NAT1_YEAST
ID NAT1_YEAST Reviewed; 854 AA.
AC P12945; D6VRV5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=N-terminal acetyltransferase A complex subunit NAT1;
DE Short=NatA complex subunit NAT1;
DE AltName: Full=Amino-terminal, alpha-amino, acetyltransferase 1;
GN Name=NAT1; Synonyms=AAA1; OrderedLocusNames=YDL040C; ORFNames=D2720;
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 [MRNA], AND PROTEIN SEQUENCE OF 61-101; 130-142;
RP 151-159; 301-307; 313-327; 331-354; 471-479; 587-596; 598-606; 614-622;
RP 668-683 AND 685-705.
RX PubMed=2663856; DOI=10.1016/s0021-9258(18)63863-3;
RA Lee F.-J.S., Lin L.-W., Smith J.A.;
RT "Molecular cloning and sequencing of a cDNA encoding N alpha-
RT acetyltransferase from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 264:12339-12343(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2551674; DOI=10.1002/j.1460-2075.1989.tb03615.x;
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-terminal
RT acetyltransferase from yeast.";
RL EMBO J. 8:2067-2075(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH ARD1.
RX PubMed=1600941; DOI=10.1002/j.1460-2075.1992.tb05267.x;
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 FUNCTION, AND 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 to
RT the ribosome and interacts with nascent polypeptides.";
RL Mol. Cell. Biol. 23:7403-7414(2003).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Non-catalytic component of the NatA N-terminal
CC acetyltransferase, which catalyzes acetylation of proteins beginning
CC with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal
CC eukaryotic translation and processing, protect against proteolytic
CC degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the
CC ribosome and may present the N termini of nascent polypeptides for
CC acetylation. {ECO:0000269|PubMed:14517307, ECO:0000269|PubMed:1600941}.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)
CC complex, which is composed of ARD1, NAT1 and NAT5. Can self-associate.
CC NAT1 associates with the nascent polypeptide chain and the ribosome.
CC {ECO:0000269|PubMed:14517307}.
CC -!- INTERACTION:
CC P12945; P07347: ARD1; NbExp=10; IntAct=EBI-11868, EBI-2796;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 7600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M23166; AAA88728.1; -; mRNA.
DR EMBL; X15135; CAA33233.1; -; Genomic_DNA.
DR EMBL; Z71781; CAA96449.1; -; Genomic_DNA.
DR EMBL; Z74088; CAA98599.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11815.1; -; Genomic_DNA.
DR PIR; S05783; XYBYT1.
DR RefSeq; NP_010244.1; NM_001180099.1.
DR PDB; 4HNW; X-ray; 2.80 A; A=1-854.
DR PDB; 4HNY; X-ray; 2.25 A; A/C=1-854.
DR PDB; 4XNH; X-ray; 2.10 A; A=1-854.
DR PDB; 4XPD; X-ray; 2.81 A; A=1-854.
DR PDB; 4Y49; X-ray; 3.95 A; A/G/M=1-854.
DR PDB; 6HD5; EM; 4.80 A; t=1-854.
DR PDB; 6HD7; EM; 3.40 A; t=1-854.
DR PDB; 6O07; X-ray; 2.70 A; A=1-854.
DR PDBsum; 4HNW; -.
DR PDBsum; 4HNY; -.
DR PDBsum; 4XNH; -.
DR PDBsum; 4XPD; -.
DR PDBsum; 4Y49; -.
DR PDBsum; 6HD5; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6O07; -.
DR AlphaFoldDB; P12945; -.
DR SMR; P12945; -.
DR BioGRID; 32018; 288.
DR ComplexPortal; CPX-783; NatA N-alpha-acetyltransferase complex.
DR DIP; DIP-6329N; -.
DR IntAct; P12945; 19.
DR MINT; P12945; -.
DR STRING; 4932.YDL040C; -.
DR iPTMnet; P12945; -.
DR MaxQB; P12945; -.
DR PaxDb; P12945; -.
DR PRIDE; P12945; -.
DR EnsemblFungi; YDL040C_mRNA; YDL040C; YDL040C.
DR GeneID; 851521; -.
DR KEGG; sce:YDL040C; -.
DR SGD; S000002198; NAT1.
DR VEuPathDB; FungiDB:YDL040C; -.
DR eggNOG; KOG1156; Eukaryota.
DR GeneTree; ENSGT00950000183174; -.
DR HOGENOM; CLU_006686_1_1_1; -.
DR InParanoid; P12945; -.
DR OMA; WQEDQFD; -.
DR BioCyc; YEAST:YDL040C-MON; -.
DR BRENDA; 2.3.1.255; 984.
DR BRENDA; 2.3.1.258; 984.
DR PRO; PR:P12945; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P12945; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0031415; C:NatA complex; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:SGD.
DR InterPro; IPR021183; NatA_aux_su.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12569; NARP1; 2.
DR PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..854
FT /note="N-terminal acetyltransferase A complex subunit NAT1"
FT /id="PRO_0000096739"
FT REPEAT 20..53
FT /note="TPR 1"
FT REPEAT 54..87
FT /note="TPR 2"
FT REPEAT 91..124
FT /note="TPR 3"
FT REPEAT 126..162
FT /note="TPR 4"
FT REPEAT 241..274
FT /note="TPR 5"
FT REPEAT 384..417
FT /note="TPR 6"
FT REPEAT 452..485
FT /note="TPR 7"
FT REPEAT 728..761
FT /note="TPR 8"
FT REGION 626..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 623..667
FT /evidence="ECO:0000255"
FT COMPBIAS 647..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000255"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 198..216
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:6O07"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6O07"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 322..339
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 356..372
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 380..396
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 452..464
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 468..475
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:4HNY"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 488..493
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 497..523
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 536..570
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 575..582
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 585..595
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 596..600
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 602..621
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 623..625
FT /evidence="ECO:0007829|PDB:6O07"
FT TURN 629..631
FT /evidence="ECO:0007829|PDB:4HNY"
FT HELIX 662..669
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 674..676
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 683..686
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 691..698
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 700..706
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 709..711
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 714..721
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 722..725
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 727..741
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:4HNY"
FT HELIX 746..758
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 763..765
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 767..781
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 782..784
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 787..791
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 797..805
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 806..808
FT /evidence="ECO:0007829|PDB:6O07"
FT HELIX 810..818
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 819..822
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 827..837
FT /evidence="ECO:0007829|PDB:4XNH"
FT TURN 838..840
FT /evidence="ECO:0007829|PDB:4HNY"
FT HELIX 843..852
FT /evidence="ECO:0007829|PDB:4XNH"
SQ SEQUENCE 854 AA; 98905 MW; DCFB870D049F91E6 CRC64;
MSRKRSTKPK PAAKIALKKE NDQFLEALKL YEGKQYKKSL KLLDAILKKD GSHVDSLALK
GLDLYSVGEK DDAASYVANA IRKIEGASAS PICCHVLGIY MRNTKEYKES IKWFTAALNN
GSTNKQIYRD LATLQSQIGD FKNALVSRKK YWEAFLGYRA NWTSLAVAQD VNGERQQAIN
TLSQFEKLAE GKISDSEKYE HSECLMYKND IMYKAASDNQ DKLQNVLKHL NDIEPCVFDK
FGLLERKATI YMKLGQLKDA SIVYRTLIKR NPDNFKYYKL LEVSLGIQGD NKLKKALYGK
LEQFYPRCEP PKFIPLTFLQ DKEELSKKLR EYVLPQLERG VPATFSNVKP LYQRRKSKVS
PLLEKIVLDY LSGLDPTQDP IPFIWTNYYL SQHFLFLKDF PKAQEYIDAA LDHTPTLVEF
YILKARILKH LGLMDTAAGI LEEGRQLDLQ DRFINCKTVK YFLRANNIDK AVEVASLFTK
NDDSVNGIKD LHLVEASWFI VEQAEAYYRL YLDRKKKLDD LASLKKEVES DKSEQIANDI
KENQWLVRKY KGLALKRFNA IPKFYKQFED DQLDFHSYCM RKGTPRAYLE MLEWGKALYT
KPMYVRAMKE ASKLYFQMHD DRLKRKSDSL DENSDEIQNN GQNSSSQKKK AKKEAAAMNK
RKETEAKSVA AYPSDQDNDV FGEKLIETST PMEDFATEFY NNYSMQVRED ERDYILDFEF
NYRIGKLALC FASLNKFAKR FGTTSGLFGS MAIVLLHATR NDTPFDPILK KVVTKSLEKE
YSENFPLNEI SNNSFDWLNF YQEKFGKNDI NGLLFLYRYR DDVPIGSSNL KEMIISSLSP
LEPHSQNEIL QYYL
