P80235 (CACM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative mitochondrial carnitine O-acetyltransferase
EC=2.3.1.7

Gene names

Name:	YAT1
Ordered Locus Names:	YAR035W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	687 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the transfer of acetyl-CoA into mitochondria. May also be involved in the metabolism of acetate and of ethanol.
Catalytic activity	Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Induction	By ethanol and by acetate. Repressed by glucose, and to a lesser extent, by galactose. Derepressed by glycerol.
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alcohol metabolic process Inferred from genetic interaction PubMed 11329169. Source: SGD carnitine metabolic process Inferred from mutant phenotype PubMed 11329169. Source: SGD fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 11914276PubMed 14576278PubMed 16823961PubMed 18427809. Source: SGD
Molecular_function	carnitine O-acetyltransferase activity Inferred from sequence or structural similarity PubMed 11329169. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACS1	Q01574	1	EBI-3928,EBI-2128

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 687	687	Putative mitochondrial carnitine O-acetyltransferase		PRO_0000210175
Regions
	Region	446 – 459	14	Coenzyme A binding By similarity
Sites
	Active site	346	1	Proton acceptor By similarity
	Binding site	481	1	Carnitine By similarity
	Binding site	494	1	Carnitine By similarity
Amino acid modifications
	Modified residue	517	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	25	1	P → T in CAA52647. Ref.1
	Sequence conflict	392	1	S → SS in CAA52647. Ref.1
	Sequence conflict	595 – 596	2	SF → AS in CAA52647. Ref.1
	Sequence conflict	653	1	A → T in CAA52647. Ref.1
	Sequence conflict	660	1	T → A in CAA52647. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P80235 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: F00B628893B8BB39	FASTA	687	77,766
	10 20 30 40 50 60 MPNLKRLPIP PLQDTLNRYL ARVEPLQDER QNRRTRRTVL SAENLDALNT LHERLLEYDA 70 80 90 100 110 120 RLAESNPESS YIEQFWYDAY LLYDATVVLN VNPYFQLQDD PTIKDTPETA AQGPYGAHTV 130 140 150 160 170 180 QVRRAARLTT SILKFIRQIR HGTLRTDTVR GKTPLSMDQY ERLFGSSRIP PGPGEPSCHL 190 200 210 220 230 240 QTDATSHHVV AMYRGQFYWF DVLDTRNEPI FATPEQLEWN LYSIIMDAES AGSGSAPFGV 250 260 270 280 290 300 FTTESRRVWS NIRDYLFHAD DCTNWRNLKL IDSALFVVCL DDVAFAADQQ DELTRSMLCG 310 320 330 340 350 360 TSTINLDPHQ HQPPLNVQTG TCLNRWYDKL QLIVTKNGKA GINFEHTGVD GHTVLRLATD 370 380 390 400 410 420 IYTDSILSFA RGVTKNVVDI FSDDDGKPSS SSLASAAHSA NLITIPRKLE WRTDNFLQSS 430 440 450 460 470 480 LHFAETRISD LISQYEFVNL DFSNYGASHI KTVFKCSPDA FVQQVFQVAY FALYGRFETV 490 500 510 520 530 540 YEPAMTKAFQ NGRTEAIRSV TGQSKLFVKS LLDQDASDAT KIQLLHDACT AHSQITRECS 550 560 570 580 590 600 QGLGQDRHLY ALYCLWNQWY KDKLELPPIF RDKSWTTMQN NVLSTSNCGN PCLKSFGFGP 610 620 630 640 650 660 VTANGFGIGY IIRDHSVSVV VSSRHRQTAR FASLMEKSLL EIDRIFKRQQ ARAAKPAART 670 680 TASANTKSED MKYLLSGYDY FDVSVSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ethanol-inducible YAT1 gene from yeast encodes a presumptive mitochondrial outer carnitine acetyltransferase." Schmalix W.A., Bandlow W. J. Biol. Chem. 268:27428-27439(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DL-1.
[2]	"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52 Kbp CDC15-FLO1-PHO11-YAR074 region." Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B., Kaback D.B., Clark M.W. Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase." Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C. Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74553 Genomic DNA. Translation: CAA52647.1. L28920 Genomic DNA. Translation: AAC09495.1. BK006935 Genomic DNA. Translation: DAA07004.1.
PIR	S53485.
RefSeq	NP_009420.1. NM_001178226.1.
3D structure databases
ProteinModelPortal	P80235.
SMR	P80235. Positions 3-655.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3795N.
IntAct	P80235. 9 interactions.
MINT	MINT-541328.
STRING	4932.YAR035W.
Proteomic databases
PaxDb	P80235.
PeptideAtlas	P80235.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YAR035W; YAR035W; YAR035W.
GeneID	851285.
KEGG	sce:YAR035W.
Organism-specific databases
CYGD	YAR035w.
SGD	S000000080. YAT1.
Phylogenomic databases
eggNOG	NOG70127.
GeneTree	ENSGT00550000074786.
HOGENOM	HOG000206461.
KO	K00624.
OMA	YNDQLTR.
OrthoDB	EOG4B01XJ.
Enzyme and pathway databases
BioCyc	YEAST:YAR035W-MONOMER.
Gene expression databases
Genevestigator	P80235.
GermOnline	YAR035W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000542. Carn_acyl_trans. [Graphical view]
PANTHER	PTHR22589. PTHR22589. 1 hit.
Pfam	PF00755. Carn_acyltransf. 1 hit. [Graphical view]
PROSITE	PS00439. ACYLTRANSF_C_1. 1 hit. PS00440. ACYLTRANSF_C_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968285.

Entry information

Entry name

CACM_YEAST

Accession

Primary (citable) accession number: P80235
Secondary accession number(s): D6VPN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	December 6, 2005
Last modified:	May 29, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program