NACB1_YEAST
ID NACB1_YEAST Reviewed; 157 AA.
AC Q02642; D6W3X7; Q02107;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Nascent polypeptide-associated complex subunit beta-1;
DE Short=NAC-beta-1;
DE AltName: Full=BTF3 homolog EGD1;
DE AltName: Full=Beta-1-NAC;
DE AltName: Full=GAL4 DNA-binding enhancer protein 1;
GN Name=EGD1; OrderedLocusNames=YPL037C;
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 [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=YJJ160;
RX PubMed=1448098; DOI=10.1128/mcb.12.12.5683-5689.1992;
RA Parthun M.R., Mangus D.A., Jaehning J.A.;
RT "The EGD1 product, a yeast homolog of human BTF3, may be involved in GAL4
RT DNA binding.";
RL Mol. Cell. Biol. 12:5683-5689(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=8052529; DOI=10.1093/nar/22.14.2740;
RA Hu G.-Z., Ronne H.;
RT "Yeast BTF3 protein is encoded by duplicated genes and inhibits the
RT expression of some genes in vivo.";
RL Nucleic Acids Res. 22:2740-2743(1994).
RN [3]
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 [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 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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=2904437; DOI=10.1016/s0021-9258(19)77659-5;
RA Schlesser A., Ulaszewski S., Ghislain M., Goffeau A.;
RT "A second transport ATPase gene in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 263:19480-19487(1988).
RN [7]
RP FUNCTION, INTERACTION WITH EGD2 AND RIBOSOMES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10512867; DOI=10.1091/mbc.10.10.3289;
RA Fuenfschilling U., Rospert S.;
RT "Nascent polypeptide-associated complex stimulates protein import into
RT yeast mitochondria.";
RL Mol. Biol. Cell 10:3289-3299(1999).
RN [8]
RP FUNCTION, AND INTERACTION WITH EGD2 AND RIBOSOMES.
RX PubMed=10219998;
RX DOI=10.1002/(sici)1097-0061(19990330)15:5<397::aid-yea384>3.0.co;2-u;
RA Reimann B., Bradsher J., Franke J., Hartmann E., Wiedmann M., Prehn S.,
RA Wiedmann B.;
RT "Initial characterization of the nascent polypeptide-associated complex in
RT yeast.";
RL Yeast 15:397-407(1999).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11683391; DOI=10.1242/jcs.114.14.2641;
RA Franke J., Reimann B., Hartmann E., Koehler M., Wiedmann B.;
RT "Evidence for a nuclear passage of nascent polypeptide-associated complex
RT subunits in yeast.";
RL J. Cell Sci. 114:2641-2648(2001).
RN [10]
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 [11]
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 [12]
RP FUNCTION, ASSOCIATION WITH THE CCR4-NOT COMPLEX, INTERACTION WITH EGD1,
RP UBIQUITINATION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=16926149; DOI=10.1074/jbc.m604986200;
RA Panasenko O., Landrieux E., Feuermann M., Finka A., Paquet N.,
RA Collart M.A.;
RT "The yeast Ccr4-Not complex controls ubiquitination of the nascent-
RT associated polypeptide (NAC-EGD) complex.";
RL J. Biol. Chem. 281:31389-31398(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, 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).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the nascent polypeptide-associated complex
CC (NAC), a dynamic component of the ribosomal exit tunnel, protecting the
CC emerging polypeptides from interaction with other cytoplasmic proteins
CC to ensure appropriate nascent protein targeting. The NAC complex also
CC promotes mitochondrial protein import by enhancing productive ribosome
CC interactions with the outer mitochondrial membrane and blocks the
CC inappropriate interaction of ribosomes translating non-secretory
CC nascent polypeptides with translocation sites in the membrane of the
CC endoplasmic reticulum EGD1 may act as a transcription factor that exert
CC a negative effect on the expression of several genes that are
CC transcribed by RNA polymerase II. Can enhance DNA binding of the GAL4
CC protein activator. {ECO:0000269|PubMed:10219998,
CC ECO:0000269|PubMed:10512867, ECO:0000269|PubMed:16926149}.
CC -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC consisting of EGD2 and either EGD1 or BTT1. NAC associates with
CC ribosomes via EGD1 or BTT1, and with the CCR4-NOT complex.
CC -!- INTERACTION:
CC Q02642; P38879: EGD2; NbExp=4; IntAct=EBI-6371, EBI-6379;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic, may also transiently localize to the nucleus.
CC -!- PTM: Ubiquitinated by the NOT4 E3 ligase and the UBC4 E2 ubiquitin
CC conjugation enzyme. {ECO:0000269|PubMed:16926149}.
CC -!- MISCELLANEOUS: Present with 18000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAC-beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB24290.1; Type=Frameshift; Evidence={ECO:0000305};
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; L05185; AAB63973.1; ALT_FRAME; Genomic_DNA.
DR EMBL; S49596; AAB24290.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X78725; CAA55371.1; -; Genomic_DNA.
DR EMBL; U44030; AAB68183.1; -; Genomic_DNA.
DR EMBL; AY558440; AAS56766.1; -; Genomic_DNA.
DR EMBL; J04421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006949; DAA11393.1; -; Genomic_DNA.
DR PIR; S47575; S47575.
DR RefSeq; NP_015288.1; NM_001183851.1.
DR AlphaFoldDB; Q02642; -.
DR SMR; Q02642; -.
DR BioGRID; 36142; 192.
DR ComplexPortal; CPX-1306; Nascent polypeptide-associated complex, EGD1-EGD2 variant.
DR DIP; DIP-6561N; -.
DR IntAct; Q02642; 16.
DR MINT; Q02642; -.
DR STRING; 4932.YPL037C; -.
DR iPTMnet; Q02642; -.
DR MaxQB; Q02642; -.
DR PaxDb; Q02642; -.
DR PRIDE; Q02642; -.
DR TopDownProteomics; Q02642; -.
DR EnsemblFungi; YPL037C_mRNA; YPL037C; YPL037C.
DR GeneID; 856070; -.
DR KEGG; sce:YPL037C; -.
DR SGD; S000005958; EGD1.
DR VEuPathDB; FungiDB:YPL037C; -.
DR eggNOG; KOG2240; Eukaryota.
DR GeneTree; ENSGT00940000176500; -.
DR HOGENOM; CLU_098726_2_2_1; -.
DR InParanoid; Q02642; -.
DR OMA; HFKNPRV; -.
DR BioCyc; YEAST:G3O-33951-MON; -.
DR PRO; PR:Q02642; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02642; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042788; C:polysomal ribosome; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IC:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IGI:SGD.
DR Gene3D; 2.20.70.30; -; 1.
DR InterPro; IPR039370; BTF3.
DR InterPro; IPR038187; NAC_A/B_dom_sf.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR PANTHER; PTHR10351; PTHR10351; 1.
DR Pfam; PF01849; NAC; 1.
DR SMART; SM01407; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..157
FT /note="Nascent polypeptide-associated complex subunit beta-
FT 1"
FT /id="PRO_0000213552"
FT DOMAIN 38..103
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT REGION 19..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 157 AA; 17020 MW; 7C278A3DC79BF95B CRC64;
MPIDQEKLAK LQKLSANNKV GGTRRKLNKK AGSSAGANKD DTKLQSQLAK LHAVTIDNVA
EANFFKDDGK VMHFNKVGVQ VAAQHNTSVF YGLPQEKNLQ DLFPGIISQL GPEAIQALSQ
LAAQMEKHEA KAPADAEKKD EAIPELVEGQ TFDADVE
