CACP_RAT
ID CACP_RAT Reviewed; 626 AA.
AC Q704S8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Carnitine O-acetyltransferase;
DE Short=Carnitine acetylase;
DE EC=2.3.1.137 {ECO:0000250|UniProtKB:P43155};
DE EC=2.3.1.7 {ECO:0000250|UniProtKB:P43155};
DE AltName: Full=Carnitine acetyltransferase;
DE Short=CAT;
DE Short=CrAT;
GN Name=Crat {ECO:0000312|RGD:1303031};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF HIS-343; GLU-347 AND
RP MET-564, AND 3D-STRUCTURE MODELING.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=15155769; DOI=10.1074/jbc.m402685200;
RA Cordente A.G., Lopez-Vinas E., Vazquez M.I., Swiegers J.H., Pretorius I.S.,
RA Gomez-Puertas P., Hegardt F.G., Asins G., Serra D.;
RT "Redesign of carnitine acetyltransferase specificity by protein
RT engineering.";
RL J. Biol. Chem. 279:33899-33908(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
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. Responsible for the synthesis of short- and branched-chain
CC acylcarnitines. Active towards some branched-chain amino acid oxidation
CC pathway (BCAAO) intermediates. Trans-2-enoyl-CoAs and 2-methylacyl-CoAs
CC are poor substrates. {ECO:0000250|UniProtKB:P43155}.
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21137;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44977;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44981;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44973;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17178;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44829;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44985;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44989;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44993;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44997;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45001;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44861;
CC Evidence={ECO:0000250|UniProtKB:P43155};
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:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45005;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Expressed in flagella of epididymal sperm.
CC {ECO:0000269|PubMed:19423663}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ620886; CAF06525.1; -; mRNA.
DR EMBL; BC083616; AAH83616.1; -; mRNA.
DR RefSeq; NP_001004085.1; NM_001004085.2.
DR AlphaFoldDB; Q704S8; -.
DR SMR; Q704S8; -.
DR BioGRID; 260070; 1.
DR STRING; 10116.ENSRNOP00000063089; -.
DR iPTMnet; Q704S8; -.
DR PhosphoSitePlus; Q704S8; -.
DR PaxDb; Q704S8; -.
DR PRIDE; Q704S8; -.
DR GeneID; 311849; -.
DR KEGG; rno:311849; -.
DR UCSC; RGD:1303031; rat.
DR CTD; 1384; -.
DR RGD; 1303031; Crat.
DR VEuPathDB; HostDB:ENSRNOG00000018145; -.
DR eggNOG; KOG3717; Eukaryota.
DR InParanoid; Q704S8; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; Q704S8; -.
DR BioCyc; MetaCyc:MON-14440; -.
DR BRENDA; 2.3.1.7; 5301.
DR Reactome; R-RNO-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; Q704S8; -.
DR PRO; PR:Q704S8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000018145; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q704S8; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; ISO:RGD.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; ISS:UniProtKB.
DR GO; GO:0004092; F:carnitine O-acetyltransferase activity; IDA:RGD.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; ISS:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:RGD.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0046459; P:short-chain fatty acid metabolic process; ISS: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 Acetylation; Acyltransferase; Endoplasmic reticulum; Fatty acid metabolism;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Peroxisome; Reference proteome; Transferase; Transport.
FT CHAIN 1..626
FT /note="Carnitine O-acetyltransferase"
FT /id="PRO_0000210174"
FT MOTIF 624..626
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 343
FT /note="Proton acceptor"
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:0000250|UniProtKB:P43155"
FT BINDING 454
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P43155"
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:0000250|UniProtKB:P43155"
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:0000250|UniProtKB:P43155"
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:0000250|UniProtKB:P43155"
FT MUTAGEN 343
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:15155769"
FT MUTAGEN 347
FT /note="E->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:15155769"
FT MUTAGEN 564
FT /note="M->A: Increases activity towards medium chain fatty
FT acids."
FT /evidence="ECO:0000269|PubMed:15155769"
FT MUTAGEN 564
FT /note="M->G: Increases activity towards medium and long
FT chain fatty acids."
FT /evidence="ECO:0000269|PubMed:15155769"
SQ SEQUENCE 626 AA; 70801 MW; 85B0D5DEF7EB0FF1 CRC64;
MLAFAARTVV KPLGLLKPSS LMKVSGRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE
EEWAHTKQLV DEFQTSGGVG ERLQKGLERR AKKMENWLSE WWLKTAYLQF RQPVVIYSSP
GVLLPKQDFM DLQGQLRFAA KLIEGVLDFK SMIDNETLPV EFLGGQPLCM NQYYQILSSC
RVPGLKQDSV VNFLKSKKPP THITVVHNYQ FFELDVYHSD GTPLTSDQIF VQLEKIWNSS
LQSNKEPVGI LTSNHRNSWA KAYSSLIKDK VNRESVNSIQ KSIFTVCLDK QVPRVSDDVY
RSHVAGQMLH GGGSKFNSGN RWFDKTLQFI VAEDGSCGMV YEHAAAEGPP IVALVDHVME
YTKKPELVRS PMVPLPMPKK LRFNITPEIK NDIEKAKQNI SIMIQDLDIM MLVFHHFGKD
FPKSQKLSPD AFIQIALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASTDSLAFVK
GMDDPKVPEQ QRVELLRKAV QAHRAYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD
TSYAIAMHFN LSTSQVPAKT DCVMSFGPVV PDGYGICYNP MEAHINFSVS AYNSCAETNA
ARMAHYLEKA LLDMRTLLQN HPRAKL
