ID   CH10_SCHPO              Reviewed;         104 AA.
AC   O59804;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=10 kDa heat shock protein, mitochondrial;
DE            Short=HSP10;
DE   AltName: Full=10 kDa chaperonin;
GN   Name=hsp10; ORFNames=SPCC550.06c;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP   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   -!- FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial
CC       protein biogenesis, together with CPN60. Binds to CPN60 in the presence
CC       of Mg-ATP and suppresses the ATPase activity of the latter (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA19110.1; -; Genomic_DNA.
DR   PIR; T41381; T41381.
DR   RefSeq; NP_588098.1; NM_001023089.2.
DR   AlphaFoldDB; O59804; -.
DR   SMR; O59804; -.
DR   BioGRID; 276052; 2.
DR   STRING; 4896.SPCC550.06c.1; -.
DR   iPTMnet; O59804; -.
DR   MaxQB; O59804; -.
DR   PaxDb; O59804; -.
DR   PRIDE; O59804; -.
DR   EnsemblFungi; SPCC550.06c.1; SPCC550.06c.1:pep; SPCC550.06c.
DR   GeneID; 2539489; -.
DR   KEGG; spo:SPCC550.06c; -.
DR   PomBase; SPCC550.06c; hsp10.
DR   VEuPathDB; FungiDB:SPCC550.06c; -.
DR   eggNOG; KOG1641; Eukaryota.
DR   HOGENOM; CLU_132825_0_0_1; -.
DR   InParanoid; O59804; -.
DR   OMA; EVKYSGE; -.
DR   PhylomeDB; O59804; -.
DR   PRO; PR:O59804; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:PomBase.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; ISS:PomBase.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; ISS:PomBase.
DR   CDD; cd00320; cpn10; 1.
DR   Gene3D; 2.30.33.40; -; 1.
DR   HAMAP; MF_00580; CH10; 1.
DR   InterPro; IPR020818; Chaperonin_GroES.
DR   InterPro; IPR037124; Chaperonin_GroES_sf.
DR   InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   PANTHER; PTHR10772; PTHR10772; 1.
DR   Pfam; PF00166; Cpn10; 1.
DR   PRINTS; PR00297; CHAPERONIN10.
DR   SMART; SM00883; Cpn10; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Mitochondrion; Phosphoprotein; Reference proteome.
FT   CHAIN           1..104
FT                   /note="10 kDa heat shock protein, mitochondrial"
FT                   /id="PRO_0000174921"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   104 AA;  11282 MW;  16BF6870BCB10222 CRC64;
     MATKLKSAKS IVPLLDRILV QRIKADTKTA SGIFLPEKSV EKLSEGRVIS VGKGGYNKEG
     KLAQPSVAVG DRVLLPAYGG SNIKVGEEEY SLYRDHELLA IIKE