Peroxisomal carnitine O-octanoyltransferase
Details
- Name
- Peroxisomal carnitine O-octanoyltransferase
- Synonyms
- 2.3.1.137
- COT
- Gene Name
- CROT
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0000743|Peroxisomal carnitine O-octanoyltransferase MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQS GIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGT QLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYF RTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAAL TSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIG DPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVR DIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFI QLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQ QKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFV LSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAF HDMIQLMNSTHL
- Number of residues
- 612
- Molecular Weight
- 70177.935
- Theoretical pI
- 7.09
- GO Classification
- Functionscarnitine O-octanoyltransferase activity / receptor bindingProcessescarnitine metabolic process / cellular lipid metabolic process / coenzyme A metabolic process / fatty acid beta-oxidation / fatty acid beta-oxidation using acyl-CoA oxidase / fatty acid metabolic process / fatty acid transport / generation of precursor metabolites and energy / medium-chain fatty acid metabolic process / small molecule metabolic processComponentsintracellular membrane-bounded organelle / mitochondrion / peroxisomal matrix / peroxisome
- General Function
- Receptor binding
- Specific Function
- Beta-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
- Carn_acyltransf (PF00755)
- Transmembrane Regions
- Not Available
- Cellular Location
- Peroxisome
- 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
- Chromosome Location
- 7
- Locus
- 7q21.1
- External Identifiers
Resource Link UniProtKB ID Q9UKG9 UniProtKB Entry Name OCTC_HUMAN GenBank Protein ID 6066280 GenBank Gene ID AF168793 GenAtlas ID CROT HGNC ID HGNC:2366 - General References
- Ferdinandusse S, Mulders J, IJlst L, Denis S, Dacremont G, Waterham HR, Wanders RJ: 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. 1999 Sep 16;263(1):213-8. [Article]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [Article]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [Article]
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- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00583 Levocarnitine approved, investigational unknown Details DB02648 (3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-Ammonium experimental unknown Details DB03832 3-Carboxy-N,N,N-Trimethyl-2-(Octanoyloxy)Propan-1-Aminium experimental unknown Details