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Protein

Carnitine O-acetyltransferase YAT2

Gene

YAT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the shutteling of acetyl-CoA in the cell.1 Publication

Catalytic activityi

Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei576 – 5761CarnitineBy similarity

GO - Molecular functioni

  • carnitine O-acetyltransferase activity Source: SGD

GO - Biological processi

  • alcohol metabolic process Source: SGD
  • carnitine metabolic process Source: SGD
  • fatty acid metabolic process Source: UniProtKB-KW
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Transport

Enzyme and pathway databases

BioCyciYEAST:YER024W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Carnitine O-acetyltransferase YAT2 (EC:2.3.1.7)
Gene namesi
Name:YAT2
Ordered Locus Names:YER024W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

CYGDiYER024w.
EuPathDBiFungiDB:YER024W.
SGDiS000000826. YAT2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 923922Carnitine O-acetyltransferase YAT2PRO_0000210176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei783 – 7831Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP40017.
PaxDbiP40017.

Interactioni

Protein-protein interaction databases

BioGridi36758. 10 interactions.
IntActiP40017. 1 interaction.
MINTiMINT-4483798.

Structurei

3D structure databases

ProteinModelPortaliP40017.
SMRiP40017. Positions 15-713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni530 – 54112Coenzyme A bindingBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG308143.
HOGENOMiHOG000141908.
InParanoidiP40017.
KOiK00624.
OMAiDILPRNP.
OrthoDBiEOG7TQV84.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 1 hit.
PfamiPF00755. Carn_acyltransf. 2 hits.
[Graphical view]
PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40017-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGSTIVSS DKSGRTFKHE EELPKLPLPK LCDTLQRLKE SLEPLYYADG
60 70 80 90 100
YYQHPLDPEQ IEKLSSIIRD FEENPVSEKL QSKLQSYHDT RDCYLDELHL
110 120 130 140 150
DINNQTSTRE IQDDVLPRNP FLVLADDALP NITQADRSAV LVHSAARFIS
160 170 180 190 200
ALKQDLLPPD INATNGKPLS MAPFLNLFGT TRSPVFQRGE VENFDLNKPY
210 220 230 240 250
TASDLEDPDY SSDEDDNDEP TQKDFDDRKR KHEEDIFTGN GITIKRHPDS
260 270 280 290 300
KHILIISRGQ YYTLEVLDST NKIIYTAAEL TTIFNHIIKD SSGIEKSTAL
310 320 330 340 350
GSLTSHSFRN WKYARKRLQK RYPNELHRID SALFVLVLDE SQEETTNDGD
360 370 380 390 400
DTADISQMFN RTITERDKKC TSANCKRVFY GTSIINSKGH QVGSCVSRWY
410 420 430 440 450
DKLQLVVTAD AKATVIWDSF TCDGSVVLRF TSEIYTESVL RLARDVNAGD
460 470 480 490 500
PQFSLWPNVT QMDPETKKLM TATISADGGG PSEIDPKLVV NKIDWSFSNI
510 520 530 540 550
LNTHVHLSET KLADLISKYD IVRASIPLGR RSAQRLGVKP DSMVQVALQI
560 570 580 590 600
AHYALYGRMV FGLEPVSTRG FKNSRSSFIN IQSQALLELC QLFISSSIDG
610 620 630 640 650
TDKLDKFIQT CETHNNMVKH AKSGVGYEKH FNALKYLFKF HDHFGIHLSG
660 670 680 690 700
DESSAAKDLF ENPLVLPFSQ PELIVANCGN AATTTFGITP AVPHGFGIGY
710 720 730 740 750
IIKDDQVDLT VTSQFRQGDR LMFMLSWVLG EIRSYWRMSR GTSHNKTGVK
760 770 780 790 800
ISPVVDKLYE MDNAVNNPPK RNGHTVNGSR KTSSSSQVNL NRYGGFFDLE
810 820 830 840 850
GHIDSRNISK TPSMKNLQKT FNGLTMSADN DHSSSAVSVP TEKEKLNTGH
860 870 880 890 900
EILQIQPREV ASNGLEADDE TDIEIVAGNA DGTSSSASSA TSLNSKKRNV
910 920
INSRFDIDFD RSRVGRKVAT LDQ
Length:923
Mass (Da):103,334
Last modified:February 1, 1995 - v1
Checksum:iB59AB881491D68A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18778 Genomic DNA. Translation: AAB64557.1.
BK006939 Genomic DNA. Translation: DAA07677.1.
PIRiS50482.
RefSeqiNP_010941.1. NM_001178915.1.

Genome annotation databases

EnsemblFungiiYER024W; YER024W; YER024W.
GeneIDi856745.
KEGGisce:YER024W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18778 Genomic DNA. Translation: AAB64557.1.
BK006939 Genomic DNA. Translation: DAA07677.1.
PIRiS50482.
RefSeqiNP_010941.1. NM_001178915.1.

3D structure databases

ProteinModelPortaliP40017.
SMRiP40017. Positions 15-713.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36758. 10 interactions.
IntActiP40017. 1 interaction.
MINTiMINT-4483798.

Proteomic databases

MaxQBiP40017.
PaxDbiP40017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER024W; YER024W; YER024W.
GeneIDi856745.
KEGGisce:YER024W.

Organism-specific databases

CYGDiYER024w.
EuPathDBiFungiDB:YER024W.
SGDiS000000826. YAT2.

Phylogenomic databases

eggNOGiNOG308143.
HOGENOMiHOG000141908.
InParanoidiP40017.
KOiK00624.
OMAiDILPRNP.
OrthoDBiEOG7TQV84.

Enzyme and pathway databases

BioCyciYEAST:YER024W-MONOMER.

Miscellaneous databases

NextBioi982885.
PROiP40017.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 1 hit.
PfamiPF00755. Carn_acyltransf. 2 hits.
[Graphical view]
PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Carnitine-dependent metabolic activities in Saccharomyces cerevisiae: three carnitine acetyltransferases are essential in a carnitine-dependent strain."
    Swiegers J.H., Dippenaar N., Pretorius I.S., Bauer F.F.
    Yeast 18:585-595(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Carnitine and carnitine acetyltransferases in the yeast Saccharomyces cerevisiae: a role for carnitine in stress protection."
    Franken J., Kroppenstedt S., Swiegers J.H., Bauer F.F.
    Curr. Genet. 53:347-360(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYAT2_YEAST
AccessioniPrimary (citable) accession number: P40017
Secondary accession number(s): D3DLS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 319 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.