Reviewed, UniProtKB/Swiss-Prot P12945 (NAT1_YEAST)

Names and origin

Protein names

Recommended name:
    N-terminal acetyltransferase A complex subunit NAT1
      Short name=NatA complex subunit NAT1
Alternative name(s):
    Amino-terminal, alpha-amino, acetyltransferase 1

Gene names

Name:	NAT1
Synonyms:	AAA1
Ordered Locus Names:	YDL040C
ORF Names:	D2720

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	854 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the ribosome and may present the N termini of nascent polypeptides for acetylation. Ref.4 Ref.5
Subunit structure	Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5. Can self-associate. NAT1 associates with the nascent polypeptide chain and the ribosome.
Subcellular location	Cytoplasm.
Post-translational modification	The N-terminus is blocked.
Miscellaneous	Present with 7600 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Contains 8 TPR repeats.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Coiled coil Repeat TPR repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	N-terminal protein amino acid acetylation Ref.2 Inferred from direct assay. Source: SGD
Cellular component	NatA complex Ref.5 Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	protein binding Ref.4 Ref.5 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARD1	P07347	2	EBI-11868,EBI-2796
MDH1	P17505	1	EBI-11868,EBI-10594
MFAL1	P01149	1	EBI-11868,EBI-10827
RPL4A	P10664	1	EBI-11868,EBI-15390

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable
	Chain	2 – 854	853	N-terminal acetyltransferase A complex subunit NAT1		PRO_0000096739
Regions
	Repeat	20 – 53	34	TPR 1
	Repeat	54 – 87	34	TPR 2
	Repeat	91 – 124	34	TPR 3
	Repeat	126 – 162	37	TPR 4
	Repeat	241 – 274	34	TPR 5
	Repeat	384 – 417	34	TPR 6
	Repeat	452 – 485	34	TPR 7
	Repeat	728 – 761	34	TPR 8
	Coiled coil	623 – 667	45	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Potential
	Modified residue	674	1	Phosphoserine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P12945-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: DCFB870D049F91E6	FASTA	854	98,905
	10 20 30 40 50 60 MSRKRSTKPK PAAKIALKKE NDQFLEALKL YEGKQYKKSL KLLDAILKKD GSHVDSLALK 70 80 90 100 110 120 GLDLYSVGEK DDAASYVANA IRKIEGASAS PICCHVLGIY MRNTKEYKES IKWFTAALNN 130 140 150 160 170 180 GSTNKQIYRD LATLQSQIGD FKNALVSRKK YWEAFLGYRA NWTSLAVAQD VNGERQQAIN 190 200 210 220 230 240 TLSQFEKLAE GKISDSEKYE HSECLMYKND IMYKAASDNQ DKLQNVLKHL NDIEPCVFDK 250 260 270 280 290 300 FGLLERKATI YMKLGQLKDA SIVYRTLIKR NPDNFKYYKL LEVSLGIQGD NKLKKALYGK 310 320 330 340 350 360 LEQFYPRCEP PKFIPLTFLQ DKEELSKKLR EYVLPQLERG VPATFSNVKP LYQRRKSKVS 370 380 390 400 410 420 PLLEKIVLDY LSGLDPTQDP IPFIWTNYYL SQHFLFLKDF PKAQEYIDAA LDHTPTLVEF 430 440 450 460 470 480 YILKARILKH LGLMDTAAGI LEEGRQLDLQ DRFINCKTVK YFLRANNIDK AVEVASLFTK 490 500 510 520 530 540 NDDSVNGIKD LHLVEASWFI VEQAEAYYRL YLDRKKKLDD LASLKKEVES DKSEQIANDI 550 560 570 580 590 600 KENQWLVRKY KGLALKRFNA IPKFYKQFED DQLDFHSYCM RKGTPRAYLE MLEWGKALYT 610 620 630 640 650 660 KPMYVRAMKE ASKLYFQMHD DRLKRKSDSL DENSDEIQNN GQNSSSQKKK AKKEAAAMNK 670 680 690 700 710 720 RKETEAKSVA AYPSDQDNDV FGEKLIETST PMEDFATEFY NNYSMQVRED ERDYILDFEF 730 740 750 760 770 780 NYRIGKLALC FASLNKFAKR FGTTSGLFGS MAIVLLHATR NDTPFDPILK KVVTKSLEKE 790 800 810 820 830 840 YSENFPLNEI SNNSFDWLNF YQEKFGKNDI NGLLFLYRYR DDVPIGSSNL KEMIISSLSP 850 LEPHSQNEIL QYYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequencing of a cDNA encoding N alpha-acetyltransferase from Saccharomyces cerevisiae." Lee F.-J.S., Lin L.-W., Smith J.A. J. Biol. Chem. 264:12339-12343(1989) [PubMed: 2663856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-101; 130-142; 151-159; 301-307; 313-327; 331-354; 471-479; 587-596; 598-606; 614-622; 668-683 AND 685-705.
[2]	"Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast." Mullen J.R., Kayne P.S., Moerschell R.P., Tsunasawa S., Gribskov M., Colavito-Shepanski M., Grunstein M., Sherman F., Sternglanz R. EMBO J. 8:2067-2075(1989) [PubMed: 2551674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity." Park E.C., Szostak J.W. EMBO J. 11:2087-2093(1992) [PubMed: 1600941] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARD1.
[5]	"The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides." Gautschi M., Just S., Mun A., Ross S., Rucknagel P., Dubaquie Y., Ehrenhofer-Murray A., Rospert S. Mol. Cell. Biol. 23:7403-7414(2003) [PubMed: 14517307] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NATA COMPLEX.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M23166 mRNA. Translation: AAA88728.1. X15135 Genomic DNA. Translation: CAA33233.1. Z71781 Genomic DNA. Translation: CAA96449.1. Z74088 Genomic DNA. Translation: CAA98599.1.
PIR	XYBYT1. S05783.
RefSeq	NP_010244.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6329N.
IntAct	P12945. 20 interactions.
STRING	P12945.
Proteomic databases
PeptideAtlas	P12945.
PRIDE	P12945.
Genome annotation databases
Ensembl	YDL040C; YDL040C; YDL040C; Saccharomyces cerevisiae. [Genome view]
GeneID	851521.
KEGG	sce:YDL040C.
NMPDR	fig|4932.3.peg.984.
Organism-specific databases
CYGD	YDL040c.
SGD	S000002198. NAT1.
Phylogenomic databases
HOGENOM	P12945.
OMA	ASWFIVE
OrthoDB	EOG9WQ2JZ
Gene expression databases
ArrayExpress	P12945.
Genevestigator	P12945.
GermOnline	YDL040C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011990. TPR-like_helical. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 2 hits.
PROSITE	PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968899.

Entry information

Entry name

NAT1_YEAST

Accession

Primary (citable) accession number: P12945

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)