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   24-JAN-2024, entry version 209.
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; 68.
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   GlyCosmos; P43155; 2 sites, 5 glycans.
DR   GlyGen; P43155; 2 sites, 5 N-linked glycans (2 sites).
DR   iPTMnet; P43155; -.
DR   PhosphoSitePlus; P43155; -.
DR   SwissPalm; 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; 9606-ENSP00000315013; -.
DR   PeptideAtlas; P43155; -.
DR   ProteomicsDB; 55592; -. [P43155-1]
DR   ProteomicsDB; 55593; -. [P43155-2]
DR   ProteomicsDB; 55594; -. [P43155-3]
DR   Pumba; P43155; -.
DR   Antibodypedia; 17825; 259 antibodies from 30 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   AGR; HGNC:2342; -.
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; ENSGT01060000248556; -.
DR   HOGENOM; CLU_013513_5_0_1; -.
DR   InParanoid; P43155; -.
DR   OMA; ENHSKGP; -.
DR   OrthoDB; 1429709at2759; -.
DR   PhylomeDB; P43155; -.
DR   TreeFam; TF313836; -.
DR   BioCyc; MetaCyc:HS01816-MONOMER; -.
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 1161 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 204 other cell types or tissues.
DR   ExpressionAtlas; P43155; baseline and differential.
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; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 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:SF50; CARNITINE O-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
DR   Genevisible; P43155; HS.
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; uncertain significance; loss of
FT                   expression at the protein level and drastic decrease in
FT                   beta-oxidation of palmitate in homozygous patient's primary
FT                   fibroblasts as compared to wild-type cells; primary
FT                   fibroblasts from a homozygous patient show much higher
FT                   intracellular iron content than fibroblasts from control
FT                   individuals and abnormally elevated levels of transferrin
FT                   receptor 1/TFRC at the cell surface; 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
//