CROT (gene)

CROT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1XL7, 1XL8, 1XMC, 1XMD
Identifiers
Aliases	CROT , COT, carnitine O-octanoyltransferase
External IDs	OMIM: 606090 MGI: 1921364 HomoloGene: 10899 GeneCards: CROT
Gene location (Human) Chr. Chromosome 7 (human) [1] Band 7q21.12 Start 87,345,664 bp [1] End 87,399,794 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 A1 Start 9,016,033 bp [2] End 9,047,324 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in seminal vesicula jejunal mucosa mucosa of urinary bladder duodenum palpebral conjunctiva urethra hair follicle left lobe of thyroid gland right lobe of thyroid gland germinal epithelium Top expressed in left lobe of liver kidney proximal tubule lacrimal gland jejunum esophagus duodenum ileum cornea intestinal villus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity signaling receptor binding acyltransferase activity carnitine O-octanoyltransferase activity Cellular component intracellular membrane-bounded organelle peroxisome peroxisomal matrix cytosol Biological process medium-chain fatty acid metabolic process coenzyme A metabolic process lipid metabolism fatty acid transport generation of precursor metabolites and energy fatty acid metabolic process fatty acid beta-oxidation using acyl-CoA oxidase fatty acid beta-oxidation carnitine metabolic process protein targeting to peroxisome Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 54677 74114 Ensembl ENSG00000005469 ENSMUSG00000003623 UniProt Q9UKG9 Q9DC50 RefSeq (mRNA) NM_001143935 NM_001243745 NM_021151 NM_023733 RefSeq (protein) NP_001137407 NP_001230674 NP_066974 NP_076222 Location (UCSC) Chr 7: 87.35 – 87.4 Mb Chr 5: 9.02 – 9.05 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Peroxisomal carnitine O-octanoyltransferase is an enzyme that in humans is encoded by the CROT gene. ^{[5] [6]}

Carnitine octanoyltransferase (EC 2.3.1.137) is a carnitine acyltransferase that catalyzes the reversible transfer of fatty acyl groups between CoA and carnitine. This enzyme regulates the breakdown of Very Long Chain Fatty Acids (VLCFA) by performing a crucial step in the transport of medium length acyl chains out of the mammalian peroxisome to the cytosol and mitochondria for further breakdown. See also CRAT (MIM 600184). Van der Leij et al. (2000) reviewed the function, structural features, and phylogenetics of human carnitine acyltransferase genes, including CROT.[supplied by OMIM] ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000005469 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000003623 - 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. Ferdinandusse S, Mulders J, IJlst L, Denis S, Dacremont G, Waterham HR, Wanders RJ (Oct 1999). "Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids". Biochem Biophys Res Commun. 263 (1): 213–8. doi:10.1006/bbrc.1999.1340. PMID   10486279.
6. "Entrez Gene: CROT carnitine O-octanoyltransferase".

External links

• Human CROT genome location and CROT gene details page in the UCSC Genome Browser .

Further reading

• van der Leij FR, Huijkman NC, Boomsma C, et al. (2000). "Genomics of the human carnitine acyltransferase genes". Mol. Genet. Metab. 71 (1–2): 139–53. doi:10.1006/mgme.2000.3055. PMID   11001805.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology". Science. 300 (5620): 767–72. Bibcode:2003Sci...300..767S. doi:10.1126/science.1083423. PMC   2882961 . PMID   12690205.
• 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.
• Morillas M, Gómez-Puertas P, Rubí B, et al. (2002). "Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: mutational analysis of a malonyl-CoA affinity domain". J. Biol. Chem. 277 (13): 11473–80. doi: 10.1074/jbc.M111628200 . PMID   11790793.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC   139146 . PMID   9110174.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID   8619474.