LHS1_SCHPO
ID LHS1_SCHPO Reviewed; 848 AA.
AC Q10061;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Heat shock protein 70 homolog lhs1;
DE EC=3.6.1.-;
DE Flags: Precursor;
GN ORFNames=SPAC1F5.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA92234.1; -; Genomic_DNA.
DR PIR; T38089; T38089.
DR RefSeq; NP_592867.1; NM_001018267.2.
DR AlphaFoldDB; Q10061; -.
DR SMR; Q10061; -.
DR BioGRID; 278037; 1.
DR STRING; 4896.SPAC1F5.06.1; -.
DR SwissPalm; Q10061; -.
DR MaxQB; Q10061; -.
DR PaxDb; Q10061; -.
DR PRIDE; Q10061; -.
DR EnsemblFungi; SPAC1F5.06.1; SPAC1F5.06.1:pep; SPAC1F5.06.
DR GeneID; 2541537; -.
DR KEGG; spo:SPAC1F5.06; -.
DR PomBase; SPAC1F5.06; -.
DR VEuPathDB; FungiDB:SPAC1F5.06; -.
DR eggNOG; KOG0104; Eukaryota.
DR HOGENOM; CLU_005965_5_0_1; -.
DR InParanoid; Q10061; -.
DR PhylomeDB; Q10061; -.
DR Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SPO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SPO-3371568; Attenuation phase.
DR PRO; PR:Q10061; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:PomBase.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISO:PomBase.
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:0034975; P:protein folding in endoplasmic reticulum; IC:PomBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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 Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100934; SSF100934; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..848
FT /note="Heat shock protein 70 homolog lhs1"
FT /id="PRO_0000013557"
FT REGION 784..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 845..848
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 786..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
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 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 848 AA; 94898 MW; A1983FD4253F38F3 CRC64;
MKRSVLTIIL FFSCQFWHAF ASSVLAIDYG TEWTKAALIK PGIPLEIVLT KDTRRKEQSA
VAFKGNERIF GVDASNLATR FPAHSIRNVK ELLDTAGLES VLVQKYQSSY PAIQLVENEE
TTSGISFVIS DEENYSLEEI IAMTMEHYIS LAEEMAHEKI TDLVLTVPPH FNELQRSILL
EAARILNKHV LALIDDNVAV AIEYSLSRSF STDPTYNIIY DSGSGSTSAT VISFDTVEGS
SLGKKQNITR IRALASGFTL KLSGNEINRK LIGFMKNSFY QKHGIDLSHN HRALARLEKE
ALRVKHILSA NSEAIASIEE LADGIDFRLK ITRSVLESLC KDMEDAAVEP INKALKKANL
TFSEINSIIL FGGASRIPFI QSTLADYVSS DKISKNVNAD EASVKGAAFY GASLTKSFRV
KPLIVQDIIN YPYLLSLGTS EYIVALPDST PYGMQHNVTI HNVSTIGKHP SFPLSNNGEL
IGEFTLSNIT DVEKVCACSN KNIQISFSSD RTKGILVPLS AIMTCEHGEL SSKHKLGDRV
KSLFGSHDES GLRNNESYPI GFTYKKYGEM SDNALRLASA KLERRLQIDK SKAAHDNALN
ELETLLYRAQ AMVDDDEFLE FANPEETKIL KNDSVESYDW LIEYGSQSPT SEVTDRYKKL
DDTLKSISFR FDQAKQFNTS LENFKNALER AESLLTNFDV PDYPLNVYDE KDVKRVNSLR
GTSYKKLGNQ YYNDTQWLKD NLDSHLSHTL SEDPLIKVEE LEEKAKRLQE LTYEYLRRSL
QQPKLKAKKG ASSSSTAESK VEDETFTNDI EPTTALNSTS TQETEKSRAS VTQRPSSLQQ
EIDDSDEL
