SSZ1_YEAST
ID SSZ1_YEAST Reviewed; 538 AA.
AC P38788; D3DL13; Q6B1F3; Q6TQT7; Q6TQT8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ribosome-associated complex subunit SSZ1;
DE AltName: Full=DnaK-related protein SSZ1;
DE AltName: Full=Heat shock protein 70 homolog SSZ1;
DE AltName: Full=Pleiotropic drug resistance protein 13;
GN Name=SSZ1; Synonyms=PDR13; OrderedLocusNames=YHR064C;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-72 AND 504-538.
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Kennedy M.C., Dietrich F.S.;
RT "Verification of 3' and 5' ends of S. cerevisiae transcripts.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8962070; DOI=10.1073/pnas.93.25.14440;
RA Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M.,
RA Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.;
RT "Linking genome and proteome by mass spectrometry: large-scale
RT identification of yeast proteins from two dimensional gels.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996).
RN [6]
RP INTERACTION WITH ZUO1.
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 FUNCTION.
RX PubMed=11929993; DOI=10.1073/pnas.062048399;
RA Hundley H., Eisenman H., Walter W., Evans T., Hotokezaka Y., Wiedmann M.,
RA Craig E.A.;
RT "The in vivo function of the ribosome-associated Hsp70, Ssz1, does not
RT require its putative peptide-binding domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4203-4208(2002).
RN [9]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
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, AND MUTAGENESIS OF SER-295.
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 [13]
RP FUNCTION, AND ATP-BINDING.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-480, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-480, AND
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-480, AND
RP IDENTIFICATION BY 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. SSZ1 is required
CC for ZUO1 to function efficiently as a J-protein for SSB1/SSB2. Also
CC involved in pleiotropic drug resistance by post-translational
CC activation of transcription factor PDR1. {ECO:0000269|PubMed:11929993,
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 P38788; P32527: ZUO1; NbExp=9; IntAct=EBI-24570, EBI-29684;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: Neither ATP binding nor ATP hydrolysis is required for SSZ1
CC function.
CC -!- DOMAIN: Does not seem to bind unfolded protein substrates, as its C-
CC terminal putative peptide-binding domain is not required for its
CC function.
CC -!- MISCELLANEOUS: Present with 73600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68391.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAT93146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00061; AAB68391.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY693127; AAT93146.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY389300; AAQ97232.1; -; mRNA.
DR EMBL; AY389301; AAQ97233.1; -; mRNA.
DR EMBL; BK006934; DAA06757.1; -; Genomic_DNA.
DR PIR; S46712; S46712.
DR RefSeq; NP_011931.2; NM_001179194.1.
DR AlphaFoldDB; P38788; -.
DR SMR; P38788; -.
DR BioGRID; 36496; 139.
DR ComplexPortal; CPX-1743; Ribosome-associated complex.
DR DIP; DIP-6305N; -.
DR IntAct; P38788; 63.
DR MINT; P38788; -.
DR STRING; 4932.YHR064C; -.
DR iPTMnet; P38788; -.
DR MaxQB; P38788; -.
DR PaxDb; P38788; -.
DR PRIDE; P38788; -.
DR EnsemblFungi; YHR064C_mRNA; YHR064C; YHR064C.
DR GeneID; 856461; -.
DR KEGG; sce:YHR064C; -.
DR SGD; S000001106; SSZ1.
DR VEuPathDB; FungiDB:YHR064C; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000156380; -.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; P38788; -.
DR OMA; HENTIAF; -.
DR BioCyc; YEAST:G3O-31115-MON; -.
DR PRO; PR:P38788; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38788; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IDA:ComplexPortal.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IC:ComplexPortal.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006450; P:regulation of translational fidelity; IDA:ComplexPortal.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0006452; P:translational frameshifting; IMP:SGD.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..538
FT /note="Ribosome-associated complex subunit SSZ1"
FT /id="PRO_0000078400"
FT REGION 400..538
FT /note="Peptide-binding domain"
FT /evidence="ECO:0000255"
FT REGION 464..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 295
FT /note="S->F: Increases readthrough in translation
FT termination."
FT /evidence="ECO:0000269|PubMed:15456889"
FT CONFLICT 208
FT /note="V -> A (in Ref. 3; AAT93146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 58238 MW; 07B1A409B213E0B4 CRC64;
MSSPVIGITF GNTSSSIAYI NPKNDVDVIA NPDGERAIPS ALSYVGEDEY HGGQALQQLI
RNPKNTIINF RDFIGLPFDK CDVSKCANGA PAVEVDGKVG FVISRGEGKE EKLTVDEVVS
RHLNRLKLAA EDYIGSAVKE AVLTVPTNFS EEQKTALKAS AAKIGLQIVQ FINEPSAALL
AHAEQFPFEK DVNVVVADFG GIRSDAAVIA VRNGIFTILA TAHDLSLGGD NLDTELVEYF
ASEFQKKYQA NPRKNARSLA KLKANSSITK KTLSNATSAT ISIDSLADGF DYHASINRMR
YELVANKVFA QFSSFVDSVI AKAELDPLDI DAVLLTGGVS FTPKLTTNLE YTLPESVEIL
GPQNKNASNN PNELAASGAA LQARLISDYD ADELAEALQP VIVNTPHLKK PIGLIGAKGE
FHPVLLAETS FPVQKKLTLK QAKGDFLIGV YEGDHHIEEK TLEPIPKEEN AEEDDESEWS
DDEPEVVREK LYTLGTKLME LGIKNANGVE IIFNINKDGA LRVTARDLKT GNAVKGEL
