YDMC_SCHPO
ID YDMC_SCHPO Reviewed; 566 AA.
AC P87142; P78911;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Heat shock protein 70 homolog C57A7.12;
GN ORFNames=SPAC57A7.12;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-566.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-500, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB08770.1; -; Genomic_DNA.
DR EMBL; D89262; BAA13923.1; -; mRNA.
DR PIR; T38942; T38942.
DR PIR; T43188; T43188.
DR RefSeq; NP_593369.1; NM_001018801.2.
DR AlphaFoldDB; P87142; -.
DR SMR; P87142; -.
DR BioGRID; 278607; 5.
DR IntAct; P87142; 1.
DR STRING; 4896.SPAC57A7.12.1; -.
DR iPTMnet; P87142; -.
DR MaxQB; P87142; -.
DR PaxDb; P87142; -.
DR PRIDE; P87142; -.
DR EnsemblFungi; SPAC57A7.12.1; SPAC57A7.12.1:pep; SPAC57A7.12.
DR GeneID; 2542131; -.
DR KEGG; spo:SPAC57A7.12; -.
DR PomBase; SPAC57A7.12; -.
DR VEuPathDB; FungiDB:SPAC57A7.12; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; P87142; -.
DR OMA; RGGIYTI; -.
DR PhylomeDB; P87142; -.
DR PRO; PR:P87142; -.
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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
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; ISO:PomBase.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; ISO:PomBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
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; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..566
FT /note="Heat shock protein 70 homolog C57A7.12"
FT /id="PRO_0000078399"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 63
FT /note="S -> P (in Ref. 2; BAA13923)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="L -> H (in Ref. 2; BAA13923)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="A -> S (in Ref. 2; BAA13923)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="D -> G (in Ref. 2; BAA13923)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="A -> V (in Ref. 2; BAA13923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 61286 MW; 9381A1793027D93B CRC64;
MQLKLTKTLP FSENFIMADS EEYKTVIGIS FGNQNSSIAF NRDGKTDVLA NEEGNRQIPS
ILSYHGDQEY HGVQARGQLV RNADNSVTNF RDLLGKSHDE LTLHHCHYSA NPVNVEGQIG
FKITVQEDEE SDPKEKILTA HEASVRHLRR LTESAEDFLG TKVNGCVMSV PVYFTDAQRK
ALESAANEAG LPVLQLIHDP AAVILALMYS EEVLIDKTVV VANFGATRSE VSVVSVKGGL
MTILASVHDE NLGGEQLTDV LVNFFAKEFE KKNGIDPRKN ARSLAKLRAQ CEITKRVLSN
GTTASAAVDS LADGIDFHSS INRLRYDLAA SATLNRMADL VTEAVEKANM EPFDISEVIL
AGGASNTPKL TSLMESIFPE QTIIRSSSSV TPLQLDPSEL TAIGSGVQAS LIGHFDAADI
AASTDAQVVD VPHLTAPIGI NEGENFVTIF DIETALPARK TVEVIAPKEG AAFIPIYEAE
RSVKVTKVEP EPIDEEEAFS DDEEEEPEEI KERIAIPKTL IATITLPDVS PNAKIELVLQ
IDAEGKLTAS ARPKDGKGTN VRGSTA
