HSP7F_YEAST
ID HSP7F_YEAST Reviewed; 693 AA.
AC P32589; D6W3R1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Heat shock protein homolog SSE1;
DE AltName: Full=Chaperone protein MSI3;
GN Name=SSE1; Synonyms=MSI3; OrderedLocusNames=YPL106C; ORFNames=LPG3C;
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=8413180; DOI=10.1007/bf00280382;
RA Shirayama M., Kawakami K., Matsui Y., Tanaka K., Toh-e A.;
RT "MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP
RT pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 240:323-332(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 PROTEIN SEQUENCE OF 100-110.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [6]
RP PROTEIN SEQUENCE OF 330-339.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [7]
RP ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, AND IDENTIFICATION BY
RP 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 [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Has a calcium-dependent calmodulin-binding activity. Required
CC for normal growth at various temperatures.
CC -!- INTERACTION:
CC P32589; P02829: HSP82; NbExp=3; IntAct=EBI-8648, EBI-8659;
CC P32589; P25294: SIS1; NbExp=2; IntAct=EBI-8648, EBI-17244;
CC P32589; P10591: SSA1; NbExp=8; IntAct=EBI-8648, EBI-8591;
CC P32589; P11484: SSB1; NbExp=2; IntAct=EBI-8648, EBI-8627;
CC P32589; P08107: HSPA1B; Xeno; NbExp=2; IntAct=EBI-8648, EBI-629985;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Increases a few-fold upon upshift to 37 degrees Celsius.
CC -!- MISCELLANEOUS: Present with 71700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; D13319; BAA02576.1; -; mRNA.
DR EMBL; D38368; BAA07449.1; -; mRNA.
DR EMBL; D38370; BAA07451.1; -; Genomic_DNA.
DR EMBL; D13743; BAA02888.1; -; Genomic_DNA.
DR EMBL; U43281; AAB68194.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11327.1; -; Genomic_DNA.
DR PIR; S46417; S46417.
DR RefSeq; NP_015219.1; NM_001183920.1.
DR PDB; 2QXL; X-ray; 2.41 A; A/B=2-659.
DR PDB; 3C7N; X-ray; 3.12 A; A=1-666.
DR PDB; 3D2E; X-ray; 2.35 A; A/C=1-502, A/C=525-693.
DR PDB; 3D2F; X-ray; 2.30 A; A/C=1-502, A/C=525-693.
DR PDBsum; 2QXL; -.
DR PDBsum; 3C7N; -.
DR PDBsum; 3D2E; -.
DR PDBsum; 3D2F; -.
DR AlphaFoldDB; P32589; -.
DR SMR; P32589; -.
DR BioGRID; 36075; 665.
DR DIP; DIP-6645N; -.
DR IntAct; P32589; 127.
DR MINT; P32589; -.
DR STRING; 4932.YPL106C; -.
DR CarbonylDB; P32589; -.
DR iPTMnet; P32589; -.
DR SWISS-2DPAGE; P32589; -.
DR MaxQB; P32589; -.
DR PaxDb; P32589; -.
DR PRIDE; P32589; -.
DR EnsemblFungi; YPL106C_mRNA; YPL106C; YPL106C.
DR GeneID; 855998; -.
DR KEGG; sce:YPL106C; -.
DR SGD; S000006027; SSE1.
DR VEuPathDB; FungiDB:YPL106C; -.
DR eggNOG; KOG0103; Eukaryota.
DR GeneTree; ENSGT00940000168707; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; P32589; -.
DR OMA; AYDRHFG; -.
DR BioCyc; YEAST:G3O-34008-MON; -.
DR EvolutionaryTrace; P32589; -.
DR PRO; PR:P32589; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32589; 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:0005844; C:polysome; IDA:SGD.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
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:0042277; F:peptide binding; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
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; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IDA: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 3D-structure; Acetylation; ATP-binding; Calmodulin-binding; Chaperone;
KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Stress response; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..693
FT /note="Heat shock protein homolog SSE1"
FT /id="PRO_0000078396"
FT REGION 653..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 269..270
FT /note="TA -> NT (in Ref. 1; BAA02576/BAA07449)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 234..252
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 261..280
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:3D2F"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 319..328
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:3D2F"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:2QXL"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 423..437
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 457..465
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 476..484
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3C7N"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:3C7N"
FT STRAND 529..532
FT /evidence="ECO:0007829|PDB:3D2F"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 544..585
FT /evidence="ECO:0007829|PDB:3D2F"
FT TURN 586..589
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 595..611
FT /evidence="ECO:0007829|PDB:3D2F"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 615..618
FT /evidence="ECO:0007829|PDB:3D2F"
FT HELIX 621..653
FT /evidence="ECO:0007829|PDB:3D2F"
SQ SEQUENCE 693 AA; 77366 MW; 6558259111B0BC38 CRC64;
MSTPFGLDLG NNNSVLAVAR NRGIDIVVNE VSNRSTPSVV GFGPKNRYLG ETGKNKQTSN
IKNTVANLKR IIGLDYHHPD FEQESKHFTS KLVELDDKKT GAEVRFAGEK HVFSATQLAA
MFIDKVKDTV KQDTKANITD VCIAVPPWYT EEQRYNIADA ARIAGLNPVR IVNDVTAAGV
SYGIFKTDLP EGEEKPRIVA FVDIGHSSYT CSIMAFKKGQ LKVLGTACDK HFGGRDFDLA
ITEHFADEFK TKYKIDIREN PKAYNRILTA AEKLKKVLSA NTNAPFSVES VMNDVDVSSQ
LSREELEELV KPLLERVTEP VTKALAQAKL SAEEVDFVEI IGGTTRIPTL KQSISEAFGK
PLSTTLNQDE AIAKGAAFIC AIHSPTLRVR PFKFEDIHPY SVSYSWDKQV EDEDHMEVFP
AGSSFPSTKL ITLNRTGDFS MAASYTDITQ LPPNTPEQIA NWEITGVQLP EGQDSVPVKL
KLRCDPSGLH TIEEAYTIED IEVEEPIPLP EDAPEDAEQE FKKVTKTVKK DDLTIVAHTF
GLDAKKLNEL IEKENEMLAQ DKLVAETEDR KNTLEEYIYT LRGKLEEEYA PFASDAEKTK
LQGMLNKAEE WLYDEGFDSI KAKYIAKYEE LASLGNIIRG RYLAKEEEKK QAIRSKQEAS
QMAAMAEKLA AQRKAEAEKK EEKKDTEGDV DMD
