Carboxylesterase 3

CES3
Identifiers
Aliases	CES3 , ES31, carboxylesterase 3
External IDs	OMIM: 605279; MGI: 102773; HomoloGene: 84407; GeneCards: CES3; OMA:CES3 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) [1] Band 16q22.1 Start 66,961,245 bp [1] End 66,975,149 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8|8 D3 Start 105,775,233 bp [2] End 105,785,045 bp [2]
RNA expression pattern Bgee Human Mouse (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 Species Human Mouse 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 Mb Chr 8: 105.78 – 105.79 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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. GRCh38: Ensembl release 89: ENSG00000172828 – Ensembl, May 2017
2. 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. "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.