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Protein

Carboxylesterase 1D

Gene

Ces1d

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major lipase in white adipose tissue. 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.1 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

Sites

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

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: UniProtKB
  • fatty-acyl-ethyl-ester synthase activity Source: UniProtKB-EC
  • sterol esterase activity Source: UniProtKB
  • triglyceride lipase activity Source: UniProtKB

GO - Biological processi

  • acyl-CoA metabolic process Source: ProtInc
  • acylglycerol catabolic process Source: UniProtKB
  • epithelial cell differentiation Source: MGI
  • lipid catabolic process Source: UniProtKB
  • response to toxic substance Source: ProtInc
  • short-chain fatty acid catabolic process Source: MGI
  • very-low-density lipoprotein particle assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.

Protein family/group databases

ESTHERimouse-Ces1d. Carb_B_Chordata.
MEROPSiS09.983.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxylesterase 1D
Alternative name(s):
Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67)
Fatty acid ethyl ester synthase
Short name:
FAEE synthase
Triacylglycerol hydrolase
Short name:
TGH
Gene namesi
Name:Ces1d
Synonyms:Ces11 Publication, Ces3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2148202. Ces1d.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: ProtInc
  • endoplasmic reticulum lumen Source: UniProtKB
  • lipid particle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Lipid droplet

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3137293.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 565547Carboxylesterase 1DPRO_0000008583Add
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-succinyllysineCombined sources
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8VCT4.
MaxQBiQ8VCT4.
PaxDbiQ8VCT4.
PRIDEiQ8VCT4.

PTM databases

iPTMnetiQ8VCT4.
PhosphoSiteiQ8VCT4.
SwissPalmiQ8VCT4.

Expressioni

Tissue specificityi

Highest expression occurs in liver with lower levels in adipose tissue, kidney, heart, intestine, lung, testis and thymus.2 Publications

Inductioni

By di-(2-ethylhexyl) phthalate.1 Publication

Gene expression databases

BgeeiQ8VCT4.
CleanExiMM_CES1.
MM_CES3.
GenevisibleiQ8VCT4. MM.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

IntActiQ8VCT4. 6 interactions.
MINTiMINT-4090638.
STRINGi10090.ENSMUSP00000034172.

Chemistry

BindingDBiQ8VCT4.

Structurei

3D structure databases

ProteinModelPortaliQ8VCT4.
SMRiQ8VCT4. Positions 21-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the type-B carboxylesterase/lipase family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ8VCT4.
KOiK01044.
OMAiKFNSVPY.
OrthoDBiEOG75XGKD.
PhylomeDBiQ8VCT4.
TreeFamiTF315470.

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.

Q8VCT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLYPLIWLS LAACTAWGYP SSPPVVNTVK GKVLGKYVNL EGFTQPVAVF
60 70 80 90 100
LGVPFAKPPL GSLRFAPPQP AEPWSFVKNT TSYPPMCSQD AVGGQVLSEL
110 120 130 140 150
FTNRKENIPL QFSEDCLYLN IYTPADLTKN SRLPVMVWIH GGGLVVGGAS
160 170 180 190 200
TYDGLALSAH ENVVVVTIQY RLGIWGFFST GDEHSRGNWG HLDQVAALRW
210 220 230 240 250
VQDNIANFGG NPGSVTIFGE SAGGFSVSVL VLSPLAKNLF HRAISESGVS
260 270 280 290 300
LTAALITTDV KPIAGLVATL SGCKTTTSAV MVHCLRQKTE DELLETSLKL
310 320 330 340 350
NLFKLDLLGN PKESYPFLPT VIDGVVLPKA PEEILAEKSF STVPYIVGIN
360 370 380 390 400
KQEFGWIIPT LMGYPLAEGK LDQKTANSLL WKSYPTLKIS ENMIPVVAEK
410 420 430 440 450
YLGGTDDLTK KKDLFQDLMA DVVFGVPSVI VSRSHRDAGA STYMYEFEYR
460 470 480 490 500
PSFVSAMRPK AVIGDHGDEI FSVFGSPFLK DGASEEETNL SKMVMKFWAN
510 520 530 540 550
FARNGNPNGG GLPHWPEYDQ KEGYLKIGAS TQAAQRLKDK EVSFWAELRA
560
KESAQRPSHR EHVEL
Length:565
Mass (Da):61,788
Last modified:March 1, 2002 - v1
Checksum:iE85A9976F9916B34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21G → R in BAA84996 (PubMed:10518925).Curated
Sequence conflicti2 – 21G → R in AAK58067 (PubMed:11470237).Curated
Sequence conflicti49 – 491V → F in BAA84996 (PubMed:10518925).Curated
Sequence conflicti94 – 941G → W in BAA84996 (PubMed:10518925).Curated
Sequence conflicti407 – 4071D → H in BAB60698 (PubMed:15269189).Curated
Sequence conflicti456 – 4583AMR → RHED in BAA84996 (PubMed:10518925).Curated
Sequence conflicti517 – 5204EYDQ → RNMTK in BAA84996 (PubMed:10518925).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025028 mRNA. Translation: BAA84996.1.
AF378751 mRNA. Translation: AAK58067.1.
AB023631 mRNA. Translation: BAB60698.1.
AK078879 mRNA. Translation: BAC37439.1.
BC019198 mRNA. Translation: AAH19198.1.
CCDSiCCDS22528.1.
RefSeqiNP_444430.2. NM_053200.2.
UniGeneiMm.292803.

Genome annotation databases

EnsembliENSMUST00000034172; ENSMUSP00000034172; ENSMUSG00000056973.
GeneIDi104158.
KEGGimmu:104158.
UCSCiuc009mun.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025028 mRNA. Translation: BAA84996.1.
AF378751 mRNA. Translation: AAK58067.1.
AB023631 mRNA. Translation: BAB60698.1.
AK078879 mRNA. Translation: BAC37439.1.
BC019198 mRNA. Translation: AAH19198.1.
CCDSiCCDS22528.1.
RefSeqiNP_444430.2. NM_053200.2.
UniGeneiMm.292803.

3D structure databases

ProteinModelPortaliQ8VCT4.
SMRiQ8VCT4. Positions 21-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VCT4. 6 interactions.
MINTiMINT-4090638.
STRINGi10090.ENSMUSP00000034172.

Chemistry

BindingDBiQ8VCT4.
ChEMBLiCHEMBL3137293.

Protein family/group databases

ESTHERimouse-Ces1d. Carb_B_Chordata.
MEROPSiS09.983.

PTM databases

iPTMnetiQ8VCT4.
PhosphoSiteiQ8VCT4.
SwissPalmiQ8VCT4.

Proteomic databases

EPDiQ8VCT4.
MaxQBiQ8VCT4.
PaxDbiQ8VCT4.
PRIDEiQ8VCT4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034172; ENSMUSP00000034172; ENSMUSG00000056973.
GeneIDi104158.
KEGGimmu:104158.
UCSCiuc009mun.1. mouse.

Organism-specific databases

CTDi104158.
MGIiMGI:2148202. Ces1d.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ8VCT4.
KOiK01044.
OMAiKFNSVPY.
OrthoDBiEOG75XGKD.
PhylomeDBiQ8VCT4.
TreeFamiTF315470.

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.

Miscellaneous databases

NextBioi356634.
PROiQ8VCT4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VCT4.
CleanExiMM_CES1.
MM_CES3.
GenevisibleiQ8VCT4. MM.

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. "cDNA cloning, characterization and stable expression of novel human brain carboxylesterase."
    Mori M., Hosokawa M., Ogasawara Y., Tsukada E., Chiba K.
    FEBS Lett. 458:17-22(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The cloning and expression of a murine triacylglycerol hydrolase cDNA and the structure of its corresponding gene."
    Dolinsky V.W., Sipione S., Lehner R., Vance D.E.
    Biochim. Biophys. Acta 1532:162-172(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: 129/JImported.
    Tissue: LiverImported.
  3. "Identification of di-(2-ethylhexyl) phthalate-induced carboxylesterase 1 in C57BL/6 mouse liver microsomes: purification, cDNA cloning, and baculovirus-mediated expression."
    Furihata T., Hosokawa M., Koyano N., Nakamura T., Satoh T., Chiba K.
    Drug Metab. Dispos. 32:1170-1177(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, INDUCTION.
    Strain: C57BL/6JImported.
    Tissue: LiverImported.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Colon.
  5. "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].
    Strain: FVB/NImported.
    Tissue: KidneyImported.
  6. Cited for: PROTEIN SEQUENCE OF 331-337 AND 390-398, FUNCTION, LIPASE AND NEUTRAL CHOLESTERYL ESTER HYDROLASE ACTIVITIES, SUBCELLULAR LOCATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCES1D_MOUSE
AccessioniPrimary (citable) accession number: Q8VCT4
Secondary accession number(s): Q91ZV9, Q924V8, Q9ULY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to originate from human.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.