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   27-MAR-2024, entry version 149.
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; 284812.Q10061; -.
DR   iPTMnet; Q10061; -.
DR   SwissPalm; Q10061; -.
DR   MaxQB; Q10061; -.
DR   PaxDb; 4896-SPAC1F5-06-1; -.
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   PRO; PR:Q10061; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:PomBase.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
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:0034975; P:protein folding in endoplasmic reticulum; IC:PomBase.
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   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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
//