ID ARD1_YEAST Reviewed; 238 AA. AC P07347; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 01-MAY-2007, entry version 69. DE N-terminal acetyltransferase A complex catalytic subunit ARD1 DE (EC 2.3.1.88) (NatA complex subunit ARD1) (Arrest-defective protein DE 1). GN Name=ARD1; OrderedLocusNames=YHR013C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86079530; PubMed=3907857; DOI=10.1016/0092-8674(85)90178-3; RA Whiteway M., Szostak J.W.; RT "The ARD1 gene of yeast functions in the switch between the mitotic RT cell cycle and alternative developmental pathways."; RL Cell 43:483-492(1985). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=94378003; PubMed=8091229; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., RA Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., RA Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., RA Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., RA Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., RA Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., RA Vaudin M.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT VIII."; RL Science 265:2077-2082(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP CHARACTERIZATION. RX MEDLINE=90005412; PubMed=2551674; RA Mullen J.R., Kayne P.S., Moerschell R.P., Tsunasawa S., Gribskov M., RA Colavito-Shepanski M., Grunstein M., Sherman F., Sternglanz R.; RT "Identification and characterization of genes and mutants for an N- RT terminal acetyltransferase from yeast."; RL EMBO J. 8:2067-2075(1989). RN [5] RP FUNCTION, INTERACTION WITH NAT1, AND SELF-ASSOCIATION. RX PubMed=1600941; RA Park E.C., Szostak J.W.; RT "ARD1 and NAT1 proteins form a complex that has N-terminal RT acetyltransferase activity."; RL EMBO J. 11:2087-2093(1992). RN [6] RP IDENTIFICATION IN THE NATA COMPLEX. RX PubMed=14517307; DOI=10.1128/MCB.23.20.7403-7414.2003; RA Gautschi M., Just S., Mun A., Ross S., Rucknagel P., Dubaquie Y., RA Ehrenhofer-Murray A., Rospert S.; RT "The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored RT to the ribosome and interacts with nascent polypeptides."; RL Mol. Cell. Biol. 23:7403-7414(2003). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; 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 [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Catalytic component of the NatA N-terminal CC acetyltransferase, which catalyzes acetylation of proteins CC beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a CC role in normal eukaryotic translation and processing, protect CC against proteolytic degradation and protein turnover. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + peptide = CoA + N(alpha)- CC acetylpeptide. CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA) CC complex, which is composed of ARD1, NAT1 and NAT5. Can self- CC associate. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Present with 3310 molecules/cell. CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 CC subfamily. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M11621; AAA66323.1; -; Genomic_DNA. DR EMBL; U10400; AAB68937.1; -; Genomic_DNA. DR EMBL; AY557822; AAS56148.1; -; Genomic_DNA. DR PIR; S46783; TWBYA1. DR DIP; DIP:6788N; -. DR IntAct; P07347; -. DR Ensembl; YHR013C; Saccharomyces cerevisiae. DR GenomeReviews; U00093_GR; YHR013C. DR KEGG; sce:YHR013C; -. DR CYGD; YHR013c; -. DR SGD; S000001055; ARD1. DR BioCyc; SCER-S28-01:SCER-S28-01-002640-MONOMER; -. DR LinkHub; P07347; -. DR GermOnline; YHR013C; Saccharomyces cerevisiae. DR GO; GO:0031415; C:NatA complex; IDA:SGD. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:SGD. DR GO; GO:0000723; P:telomere maintenance; IMP:SGD. DR InterPro; IPR000182; GCN5acetyl_trans. DR Gene3D; G3DSA:3.40.630.30; G3DSA:3.40.630.30; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR PROSITE; PS51186; GNAT; 1. KW Acyltransferase; Complete proteome; Transferase. FT CHAIN 1 238 N-terminal acetyltransferase A complex FT catalytic subunit ARD1. FT /FTId=PRO_0000074529. FT DOMAIN 35 195 N-acetyltransferase. FT CONFLICT 37 37 I -> T (in Ref. 1). SQ SEQUENCE 238 AA; 27603 MW; AEB02BA5012D1137 CRC64; MPINIRRATI NDIICMQNAN LHNLPENYMM KYYMYHILSW PEASFVATTT TLDCEDSDEQ DENDKLELTL DGTNDGRTIK LDPTYLAPGE KLVGYVLVKM NDDPDQQNEP PNGHITSLSV MRTYRRMGIA ENLMRQALFA LREVHQAEYV SLHVRQSNRA ALHLYRDTLA FEVLSIEKSY YQDGEDAYAM KKVLKLEELQ ISNFTHRRLK ENEEKLEDDL ESDLLEDIIK QGVNDIIV //