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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

Cross database links:

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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Predict TMSs (Predict number of transmembrane segments)
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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