CACP_HUMAN
ID CACP_HUMAN Reviewed; 626 AA.
AC P43155; Q5T952; Q9BW16;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 5.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Carnitine O-acetyltransferase {ECO:0000305};
DE Short=Carnitine acetylase;
DE EC=2.3.1.137 {ECO:0000269|PubMed:23485643};
DE EC=2.3.1.7 {ECO:0000269|PubMed:15099582, ECO:0000269|PubMed:23485643};
DE AltName: Full=Carnitine acetyltransferase;
DE Short=CAT;
DE Short=CrAT {ECO:0000303|PubMed:23485643};
GN Name=CRAT {ECO:0000312|HGNC:HGNC:2342}; Synonyms=CAT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-372.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-372.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 (ISOFORMS 1 AND 2), AND
RP ALTERNATIVE SPLICING.
RX PubMed=7945262; DOI=10.1042/bj3030037;
RA Corti O., DiDonato S., Finocchiaro G.;
RT "Divergent sequences in the 5' region of cDNA suggest alternative splicing
RT as a mechanism for the generation of carnitine acetyltransferases with
RT different subcellular localizations.";
RL Biochem. J. 303:37-41(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-626 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
RP AND VARIANT MET-372.
RX PubMed=7829107; DOI=10.1006/geno.1994.1463;
RA Corti O., Finocchiaro G., Rossi E., Zuffardi O., Didonato S.;
RT "Molecular cloning of cDNAs encoding human carnitine acetyltransferase and
RT mapping of the corresponding gene to chromosome 9q34.1.";
RL Genomics 23:94-99(1994).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-261 AND LYS-268, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23485643; DOI=10.1016/j.bbadis.2013.02.012;
RA Violante S., Ijlst L., Ruiter J., Koster J., van Lenthe H., Duran M.,
RA de Almeida I.T., Wanders R.J., Houten S.M., Ventura F.V.;
RT "Substrate specificity of human carnitine acetyltransferase: Implications
RT for fatty acid and branched-chain amino acid metabolism.";
RL Biochim. Biophys. Acta 1832:773-779(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP INVOLVEMENT IN NBIA8, VARIANT NBIA8 HIS-321, CHARACTERIZATION OF VARIANT
RP NBIA8 HIS-321, AND FUNCTION.
RX PubMed=29395073; DOI=10.1016/j.ajhg.2018.01.003;
RA Drecourt A., Babdor J., Dussiot M., Petit F., Goudin N., Garfa-Traore M.,
RA Habarou F., Bole-Feysot C., Nitschke P., Ottolenghi C., Metodiev M.D.,
RA Serre V., Desguerre I., Boddaert N., Hermine O., Munnich A., Roetig A.;
RT "Impaired Transferrin Receptor Palmitoylation and Recycling in
RT Neurodegeneration with Brain Iron Accumulation.";
RL Am. J. Hum. Genet. 102:266-277(2018).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 35-626, AND SUBUNIT.
RX PubMed=12562770; DOI=10.1074/jbc.m212356200;
RA Wu D., Govindasamy L., Lian W., Gu Y., Kukar T., Agbandje-McKenna M.,
RA McKenna R.;
RT "Structure of human carnitine acetyltransferase. Molecular basis for fatty
RT acyl transfer.";
RL J. Biol. Chem. 278:13159-13165(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 35-626 IN COMPLEX WITH CARNITINE,
RP MUTAGENESIS OF TYR-452; THR-465; ARG-518 AND PHE-566, CATALYTIC ACTIVITY,
RP AND FUNCTION.
RX PubMed=15099582; DOI=10.1016/j.jsb.2004.01.011;
RA Govindasamy L., Kukar T., Lian W., Pedersen B., Gu Y., Agbandje-McKenna M.,
RA Jin S., McKenna R., Wu D.;
RT "Structural and mutational characterization of L-carnitine binding to human
RT carnitine acetyltransferase.";
RL J. Struct. Biol. 146:416-424(2004).
CC -!- FUNCTION: Catalyzes the reversible transfer of acyl groups from
CC carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio.
CC Also plays a crucial role in the transport of fatty acids for beta-
CC oxidation (PubMed:15099582, PubMed:29395073). Responsible for the
CC synthesis of short- and branched-chain acylcarnitines
CC (PubMed:23485643). Active towards some branched-chain amino acid
CC oxidation pathway (BCAAO) intermediates (PubMed:23485643). Trans-2-
CC enoyl-CoAs and 2-methylacyl-CoAs are poor substrates (PubMed:23485643).
CC {ECO:0000269|PubMed:15099582, ECO:0000269|PubMed:23485643,
CC ECO:0000269|PubMed:29395073}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + acetyl-CoA = CoA + O-acetyl-(R)-carnitine;
CC Xref=Rhea:RHEA:21136, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57589; EC=2.3.1.7;
CC Evidence={ECO:0000269|PubMed:15099582};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21137;
CC Evidence={ECO:0000305|PubMed:15099582};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + propanoyl-CoA = CoA + O-propanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44976, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:53210, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392;
CC Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44977;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + butanoyl-CoA = CoA + O-butanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:44980, ChEBI:CHEBI:16347, ChEBI:CHEBI:21949,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57371;
CC Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44981;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + hexanoyl-CoA = CoA + O-hexanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:44972, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:84834;
CC Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44973;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:17177, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; EC=2.3.1.137;
CC Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17178;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + decanoyl-CoA = CoA + O-decanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:44828, ChEBI:CHEBI:16347, ChEBI:CHEBI:28717,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44829;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 3-methylbutanoyl-CoA = CoA + O-3-
CC methylbutanoyl-(R)-carnitine; Xref=Rhea:RHEA:44984,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57345,
CC ChEBI:CHEBI:70819; Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44985;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 2-methylpropanoyl-CoA = CoA + O-isobutanoyl-
CC (R)-carnitine; Xref=Rhea:RHEA:44988, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:84838;
CC Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44989;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 2-methylbutanoyl-CoA = CoA + O-2-
CC methylbutanoyl-(R)-carnitine; Xref=Rhea:RHEA:44992,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57336,
CC ChEBI:CHEBI:84840; Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44993;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + acetoacetyl-CoA = CoA + O-3-oxobutanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44996, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:84841;
CC Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44997;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 3-hydroxybutanoyl-CoA = CoA + O-3-
CC hydroxybutanoyl-(R)-carnitine; Xref=Rhea:RHEA:45000,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:78611,
CC ChEBI:CHEBI:84842; Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45001;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC ChEBI:CHEBI:84654; Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44861;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 2,6-dimethylheptanoyl-CoA = CoA + O-2,6-
CC dimethylheptanoyl-(R)-carnitine; Xref=Rhea:RHEA:45004,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:84843,
CC ChEBI:CHEBI:84847; Evidence={ECO:0000269|PubMed:23485643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45005;
CC Evidence={ECO:0000305|PubMed:23485643};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC Kinetic parameters:
CC KM=240 uM for acetyl-CoA {ECO:0000269|PubMed:23485643};
CC KM=499 uM for butyryl-CoA {ECO:0000269|PubMed:23485643};
CC KM=590 uM for trans-2-butenoyl-CoA {ECO:0000269|PubMed:23485643};
CC Vmax=2.5 nmol/min/ug enzyme towards acetyl-CoA
CC {ECO:0000269|PubMed:23485643};
CC Vmax=10.7 nmol/min/ug enzyme towards butyryl-CoA
CC {ECO:0000269|PubMed:23485643};
CC Vmax=0.13 nmol/min/ug enzyme towards trans-2-butenoyl-CoA
CC {ECO:0000269|PubMed:23485643};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC Kinetic parameters:
CC KM=78 uM for acetyl-CoA {ECO:0000269|PubMed:23485643};
CC Vmax=4.4 nmol/min/ug enzyme towards acetyl-CoA
CC {ECO:0000269|PubMed:23485643};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12562770,
CC ECO:0000269|PubMed:15099582}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}. Peroxisome
CC {ECO:0000305}. Mitochondrion inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000305|PubMed:23485643}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Peroxisome
CC {ECO:0000305|PubMed:23485643}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SM-1400;
CC IsoId=P43155-1; Sequence=Displayed;
CC Name=2; Synonyms=SM-1200;
CC IsoId=P43155-2; Sequence=VSP_000792;
CC Name=3;
CC IsoId=P43155-3; Sequence=VSP_012798;
CC -!- TISSUE SPECIFICITY: Mostly in skeletal muscle, less in heart, liver and
CC pancreas, only weakly detectable in brain, placenta, lung and kidney.
CC -!- DISEASE: Neurodegeneration with brain iron accumulation 8 (NBIA8)
CC [MIM:617917]: A neurodegenerative disorder associated with iron
CC accumulation, primarily in the basal ganglia. Disease onset is in early
CC childhood. Clinical features include speech delay, progressive
CC cerebellar ataxia, unbalanced gait, and loss of ambulation. NBIA8
CC transmission pattern is consistent with autosomal recessive
CC inheritance. {ECO:0000269|PubMed:29395073}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BT006801; AAP35447.1; -; mRNA.
DR EMBL; AL158151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000723; AAH00723.1; -; mRNA.
DR EMBL; X79825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X79827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X78706; CAA55359.1; -; mRNA.
DR CCDS; CCDS6919.1; -. [P43155-1]
DR PIR; A55720; A55720.
DR RefSeq; XP_005251765.1; XM_005251708.3. [P43155-2]
DR PDB; 1NM8; X-ray; 1.60 A; A=35-626.
DR PDB; 1S5O; X-ray; 1.80 A; A=35-626.
DR PDBsum; 1NM8; -.
DR PDBsum; 1S5O; -.
DR AlphaFoldDB; P43155; -.
DR SMR; P43155; -.
DR BioGRID; 107774; 64.
DR IntAct; P43155; 15.
DR STRING; 9606.ENSP00000315013; -.
DR BindingDB; P43155; -.
DR ChEMBL; CHEMBL3184; -.
DR DrugBank; DB02648; (3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-Ammonium.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB00583; Levocarnitine.
DR SwissLipids; SLP:000001053; -.
DR SwissLipids; SLP:000001057; -. [P43155-1]
DR SwissLipids; SLP:000001058; -. [P43155-2]
DR TCDB; 4.C.2.1.1; the carnitine o-acyl transferase (carat) family.
DR GlyConnect; 1073; 4 N-Linked glycans (2 sites).
DR GlyGen; P43155; 2 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; P43155; -.
DR PhosphoSitePlus; P43155; -.
DR BioMuta; CRAT; -.
DR DMDM; 215274265; -.
DR CPTAC; CPTAC-341; -.
DR CPTAC; CPTAC-342; -.
DR EPD; P43155; -.
DR jPOST; P43155; -.
DR MassIVE; P43155; -.
DR MaxQB; P43155; -.
DR PaxDb; P43155; -.
DR PeptideAtlas; P43155; -.
DR PRIDE; P43155; -.
DR ProteomicsDB; 55592; -. [P43155-1]
DR ProteomicsDB; 55593; -. [P43155-2]
DR ProteomicsDB; 55594; -. [P43155-3]
DR Antibodypedia; 17825; 236 antibodies from 29 providers.
DR DNASU; 1384; -.
DR Ensembl; ENST00000318080.7; ENSP00000315013.2; ENSG00000095321.18. [P43155-1]
DR GeneID; 1384; -.
DR MANE-Select; ENST00000318080.7; ENSP00000315013.2; NM_000755.5; NP_000746.3.
DR UCSC; uc004bxh.4; human. [P43155-1]
DR CTD; 1384; -.
DR DisGeNET; 1384; -.
DR GeneCards; CRAT; -.
DR HGNC; HGNC:2342; CRAT.
DR HPA; ENSG00000095321; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; CRAT; -.
DR MIM; 600184; gene.
DR MIM; 617917; phenotype.
DR neXtProt; NX_P43155; -.
DR OpenTargets; ENSG00000095321; -.
DR PharmGKB; PA26862; -.
DR VEuPathDB; HostDB:ENSG00000095321; -.
DR eggNOG; KOG3717; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_5_0_1; -.
DR InParanoid; P43155; -.
DR OMA; YYRMYGH; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P43155; -.
DR TreeFam; TF313836; -.
DR BioCyc; MetaCyc:HS01816-MON; -.
DR BRENDA; 2.3.1.7; 2681.
DR PathwayCommons; P43155; -.
DR Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; P43155; -.
DR SignaLink; P43155; -.
DR BioGRID-ORCS; 1384; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; CRAT; human.
DR EvolutionaryTrace; P43155; -.
DR GeneWiki; CRAT_(gene); -.
DR GenomeRNAi; 1384; -.
DR Pharos; P43155; Tbio.
DR PRO; PR:P43155; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P43155; protein.
DR Bgee; ENSG00000095321; Expressed in sperm and 202 other tissues.
DR ExpressionAtlas; P43155; baseline and differential.
DR Genevisible; P43155; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IDA:UniProtKB.
DR GO; GO:0004092; F:carnitine O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IDA:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IDA:UniProtKB.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0046459; P:short-chain fatty acid metabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR PANTHER; PTHR22589; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW Direct protein sequencing; Endoplasmic reticulum; Fatty acid metabolism;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Neurodegeneration; Peroxisome; Reference proteome; Transferase; Transport.
FT CHAIN 1..626
FT /note="Carnitine O-acetyltransferase"
FT /id="PRO_0000210172"
FT MOTIF 624..626
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 419
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT BINDING 423..430
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000269|PubMed:15099582"
FT BINDING 454
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000269|PubMed:15099582"
FT BINDING 456
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT BINDING 465
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000269|PubMed:15099582"
FT BINDING 504
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT BINDING 555
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT MOD_RES 93
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT MOD_RES 261
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 261
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT MOD_RES 268
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000792"
FT VAR_SEQ 282..363
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_012798"
FT VARIANT 321
FT /note="R -> H (in NBIA8; unknown pathological significance;
FT loss of expression at the protein level and drastic
FT decrease in beta-oxidation of palmitate in homozygous
FT patient's primary fibroblasts as compared to wild-type
FT cells; primary fibroblasts from a homozygous patient show
FT much higher intracellular iron content than fibroblasts
FT from control individuals and abnormally elevated levels of
FT transferrin receptor 1/TFRC at the cell surface;
FT dbSNP:rs138665095)"
FT /evidence="ECO:0000269|PubMed:29395073"
FT /id="VAR_080636"
FT VARIANT 372
FT /note="L -> M (in dbSNP:rs3118635)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7829107, ECO:0000269|Ref.1"
FT /id="VAR_047780"
FT VARIANT 624
FT /note="A -> P (in dbSNP:rs17459086)"
FT /id="VAR_047781"
FT MUTAGEN 452
FT /note="Y->A: Increases the KM for carnitine 100-fold."
FT /evidence="ECO:0000269|PubMed:15099582"
FT MUTAGEN 452
FT /note="Y->F: Increases the KM for carnitine 320-fold and
FT reduces enzyme activity 10000-fold."
FT /evidence="ECO:0000269|PubMed:15099582"
FT MUTAGEN 465
FT /note="T->A: Increases the KM for carnitine almost 70-fold
FT and reduces enzyme activity 450-fold."
FT /evidence="ECO:0000269|PubMed:15099582"
FT MUTAGEN 518
FT /note="R->Q: Increases the KM for carnitine 230-fold and
FT reduces enzyme activity almost 100-fold."
FT /evidence="ECO:0000269|PubMed:15099582"
FT MUTAGEN 566
FT /note="F->A: Increases the KM for carnitine 18-fold and
FT reduces enzyme activity 100-fold."
FT /evidence="ECO:0000269|PubMed:15099582"
FT MUTAGEN 566
FT /note="F->Y: No effect."
FT /evidence="ECO:0000269|PubMed:15099582"
FT CONFLICT 88
FT /note="E -> G (in Ref. 5; CAA55359)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="P -> F (in Ref. 5; CAA55359)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="D -> G (in Ref. 5; CAA55359)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="M -> T (in Ref. 5; CAA55359)"
FT /evidence="ECO:0000305"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1NM8"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 79..93
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:1NM8"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1NM8"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 132..154
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1S5O"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:1NM8"
FT TURN 314..319
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 387..406
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 407..414
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 429..445
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 473..482
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 489..511
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 517..529
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 536..539
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 541..546
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:1NM8"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:1NM8"
FT HELIX 600..619
FT /evidence="ECO:0007829|PDB:1NM8"
SQ SEQUENCE 626 AA; 70858 MW; 51B65E7C94E458D7 CRC64;
MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE
EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE WWLKTAYLQY RQPVVIYSSP
GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK VMIDNETLPV EYLGGKPLCM NQYYQILSSC
RVPGPKQDTV SNFSKTKKPP THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS
LQTNKEPVGI LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP IVTLLDYVIE
YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD
FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK
AMDDSSVTEH QKVELLRKAV QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD
TSYAIAMHFH LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA
ARLAHYLEKA LLDMRALLQS HPRAKL
