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   27-MAR-2024, entry version 194.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 390.
DR   DIP; DIP-6520N; -.
DR   IntAct; P36016; 7.
DR   MINT; P36016; -.
DR   STRING; 4932.YKL073W; -.
DR   TCDB; 1.A.33.1.6; the cation channel-forming heat shock protein-70 (hsp70) family.
DR   GlyCosmos; P36016; 7 sites, No reported glycans.
DR   GlyGen; P36016; 7 sites.
DR   MaxQB; P36016; -.
DR   PaxDb; 4932-YKL073W; -.
DR   PeptideAtlas; P36016; -.
DR   EnsemblFungi; YKL073W_mRNA; YKL073W; YKL073W.
DR   GeneID; 853789; -.
DR   KEGG; sce:YKL073W; -.
DR   AGR; SGD:S000001556; -.
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; DYGQQNI; -.
DR   OrthoDB; 5491443at2759; -.
DR   BioCyc; YEAST:G3O-31869-MONOMER; -.
DR   BioGRID-ORCS; 853789; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P36016; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36016; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR   GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IMP:SGD.
DR   GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
DR   CDD; cd10230; HYOU1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 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
//