NAT3_YEAST
ID NAT3_YEAST Reviewed; 195 AA.
AC Q06504; D6W4C7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT3;
DE Short=NatB complex subunit NAT3;
DE EC=2.3.1.254 {ECO:0000269|PubMed:10545125};
DE AltName: Full=NatB Nalpha terminal acetyltransferase 3;
GN Name=NAT3 {ECO:0000312|SGD:S000006335}; OrderedLocusNames=YPR131C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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, AND CATALYTIC ACTIVITY.
RX PubMed=10545125; DOI=10.1093/emboj/18.21.6155;
RA Polevoda B., Norbeck J., Takakura H., Blomberg A., Sherman F.;
RT "Identification and specificities of N-terminal acetyltransferases from
RT Saccharomyces cerevisiae.";
RL EMBO J. 18:6155-6168(1999).
RN [4]
RP IDENTIFICATION OF INITIATION SITE, FUNCTION, SUBUNIT, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=12783868; DOI=10.1074/jbc.m304690200;
RA Polevoda B., Cardillo T.S., Doyle T.C., Bedi G.S., Sherman F.;
RT "Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal
RT acetyltransferase and of actin and tropomyosin.";
RL J. Biol. Chem. 278:30686-30697(2003).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=12808144; DOI=10.1073/pnas.1232343100;
RA Singer J.M., Shaw J.M.;
RT "Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and
RT regulate tropomyosin-actin interactions in budding yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7644-7649(2003).
CC -!- FUNCTION: Catalytic subunit of the NatB N-terminal acetyltransferase,
CC which catalyzes acetylation of the amino-terminal methionine residues
CC of all proteins beginning with Met-Asp or Met-Glu and of some proteins
CC beginning with Met-Asn, Met-Gln or Met-Met. NatB acetylates TPM1
CC protein and regulates tropomyocin-actin interactions, it is presumed to
CC N-acetylate 15% of all yeast proteins. {ECO:0000269|PubMed:10545125,
CC ECO:0000269|PubMed:12783868, ECO:0000269|PubMed:12808144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:50484, Rhea:RHEA-COMP:12694, Rhea:RHEA-
CC COMP:12695, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133356, ChEBI:CHEBI:133358; EC=2.3.1.254;
CC Evidence={ECO:0000269|PubMed:10545125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-
CC [protein]; Xref=Rhea:RHEA:50492, Rhea:RHEA-COMP:12698, Rhea:RHEA-
CC COMP:12699, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133361, ChEBI:CHEBI:133362; EC=2.3.1.254;
CC Evidence={ECO:0000269|PubMed:10545125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein];
CC Xref=Rhea:RHEA:50480, Rhea:RHEA-COMP:12692, Rhea:RHEA-COMP:12693,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133045, ChEBI:CHEBI:133063; EC=2.3.1.254;
CC Evidence={ECO:0000269|PubMed:10545125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein];
CC Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133359, ChEBI:CHEBI:133360; EC=2.3.1.254;
CC Evidence={ECO:0000269|PubMed:10545125};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB)
CC complex, which is composed of NAT3 and MDM20.
CC {ECO:0000269|PubMed:12783868}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U40829; AAB68272.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006949; DAA11543.1; -; Genomic_DNA.
DR PIR; S69021; S69021.
DR RefSeq; NP_015456.2; NM_001184228.1.
DR AlphaFoldDB; Q06504; -.
DR SMR; Q06504; -.
DR BioGRID; 36297; 44.
DR ComplexPortal; CPX-782; NatB N-alpha-acetyltransferase complex.
DR IntAct; Q06504; 1.
DR MINT; Q06504; -.
DR STRING; 4932.YPR131C; -.
DR MaxQB; Q06504; -.
DR PaxDb; Q06504; -.
DR PRIDE; Q06504; -.
DR EnsemblFungi; YPR131C_mRNA; YPR131C; YPR131C.
DR GeneID; 856249; -.
DR KEGG; sce:YPR131C; -.
DR SGD; S000006335; NAT3.
DR VEuPathDB; FungiDB:YPR131C; -.
DR eggNOG; KOG3234; Eukaryota.
DR GeneTree; ENSGT00550000075046; -.
DR HOGENOM; CLU_013985_7_1_1; -.
DR InParanoid; Q06504; -.
DR OMA; SGEIMGY; -.
DR BioCyc; YEAST:G3O-34267-MON; -.
DR BRENDA; 2.3.1.254; 984.
DR PRO; PR:Q06504; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06504; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0031416; C:NatB complex; IDA:SGD.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IMP:SGD.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IMP:SGD.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IMP:ComplexPortal.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..195
FT /note="N-terminal acetyltransferase B complex catalytic
FT subunit NAT3"
FT /id="PRO_0000074635"
FT DOMAIN 2..172
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 195 AA; 22921 MW; 093EC599E326D338 CRC64;
MTTIQPFEPV DLFKTNNVNL DILTENFPLE FYFEYMIIWP DLFFKSSEMT VDPTFKHNIS
GYMMAKTEGK TTEWHTHITA VTVAPRFRRI SLASKLCNTL ETMTDVMPHE VNFIDLFVKC
NNQLAIKLYE KLGYSVYRRV VGYYNSAEDG YPDTLKKVDD NKDAFDMRKA MARDRNRSVR
PDGRSHKCYP HDVRF
