HSP71_SCHPO
ID HSP71_SCHPO Reviewed; 644 AA.
AC Q10265;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable heat shock protein ssa1;
GN Name=ssa1; ORFNames=SPAC13G7.02c;
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93590.1; -; Genomic_DNA.
DR PIR; S67431; S67431.
DR RefSeq; NP_593704.1; NM_001019135.2.
DR PDB; 3FP4; X-ray; 2.14 A; Q=633-644.
DR PDBsum; 3FP4; -.
DR AlphaFoldDB; Q10265; -.
DR SMR; Q10265; -.
DR BioGRID; 279320; 59.
DR DIP; DIP-54582N; -.
DR IntAct; Q10265; 4.
DR MINT; Q10265; -.
DR STRING; 4896.SPAC13G7.02c.1; -.
DR iPTMnet; Q10265; -.
DR MaxQB; Q10265; -.
DR PaxDb; Q10265; -.
DR PRIDE; Q10265; -.
DR EnsemblFungi; SPAC13G7.02c.1; SPAC13G7.02c.1:pep; SPAC13G7.02c.
DR GeneID; 2542875; -.
DR KEGG; spo:SPAC13G7.02c; -.
DR PomBase; SPAC13G7.02c; ssa1.
DR VEuPathDB; FungiDB:SPAC13G7.02c; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; Q10265; -.
DR OMA; KANPIMM; -.
DR PhylomeDB; Q10265; -.
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 Reactome; R-SPO-3371571; HSF1-dependent transactivation.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SPO-8876725; Protein methylation.
DR EvolutionaryTrace; Q10265; -.
DR PRO; PR:Q10265; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
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; ISO:PomBase.
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:0042026; P:protein refolding; ISO:PomBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
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; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..644
FT /note="Probable heat shock protein ssa1"
FT /id="PRO_0000078379"
FT REGION 610..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 644 AA; 70143 MW; 1AD5E3B18FAC304E CRC64;
MSKSIGIDLG TTYSCVGHFS NNRVEIIAND QGNRTTPSYV AFTDTERLIG DAAKNQVAMN
PHNTIFDAKR LIGRRFNDPE VQSDMKHWPF KVIEKDGKPL IQVEFKGETK TFTPEEISSM
VLLKMRESAE AFLGGKVTDA VVTVPAYFND SQRQATKDAG LIAGLNVLRI INEPTAAAIA
YGLDRSNQHE TNVLIFDLGG GTFDVSLLTI EEGIFEVKAT AGDTHLGGED FDSRLVNHFA
QEFKRKNKKD ITGNARAVRR LRTACERAKR TLSSSAQASI EIDSLYEGID FYTSITRARF
EELCADLFRN TMEPVEKVLR DSKIDKSSVN EIVLVGGSTR IPRIQKLVSD FFNGKEPCKS
INPDEAVAYG AAVQAAILVG DTSEKTQDLL LLDVAPLSLG IETAGGVMTP LIKRNTTIPT
KKSEVFSTYA DNQPGVLIQV FEGERARTKD CNLLGKFELS GIPPAPRGVP QIEVTFDVDA
NGILNVSALE KGTGKTQKIT ITNDKGRLSK EEIDRMVSEA EKYKAEDEAE TSRIQAKNHL
ESYAYSLRNS LDDPNLKDKV DASDKEAIDK AVKETIEWLD HNTTAAKDEY EDKQKELEGV
ANPIMAKIYQ AGGAPGGAPG GMPGGAPGGA PGGADNGPEV EEVD