CNS1_YEAST
ID CNS1_YEAST Reviewed; 385 AA.
AC P33313; D6VQF0; Q02125;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Hsp70/Hsp90 co-chaperone CNS1;
DE AltName: Full=Cyclophilin seven suppressor 1;
DE AltName: Full=STI1 stress-inducible protein homolog;
GN Name=CNS1; OrderedLocusNames=YBR155W; ORFNames=YBR1205;
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 204508 / S288c;
RX PubMed=8488729; DOI=10.1002/yea.320090308;
RA Baur A., Schaaff-Gerstenschlaeger I., Boles E., Miosga T., Rose M.,
RA Zimmermann F.K.;
RT "Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae chromosome II
RT including three essential open reading frames.";
RL Yeast 9:289-293(1993).
RN [2]
RP ERRATUM OF PUBMED:8488729.
RX PubMed=8203148; DOI=10.1002/yea.320100113;
RA Baur A., Schaaff-Gerstenschlaeger I., Boles E., Miosga T., Rose M.,
RA Zimmermann F.K.;
RL Yeast 10:131-131(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 CHARACTERIZATION, INTERACTION WITH CPR7 AND HSC82, AND INDUCTION.
RX PubMed=9819421; DOI=10.1128/mcb.18.12.7344;
RA Dolinski K.J., Cardenas M.E., Heitman J.;
RT "CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae
RT that suppresses cyclophilin 40 mutations and interacts with Hsp90.";
RL Mol. Cell. Biol. 18:7344-7352(1998).
RN [7]
RP CHARACTERIZATION, AND INTERACTION WITH HSP82.
RX PubMed=9819422; DOI=10.1128/mcb.18.12.7353;
RA Marsh J.A., Kalton H.M., Gaber R.F.;
RT "Cns1 is an essential protein associated with the hsp90 chaperone complex
RT in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent
RT functions in cpr7Delta cells.";
RL Mol. Cell. Biol. 18:7353-7359(1998).
RN [8]
RP FUNCTION, SUBUNIT, INTERACTION WITH HSP82, AND MUTAGENESIS OF GLY-90;
RP CYS-140; ASP-260; GLU-324 AND LEU-330.
RX PubMed=12788914; DOI=10.1074/jbc.m304315200;
RA Tesic M., Marsh J.A., Cullinan S.B., Gaber R.F.;
RT "Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7
RT in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:32692-32701(2003).
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, SUBUNIT, AND INTERACTION WITH HSP82 AND SSA1.
RX PubMed=15044454; DOI=10.1074/jbc.m402189200;
RA Hainzl O., Wegele H., Richter K., Buchner J.;
RT "Cns1 is an activator of the Ssa1 ATPase activity.";
RL J. Biol. Chem. 279:23267-23273(2004).
CC -!- FUNCTION: Co-chaperone that binds to the molecular chaperones Hsp90
CC (HSC82 and HSP82) and Hsp70 (SSA1). Stimulates SSA1 ATPase activity,
CC but not Hsp90 ATPase activity. Involved in only a subset of Hsp90
CC functions. {ECO:0000269|PubMed:12788914, ECO:0000269|PubMed:15044454}.
CC -!- SUBUNIT: Monomer. Component of Hsp70 and Hsp90 chaperone complexes.
CC Interacts (via TPR repeats) with HSC82 and HSP82 (via C-terminal MEEVD
CC pentapeptide). Interacts with CPR7, SSA1 and SPI1.
CC {ECO:0000269|PubMed:12788914, ECO:0000269|PubMed:15044454,
CC ECO:0000269|PubMed:9819421, ECO:0000269|PubMed:9819422}.
CC -!- INTERACTION:
CC P33313; P47103: CPR7; NbExp=2; IntAct=EBI-4806, EBI-5436;
CC P33313; P15108: HSC82; NbExp=2; IntAct=EBI-4806, EBI-8666;
CC P33313; P02829: HSP82; NbExp=6; IntAct=EBI-4806, EBI-8659;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Not induced by heat shock. {ECO:0000269|PubMed:9819421}.
CC -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TTC4 family. {ECO:0000305}.
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DR EMBL; X71329; CAA50473.1; -; Genomic_DNA.
DR EMBL; Z36024; CAA85114.1; -; Genomic_DNA.
DR EMBL; S59774; AAC60555.2; -; Genomic_DNA.
DR EMBL; AY557873; AAS56199.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07270.1; -; Genomic_DNA.
DR PIR; S40699; S40699.
DR RefSeq; NP_009713.1; NM_001178503.1.
DR PDB; 6HFM; X-ray; 1.55 A; A/B=221-385.
DR PDB; 6HFT; X-ray; 2.80 A; A=70-385.
DR PDBsum; 6HFM; -.
DR PDBsum; 6HFT; -.
DR AlphaFoldDB; P33313; -.
DR SMR; P33313; -.
DR BioGRID; 32854; 42.
DR DIP; DIP-1271N; -.
DR IntAct; P33313; 15.
DR MINT; P33313; -.
DR STRING; 4932.YBR155W; -.
DR MaxQB; P33313; -.
DR PaxDb; P33313; -.
DR PRIDE; P33313; -.
DR EnsemblFungi; YBR155W_mRNA; YBR155W; YBR155W.
DR GeneID; 852452; -.
DR KEGG; sce:YBR155W; -.
DR SGD; S000000359; CNS1.
DR VEuPathDB; FungiDB:YBR155W; -.
DR eggNOG; KOG0551; Eukaryota.
DR HOGENOM; CLU_040446_0_0_1; -.
DR InParanoid; P33313; -.
DR OMA; HPMFEGL; -.
DR BioCyc; YEAST:G3O-29105-MON; -.
DR PRO; PR:P33313; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P33313; protein.
DR GO; GO:0005737; C:cytoplasm; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:SGD.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IPI:SGD.
DR GO; GO:0042026; P:protein refolding; IGI:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR044059; Csn1/TTC4_wheel.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF18972; Wheel; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..385
FT /note="Hsp70/Hsp90 co-chaperone CNS1"
FT /id="PRO_0000106279"
FT REPEAT 83..116
FT /note="TPR 1"
FT REPEAT 121..154
FT /note="TPR 2"
FT REPEAT 155..189
FT /note="TPR 3"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 90
FT /note="G->D: In CNS1-1; disrupts interaction with Hsp90,
FT temperature-sensitive defect impairing Hsp90-dependent
FT function."
FT /evidence="ECO:0000269|PubMed:12788914"
FT MUTAGEN 140
FT /note="C->R: In CNS1-2; disrupts interaction with Hsp90,
FT temperature-sensitive defect impairing Hsp90-dependent
FT function."
FT /evidence="ECO:0000269|PubMed:12788914"
FT MUTAGEN 260
FT /note="D->G: In CNS1-3; temperature-sensitive defect
FT impairing Hsp90-dependent function; when associated with G-
FT 324 and S-330."
FT /evidence="ECO:0000269|PubMed:12788914"
FT MUTAGEN 324
FT /note="E->G: In CNS1-3; temperature-sensitive defect
FT impairing Hsp90-dependent function; when associated with G-
FT 260 and S-330."
FT /evidence="ECO:0000269|PubMed:12788914"
FT MUTAGEN 330
FT /note="L->S: In CNS1-3; temperature-sensitive defect
FT impairing Hsp90-dependent function; when associated with G-
FT 260 and G-324."
FT /evidence="ECO:0000269|PubMed:12788914"
FT CONFLICT 6..13
FT /note="ANGGYTKP -> RQMEDIPNQ (in Ref. 1; AAC60555)"
FT /evidence="ECO:0000305"
FT HELIX 79..96
FT /evidence="ECO:0007829|PDB:6HFT"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:6HFT"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:6HFT"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:6HFT"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:6HFT"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:6HFT"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6HFM"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:6HFM"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:6HFM"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:6HFM"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6HFM"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6HFT"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:6HFT"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:6HFM"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:6HFM"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:6HFM"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:6HFM"
SQ SEQUENCE 385 AA; 44112 MW; 742F8254DFDB02A6 CRC64;
MSSVNANGGY TKPQKYVPGP GDPELPPQLS EFKDKTSDEI LKEMNRMPFF MTKLDETDGA
GGENVELEAL KALAYEGEPH EIAENFKKQG NELYKAKRFK DARELYSKGL AVECEDKSIN
ESLYANRAAC ELELKNYRRC IEDCSKALTI NPKNVKCYYR TSKAFFQLNK LEEAKSAATF
ANQRIDPENK SILNMLSVID RKEQELKAKE EKQQREAQER ENKKIMLESA MTLRNITNIK
THSPVELLNE GKIRLEDPMD FESQLIYPAL IMYPTQDEFD FVGEVSELTT VQELVDLVLE
GPQERFKKEG KENFTPKKVL VFMETKAGGL IKAGKKLTFH DILKKESPDV PLFDNALKIY
IVPKVESEGW ISKWDKQKAL ERRSV
