Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O43772

- MCAT_HUMAN

UniProt

O43772 - MCAT_HUMAN

Protein

Mitochondrial carnitine/acylcarnitine carrier protein

Gene

SLC25A20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.

    GO - Biological processi

    1. carnitine shuttle Source: Reactome
    2. cellular lipid metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000178537-MONOMER.
    ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.

    Protein family/group databases

    TCDBi2.A.29.8.3. the mitochondrial carrier (mc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial carnitine/acylcarnitine carrier protein
    Alternative name(s):
    Carnitine/acylcarnitine translocase
    Short name:
    CAC
    Solute carrier family 25 member 20
    Gene namesi
    Name:SLC25A20
    Synonyms:CAC, CACT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:1421. SLC25A20.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: Reactome
    3. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Carnitine-acylcarnitine translocase deficiency (CACTD) [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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti133 – 1331R → W in CACTD. 1 Publication
    VAR_021818
    Natural varianti231 – 2311D → H in CACTD. 1 Publication
    VAR_021819
    Natural varianti238 – 2381Q → R in CACTD. 2 Publications
    Corresponds to variant rs28934589 [ dbSNP | Ensembl ].
    VAR_021820

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi212138. phenotype.
    Orphaneti159. Carnitine-acylcarnitine translocase deficiency.
    PharmGKBiPA35031.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 301301Mitochondrial carnitine/acylcarnitine carrier proteinPRO_0000090628Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei148 – 1481N6-acetyllysineBy similarity
    Modified residuei157 – 1571N6-acetyllysineBy similarity
    Modified residuei170 – 1701N6-acetyllysine; alternateBy similarity
    Modified residuei170 – 1701N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO43772.
    PaxDbiO43772.
    PeptideAtlasiO43772.
    PRIDEiO43772.

    PTM databases

    PhosphoSiteiO43772.

    Expressioni

    Gene expression databases

    ArrayExpressiO43772.
    BgeeiO43772.
    CleanExiHS_SLC25A20.
    GenevestigatoriO43772.

    Organism-specific databases

    HPAiHPA016862.
    HPA029863.

    Interactioni

    Protein-protein interaction databases

    BioGridi107241. 3 interactions.
    IntActiO43772. 1 interaction.
    MINTiMINT-1370660.
    STRINGi9606.ENSP00000326305.

    Structurei

    3D structure databases

    ProteinModelPortaliO43772.
    SMRiO43772. Positions 14-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini32 – 7342Mitochondrial matrixSequence AnalysisAdd
    BLAST
    Topological domaini94 – 11219CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini132 – 17039Mitochondrial matrixSequence AnalysisAdd
    BLAST
    Topological domaini191 – 21121CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini231 – 26737Mitochondrial matrixSequence AnalysisAdd
    BLAST
    Topological domaini288 – 30114CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3119Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei74 – 9320Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei113 – 13119Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei171 – 19020Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei212 – 23019Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei268 – 28720Helical; Name=6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati8 – 9992Solcar 1Add
    BLAST
    Repeati108 – 19689Solcar 2Add
    BLAST
    Repeati207 – 29387Solcar 3Add
    BLAST

    Sequence similaritiesi

    Contains 3 Solcar repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG245605.
    HOGENOMiHOG000168307.
    HOVERGENiHBG003500.
    InParanoidiO43772.
    KOiK15109.
    OMAiLSYPQIF.
    PhylomeDBiO43772.
    TreeFamiTF300894.

    Family and domain databases

    Gene3Di1.50.40.10. 1 hit.
    InterProiIPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view]
    PfamiPF00153. Mito_carr. 3 hits.
    [Graphical view]
    SUPFAMiSSF103506. SSF103506. 1 hit.
    PROSITEiPS50920. SOLCAR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O43772-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADQPKPISP LKNLLAGGFG GVCLVFVGHP LDTVKVRLQT QPPSLPGQPP    50
    MYSGTFDCFR KTLFREGITG LYRGMAAPII GVTPMFAVCF FGFGLGKKLQ 100
    QKHPEDVLSY PQLFAAGMLS GVFTTGIMTP GERIKCLLQI QASSGESKYT 150
    GTLDCAKKLY QEFGIRGIYK GTVLTLMRDV PASGMYFMTY EWLKNIFTPE 200
    GKRVSELSAP RILVAGGIAG IFNWAVAIPP DVLKSRFQTA PPGKYPNGFR 250
    DVLRELIRDE GVTSLYKGFN AVMIRAFPAN AACFLGFEVA MKFLNWATPN 300
    L 301
    Length:301
    Mass (Da):32,944
    Last modified:June 1, 1998 - v1
    Checksum:iAEB34E4E335102B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti203 – 2031R → S in CAB55356. (PubMed:9837782)Curated
    Sequence conflicti240 – 2401A → G in CAB55356. (PubMed:9837782)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti133 – 1331R → W in CACTD. 1 Publication
    VAR_021818
    Natural varianti231 – 2311D → H in CACTD. 1 Publication
    VAR_021819
    Natural varianti238 – 2381Q → R in CACTD. 2 Publications
    Corresponds to variant rs28934589 [ dbSNP | Ensembl ].
    VAR_021820

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10319 mRNA. Translation: CAA71367.1.
    Y17775
    , Y17776, Y17777, Y17778, Y17779 Genomic DNA. Translation: CAB55356.1.
    AK312962 mRNA. Translation: BAG35801.1.
    BC001689 mRNA. Translation: AAH01689.1.
    CCDSiCCDS2779.1.
    RefSeqiNP_000378.1. NM_000387.5.
    UniGeneiHs.13845.

    Genome annotation databases

    EnsembliENST00000319017; ENSP00000326305; ENSG00000178537.
    GeneIDi788.
    KEGGihsa:788.
    UCSCiuc003cva.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10319 mRNA. Translation: CAA71367.1 .
    Y17775
    , Y17776 , Y17777 , Y17778 , Y17779 Genomic DNA. Translation: CAB55356.1 .
    AK312962 mRNA. Translation: BAG35801.1 .
    BC001689 mRNA. Translation: AAH01689.1 .
    CCDSi CCDS2779.1.
    RefSeqi NP_000378.1. NM_000387.5.
    UniGenei Hs.13845.

    3D structure databases

    ProteinModelPortali O43772.
    SMRi O43772. Positions 14-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107241. 3 interactions.
    IntActi O43772. 1 interaction.
    MINTi MINT-1370660.
    STRINGi 9606.ENSP00000326305.

    Chemistry

    ChEMBLi CHEMBL2216740.
    DrugBanki DB00583. L-Carnitine.

    Protein family/group databases

    TCDBi 2.A.29.8.3. the mitochondrial carrier (mc) family.

    PTM databases

    PhosphoSitei O43772.

    Proteomic databases

    MaxQBi O43772.
    PaxDbi O43772.
    PeptideAtlasi O43772.
    PRIDEi O43772.

    Protocols and materials databases

    DNASUi 788.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319017 ; ENSP00000326305 ; ENSG00000178537 .
    GeneIDi 788.
    KEGGi hsa:788.
    UCSCi uc003cva.4. human.

    Organism-specific databases

    CTDi 788.
    GeneCardsi GC03M048869.
    HGNCi HGNC:1421. SLC25A20.
    HPAi HPA016862.
    HPA029863.
    MIMi 212138. phenotype.
    613698. gene.
    neXtProti NX_O43772.
    Orphaneti 159. Carnitine-acylcarnitine translocase deficiency.
    PharmGKBi PA35031.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245605.
    HOGENOMi HOG000168307.
    HOVERGENi HBG003500.
    InParanoidi O43772.
    KOi K15109.
    OMAi LSYPQIF.
    PhylomeDBi O43772.
    TreeFami TF300894.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000178537-MONOMER.
    Reactomei REACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.

    Miscellaneous databases

    GenomeRNAii 788.
    NextBioi 3206.
    PROi O43772.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43772.
    Bgeei O43772.
    CleanExi HS_SLC25A20.
    Genevestigatori O43772.

    Family and domain databases

    Gene3Di 1.50.40.10. 1 hit.
    InterProi IPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view ]
    Pfami PF00153. Mito_carr. 3 hits.
    [Graphical view ]
    SUPFAMi SSF103506. SSF103506. 1 hit.
    PROSITEi PS50920. SOLCAR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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 CACTD 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 CACTD 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 CACTD TRP-133 AND HIS-231.

    Entry informationi

    Entry nameiMCAT_HUMAN
    AccessioniPrimary (citable) accession number: O43772
    Secondary accession number(s): B2R7F4, Q9UIQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3