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O43772 (MCAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial carnitine/acylcarnitine carrier protein
Alternative name(s):
Carnitine/acylcarnitine translocase
Short name=CAC
Solute carrier family 25 member 20
Gene names
Name:SLC25A20
Synonyms:CAC, CACT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates 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.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Involvement in disease

Carnitine-acylcarnitine translocase deficiency (CACT deficiency) [MIM:212138]: A rare long-chain fatty acid oxidation disorder. Metabolic consequences include hypoketotic hypoglycemia under fasting conditions, hyperammonemia, elevated creatine kinase and transaminases, dicarboxylic aciduria, very low free carnitine and abnormal acylcarnitine profile with marked elevation of the long-chain acylcarnitines. Clinical features include neurologic abnormalities, cardiomyopathy, arrhythmias, skeletal muscle damage, liver dysfunction and episodes of life-threatening coma, which eventually lead to death. Most patients become symptomatic in the neonatal period with a rapidly progressive deterioration and a high mortality rate.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

Sequence similarities

Belongs to the mitochondrial carrier (TC 2.A.29) family. [View classification]

Contains 3 Solcar repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 301301Mitochondrial carnitine/acylcarnitine carrier protein
PRO_0000090628

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3119Helical; Name=1; Potential
Topological domain32 – 7342Mitochondrial matrix Potential
Transmembrane74 – 9320Helical; Name=2; Potential
Topological domain94 – 11219Cytoplasmic Potential
Transmembrane113 – 13119Helical; Name=3; Potential
Topological domain132 – 17039Mitochondrial matrix Potential
Transmembrane171 – 19020Helical; Name=4; Potential
Topological domain191 – 21121Cytoplasmic Potential
Transmembrane212 – 23019Helical; Name=5; Potential
Topological domain231 – 26737Mitochondrial matrix Potential
Transmembrane268 – 28720Helical; Name=6; Potential
Topological domain288 – 30114Cytoplasmic Potential
Repeat8 – 9992Solcar 1
Repeat108 – 19689Solcar 2
Repeat207 – 29387Solcar 3

Amino acid modifications

Modified residue1481N6-acetyllysine By similarity
Modified residue1571N6-acetyllysine By similarity
Modified residue1701N6-acetyllysine; alternate By similarity
Modified residue1701N6-succinyllysine; alternate By similarity

Natural variations

Natural variant1331R → W in CACT deficiency. Ref.8
VAR_021818
Natural variant2311D → H in CACT deficiency. Ref.8
VAR_021819
Natural variant2381Q → R in CACT deficiency. Ref.6 Ref.7
Corresponds to variant rs28934589 [ dbSNP | Ensembl ].
VAR_021820

Experimental info

Sequence conflict2031R → S in CAB55356. Ref.2
Sequence conflict2401A → G in CAB55356. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O43772 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: AEB34E4E335102B0

FASTA30132,944
        10         20         30         40         50         60 
MADQPKPISP LKNLLAGGFG GVCLVFVGHP LDTVKVRLQT QPPSLPGQPP MYSGTFDCFR 

        70         80         90        100        110        120 
KTLFREGITG LYRGMAAPII GVTPMFAVCF FGFGLGKKLQ QKHPEDVLSY PQLFAAGMLS 

       130        140        150        160        170        180 
GVFTTGIMTP GERIKCLLQI QASSGESKYT GTLDCAKKLY QEFGIRGIYK GTVLTLMRDV 

       190        200        210        220        230        240 
PASGMYFMTY EWLKNIFTPE GKRVSELSAP RILVAGGIAG IFNWAVAIPP DVLKSRFQTA 

       250        260        270        280        290        300 
PPGKYPNGFR DVLRELIRDE GVTSLYKGFN AVMIRAFPAN AACFLGFEVA MKFLNWATPN 


L 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the human carnitine-acylcarnitine carrier cDNA and identification of the molecular defect in a patient."
Huizing M., Iacobazzi V., Ijlst L., Savelkoul P., Ruitenbeek W., van den Heuvel L., Indiveri C., Smeitink J., Trijbels F., Wanders R., Palmieri F.
Am. J. Hum. Genet. 61:1239-1245(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISEASE.
Tissue: Liver.
[2]"The structure and organization of the human carnitine/acylcarnitine translocase (CACT) gene."
Iacobazzi V., Naglieri M.A., Stanley C.A., Wanders R.J.A., Palmieri F.
Biochem. Biophys. Res. Commun. 252:770-774(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"A novel molecular defect of the carnitine acylcarnitine translocase gene in a Saudi patient."
Al-Aqeel A.I., Rashid M.S., Ruiter J.P., Ijlst L., Wanders R.J.A.
Clin. Genet. 64:163-165(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CACT DEFICIENCY ARG-238.
[7]"Response to therapy in carnitine/acylcarnitine translocase (CACT) deficiency due to a novel missense mutation."
Iacobazzi V., Pasquali M., Singh R., Matern D., Rinaldo P., Amat di San Filippo C., Palmieri F., Longo N.
Am. J. Med. Genet. A 126:150-155(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CACT DEFICIENCY ARG-238.
[8]"Molecular and functional analysis of SLC25A20 mutations causing carnitine-acylcarnitine translocase deficiency."
Iacobazzi V., Invernizzi F., Baratta S., Pons R., Chung W., Garavaglia B., Dionisi-Vici C., Ribes A., Parini R., Huertas M.D., Roldan S., Lauria G., Palmieri F., Taroni F.
Hum. Mutat. 24:312-320(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CACT DEFICIENCY TRP-133 AND HIS-231.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10319 mRNA. Translation: CAA71367.1.
Y17775 expand/collapse EMBL AC list , Y17776, Y17777, Y17778, Y17779 Genomic DNA. Translation: CAB55356.1.
AK312962 mRNA. Translation: BAG35801.1.
BC001689 mRNA. Translation: AAH01689.1.
CCDSCCDS2779.1.
RefSeqNP_000378.1. NM_000387.5.
UniGeneHs.13845.

3D structure databases

ProteinModelPortalO43772.
SMRO43772. Positions 14-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107241. 3 interactions.
IntActO43772. 1 interaction.
MINTMINT-1370660.
STRING9606.ENSP00000326305.

Chemistry

ChEMBLCHEMBL2216740.
DrugBankDB00583. L-Carnitine.

Protein family/group databases

TCDB2.A.29.8.3. the mitochondrial carrier (mc) family.

PTM databases

PhosphoSiteO43772.

Proteomic databases

MaxQBO43772.
PaxDbO43772.
PeptideAtlasO43772.
PRIDEO43772.

Protocols and materials databases

DNASU788.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319017; ENSP00000326305; ENSG00000178537.
GeneID788.
KEGGhsa:788.
UCSCuc003cva.4. human.

Organism-specific databases

CTD788.
GeneCardsGC03M048869.
HGNCHGNC:1421. SLC25A20.
HPAHPA016862.
HPA029863.
MIM212138. phenotype.
613698. gene.
neXtProtNX_O43772.
Orphanet159. Carnitine-acylcarnitine translocase deficiency.
PharmGKBPA35031.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245605.
HOGENOMHOG000168307.
HOVERGENHBG003500.
InParanoidO43772.
KOK15109.
OMALSYPQIF.
PhylomeDBO43772.
TreeFamTF300894.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000178537-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO43772.
BgeeO43772.
CleanExHS_SLC25A20.
GenevestigatorO43772.

Family and domain databases

Gene3D1.50.40.10. 1 hit.
InterProIPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamPF00153. Mito_carr. 3 hits.
[Graphical view]
SUPFAMSSF103506. SSF103506. 1 hit.
PROSITEPS50920. SOLCAR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi788.
NextBio3206.
PROO43772.
SOURCESearch...

Entry information

Entry nameMCAT_HUMAN
AccessionPrimary (citable) accession number: O43772
Secondary accession number(s): B2R7F4, Q9UIQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM