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NameMitochondrial carnitine/acylcarnitine carrier protein
Synonyms
  • CAC
  • CACT
  • Carnitine/acylcarnitine translocase
  • Solute carrier family 25 member 20
Gene NameSLC25A20
OrganismHuman
Amino acid sequence
>lcl|BSEQ0018977|Mitochondrial carnitine/acylcarnitine carrier protein
MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFR
KTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKHPEDVLSYPQLFAAGMLS
GVFTTGIMTPGERIKCLLQIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDV
PASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTA
PPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPN
L
Number of residues301
Molecular Weight32943.46
Theoretical pI9.84
GO Classification
Processes
  • cellular lipid metabolic process
  • carnitine shuttle
  • small molecule metabolic process
Components
  • cytoplasm
  • mitochondrion
  • mitochondrial inner membrane
  • integral component of membrane
General FunctionNot Available
Specific FunctionMediates the transport of acylcarnitines of different length across the mitochondrial inner membrane from the cytosol to the mitochondrial matrix for their oxidation by the mitochondrial fatty acid-oxidation pathway.
Pfam Domain Function
Transmembrane Regions13-31 74-93 113-131 171-190 212-230 268-287
GenBank Protein ID2765075
UniProtKB IDO43772
UniProtKB Entry NameMCAT_HUMAN
Cellular LocationMitochondrion inner membrane
Gene sequence
>lcl|BSEQ0018978|Mitochondrial carnitine/acylcarnitine carrier protein (SLC25A20)
ATGGCCGACCAGCCAAAACCCATCAGCCCGCTCAAGAACCTGCTGGCCGGCGGCTTTGGC
GGCGTGTGCCTGGTGTTCGTCGGTCACCCTCTGGACACGGTCAAGGTCCGACTGCAGACA
CAGCCACCGAGTTTGCCTGGACAACCTCCCATGTACTCTGGGACCTTTGACTGTTTCCGG
AAGACTCTTTTTAGAGAGGGCATCACGGGGCTATATCGGGGAATGGCTGCCCCTATCATC
GGGGTCACTCCCATGTTTGCCGTGTGCTTCTTTGGGTTTGGTTTGGGGAAGAAACTACAA
CAGAAACACCCAGAAGATGTGCTCAGCTATCCCCAGCTTTTTGCAGCTGGGATGTTATCT
GGCGTATTCACCACAGGAATCATGACTCCTGGAGAACGGATCAAGTGCTTATTACAGATT
CAGGCTTCTTCAGGAGAAAGCAAGTACACTGGTACCTTGGACTGTGCAAAGAAGCTGTAC
CAGGAGTTTGGGATCCGAGGCATCTACAAAGGGACTGTGCTTACCCTTATGCGAGATGTC
CCAGCTAGTGGAATGTATTTCATGACATATGAATGGCTGAAAAATATCTTCACTCCGGAG
GGAAAGAGGGTCAGTGAGCTCAGTGCCCCTCGGATCTTGGTGGCTGGGGGCATTGCAGGG
ATCTTCAACTGGGCTGTGGCAATCCCCCCAGATGTGCTCAAGTCTCGATTCCAGACTGCA
CCTCCTGGGAAATATCCTAATGGTTTCAGAGATGTGCTGAGGGAGCTGATCCGGGATGAA
GGAGTCACATCCTTGTACAAAGGGTTCAATGCAGTGATGATCCGAGCCTTCCCAGCCAAT
GCGGCCTGTTTCCTTGGCTTTGAAGTTGCCATGAAGTTCCTTAATTGGGCCACCCCCAAC
TTGTGA
GenBank Gene IDY10319
GeneCard IDNot Available
GenAtlas IDSLC25A20
HGNC IDHGNC:1421
Chromosome Location3
Locus3p21.31
References
  1. Huizing M, Iacobazzi V, Ijlst L, Savelkoul P, Ruitenbeek W, van den Heuvel L, Indiveri C, Smeitink J, Trijbels F, Wanders R, Palmieri F: Cloning of the human carnitine-acylcarnitine carrier cDNA and identification of the molecular defect in a patient. Am J Hum Genet. 1997 Dec;61(6):1239-45. 9399886
  2. Iacobazzi V, Naglieri MA, Stanley CA, Wanders RJ, Palmieri F: The structure and organization of the human carnitine/acylcarnitine translocase (CACT1) gene2. Biochem Biophys Res Commun. 1998 Nov 27;252(3):770-4. 9837782
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  5. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  6. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
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  8. Al Aqeel AI, Rashid MS, Ruiter JP, Ijlst L, Wanders RJ: A novel molecular defect of the carnitine acylcarnitine translocase gene in a Saudi patient. Clin Genet. 2003 Aug;64(2):163-5. 12859414
  9. Iacobazzi V, Pasquali M, Singh R, Matern D, Rinaldo P, Amat di San Filippo C, Palmieri F, Longo N: Response to therapy in carnitine/acylcarnitine translocase (CACT) deficiency due to a novel missense mutation. Am J Med Genet A. 2004 Apr 15;126A(2):150-5. 15057979
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