HSP79_YEAST
ID HSP79_YEAST Reviewed; 693 AA.
AC P32590; D6VQG5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Heat shock protein homolog SSE2;
GN Name=SSE2; Synonyms=HSP; OrderedLocusNames=YBR169C; ORFNames=YBR1221;
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 [MRNA].
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=8406043; DOI=10.1016/0378-1119(93)90514-4;
RA Mukai H., Kuno T., Tanaka H., Hirata D., Miyakawa T., Tanaka C.;
RT "Isolation and characterization of SSE1 and SSE2, new members of the yeast
RT HSP70 multigene family.";
RL Gene 132:57-66(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8257794; DOI=10.1091/mbc.4.9.919;
RA Kurihara T., Silver P.A.;
RT "Suppression of a sec63 mutation identifies a novel component of the yeast
RT endoplasmic reticulum translocation apparatus.";
RL Mol. Biol. Cell 4:919-930(1993).
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 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: Has a calcium-dependent calmodulin-binding activity.
CC -!- INDUCTION: By upshift to 37 degrees Celsius.
CC -!- MISCELLANEOUS: Present with 6300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; D38369; BAA07450.1; -; mRNA.
DR EMBL; D38371; BAA07452.1; -; Genomic_DNA.
DR EMBL; X72224; CAA51027.1; -; Genomic_DNA.
DR EMBL; Z36038; CAA85130.1; -; Genomic_DNA.
DR EMBL; AY692880; AAT92899.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07285.1; -; Genomic_DNA.
DR PIR; JN0843; JN0843.
DR RefSeq; NP_009728.1; NM_001178517.1.
DR AlphaFoldDB; P32590; -.
DR SMR; P32590; -.
DR BioGRID; 32869; 97.
DR DIP; DIP-4862N; -.
DR IntAct; P32590; 19.
DR MINT; P32590; -.
DR STRING; 4932.YBR169C; -.
DR iPTMnet; P32590; -.
DR UCD-2DPAGE; P32590; -.
DR MaxQB; P32590; -.
DR PaxDb; P32590; -.
DR PRIDE; P32590; -.
DR EnsemblFungi; YBR169C_mRNA; YBR169C; YBR169C.
DR GeneID; 852467; -.
DR KEGG; sce:YBR169C; -.
DR SGD; S000000373; SSE2.
DR VEuPathDB; FungiDB:YBR169C; -.
DR eggNOG; KOG0103; Eukaryota.
DR GeneTree; ENSGT00940000168707; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; P32590; -.
DR OMA; AHFLVQK; -.
DR BioCyc; YEAST:G3O-29117-MON; -.
DR PRO; PR:P32590; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32590; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IGI:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:SGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IGI:SGD.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..693
FT /note="Heat shock protein homolog SSE2"
FT /id="PRO_0000078397"
FT REGION 653..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 160..167
FT /note="Missing (in Ref. 2; CAA51027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 77621 MW; D6BC9656D93895C2 CRC64;
MSTPFGLDLG NNNSVLAVAR NRGIDVVVNE VSNRSTPSLV GFGPRNRYLG ESGKTKQTSN
VKNTVENLKR IIGLKFKDPE FDIENKFFTS KLVQLKNGKV GVEVEFGGKT HVFSATQLTA
MFIDKVKHTV QEETKSSITD VCLAVPVWYS EEQRYNIADA ARIAGLNPVR IVNDVTAAAV
SYGVFKNDLP GPEEKPRIIG LVDIGHSTYT CSIMAFRKGE MKVLGTAYDK HFGGRDFDRA
ITEHFADQFK DKYKIDIRKN PKAYNRILIA AEKLKKVLSA NTTAPFSVES VMDDIDVSSQ
LSREELEELV EPLLKRVTYP ITNALAQAKL TVNDIDFVEI IGGTTRIPVL KKSISDVFGK
PLSSTLNQDE AVAKGAAFIC AIHSPTLRVR PFKFEDIDPY SVSYTWDKQV DDEDRLEVFP
ANSSYPSTKL ITLHRTGDFS MKAVYTHPSK LPKGTSTTIA KWSFTGVKVP KDQDFIPVKV
KLRCDPSGLH IIENAYTTED ITVQEPVPLP EDAPEDAEPQ FKEVTKTIKK DVLGMTAKTF
ALNPVELNDL IEKENELRNQ DKLVAETEDR KNALEEYIYT LRAKLDDEYS DFASDAEKEK
LKNMLATTEN WLYGDGDDST KAKYIAKYEE LASLGNIIRG RYLAKEEEKR QALRANQETS
KMNDIAEKLA EQRRARAASD DSDDNNDENM DLD
