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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 |
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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
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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 |
External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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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