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NamePeroxisomal carnitine O-octanoyltransferase
Synonyms
  • 2.3.1.137
  • COT
Gene NameCROT
OrganismHuman
Amino acid sequence
>lcl|BSEQ0000743|Peroxisomal carnitine O-octanoyltransferase
MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQS
GIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGT
QLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYF
RTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAAL
TSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIG
DPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVR
DIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFI
QLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQ
QKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFV
LSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAF
HDMIQLMNSTHL
Number of residues612
Molecular Weight70177.935
Theoretical pI7.09
GO Classification
Functions
  • receptor binding
  • carnitine O-octanoyltransferase activity
Processes
  • fatty acid beta-oxidation
  • small molecule metabolic process
  • coenzyme A metabolic process
  • carnitine metabolic process
  • cellular lipid metabolic process
  • fatty acid metabolic process
  • fatty acid transport
  • fatty acid beta-oxidation using acyl-CoA oxidase
  • medium-chain fatty acid metabolic process
  • generation of precursor metabolites and energy
Components
  • peroxisome
  • intracellular membrane-bounded organelle
  • peroxisomal matrix
  • mitochondrion
General FunctionReceptor binding
Specific FunctionBeta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl-CoA, to its corresponding carnitine ester.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID6066280
UniProtKB IDQ9UKG9
UniProtKB Entry NameOCTC_HUMAN
Cellular LocationPeroxisome
Gene sequence
>lcl|BSEQ0016074|Peroxisomal carnitine O-octanoyltransferase (CROT)
ATGGAAAATCAATTGGCTAAATCAACTGAAGAACGAACATTTCAGTACCAGGATTCTCTT
CCATCACTGCCTGTTCCTTCACTTGAAGAATCATTAAAAAAATACCTTGAATCAGTCACC
AGAACATGCTACCAGATAAGGGGTCTTGATCCAGATGCTAAGAGAGGGTTCTTGGATCTC
ACGCGGGAAGGAATTCAAGTGAAACCATTTGCAAATCAAGAAGAATATAAGAAAACTGAA
GAAATAGTTCAAAAATTTCAAAGTGGGATTGGAGAAAAATTGCACCAGAAATTGCTTGAA
AGAGCAAAAGGAAAAAGAAATTGGCTGGAAGAGTGGTGGCTGAATGTTGCCTATCTGGAT
GTTCGTATACCATCACAATTGAATGTCAACTTTGCGGGTCCTGCAGCTCATTTTGAACAC
TACTGGCCTCCAAAGGAAGGGACTCAATTAGAAAGAGGAAGTATAACTCTTTGGCATAAC
TTGAACTACTGGCAGCTATTAAGAAAAGAAAAAGTGCCTGTTCATAAAGTTGGAAATACT
CCTCTAGATATGAATCAATTCCGAATGCTATTTTCTACCTGCAAGGTTCCAGGAATTACT
AGAGACTCCATTATGAATTATTTTAGGACTGAGAGTGAAGGGCGTTCCCCAAACCACATT
GTAGTGCTGTGTCGAGGCCGAGCTTTTGTCTTTGATGTAATACATGAAGGATGTTTGGTC
ACCCCGCCAGAGCTTCTCAGACAACTGACATATATCCACAAGAAGTGCCATAGTGAACCT
GATGGACCTGGGATTGCAGCATTAACTAGTGAGGAGCGAACTCGATGGGCTAAGGCACGA
GAATATCTGATTGGTCTTGATCCAGAGAACTTGGCTTTGTTAGAAAAAATTCAGAGTAGT
TTACTGGTATATTCCATGGAGGATAGCAGTCCACATGTAACACCAGAGGATTATTCTGAG
ATTATTGCAGCCATCCTTATTGGAGATCCAACAGTACGCTGGGGTGACAAATCCTATAAC
TTGATTTCCTTTTCTAATGGAGTATTTGGCTGTAATTGTGATCATGCTCCTTTTGATGCA
ATGATTATGGTGAACATCAGTTATTATGTGGATGAGAAAATTTTTCAGAATGAAGGAAGA
TGGAAGGGTTCAGAGAAGGTACGAGATATACCACTTCCAGAAGAGCTCATTTTCATTGTG
GATGAGAAAGTTTTAAATGACATCAACCAAGCTAAAGCCCAGTATCTCAGGGAGGCATCT
GATCTACAGATTGCGGCTTATGCCTTTACATCTTTTGGCAAAAAGCTAACCAAGAACAAG
ATGCTTCACCCGGATACGTTTATTCAGCTTGCACTTCAGCTGGCCTATTACAGACTTCAT
GGACACCCTGGTTGTTGCTATGAAACAGCTATGACAAGACATTTTTATCATGGCCGTACA
GAGACTATGCGATCATGCACAGTTGAAGCAGTGAGGTGGTGCCAGTCCATGCAGGATCCT
TCTGTCAATCTTCGTGAGCGGCAGCAAAAGATGTTACAAGCTTTTGCAAAGCATAATAAA
ATGATGAAAGATTGTTCAGCTGGAAAAGGATTTGATCGTCACCTTTTAGGTCTCTTACTC
ATAGCAAAAGAGGAAGGTCTTCCTGTTCCAGAACTCTTTACGGACCCACTTTTTTCCAAA
AGCGGAGGAGGTGGAAATTTTGTTCTCTCAACAAGTCTGGTTGGCTATTTACGAGTCCAG
GGAGTGGTAGTTCCCATGGTACACAATGGTTATGGATTTTTCTACCATATCAGAGATGAC
AGGTTTGTTGTGGCCTGTTCAGCCTGGAAATCCTGTCCCGAGACTGATGCGGAAAAGCTA
GTTCAGCTGACTTTTTGTGCTTTTCATGATATGATACAGCTGATGAACTCTACTCATCTT
TAG
GenBank Gene IDAF168793
GeneCard IDNot Available
GenAtlas IDCROT
HGNC IDHGNC:2366
Chromosome Location7
Locus7q21.1
References
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  5. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. 22814378
  6. Morillas M, Gomez-Puertas P, Rubi B, Clotet J, Arino J, Valencia A, Hegardt FG, Serra D, Asins G: 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. 2002 Mar 29;277(13):11473-80. Epub 2002 Jan 14. 11790793