ID ZUO1_YEAST Reviewed; 433 AA.
AC P32527; D6VV62;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 27-MAR-2024, entry version 198.
DE RecName: Full=Zuotin;
DE AltName: Full=DnaJ-related protein ZUO1;
DE Short=J protein ZUO1;
DE AltName: Full=Heat shock protein 40 homolog ZUO1;
DE AltName: Full=Ribosome-associated complex subunit ZUO1;
GN Name=ZUO1; OrderedLocusNames=YGR285C;
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 PROTEIN SEQUENCE OF 1-10.
RC STRAIN=20B-12;
RX PubMed=1396572; DOI=10.1002/j.1460-2075.1992.tb05464.x;
RA Zhang S., Lockshin C., Herbert A., Winter E., Rich A.;
RT "Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae.";
RL EMBO J. 11:3787-3796(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 INTERACTION WITH SSZ1.
RX PubMed=11054575; DOI=10.1016/s0378-1119(00)00381-4;
RA Michimoto T., Aoki T., Toh-e A., Kikuchi Y.;
RT "Yeast Pdr13p and Zuo1p molecular chaperones are new functional Hsp70 and
RT Hsp40 partners.";
RL Gene 257:131-137(2000).
RN [7]
RP IDENTIFICATION IN RAC.
RX PubMed=11274393; DOI=10.1073/pnas.071057198;
RA Gautschi M., Lilie H., Fuenfschilling U., Mun A., Ross S., Lithgow T.,
RA Ruecknagel P., Rospert S.;
RT "RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ
RT homologs Ssz1p and zuotin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3762-3767(2001).
RN [8]
RP MUTAGENESIS OF HIS-128.
RX PubMed=11929994; DOI=10.1073/pnas.062048599;
RA Gautschi M., Mun A., Ross S., Rospert S.;
RT "A functional chaperone triad on the yeast ribosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4209-4214(2002).
RN [9]
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 [10]
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 [11]
RP FUNCTION.
RX PubMed=15456889; DOI=10.1128/mcb.24.20.9186-9197.2004;
RA Rakwalska M., Rospert S.;
RT "The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate
RT translation in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 24:9186-9197(2004).
RN [12]
RP FUNCTION.
RX PubMed=15908962; DOI=10.1038/nsmb942;
RA Huang P., Gautschi M., Walter W., Rospert S., Craig E.A.;
RT "The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein
RT Zuo1.";
RL Nat. Struct. Mol. Biol. 12:497-504(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, 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 SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [15]
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, 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).
CC -!- FUNCTION: Component of the ribosome-associated complex (RAC), a
CC heterodimeric chaperone complex involved in regulation of accurate
CC translation termination and in folding or maintaining nascent
CC polypeptides in a folding-competent state. RAC stimulates the ATPase
CC activity of the ribosome-associated pool of Hsp70-type chaperones
CC SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a
CC J-protein for SSB1/SSB2 only when associated with SSZ1.
CC {ECO:0000269|PubMed:15456889, ECO:0000269|PubMed:15908962}.
CC -!- SUBUNIT: RAC is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and
CC the Hsp40/DnaJ-type chaperone ZUO1. RAC associates with ribosomes via
CC ZUO1. {ECO:0000269|PubMed:11274393}.
CC -!- INTERACTION:
CC P32527; P38788: SSZ1; NbExp=9; IntAct=EBI-29684, EBI-24570;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 86400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; X63612; CAA45156.1; -; Genomic_DNA.
DR EMBL; Z73070; CAA97317.1; -; Genomic_DNA.
DR EMBL; AY692823; AAT92842.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08373.1; -; Genomic_DNA.
DR PIR; S25194; S25194.
DR RefSeq; NP_011801.1; NM_001181414.1.
DR PDB; 2LWX; NMR; -; A=348-433.
DR PDB; 5DJE; X-ray; 1.85 A; A/B=166-303.
DR PDB; 7X34; EM; 3.10 A; C=334-433.
DR PDB; 7X3K; EM; 6.00 A; A=1-433.
DR PDBsum; 2LWX; -.
DR PDBsum; 5DJE; -.
DR PDBsum; 7X34; -.
DR PDBsum; 7X3K; -.
DR AlphaFoldDB; P32527; -.
DR EMDB; EMD-32978; -.
DR EMDB; EMD-32991; -.
DR SMR; P32527; -.
DR BioGRID; 33535; 240.
DR ComplexPortal; CPX-1743; Ribosome-associated complex.
DR DIP; DIP-4720N; -.
DR IntAct; P32527; 32.
DR MINT; P32527; -.
DR STRING; 4932.YGR285C; -.
DR MoonProt; P32527; -.
DR iPTMnet; P32527; -.
DR MaxQB; P32527; -.
DR PaxDb; 4932-YGR285C; -.
DR PeptideAtlas; P32527; -.
DR EnsemblFungi; YGR285C_mRNA; YGR285C; YGR285C.
DR GeneID; 853202; -.
DR KEGG; sce:YGR285C; -.
DR AGR; SGD:S000003517; -.
DR SGD; S000003517; ZUO1.
DR VEuPathDB; FungiDB:YGR285C; -.
DR eggNOG; KOG0724; Eukaryota.
DR GeneTree; ENSGT00940000155441; -.
DR HOGENOM; CLU_019916_1_0_1; -.
DR InParanoid; P32527; -.
DR OMA; SNRDHKR; -.
DR OrthoDB; 168809at2759; -.
DR BioCyc; YEAST:G3O-30947-MONOMER; -.
DR BioGRID-ORCS; 853202; 8 hits in 10 CRISPR screens.
DR PRO; PR:P32527; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32527; Protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IMP:SGD.
DR GO; GO:0101031; C:protein folding chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005840; C:ribosome; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IDA:ComplexPortal.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; NAS:ComplexPortal.
DR GO; GO:0006450; P:regulation of translational fidelity; IDA:ComplexPortal.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0006452; P:translational frameshifting; IMP:SGD.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.10.8.840; Ribosome-associated complex head domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR032003; RAC_head.
DR InterPro; IPR042569; RAC_head_sf.
DR InterPro; IPR044634; Zuotin/DnaJC2.
DR PANTHER; PTHR43999; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR PANTHER; PTHR43999:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF16717; RAC_head; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..433
FT /note="Zuotin"
FT /id="PRO_0000071122"
FT DOMAIN 98..170
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 292..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MUTAGEN 128
FT /note="H->Q: Loss of function, but still forms a
FT heterodimer with SSZ1 and associates with ribosomes."
FT /evidence="ECO:0000269|PubMed:11929994"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:5DJE"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5DJE"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:5DJE"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:5DJE"
FT HELIX 249..282
FT /evidence="ECO:0007829|PDB:5DJE"
FT HELIX 284..300
FT /evidence="ECO:0007829|PDB:5DJE"
FT HELIX 335..364
FT /evidence="ECO:0007829|PDB:7X34"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:2LWX"
FT HELIX 374..386
FT /evidence="ECO:0007829|PDB:7X34"
FT HELIX 390..402
FT /evidence="ECO:0007829|PDB:7X34"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:2LWX"
FT HELIX 408..420
FT /evidence="ECO:0007829|PDB:7X34"
FT TURN 426..432
FT /evidence="ECO:0007829|PDB:7X34"
SQ SEQUENCE 433 AA; 49020 MW; 0AA76BC11D3C7DAB CRC64;
MFSLPTLTSD ITVEVNSSAT KTPFVRRPVE PVGKFFLQHA QRTLRNHTWS EFERIEAEKN
VKTVDESNVD PDELLFDTEL ADEDLLTHDA RDWKTADLYA AMGLSKLRFR ATESQIIKAH
RKQVVKYHPD KQSAAGGSLD QDGFFKIIQK AFETLTDSNK RAQYDSCDFV ADVPPPKKGT
DYDFYEAWGP VFEAEARFSK KTPIPSLGNK DSSKKEVEQF YAFWHRFDSW RTFEFLDEDV
PDDSSNRDHK RYIERKNKAA RDKKKTADNA RLVKLVERAV SEDPRIKMFK EEEKKEKERR
KWEREAGARA EAEAKAKAEA EAKAKAESEA KANASAKADK KKAKEAAKAA KKKNKRAIRN
SAKEADYFGD ADKATTIDEQ VGLIVDSLND EELVSTADKI KANAAGAKEV LKESAKTIVD
SGKLPSSLLS YFV
//
