Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei221Acyl-ester intermediatePROSITE-ProRule annotation1
Active sitei353Charge relay systemBy similarity1
Active sitei466Charge relay systemBy similarity1

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 databases

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)DescriptionActionsGraphical viewLength
Mutagenesisi186Q → 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 Publication1
Mutagenesisi423M → 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 Publication1
Mutagenesisi491S → 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 Publication1
Mutagenesisi492K → 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 Publication1
Mutagenesisi506N → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 182 PublicationsAdd BLAST18
ChainiPRO_000000858419 – 565Carboxylesterase 1DAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...)By similarity1
Disulfide bondi87 ↔ 116By similarity
Disulfide bondi273 ↔ 284By similarity
Modified residuei382N6-succinyllysineBy similarity1
Glycosylationi489N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP16303.
PRIDEiP16303.

PTM databases

iPTMnetiP16303.
PhosphoSitePlusiP16303.

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi562 – 565Prevents secretion from ERSequence analysis4

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)DescriptionActionsGraphical viewLength
Sequence conflicti186Q → R in CAA36236 (PubMed:2386485).Curated1
Sequence conflicti186Q → R in AAA88507 (PubMed:8541339).Curated1
Sequence conflicti186Q → R in AAD49369 (Ref. 5) Curated1
Sequence conflicti265N → K in CAA36236 (PubMed:2386485).Curated1
Sequence conflicti420A → E in AAA88507 (PubMed:8541339).Curated1
Sequence conflicti423M → I in CAA36236 (PubMed:2386485).Curated1
Sequence conflicti423M → I in AAA88507 (PubMed:8541339).Curated1
Sequence conflicti423M → I in AAD49369 (Ref. 5) Curated1
Sequence conflicti444M → T in AAL00849 (PubMed:11429416).Curated1
Sequence conflicti491 – 492SK → TQ in AAA88507 (PubMed:8541339).Curated2
Sequence conflicti506N → S in CAA36236 (PubMed:2386485).Curated1
Sequence conflicti506N → S in AAA88507 (PubMed:8541339).Curated1
Sequence conflicti506N → S in AAD49369 (Ref. 5) Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4564205.
STRINGi10116.ENSRNOP00000021812.

Chemistry databases

SwissLipidsiSLP:000001457.

Protein family/group databases

ESTHERiratno-Ces1d. Carb_B_Chordata.
MEROPSiS09.983.

PTM databases

iPTMnetiP16303.
PhosphoSitePlusiP16303.

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

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...

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: November 2, 2016
This is version 136 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.