LHS1_YEAST
ID LHS1_YEAST Reviewed; 881 AA.
AC P36016; D6VXL3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Heat shock protein 70 homolog LHS1;
DE EC=3.6.1.-;
DE Flags: Precursor;
GN Name=LHS1; OrderedLocusNames=YKL073W; ORFNames=YKL355;
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=8091863; DOI=10.1002/yea.320100009;
RA Rasmussen S.W.;
RT "Sequence of a 20.7 kb region of yeast chromosome XI includes the NUP100
RT gene, an open reading frame (ORF) possibly representing a nucleoside
RT diphosphate kinase gene, tRNAs for His, Val and Trp in addition to seven
RT ORFs with weak or no significant similarity to known proteins.";
RL Yeast 10:S69-S74(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP CHARACTERIZATION.
RX PubMed=8654361; DOI=10.1002/j.1460-2075.1996.tb00624.x;
RA Craven R.A., Egerton M., Stirling C.J.;
RT "A novel Hsp70 of the yeast ER lumen is required for the efficient
RT translocation of a number of protein precursors.";
RL EMBO J. 15:2640-2650(1996).
RN [5]
RP INDUCTION.
RX PubMed=10847680; DOI=10.1016/s0092-8674(00)80835-1;
RA Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S.,
RA Walter P.;
RT "Functional and genomic analyses reveal an essential coordination between
RT the unfolded protein response and ER-associated degradation.";
RL Cell 101:249-258(2000).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION.
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 [7]
RP FUNCTION, INTERACTION WITH KAR2, AND MUTAGENESIS OF GLY-239.
RX PubMed=14704430; DOI=10.1126/science.1092287;
RA Steel G.J., Fullerton D.M., Tyson J.R., Stirling C.J.;
RT "Coordinated activation of Hsp70 chaperones.";
RL Science 303:98-101(2004).
CC -!- FUNCTION: Chaperone required for protein translocation and folding in
CC the endoplasmic reticulum. {ECO:0000269|PubMed:14704430}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBUNIT: Interacts with the heat shock protein 70 (HSP70) KAR2, and
CC this stimulates nucleotide exchange on KAR2. KAR2 in turn acts to
CC stimulate the ATPase activity of LHS1. {ECO:0000269|PubMed:14704430}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- INDUCTION: By the unfolded protein response (UPR).
CC {ECO:0000269|PubMed:10847680}.
CC -!- PTM: N-glycosylated.
CC -!- MISCELLANEOUS: Present with 137 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; X75780; CAA53401.1; -; Genomic_DNA.
DR EMBL; Z28073; CAA81910.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09083.1; -; Genomic_DNA.
DR PIR; S37895; S37895.
DR RefSeq; NP_012850.1; NM_001179639.1.
DR AlphaFoldDB; P36016; -.
DR SMR; P36016; -.
DR BioGRID; 34058; 378.
DR DIP; DIP-6520N; -.
DR IntAct; P36016; 7.
DR MINT; P36016; -.
DR STRING; 4932.YKL073W; -.
DR MaxQB; P36016; -.
DR PaxDb; P36016; -.
DR PRIDE; P36016; -.
DR EnsemblFungi; YKL073W_mRNA; YKL073W; YKL073W.
DR GeneID; 853789; -.
DR KEGG; sce:YKL073W; -.
DR SGD; S000001556; LHS1.
DR VEuPathDB; FungiDB:YKL073W; -.
DR eggNOG; KOG0104; Eukaryota.
DR GeneTree; ENSGT00940000175983; -.
DR HOGENOM; CLU_005965_5_0_1; -.
DR InParanoid; P36016; -.
DR OMA; IRTDELH; -.
DR BioCyc; YEAST:G3O-31869-MON; -.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SCE-3371568; Attenuation phase.
DR PRO; PR:P36016; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36016; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
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: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:0031204; P:post-translational protein targeting to membrane, translocation; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
DR Gene3D; 1.20.1270.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..881
FT /note="Heat shock protein 70 homolog LHS1"
FT /id="PRO_0000013556"
FT REGION 833..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 878..881
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 844..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 239
FT /note="G->D: In allele LHS1-1; constitutive ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:14704430"
SQ SEQUENCE 881 AA; 99572 MW; ACED092CA3A34785 CRC64;
MRNVLRLLFL TAFVAIGSLA AVLGVDYGQQ NIKAIVVSPQ APLELVLTPE AKRKEISGLS
IKRLPGYGKD DPNGIERIYG SAVGSLATRF PQNTLLHLKP LLGKSLEDET TVTLYSKQHP
GLEMVSTNRS TIAFLVDNVE YPLEELVAMN VQEIANRANS LLKDRDARTE DFVNKMSFTI
PDFFDQHQRK ALLDASSITT GIEETYLVSE GMSVAVNFVL KQRQFPPGEQ QHYIVYDMGS
GSIKASMFSI LQPEDTTQPV TIEFEGYGYN PHLGGAKFTM DIGSLIENKF LETHPAIRTD
ELHANPKALA KINQAAEKAK LILSANSEAS INIESLINDI DFRTSITRQE FEEFIADSLL
DIVKPINDAV TKQFGGYGTN LPEINGVILA GGSSRIPIVQ DQLIKLVSEE KVLRNVNADE
SAVNGVVMRG IKLSNSFKTK PLNVVDRSVN TYSFKLSNES ELYDVFTRGS AYPNKTSILT
NTTDSIPNNF TIDLFENGKL FETITVNSGA IKNSYSSDKC SSGVAYNITF DLSSDRLFSI
QEVNCICQSE NDIGNSKQIK NKGSRLAFTS EDVEIKRLSP SERSRLHEHI KLLDKQDKER
FQFQENLNVL ESNLYDARNL LMDDEVMQNG PKSQVEELSE MVKVYLDWLE DASFDTDPED
IVSRIREIGI LKKKIELYMD SAKEPLNSQQ FKGMLEEGHK LLQAIETHKN TVEEFLSQFE
TEFADTIDNV REEFKKIKQP AYVSKALSTW EETLTSFKNS ISEIEKFLAK NLFGEDLREH
LFEIKLQFDM YRTKLEEKLR LIKSGDESRL NEIKKLHLRN FRLQKRKEEK LKRKLEQEKS
RNNNETESTV INSADDKTTI VNDKTTESNP SSEEDILHDE L
