HSP7E_YEAST
ID HSP7E_YEAST Reviewed; 644 AA.
AC P39987; D3DLL9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Heat shock protein SSC3, mitochondrial;
DE AltName: Full=Extracellular mutant protein 10;
DE Flags: Precursor;
GN Name=ECM10; Synonyms=SSC3; OrderedLocusNames=YEL030W;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11150530; DOI=10.1016/s0014-5793(00)02364-4;
RA Baumann F., Milisav I., Neupert W., Herrmann J.M.;
RT "Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 487:307-312(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12943685; DOI=10.1016/s0006-291x(03)01548-1;
RA Sakasegawa Y., Hachiya N.S., Tsukita S., Kaneko K.;
RT "Ecm10p localizes in yeast mitochondrial nucleoids and its overexpression
RT induces extensive mitochondrial DNA aggregations.";
RL Biochem. Biophys. Res. Commun. 309:217-221(2003).
CC -!- FUNCTION: Plays a role in facilitating the assembly of some protein
CC complexes inside the mitochondria. It may initiate the events that lead
CC to refolding of imported precursors in the matrix space.
CC {ECO:0000269|PubMed:11150530}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000269|PubMed:11150530, ECO:0000269|PubMed:12943685}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U18530; AAB64507.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07623.1; -; Genomic_DNA.
DR PIR; S50429; S50429.
DR RefSeq; NP_010884.1; NM_001178845.1.
DR AlphaFoldDB; P39987; -.
DR SMR; P39987; -.
DR BioGRID; 36699; 105.
DR DIP; DIP-6541N; -.
DR IntAct; P39987; 19.
DR MINT; P39987; -.
DR STRING; 4932.YEL030W; -.
DR iPTMnet; P39987; -.
DR MaxQB; P39987; -.
DR PaxDb; P39987; -.
DR PRIDE; P39987; -.
DR EnsemblFungi; YEL030W_mRNA; YEL030W; YEL030W.
DR GeneID; 856682; -.
DR KEGG; sce:YEL030W; -.
DR SGD; S000000756; ECM10.
DR VEuPathDB; FungiDB:YEL030W; -.
DR eggNOG; KOG0102; Eukaryota.
DR GeneTree; ENSGT00920000149123; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P39987; -.
DR OMA; DINQVPF; -.
DR BioCyc; YEAST:G3O-30152-MON; -.
DR PRO; PR:P39987; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39987; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; 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; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IDA:SGD.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Mitochondrion; Mitochondrion nucleoid;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..644
FT /note="Heat shock protein SSC3, mitochondrial"
FT /id="PRO_0000013554"
SQ SEQUENCE 644 AA; 70084 MW; 6A248DE208F513CB CRC64;
MLPSWKAFKA HNILRILTRF QSTKIPDAVI GIDLGTTNSA VAIMEGKVPR IIENAEGSRT
TPSVVAFTKD GERLVGEPAK RQSVINSENT LFATKRLIGR RFEDAEVQRD INQVPFKIVK
HSNGDAWVEA RNRTYSPAQI GGFILNKMKE TAEAYLAKSV KNAVVTVPAY FNDAQRQATK
DAGQIIGLNV LRVVNEPTAA ALAYGLDKSE PKVIAVFDLG GGTFDISILD IDNGIFEVKS
TNGDTHLGGE DFDIYLLQEI ISHFKKETGI DLSNDRMAVQ RIREAAEKAK IELSSTLSTE
INLPFITADA AGPKHIRMPF SRVQLENITA PLIDRTVDPV KKALKDARIT ASDISDVLLV
GGMSRMPKVA DTVKKLFGKD ASKAVNPDEA VALGAAIQAA VLSGEVTDVL LLDVTPLSLG
IETLGGVFTK LIPRNSTIPN KKSQIFSTAA SGQTSVEVKV FQGERELVKD NKLIGNFTLA
GIPPAPKGTP QIEVTFDIDA NGIINVSAKD LASHKDSSIT VAGASGLSDT EIDRMVNEAE
RYKNQDRARR NAIETANKAD QLANDTENSI KEFEGKLDKT DSQRLKDQIS SLRELVSRSQ
AGDEVNDDDV GTKIDNLRTS SMKLFEQLYK NSDNPETKNG RENK
