:Q8VCT4}. Microsome
            {ECO:0000269|PubMed:12230550}.
            [TISSUE SPECIFICITY] Detected in liver, lung and testis, but not in
            kidney (at protein level). {ECO:0000269|PubMed:12230550,
            ECO:0000269|PubMed:1429692}.
            [SIMILARITY] Belongs to the type-B carboxylesterase/lipase family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..565
                     /gene="Ces1d"
                     /gene_synonym="Ces3"
     Protein         1..565
                     /product="Carboxylesterase 1D"
                     /EC_number="3.1.1.1"
                     /EC_number="3.1.1.67"
                     /note="Carboxyesterase ES-10; Carboxylesterase 3; ES-HVEL;
                     Fatty acid ethyl ester synthase; Liver carboxylesterase
                     10; pI 6.1 esterase; FAEE synthase"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..18
                     /region_name="Signal"
                     /note="/evidence=ECO:0000269|PubMed:1429692,
                     ECO:0000269|PubMed:8597091."
     Region          19..565
                     /region_name="Mature chain"
                     /note="Carboxylesterase 1D. /id=PRO_0000008584."
     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."
     Bond            bond(87,116)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:P23141."
     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"
     Region          186
                     /region_name="Conflict"
                     /note="Q -> R (in Ref. 1; CAA36236, 3; AAA88507 and 5;
                     AAD49369). /evidence=ECO:0000305."
     Site            186
                     /site_type="mutagenized"
                     /note="Q->R: No effect on the hydrolysis of PNPC or PNPA,
                     no activity on cholesteryl oleate. No effect on the
                     hydrolysis of PNPC or PNPA, no activity on cholesteryl
                     oleate; when associated with E-492; or with T-491 and
                     E-492. Increases activity on PNPC compared to activity on
                     PNPA; when associated with I-423; T-491 and E-492.
                     /evidence=ECO:0000269|PubMed:11429416."
     Site            order(221,353,466)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            221
                     /site_type="active"
                     /note="Acyl-ester intermediate.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU10039."
     Region          265
                     /region_name="Conflict"
                     /note="N -> K (in Ref. 1; CAA36236).
                     /evidence=ECO:0000305."
     Bond            bond(273,284)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:P23141."
     Site            353
                     /site_type="active"
                     /note="Charge relay system.
                     /evidence=ECO:0000250|UniProtKB:P23141."
     Site            382
                     /site_type="modified"
                     /note="N6-succinyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCT4."
     Region          420
                     /region_name="Conflict"
                     /note="A -> E (in Ref. 3; AAA88507).
                     /evidence=ECO:0000305."
     Region          423
                     /region_name="Conflict"
                     /note="M -> I (in Ref. 1; CAA36236, 3; AAA88507 and 5;
                     AAD49369). /evidence=ECO:0000305."
     Site            423
                     /site_type="mutagenized"
                     /note="M->I: Increases specific activity against PNPC by
                     8-fold, does not increase activity against PNPA, no
                     activity on cholesteryl oleate. Increases activity on PNPC
                     compared to activity on PNPA; when associated with R-186;
                     T-491 and E-492. Increases specific activity against PNPC
                     by 7.5-fold and against PNPA by 3.6-fold, and increases
                     cholesteryl esterase activity by 2.7 fold; when associated
                     with S-506. /evidence=ECO:0000269|PubMed:11429416."
     Region          444
                     /region_name="Conflict"
                     /note="M -> T (in Ref. 4; AAL00849).
                     /evidence=ECO:0000305."
     Site            466
                     /site_type="active"
                     /note="Charge relay system.
                     /evidence=ECO:0000250|UniProtKB:P23141."
     Site            489
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          491..492
                     /region_name="Conflict"
                     /note="SK -> TQ (in Ref. 3; AAA88507).
                     /evidence=ECO:0000305."
     Site            491
                     /site_type="mutagenized"
                     /note="S->T: No effect on the hydrolysis of PNPC or PNPA,
                     no activity on cholesteryl oleate; when associated with
                     R-186 and E-492. Increases activity on PNPC compared to
                     activity on PNPA; when associated with R-186; I-423 and
                     E-492. /evidence=ECO:0000269|PubMed:11429416."
     Site            492
                     /site_type="mutagenized"
                     /note="K->E: No effect on the hydrolysis of PNPC or PNPA,
                     no activity on cholesteryl oleate; when associated with
                     R-186; or with R-186 and T-491. Increases activity on PNPC
                     compared to activity on PNPA; when associated with R-186;
                     I-423 and T-491. /evidence=ECO:0000269|PubMed:11429416."
     Region          506
                     /region_name="Conflict"
                     /note="N -> S (in Ref. 1; CAA36236, 3; AAA88507 and 5;
                     AAD49369). /evidence=ECO:0000305."
     Site            506
                     /site_type="mutagenized"
                     /note="N->S: Increases specific activity against PNPC by
                     6-fold and against PNPA by 8.7-fold, no activity on
                     cholesteryl oleate. Increases specific activity against
                     PNPC by 7.5-fold and against PNPA by 3.6-fold, and
                     increases cholesteryl esterase activity by 2.7 fold; when
                     associated with I-423.
                     /evidence=ECO:0000269|PubMed:11429416."
     Region          562..565
                     /region_name="Short sequence motif of biological interest"
                     /note="Prevents secretion from ER. /evidence=ECO:0000255."
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 peeilaeksf ntvpyivgin kqefgwiipt
      361 lmgyplsegk ldqktaksll wksyptlkis ekmipvvaek yfggtddpak rkdlfqdlva
      421 dvmfgvpsvm vsrshrdaga ptfmyefeyr psfvsamrpk tvigdhgdel fsvfgspflk
      481 dgaseeetnl skmvmkywan farngnpngg glphwpeydq kegylkigas tqaaqrlkdk
      541 evafwselra keaaeepshw khvel
//
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Reference sequence information

  • RefSeq protein
    See the reference protein sequence for carboxylesterase 1D precursor (NP_579829.3).

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