NACA_YEAST
ID NACA_YEAST Reviewed; 174 AA.
AC P38879; D3DLE1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE Short=NAC-alpha;
DE AltName: Full=Alpha-NAC;
DE AltName: Full=GAL4 DNA-binding enhancer protein 2;
GN Name=EGD2; OrderedLocusNames=YHR193C;
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].
RX PubMed=8522175; DOI=10.1016/0378-1119(95)00577-s;
RA Shi X., Parthun M.R., Jaehning J.A.;
RT "The yeast EGD2 gene encodes a homologue of the alpha NAC subunit of the
RT human nascent-polypeptide-associated complex.";
RL Gene 165:199-202(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-19 AND 58-70, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-174.
RX PubMed=8509419; DOI=10.1016/s0021-9258(18)31466-2;
RA Chow C.M., RajBhandary U.L.;
RT "Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene.
RT Isolation by complementation of a mutant Escherichia coli suppressor tRNA
RT defective in aminoacylation and sequence analysis.";
RL J. Biol. Chem. 268:12855-12863(1993).
RN [7]
RP FUNCTION, AND INTERACTION WITH RIBOSOMES.
RX PubMed=9482879; DOI=10.1073/pnas.95.5.2296;
RA George R., Beddoe T., Landl K., Lithgow T.;
RT "The yeast nascent polypeptide-associated complex initiates protein
RT targeting to mitochondria in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2296-2301(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH RIBOSOMES.
RX PubMed=10518932; DOI=10.1016/s0014-5793(99)01118-7;
RA Wiedmann B., Prehn S.;
RT "The nascent polypeptide-associated complex (NAC) of yeast functions in the
RT targeting process of ribosomes to the ER membrane.";
RL FEBS Lett. 458:51-54(1999).
RN [9]
RP FUNCTION, INTERACTION WITH EGD1 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 [10]
RP FUNCTION, AND INTERACTION WITH EGD1; BTT1 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 [11]
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 [12]
RP FUNCTION, AND INTERACTION WITH RIBOSOMES.
RX PubMed=11959135; DOI=10.1016/s0014-5793(02)02528-0;
RA George R., Walsh P., Beddoe T., Lithgow T.;
RT "The nascent polypeptide-associated complex (NAC) promotes interaction of
RT ribosomes with the mitochondrial surface in vivo.";
RL FEBS Lett. 516:213-216(2002).
RN [13]
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 [14]
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 [15]
RP FUNCTION, ASSOCIATION WITH THE CCR4-NOT COMPLEX, INTERACTION WITH EGD2,
RP UBIQUITINATION, AND SUBCELLULAR LOCATION.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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. EGD2 may also be involved in transcription
CC regulation. {ECO:0000269|PubMed:10219998, ECO:0000269|PubMed:10512867,
CC ECO:0000269|PubMed:10518932, ECO:0000269|PubMed:11959135,
CC ECO:0000269|PubMed:16926149, ECO:0000269|PubMed:9482879}.
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 P38879; Q02642: EGD1; NbExp=4; IntAct=EBI-6379, EBI-6371;
CC P38879; P15731: UBC4; NbExp=2; IntAct=EBI-6379, EBI-19735;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic, may also transiently localize to the nucleus. Nuclear
CC import may occur via redundant pathways including one requiring the
CC karyopherins PSE1 and KAP123, which also participate in nuclear import
CC of ribosomal subunits.
CC -!- DOMAIN: The UBA domain is required for the stability of EGD1.
CC -!- PTM: Ubiquitinated by the NOT4 E3 ligase and the UBC4 E2 ubiquitin
CC conjugation enzyme. {ECO:0000269|PubMed:16926149}.
CC -!- MISCELLANEOUS: Present with 38016 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
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DR EMBL; U17134; AAA92080.1; -; Genomic_DNA.
DR EMBL; U00030; AAB68367.1; -; Genomic_DNA.
DR EMBL; AY558288; AAS56614.1; -; Genomic_DNA.
DR EMBL; L12222; AAC15849.1; -; mRNA.
DR EMBL; BK006934; DAA06885.1; -; Genomic_DNA.
DR PIR; S46689; S46689.
DR RefSeq; NP_012063.3; NM_001179324.3.
DR AlphaFoldDB; P38879; -.
DR SMR; P38879; -.
DR BioGRID; 36627; 305.
DR ComplexPortal; CPX-1306; Nascent polypeptide-associated complex, EGD1-EGD2 variant.
DR ComplexPortal; CPX-1307; Nascent polypeptide-associated complex, BTT1-EGD2 variant.
DR DIP; DIP-2098N; -.
DR IntAct; P38879; 52.
DR MINT; P38879; -.
DR STRING; 4932.YHR193C; -.
DR iPTMnet; P38879; -.
DR MaxQB; P38879; -.
DR PaxDb; P38879; -.
DR PRIDE; P38879; -.
DR TopDownProteomics; P38879; -.
DR EnsemblFungi; YHR193C_mRNA; YHR193C; YHR193C.
DR GeneID; 856600; -.
DR KEGG; sce:YHR193C; -.
DR SGD; S000001236; EGD2.
DR VEuPathDB; FungiDB:YHR193C; -.
DR eggNOG; KOG2239; Eukaryota.
DR GeneTree; ENSGT00940000175567; -.
DR HOGENOM; CLU_057806_2_1_1; -.
DR InParanoid; P38879; -.
DR OMA; LVMCQAN; -.
DR BioCyc; YEAST:G3O-31221-MON; -.
DR ChiTaRS; EGD2; yeast.
DR PRO; PR:P38879; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38879; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
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:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IGI:SGD.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR Gene3D; 2.20.70.30; -; 1.
DR InterPro; IPR016641; EGD2/NACA.
DR InterPro; IPR044034; NAC-like_UBA.
DR InterPro; IPR038187; NAC_A/B_dom_sf.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR21713; PTHR21713; 1.
DR Pfam; PF19026; HYPK_UBA; 1.
DR Pfam; PF01849; NAC; 1.
DR PIRSF; PIRSF015901; NAC_alpha; 1.
DR SMART; SM01407; NAC; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT CHAIN 2..174
FT /note="Nascent polypeptide-associated complex subunit
FT alpha"
FT /id="PRO_0000135594"
FT DOMAIN 15..73
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT DOMAIN 135..174
FT /note="UBA"
FT REGION 85..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 174 AA; 18709 MW; 86CE0C4E6194C286 CRC64;
MSAIPENANV TVLNKNEKKA RELIGKLGLK QIPGIIRVTF RKKDNQIYAI EKPEVFRSAG
GNYVVFGEAK VDNFTQKLAA AQQQAQASGI MPSNEDVATK SPEDIQADMQ AAAEGSVNAA
AEEDDEEGEV DAGDLNKDDI ELVVQQTNVS KNQAIKALKA HNGDLVNAIM SLSK
