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2.A.29.8.3 Human mitochondrial carnitine/acyl carnitine carrier, CAC; carnitine/acyl carnitine translocase (CACT). Defects in CACT (SLC25A20) cause CACT deficiency [MIM212138] (autosomal recessive; lethal) (Indiveri et al., 2011). A type of fluorescent probes (BCT) have a minimalist structural design based on the highly efficient and photostable BODIPY chromophore and carnitine as a biotargeting element. Both units are orthogonally bonded through a common boron atom, thus avoiding the use of complex polyatomic connectors. In contrast to previously known mitochondria-specific dyes, BCTs selectively label these organelles regardless of their transmembrane potential and in an enantioselective way. Carnitine-acylcarnitine translocase (CACT) is the key transporter for BCTs, which behave as acylcarnitine biomimetics (Blázquez-Moraleja et al. 2019). Long-chain fatty acylcarnitine binding to the mitochondrial carnitine/acylcarnitine carrier has been demonstrated (Zhang et al. 2022). Proline/Glycine residues of the PG-levels guide conformational changes along the transport cycle in CAC (SLC25A20).
Accession Number:	O43772
Protein Name:	Human mitochondrial carnitine/acyl carnitine carrier aka carnitine/acyl carnitine translocase (CAC) aka CAC deficiency (SLC25A20)
Length:	301
Molecular Weight:	32944.00
Species:	Homo sapiens (Human) [9606]
Number of TMSs:	6
Location¹ / Topology² / Orientation³:	Mitochondrion inner membrane¹ / Multi-pass membrane protein²
Substrate	S-adenosyl-L-methionine, carnitinium

RefSeq:	NP_000378.1
Entrez Gene ID:	788
Pfam:	PF00153
OMIM:	212138 gene+phenotype
KEGG:	hsa:788 hsa:788 hsa:788
Gene Ontology GO:0016021 C:integral to membrane GO:0005743 C:mitochondrial inner membrane GO:0015227 F:acyl carnitine transporter activity GO:0005488 F:binding GO:0006853 P:carnitine shuttle GO:0046320 P:regulation of fatty acid oxidation GO:0044255 P:cellular lipid metabolic process GO:0044281 P:small molecule metabolic process
References (23) [1] “Cloning of the human carnitine-acylcarnitine carrier cDNA and identification of the molecular defect in a patient.” Huizing M.et.al. 9399886 [2] “The structure and organization of the human carnitine/acylcarnitine translocase (CACT) gene.” Iacobazzi V.et.al. 9837782 [3] “Complete sequencing and characterization of 21,243 full-length human cDNAs.” Ota T.et.al. 14702039 [4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [5] “A novel molecular defect of the carnitine acylcarnitine translocase gene in a Saudi patient.” Al-Aqeel A.I.et.al. 12859414 [6] “Response to therapy in carnitine/acylcarnitine translocase (CACT) deficiency due to a novel missense mutation.” Iacobazzi V.et.al. 15057979 [7] “Molecular and functional analysis of SLC25A20 mutations causing carnitine-acylcarnitine translocase deficiency.” Iacobazzi V.et.al. 15365988 [8] “Cloning of the human carnitine-acylcarnitine carrier cDNA and identification of the molecular defect in a patient.” Huizing M.et.al. 9399886 [9] “The structure and organization of the human carnitine/acylcarnitine translocase (CACT) gene.” Iacobazzi V.et.al. 9837782 [10] “Complete sequencing and characterization of 21,243 full-length human cDNAs.” Ota T.et.al. 14702039 [11] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [12] “Initial characterization of the human central proteome.” Burkard T.R.et.al. 21269460 [13] “A novel molecular defect of the carnitine acylcarnitine translocase gene in a Saudi patient.” Al-Aqeel A.I.et.al. 12859414 [14] “Response to therapy in carnitine/acylcarnitine translocase (CACT) deficiency due to a novel missense mutation.” Iacobazzi V.et.al. 15057979 [15] “Molecular and functional analysis of SLC25A20 mutations causing carnitine-acylcarnitine translocase deficiency.” Iacobazzi V.et.al. 15365988 [16] “Cloning of the human carnitine-acylcarnitine carrier cDNA and identification of the molecular defect in a patient.” Huizing M.et.al. 9399886 [17] “The structure and organization of the human carnitine/acylcarnitine translocase (CACT) gene.” Iacobazzi V.et.al. 9837782 [18] “Complete sequencing and characterization of 21,243 full-length human cDNAs.” Ota T.et.al. 14702039 [19] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [20] “Initial characterization of the human central proteome.” Burkard T.R.et.al. 21269460 [21] “A novel molecular defect of the carnitine acylcarnitine translocase gene in a Saudi patient.” Al-Aqeel A.I.et.al. 12859414 [22] “Response to therapy in carnitine/acylcarnitine translocase (CACT) deficiency due to a novel missense mutation.” Iacobazzi V.et.al. 15057979 [23] “Molecular and functional analysis of SLC25A20 mutations causing carnitine-acylcarnitine translocase deficiency.” Iacobazzi V.et.al. 15365988

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FASTA formatted sequence

1:	MADQPKPISP LKNLLAGGFG GVCLVFVGHP LDTVKVRLQT QPPSLPGQPP MYSGTFDCFR 
61:	KTLFREGITG LYRGMAAPII GVTPMFAVCF FGFGLGKKLQ QKHPEDVLSY PQLFAAGMLS 
121:	GVFTTGIMTP GERIKCLLQI QASSGESKYT GTLDCAKKLY QEFGIRGIYK GTVLTLMRDV 
181:	PASGMYFMTY EWLKNIFTPE GKRVSELSAP RILVAGGIAG IFNWAVAIPP DVLKSRFQTA 
241:	PPGKYPNGFR DVLRELIRDE GVTSLYKGFN AVMIRAFPAN AACFLGFEVA MKFLNWATPN 
301:	L

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Gene Ontology

References (23)

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