CACP_YEAST
ID CACP_YEAST Reviewed; 670 AA.
AC P32796; D6VZD3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Carnitine O-acetyltransferase, mitochondrial {ECO:0000303|PubMed:8420957};
DE Short=Carnitine acetylase {ECO:0000303|PubMed:8420957};
DE EC=2.3.1.7 {ECO:0000269|PubMed:8420957};
DE Flags: Precursor;
GN Name=CAT2; Synonyms=CAT, YCAT; OrderedLocusNames=YML042W;
GN ORFNames=YM8054.01;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RX PubMed=8420957; DOI=10.1016/s0021-9258(18)53928-4;
RA Kispal G., Sumegi B., Dietmeier K., Bock I., Gajdos G., Tomcsanyi T.,
RA Sandor A.;
RT "Cloning and sequencing of a cDNA encoding Saccharomyces cerevisiae
RT carnitine acetyltransferase. Use of the cDNA in gene disruption studies.";
RL J. Biol. Chem. 268:1824-1829(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP ALTERNATIVE INITIATION, AND SUBCELLULAR LOCATION.
RX PubMed=7628448; DOI=10.1002/j.1460-2075.1995.tb07353.x;
RA Elgersma Y., van Roermund C.W.T., Wanders R.J.A., Tabak H.F.;
RT "Peroxisomal and mitochondrial carnitine acetyltransferases of
RT Saccharomyces cerevisiae are encoded by a single gene.";
RL EMBO J. 14:3472-3479(1995).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Carnitine acetylase is specific for short chain fatty acids.
CC Carnitine acetylase seems to affect the flux through the pyruvate
CC dehydrogenase complex. It may be involved as well in the transport of
CC acetyl-CoA into mitochondria. {ECO:0000269|PubMed:8420957}.
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:8420957};
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion inner
CC membrane; Peripheral membrane protein; Matrix side
CC {ECO:0000269|PubMed:7628448}.
CC -!- SUBCELLULAR LOCATION: [Isoform Peroxisomal]: Peroxisome
CC {ECO:0000269|PubMed:7628448}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial {ECO:0000269|PubMed:7628448};
CC IsoId=P32796-1; Sequence=Displayed;
CC Name=Peroxisomal {ECO:0000269|PubMed:7628448};
CC IsoId=P32796-2; Sequence=VSP_018690;
CC -!- INDUCTION: By ethanol (PubMed:8420957). Repressed by galactose
CC (PubMed:8420957). {ECO:0000269|PubMed:8420957}.
CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: [Isoform Peroxisomal]: Produced by alternative
CC initiation at Met-23 of isoform Mitochondrial. {ECO:0000305}.
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; Z14021; CAA78399.1; -; Genomic_DNA.
DR EMBL; Z48430; CAA88327.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09857.1; -; Genomic_DNA.
DR PIR; S52478; S52478.
DR RefSeq; NP_013670.1; NM_001182400.1. [P32796-1]
DR AlphaFoldDB; P32796; -.
DR SMR; P32796; -.
DR BioGRID; 35127; 70.
DR DIP; DIP-2476N; -.
DR IntAct; P32796; 9.
DR STRING; 4932.YML042W; -.
DR MaxQB; P32796; -.
DR PaxDb; P32796; -.
DR PRIDE; P32796; -.
DR EnsemblFungi; YML042W_mRNA; YML042W; YML042W. [P32796-1]
DR GeneID; 854965; -.
DR KEGG; sce:YML042W; -.
DR SGD; S000004506; CAT2.
DR VEuPathDB; FungiDB:YML042W; -.
DR eggNOG; KOG3717; Eukaryota.
DR GeneTree; ENSGT01050000244969; -.
DR HOGENOM; CLU_013513_5_1_1; -.
DR InParanoid; P32796; -.
DR OMA; MAYRDPV; -.
DR BioCyc; YEAST:YML042W-MON; -.
DR BRENDA; 2.3.1.7; 984.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR Reactome; R-SCE-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-SCE-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR PRO; PR:P32796; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32796; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0004092; F:carnitine O-acetyltransferase activity; IMP:SGD.
DR GO; GO:0009437; P:carnitine metabolic process; IMP:SGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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 Acyltransferase; Alternative initiation; Fatty acid metabolism;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Peroxisome; Reference proteome; Transferase; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..670
FT /note="Carnitine O-acetyltransferase, mitochondrial"
FT /id="PRO_0000004431"
FT MOTIF 668..670
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT BINDING 461
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT BINDING 465..472
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT BINDING 494
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT BINDING 498
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT BINDING 507
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT BINDING 597
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform Peroxisomal)"
FT /evidence="ECO:0000305"
FT /id="VSP_018690"
FT CONFLICT 263
FT /note="D -> H (in Ref. 1; CAA78399)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="L -> M (in Ref. 1; CAA78399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 77242 MW; C707BAC7ECB4D095 CRC64;
MRICHSRTLS NLKDLPITSR RAMHSAIVNY STQKAQFPVE TNNGEHYWAE KPNKFYQNKR
PNFQGITFAK QQDLPSLPVP ELKSTLDKYL QTIRPFCNDV ETFERQQLLC KDFSEHMGPI
LQDRLKEYAN DKRNWMAKFW DEQSYLQYND PIVPYVSYFY SHMPLPNHLS KIDNDPLIKA
TAIISTVVKF IEAIKDESLP VEIIKGMPFC MNSFSLMFNT SRLPGKPEDN QDTNIFYSVY
ENNFVTIAYK GKFYKLMTHD GNDKPLSENE IWRQLYSVVF QGSQSDPKLG GIGSLTSLPR
DQWREVHLEL MKDPISQDSL ETIHKSSFML CLDLDQSPVT LEEKSRNCWH GDGINRFYDK
SLQFLVTGNG SSGFLAEHSK MDGTPTLFLN NYVCQQLNKL DVDDFMRKVI TPSSTVAMKP
MELPFIITPK IHKAIESAQL QFKETIGEHD LRVWHYNKYG KTFIKRHGMS PDAFIQQVIQ
LAVFKYLKRQ LPTYEAASTR KYFKGRTETG RSVSTASLEF VSKWQNGDVP IAEKIQALKH
SAKEHSTYLK NAANGNGVDR HFFGLKNMLK SNDDQIPPLF KDPLFNYSST WLISTSQLSS
EYFDGYGWSQ VNDNGFGLAY MLNNEWLHIN IVNKPAKSGA SVNRLHYYLS QAADEIFDAL
ENENKRKAKL
