NACB2_YEAST
ID NACB2_YEAST Reviewed; 149 AA.
AC P40314; D6VSN2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Nascent polypeptide-associated complex subunit beta-2;
DE Short=NAC-beta-2;
DE AltName: Full=BTF3 homolog BTT1;
DE AltName: Full=Beta-2-NAC;
GN Name=BTT1; OrderedLocusNames=YDR252W; ORFNames=YD9320A.02;
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].
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 [2]
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 [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 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 [6]
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 [7]
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).
CC -!- FUNCTION: Acts as component of the nascent polypeptide-associated
CC complex (NAC), which promotes mitochondrial protein import by enhancing
CC productive ribosome interactions with the outer mitochondrial membrane.
CC Also blocks the inappropriate interaction of ribosomes translating non-
CC secretory nascent polypeptides with translocation sites in the membrane
CC of the endoplasmic reticulum. BTT1 may act as a transcription factor
CC that exert a negative effect on the expression of several genes that
CC are transcribed by RNA polymerase II. {ECO:0000269|PubMed:10219998}.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic, may also transiently localize to the
CC nucleus. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAC-beta family. {ECO:0000305}.
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DR EMBL; X78724; CAA55370.1; -; Genomic_DNA.
DR EMBL; Z70202; CAA94091.1; -; Genomic_DNA.
DR EMBL; Z68329; CAA92709.1; -; Genomic_DNA.
DR EMBL; AY557726; AAS56052.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12092.1; -; Genomic_DNA.
DR PIR; S47574; S47574.
DR RefSeq; NP_010538.1; NM_001180560.1.
DR AlphaFoldDB; P40314; -.
DR SMR; P40314; -.
DR BioGRID; 32302; 88.
DR ComplexPortal; CPX-1307; Nascent polypeptide-associated complex, BTT1-EGD2 variant.
DR DIP; DIP-2099N; -.
DR IntAct; P40314; 2.
DR MINT; P40314; -.
DR STRING; 4932.YDR252W; -.
DR iPTMnet; P40314; -.
DR MaxQB; P40314; -.
DR PaxDb; P40314; -.
DR PRIDE; P40314; -.
DR EnsemblFungi; YDR252W_mRNA; YDR252W; YDR252W.
DR GeneID; 851839; -.
DR KEGG; sce:YDR252W; -.
DR SGD; S000002660; BTT1.
DR VEuPathDB; FungiDB:YDR252W; -.
DR eggNOG; KOG2240; Eukaryota.
DR GeneTree; ENSGT00940000176500; -.
DR HOGENOM; CLU_098726_2_2_1; -.
DR InParanoid; P40314; -.
DR OMA; GDNKAPM; -.
DR BioCyc; YEAST:G3O-29824-MON; -.
DR PRO; PR:P40314; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P40314; protein.
DR GO; GO:0030015; C:CCR4-NOT core complex; IPI:SGD.
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: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; Nucleus; Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..149
FT /note="Nascent polypeptide-associated complex subunit beta-
FT 2"
FT /id="PRO_0000213551"
FT DOMAIN 38..103
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
SQ SEQUENCE 149 AA; 16620 MW; 5EED697F1E728D09 CRC64;
MPVDQEKLAK LHKLSAANKV GGTRRKINKK GNLYNNNDKD NTKLQAELHK LHPMTIENVA
EANFFKKNGK VLHFNSAVVQ IAPQCNLTMI HGQPKENTLN GLYPSVASQL GSQELEYLTG
LAHNLENEQT VLDQLGDRCS ETKQQVMNS
