Carboxylesterase 3

Protein-coding gene in the species Homo sapiens
CES3
Identifiers
AliasesCES3, ES31, carboxylesterase 3
External IDsOMIM: 605279; MGI: 102773; HomoloGene: 84407; GeneCards: CES3; OMA:CES3 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for CES3
Genomic location for CES3
Band16q22.1Start66,961,245 bp[1]
End66,975,149 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for CES3
Genomic location for CES3
Band8|8 D3Start105,775,233 bp[2]
End105,785,045 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of transverse colon

  • rectum

  • right lobe of liver

  • mucosa of sigmoid colon

  • mucosa of ileum

  • muscle of thigh

  • gastrocnemius muscle

  • jejunal mucosa

  • duodenum

  • tendon of biceps brachii
Top expressed in
  • hepatobiliary system

  • liver

  • duodenum

  • proximal tubule

  • pancreas

  • colon

  • ileum

  • jejunum

  • spermatid

  • testicle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • hydrolase activity
  • carboxylic ester hydrolase activity
  • sterol esterase activity
  • triglyceride lipase activity
  • methyl indole-3-acetate esterase activity
Cellular component
  • endoplasmic reticulum lumen
  • endoplasmic reticulum
  • extracellular exosome
  • cytosol
  • extracellular space
Biological process
  • xenobiotic metabolic process
  • low-density lipoprotein particle clearance
  • lipid catabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23491

382053

Ensembl

ENSG00000172828

ENSMUSG00000069922

UniProt

Q6UWW8

Q63880

RefSeq (mRNA)

NM_001185176
NM_001185177
NM_012122
NM_024922

NM_001164681
NM_198672

RefSeq (protein)

NP_001172105
NP_001172106
NP_079198

NP_001158153
NP_941074

Location (UCSC)Chr 16: 66.96 – 66.98 MbChr 8: 105.78 – 105.79 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Carboxylesterase 3 is an enzyme that in humans is encoded by the CES3 gene.[5][6][7][8]

Function

Carboxylesterase 3 is a member of a large multigene family. The enzymes encoded by these genes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. The specific function of this enzyme has not yet been determined; however, it is speculated that carboxylesterases may play a role in lipid metabolism and/or the blood–brain barrier system.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172828 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000069922 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Mori M, Hosokawa M, Ogasawara Y, Tsukada E, Chiba K (Oct 1999). "cDNA cloning, characterization and stable expression of novel human brain carboxylesterase". FEBS Lett. 458 (1): 17–22. doi:10.1016/S0014-5793(99)01111-4. PMID 10518925. S2CID 5792413.
  6. ^ Sanghani SP, Quinney SK, Fredenburg TB, Sun Z, Davis WI, Murry DJ, Cummings OW, Seitz DE, Bosron WF (Oct 2003). "Carboxylesterases expressed in human colon tumor tissue and their role in CPT-11 hydrolysis". Clin Cancer Res. 9 (13): 4983–91. PMID 14581373.
  7. ^ Sanghani SP, Quinney SK, Fredenburg TB, Davis WI, Murry DJ, Bosron WF (Apr 2004). "Hydrolysis of irinotecan and its oxidative metabolites, 7-ethyl-10-[4-N-(5-aminopentanoic acid)-1-piperidino] carbonyloxycamptothecin and 7-ethyl-10-[4-(1-piperidino)-1-amino]-carbonyloxycamptothecin, by human carboxylesterases CES1A1, CES2, and a newly expressed carboxylesterase isoenzyme, CES3". Drug Metab Dispos. 32 (5): 505–11. doi:10.1124/dmd.32.5.505. PMID 15100172.
  8. ^ a b "Entrez Gene: CES3 carboxylesterase 3 (brain)".

Further reading

  • Lee CV, Hymowitz SG, Wallweber HJ, et al. (2006). "Synthetic anti-BR3 antibodies that mimic BAFF binding and target both human and murine B cells". Blood. 108 (9): 3103–11. doi:10.1182/blood-2006-03-011031. PMID 16840730.
  • Hassel S, Eichner A, Yakymovych M, et al. (2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel electrophoresis and mass spectrometry". Proteomics. 4 (5): 1346–58. doi:10.1002/pmic.200300770. PMID 15188402. S2CID 6773754.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Venter JC, Adams MD, Myers EW, et al. (2001). "The sequence of the human genome". Science. 291 (5507): 1304–51. Bibcode:2001Sci...291.1304V. doi:10.1126/science.1058040. PMID 11181995.
  • Aida K, Moore R, Negishi M (1993). "Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver". Biochim. Biophys. Acta. 1174 (1): 72–4. doi:10.1016/0167-4781(93)90093-s. PMID 7916639.
  • v
  • t
  • e
3.1.1: Carboxylic
ester hydrolases3.1.2: Thioesterase3.1.3: Phosphatase3.1.4:
Phosphodiesterase3.1.6: SulfataseNuclease (includes
deoxyribonuclease
and ribonuclease)
3.1.11-16:
Exonuclease
Exodeoxyribonuclease
Exoribonuclease
3.1.21-31:
Endonuclease
Endodeoxyribonuclease
Endoribonuclease
either deoxy- or ribo-    
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