Reviewed, UniProtKB/Swiss-Prot Q06504 (NAT3_YEAST)

Names and origin

Protein names

Recommended name:
    N-terminal acetyltransferase B complex catalytic subunit NAT3
      Short name=NatB complex subunit NAT3
    EC=2.3.1.88
Alternative name(s):
    NatB Nalpha terminal acetyltransferase 3

Gene names

Name:	NAT3
Ordered Locus Names:	YPR131C

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	195 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalytic subunit of the NatB N-terminal acetyltransferase, which catalyzes acetylation of the amino-terminal methionine residues of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn or Met-Met. NatB acetylates TPM1 protein and regulates tropomyocin-actin interactions. Ref.2 Ref.3 Ref.6
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.
Subunit structure	Component of the N-terminal acetyltransferase B (NatB) complex, which is composed of NAT3 and MDM20. Ref.3
Subcellular location	Cytoplasm. Ref.4
Miscellaneous	Present with 639 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the acetyltransferase family. GNAT subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	N-terminal peptidyl-methionine acetylation Ref.2 Inferred from mutant phenotype. Source: SGD cytoskeleton organization Ref.6 Inferred from genetic interaction. Source: SGD mitochondrion inheritance Ref.6 Inferred from genetic interaction. Source: SGD
Cellular component	NatB complex Traceable author statement. Source: SGD
Molecular function	peptide alpha-N-acetyltransferase activity Ref.2 Inferred from mutant phenotype. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RPT3	P33298	1	EBI-31002,EBI-13905

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 195	195	N-terminal acetyltransferase B complex catalytic subunit NAT3		PRO_0000074635
Regions
	Domain	2 – 172	171	N-acetyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q06504-1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 093EC599E326D338	FASTA	195	22,921
	10 20 30 40 50 60 MTTIQPFEPV DLFKTNNVNL DILTENFPLE FYFEYMIIWP DLFFKSSEMT VDPTFKHNIS 70 80 90 100 110 120 GYMMAKTEGK TTEWHTHITA VTVAPRFRRI SLASKLCNTL ETMTDVMPHE VNFIDLFVKC 130 140 150 160 170 180 NNQLAIKLYE KLGYSVYRRV VGYYNSAEDG YPDTLKKVDD NKDAFDMRKA MARDRNRSVR 190 PDGRSHKCYP HDVRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae." Polevoda B., Norbeck J., Takakura H., Blomberg A., Sherman F. EMBO J. 18:6155-6168(1999) [PubMed: 10545125] [Abstract] Cited for: FUNCTION.
[3]	"Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin." Polevoda B., Cardillo T.S., Doyle T.C., Bedi G.S., Sherman F. J. Biol. Chem. 278:30686-30697(2003) [PubMed: 12783868] [Abstract] Cited for: IDENTIFICATION OF INITIATION SITE, FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
[4]	"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].
[5]	"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].
[6]	"Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin-actin interactions in budding yeast." Singer J.M., Shaw J.M. Proc. Natl. Acad. Sci. U.S.A. 100:7644-7649(2003) [PubMed: 12808144] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U40829 Genomic DNA. Translation: AAB68272.1. Different initiation.
PIR	S69021.
RefSeq	NP_015456.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06504. 3 interactions.
STRING	Q06504.
Proteomic databases
PeptideAtlas	Q06504.
Genome annotation databases
Ensembl	YPR131C; YPR131C; YPR131C; Saccharomyces cerevisiae. [Genome view]
GeneID	856249.
GenomeReviews	Gene locus YPR131C in contig U00094_GR.
KEGG	sce:YPR131C.
NMPDR	fig|4932.3.peg.6593.
Organism-specific databases
CYGD	YPR131c.
SGD	S000006335. NAT3.
Phylogenomic databases
HOGENOM	Q06504.
OMA	MTTLRPF.
Enzyme and pathway databases
BRENDA	2.3.1.88. 250.
Gene expression databases
ArrayExpress	Q06504.
Genevestigator	Q06504.
GermOnline	YPR131C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GCN5-rel_AcTrfase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	981522.

Entry information

Entry name

NAT3_YEAST

Accession

Primary (citable) accession number: Q06504

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	November 3, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)