LHS1_CANGA
ID LHS1_CANGA Reviewed; 889 AA.
AC Q6FU50;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Heat shock protein 70 homolog LHS1;
DE EC=3.6.1.-;
DE Flags: Precursor;
GN Name=LHS1; OrderedLocusNames=CAGL0F06369g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Chaperone required for protein translocation and folding in
CC the endoplasmic reticulum. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
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; CR380952; CAG59168.1; -; Genomic_DNA.
DR RefSeq; XP_446244.1; XM_446244.1.
DR AlphaFoldDB; Q6FU50; -.
DR SMR; Q6FU50; -.
DR STRING; 5478.XP_446244.1; -.
DR EnsemblFungi; CAG59168; CAG59168; CAGL0F06369g.
DR GeneID; 2887859; -.
DR KEGG; cgr:CAGL0F06369g; -.
DR CGD; CAL0130854; CAGL0F06369g.
DR VEuPathDB; FungiDB:CAGL0F06369g; -.
DR eggNOG; KOG0104; Eukaryota.
DR HOGENOM; CLU_005965_5_0_1; -.
DR InParanoid; Q6FU50; -.
DR OMA; IRTDELH; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:EnsemblFungi.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IEA:EnsemblFungi.
DR GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
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; SSF53067; SSF53067; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..889
FT /note="Heat shock protein 70 homolog LHS1"
FT /id="PRO_0000013555"
FT REGION 811..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 886..889
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 843..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..889
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 889 AA; 99634 MW; 58CD2D752B2DD11F CRC64;
MKLSILFLFA IAVQAAFLGI DYGQQSIKAM VVSPKAMMEI VLTPEAKRKD TSGICIRNVN
GVLERHYGNS IGSLVTRFPQ NTAMHLRSLL GKSMNDKDTI ESYLRENPGA NLTSTTRNTI
AITIDGVEYP VEQLVAMNLQ EIIDRANQHI KETDTTGIDF VEQVGIAIPE QFNQAQRQAL
LDALALTSVK DEAVLVSDGL SVAIDYALKR PDLEINVPQY YIVFDVGTSA AKATLFSLTQ
PEDLSSPIKI EIGAFDSEAT VGGSKFIAAI ADIVEDKFLE KNTKITRKSL VENPRARAKI
IQAAEKAKLV LSANNEAIIS IESLVDDIDF RTTIARSEFQ DIFEDNKHTV VKAIKGAIGN
QLWDDNISLE DISGVILSGG SSRVPMVQEE IAKLVGEEKI LKNVNADETV INGATLKGLK
YFGSFKTKPL DITERSLFDY SVEMSGESSS KTVFEKGTKF PNESSILYKA PKKFGKELKF
DLFESDTRIL SNIVDTTVSS KNWTSACKKG QLYLNVTFDL DSNRVFKIKD ITVLCDSDGN
AKEEEFEFID VINDVTKATD VMPLSNAEIR QLSNAITSWN RKDRERKRVQ ESLNVLEAEL
YDCRSFIEEF EEKLGEEEFE TLKSFTAFVK EKLEYLEDNS ADMSKKDIEK LVRETRSQRD
TLSRFYNSLD AALGSKDFQK LVDTASKSIK KYKEIESKNL ADLENKAEKF NVIGLNVTEK
YNSILSKMSF SSIRRSSEEN IKTLAGLIDE VNESIKSKAI DDESLENLIK TKLAFEELIN
TLDLENRQWT YQHQLVMKEL KKMYNKKMKA IKKQEKQNEN EENGDDEGDD EDETKTKKYL
KEATSSGDSS TIKEEDSTGS NEAGNKGDEE DEEEEEDDSS AGNVFDDEL
