YAT2_YEAST
ID YAT2_YEAST Reviewed; 923 AA.
AC P40017; D3DLS3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Carnitine O-acetyltransferase YAT2 {ECO:0000303|PubMed:11329169};
DE EC=2.3.1.7 {ECO:0000305|PubMed:11329169};
GN Name=YAT2 {ECO:0000303|PubMed:11329169}; OrderedLocusNames=YER024W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11329169; DOI=10.1002/yea.712;
RA Swiegers J.H., Dippenaar N., Pretorius I.S., Bauer F.F.;
RT "Carnitine-dependent metabolic activities in Saccharomyces cerevisiae:
RT three carnitine acetyltransferases are essential in a carnitine-dependent
RT strain.";
RL Yeast 18:585-595(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18427809; DOI=10.1007/s00294-008-0191-0;
RA Franken J., Kroppenstedt S., Swiegers J.H., Bauer F.F.;
RT "Carnitine and carnitine acetyltransferases in the yeast Saccharomyces
RT cerevisiae: a role for carnitine in stress protection.";
RL Curr. Genet. 53:347-360(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Carnitine O-acetyltransferase involved in the shutteling of
CC acetyl-CoA in the cell. {ECO:0000269|PubMed:11329169}.
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:0000305|PubMed:11329169};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18427809}.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U18778; AAB64557.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07677.1; -; Genomic_DNA.
DR PIR; S50482; S50482.
DR RefSeq; NP_010941.1; NM_001178915.1.
DR AlphaFoldDB; P40017; -.
DR SMR; P40017; -.
DR BioGRID; 36758; 54.
DR IntAct; P40017; 2.
DR STRING; 4932.YER024W; -.
DR iPTMnet; P40017; -.
DR MaxQB; P40017; -.
DR PaxDb; P40017; -.
DR PRIDE; P40017; -.
DR EnsemblFungi; YER024W_mRNA; YER024W; YER024W.
DR GeneID; 856745; -.
DR KEGG; sce:YER024W; -.
DR SGD; S000000826; YAT2.
DR VEuPathDB; FungiDB:YER024W; -.
DR eggNOG; KOG3719; Eukaryota.
DR GeneTree; ENSGT01050000244969; -.
DR HOGENOM; CLU_013513_4_1_1; -.
DR InParanoid; P40017; -.
DR OMA; PRNPFLI; -.
DR BioCyc; YEAST:YER024W-MON; -.
DR PRO; PR:P40017; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40017; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0004092; F:carnitine O-acetyltransferase activity; IMP:SGD.
DR GO; GO:0006066; P:alcohol metabolic process; 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; 1.10.275.20; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR042572; Carn_acyl_trans_N.
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; Cytoplasm; Fatty acid metabolism;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..923
FT /note="Carnitine O-acetyltransferase YAT2"
FT /id="PRO_0000210176"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 529..541
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT BINDING 567
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P28329"
FT BINDING 576
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 923 AA; 103334 MW; B59AB881491D68A7 CRC64;
MSSGSTIVSS DKSGRTFKHE EELPKLPLPK LCDTLQRLKE SLEPLYYADG YYQHPLDPEQ
IEKLSSIIRD FEENPVSEKL QSKLQSYHDT RDCYLDELHL DINNQTSTRE IQDDVLPRNP
FLVLADDALP NITQADRSAV LVHSAARFIS ALKQDLLPPD INATNGKPLS MAPFLNLFGT
TRSPVFQRGE VENFDLNKPY TASDLEDPDY SSDEDDNDEP TQKDFDDRKR KHEEDIFTGN
GITIKRHPDS KHILIISRGQ YYTLEVLDST NKIIYTAAEL TTIFNHIIKD SSGIEKSTAL
GSLTSHSFRN WKYARKRLQK RYPNELHRID SALFVLVLDE SQEETTNDGD DTADISQMFN
RTITERDKKC TSANCKRVFY GTSIINSKGH QVGSCVSRWY DKLQLVVTAD AKATVIWDSF
TCDGSVVLRF TSEIYTESVL RLARDVNAGD PQFSLWPNVT QMDPETKKLM TATISADGGG
PSEIDPKLVV NKIDWSFSNI LNTHVHLSET KLADLISKYD IVRASIPLGR RSAQRLGVKP
DSMVQVALQI AHYALYGRMV FGLEPVSTRG FKNSRSSFIN IQSQALLELC QLFISSSIDG
TDKLDKFIQT CETHNNMVKH AKSGVGYEKH FNALKYLFKF HDHFGIHLSG DESSAAKDLF
ENPLVLPFSQ PELIVANCGN AATTTFGITP AVPHGFGIGY IIKDDQVDLT VTSQFRQGDR
LMFMLSWVLG EIRSYWRMSR GTSHNKTGVK ISPVVDKLYE MDNAVNNPPK RNGHTVNGSR
KTSSSSQVNL NRYGGFFDLE GHIDSRNISK TPSMKNLQKT FNGLTMSADN DHSSSAVSVP
TEKEKLNTGH EILQIQPREV ASNGLEADDE TDIEIVAGNA DGTSSSASSA TSLNSKKRNV
INSRFDIDFD RSRVGRKVAT LDQ
