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Protein

Carboxylesterase 1D

Gene

Ces1d

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

A carboxylic ester + H2O = an alcohol + a carboxylate.PROSITE-ProRule annotation1 Publication
A long-chain-fatty-acyl ethyl ester + H2O = a long-chain-fatty acid + ethanol.1 Publication

Enzyme regulationi

FAEE-synthesizing and PNPB-hydrolyzing activities are both inhibited by DFP.1 Publication

Kineticsi

  1. KM=0.71 M for oleic acid1 Publication
  1. Vmax=1482 nmol/h/mg enzyme toward oleic acid1 Publication

pH dependencei

Optimum pH for FAEE synthesis is 7.0. Optimum pH for PNPB-hydrolyzing activity is 6-8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei353 – 3531Charge relay systemBy similarity
Active sitei466 – 4661Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.1. 5301.
SABIO-RKP16303.

Protein family/group databases

ESTHERiratno-Ces1d. Carb_B_Chordata.
MEROPSiS09.983.

Chemistry

SwissLipidsiSLP:000001457.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxylesterase 1D
Alternative name(s):
Carboxyesterase ES-10
Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67)
ES-HVEL
Fatty acid ethyl ester synthase
Short name:
FAEE synthase
Liver carboxylesterase 10
pI 6.1 esterase
Gene namesi
Name:Ces1d
Synonyms:Ces3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi70896. Ces1d.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Lipid droplet

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi186 – 1861Q → 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. 1 Publication
Mutagenesisi423 – 4231M → 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. 1 Publication
Mutagenesisi491 – 4911S → 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. 1 Publication
Mutagenesisi492 – 4921K → 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. 1 Publication
Mutagenesisi506 – 5061N → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 PublicationsAdd
BLAST
Chaini19 – 565547Carboxylesterase 1DPRO_0000008584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)By similarity
Disulfide bondi87 ↔ 116By similarity
Disulfide bondi273 ↔ 284By similarity
Modified residuei382 – 3821N6-succinyllysineBy similarity
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP16303.
PRIDEiP16303.

PTM databases

iPTMnetiP16303.
PhosphoSiteiP16303.

Expressioni

Tissue specificityi

Detected in liver, lung and testis, but not in kidney (at protein level).1 Publication

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

MINTiMINT-4564205.
STRINGi10116.ENSRNOP00000021812.

Structurei

3D structure databases

ProteinModelPortaliP16303.
SMRiP16303. Positions 21-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi562 – 5654Prevents secretion from ERSequence analysis

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP16303.
KOiK01044.
PhylomeDBiP16303.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLYPLVWLF LAACTAWGYP SSPPVVNTVK GKVLGKYVNL EGFAQPVAVF
60 70 80 90 100
LGIPFAKPPL GSLRFAPPQP AEPWNFVKNT TSYPPMCSQD AVGGQVLSEL
110 120 130 140 150
FTNRKENIPL QFSEDCLYLN VYTPADLTKN SRLPVMVWIH GGGLVVGGAS
160 170 180 190 200
TYDGQVLSAH ENVVVVTIQY RLGIWGFFST GDEHSQGNWG HLDQVAALHW
210 220 230 240 250
VQDNIANFGG NPGSVTIFGE SAGGFSVSAL VLSPLAKNLF HRAISESGVV
260 270 280 290 300
LTSALITTDS KPIANLIATL SGCKTTTSAV MVHCLRQKTE DELLETSLKL
310 320 330 340 350
NLFKLDLLGN PKESYPFLPT VIDGVVLPKT PEEILAEKSF NTVPYIVGIN
360 370 380 390 400
KQEFGWIIPT LMGYPLSEGK LDQKTAKSLL WKSYPTLKIS EKMIPVVAEK
410 420 430 440 450
YFGGTDDPAK RKDLFQDLVA DVMFGVPSVM VSRSHRDAGA PTFMYEFEYR
460 470 480 490 500
PSFVSAMRPK TVIGDHGDEL FSVFGSPFLK DGASEEETNL SKMVMKYWAN
510 520 530 540 550
FARNGNPNGG GLPHWPEYDQ KEGYLKIGAS TQAAQRLKDK EVAFWSELRA
560
KEAAEEPSHW KHVEL
Length:565
Mass (Da):62,147
Last modified:October 25, 2004 - v2
Checksum:iF3277B7FAD2141A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861Q → R in CAA36236 (PubMed:2386485).Curated
Sequence conflicti186 – 1861Q → R in AAA88507 (PubMed:8541339).Curated
Sequence conflicti186 – 1861Q → R in AAD49369 (Ref. 5) Curated
Sequence conflicti265 – 2651N → K in CAA36236 (PubMed:2386485).Curated
Sequence conflicti420 – 4201A → E in AAA88507 (PubMed:8541339).Curated
Sequence conflicti423 – 4231M → I in CAA36236 (PubMed:2386485).Curated
Sequence conflicti423 – 4231M → I in AAA88507 (PubMed:8541339).Curated
Sequence conflicti423 – 4231M → I in AAD49369 (Ref. 5) Curated
Sequence conflicti444 – 4441M → T in AAL00849 (PubMed:11429416).Curated
Sequence conflicti491 – 4922SK → TQ in AAA88507 (PubMed:8541339).Curated
Sequence conflicti506 – 5061N → S in CAA36236 (PubMed:2386485).Curated
Sequence conflicti506 – 5061N → S in AAA88507 (PubMed:8541339).Curated
Sequence conflicti506 – 5061N → S in AAD49369 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51974 mRNA. Translation: CAA36236.1.
X65296 mRNA. Translation: CAA46391.1.
L46791 mRNA. Translation: AAA88507.1.
L81144 mRNA. Translation: AAL00849.1.
AF171640 mRNA. Translation: AAD49369.1.
BC061789 mRNA. Translation: AAH61789.1.
PIRiA45140.
S10367.
RefSeqiNP_579829.3. NM_133295.3.
UniGeneiRn.225887.

Genome annotation databases

GeneIDi113902.
KEGGirno:113902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51974 mRNA. Translation: CAA36236.1.
X65296 mRNA. Translation: CAA46391.1.
L46791 mRNA. Translation: AAA88507.1.
L81144 mRNA. Translation: AAL00849.1.
AF171640 mRNA. Translation: AAD49369.1.
BC061789 mRNA. Translation: AAH61789.1.
PIRiA45140.
S10367.
RefSeqiNP_579829.3. NM_133295.3.
UniGeneiRn.225887.

3D structure databases

ProteinModelPortaliP16303.
SMRiP16303. Positions 21-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4564205.
STRINGi10116.ENSRNOP00000021812.

Chemistry

SwissLipidsiSLP:000001457.

Protein family/group databases

ESTHERiratno-Ces1d. Carb_B_Chordata.
MEROPSiS09.983.

PTM databases

iPTMnetiP16303.
PhosphoSiteiP16303.

Proteomic databases

PaxDbiP16303.
PRIDEiP16303.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi113902.
KEGGirno:113902.

Organism-specific databases

CTDi104158.
RGDi70896. Ces1d.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP16303.
KOiK01044.
PhylomeDBiP16303.

Enzyme and pathway databases

BRENDAi3.1.1.1. 5301.
SABIO-RKP16303.

Miscellaneous databases

NextBioi617986.
PROiP16303.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of cDNA coding for rat liver pI 6.1 esterase (ES-10), a carboxylesterase located in the lumen of the endoplasmic reticulum."
    Robbi M., Beaufay H., Octave J.-N.
    Biochem. J. 269:451-458(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley and Wistar.
    Tissue: Liver.
  2. "The carboxylesterase family exhibits C-terminal sequence diversity reflecting the presence or absence of endoplasmic-reticulum-retention sequences."
    Medda S., Proia R.L.
    Eur. J. Biochem. 206:801-806(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Molecular cloning and expression of rat hepatic neutral cholesteryl ester hydrolase."
    Ghosh S., Mallonee D.H., Hylemon P.B., Grogan W.M.
    Biochim. Biophys. Acta 1259:305-312(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "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."
    Wallace T.J., Kodsi E.M., Langston T.B., Gergis M.R., Grogan W.M.
    J. Biol. Chem. 276:33165-33174(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLN-186; MET-423; SER-491; LYS-492 AND ASN-506.
    Strain: Sprague-Dawley.
    Tissue: Lung.
  5. "Rattus norvegicus adipocyte carboxylesterase mRNA."
    Ryu J.W., Lee W., Jung C.Y.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  7. "Fatty acid ethyl ester synthase in rat adipose tissue and its relationship to carboxylesterase."
    Tsujita T., Okuda H.
    J. Biol. Chem. 267:23489-23494(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-45, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Adipose tissue.
  8. "Molecular aspects of carboxylesterase isoforms in comparison with other esterases."
    Satoh T., Hosokawa M.
    Toxicol. Lett. 82:439-445(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-38, NUCLEOTIDE SEQUENCE [MRNA] OF 113-121; 138-149; 216-224; 350-356 AND 464-469, SUBUNIT.
    Tissue: Liver.

Entry informationi

Entry nameiCES1D_RAT
AccessioniPrimary (citable) accession number: P16303
Secondary accession number(s): Q64574
, Q6P785, Q91YG2, Q9QUX7, Q9R135
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 25, 2004
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.