CH10_MOUSE
ID CH10_MOUSE Reviewed; 102 AA.
AC Q64433;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=10 kDa heat shock protein, mitochondrial;
DE Short=Hsp10;
DE AltName: Full=10 kDa chaperonin;
DE AltName: Full=Chaperonin 10;
DE Short=CPN10;
GN Name=Hspe1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7929423; DOI=10.1016/s0021-9258(18)47098-6;
RA Dickson R., Larsen B., Viitanen P.V., Tormey M.B., Geske J., Strange R.,
RA Bemis L.T.;
RT "Cloning, expression, and purification of a functional nonacetylated
RT mammalian mitochondrial chaperonin 10.";
RL J. Biol. Chem. 269:26858-26864(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11210183; DOI=10.1007/s003350010250;
RA Fletcher B.H., Cassady A.I., Summers K.M., Cavanagh A.C.;
RT "The murine chaperonin 10 gene family contains an intronless, putative gene
RT for early pregnancy factor, Cpn10-rs1.";
RL Mamm. Genome 12:133-140(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 8-15; 29-36; 41-54 AND 71-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-28; LYS-40; LYS-54; LYS-56; LYS-66; LYS-70; LYS-80 AND
RP LYS-86, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-40; LYS-56; LYS-66;
RP LYS-70; LYS-80; LYS-86 AND LYS-99, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Co-chaperonin implicated in mitochondrial protein import and
CC macromolecular assembly. Together with Hsp60, facilitates the correct
CC folding of imported proteins. May also prevent misfolding and promote
CC the refolding and proper assembly of unfolded polypeptides generated
CC under stress conditions in the mitochondrial matrix. The functional
CC units of these chaperonins consist of heptameric rings of the large
CC subunit Hsp60, which function as a back-to-back double ring. In a
CC cyclic reaction, Hsp60 ring complexes bind one unfolded substrate
CC protein per ring, followed by the binding of ATP and association with 2
CC heptameric rings of the co-chaperonin Hsp10. This leads to
CC sequestration of the substrate protein in the inner cavity of Hsp60
CC where, for a certain period of time, it can fold undisturbed by other
CC cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits
CC results in the dissociation of the chaperonin rings and the release of
CC ADP and the folded substrate protein. {ECO:0000250|UniProtKB:P61604}.
CC -!- SUBUNIT: Homoheptamer arranged in a ring structure. 2 heptameric Hsp10
CC rings interact with a Hsp60 tetradecamer in the structure of a back-to-
CC back double heptameric ring to form the symmetrical football complex.
CC {ECO:0000250|UniProtKB:P61604}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P61604}.
CC -!- INDUCTION: By stress.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR EMBL; U09659; AAA62229.1; -; mRNA.
DR EMBL; AF251024; AAF67345.1; -; Genomic_DNA.
DR EMBL; AK088121; BAC40159.1; -; mRNA.
DR EMBL; BC024385; AAH24385.1; -; mRNA.
DR CCDS; CCDS35570.1; -.
DR PIR; A55075; A55075.
DR RefSeq; NP_032329.1; NM_008303.4.
DR AlphaFoldDB; Q64433; -.
DR SMR; Q64433; -.
DR BioGRID; 200459; 19.
DR IntAct; Q64433; 1.
DR STRING; 10090.ENSMUSP00000074724; -.
DR iPTMnet; Q64433; -.
DR PhosphoSitePlus; Q64433; -.
DR REPRODUCTION-2DPAGE; Q64433; -.
DR EPD; Q64433; -.
DR jPOST; Q64433; -.
DR MaxQB; Q64433; -.
DR PaxDb; Q64433; -.
DR PRIDE; Q64433; -.
DR ProteomicsDB; 281659; -.
DR TopDownProteomics; Q64433; -.
DR DNASU; 15528; -.
DR Ensembl; ENSMUST00000075242; ENSMUSP00000074724; ENSMUSG00000073676.
DR GeneID; 15528; -.
DR KEGG; mmu:15528; -.
DR UCSC; uc007bac.2; mouse.
DR CTD; 3336; -.
DR MGI; MGI:104680; Hspe1.
DR VEuPathDB; HostDB:ENSMUSG00000073676; -.
DR eggNOG; KOG1641; Eukaryota.
DR GeneTree; ENSGT00390000006350; -.
DR HOGENOM; CLU_132825_0_1_1; -.
DR InParanoid; Q64433; -.
DR OMA; EVKYSGE; -.
DR OrthoDB; 1580867at2759; -.
DR PhylomeDB; Q64433; -.
DR TreeFam; TF313814; -.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 15528; 14 hits in 43 CRISPR screens.
DR ChiTaRS; Hspe1; mouse.
DR PRO; PR:Q64433; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q64433; protein.
DR Bgee; ENSMUSG00000073676; Expressed in yolk sac and 197 other tissues.
DR ExpressionAtlas; Q64433; baseline and differential.
DR Genevisible; Q64433; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
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 Acetylation; Chaperone; Direct protein sequencing; Mitochondrion;
KW Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61604"
FT CHAIN 2..102
FT /note="10 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000174918"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61604"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 28
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 40
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 40
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 54
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 56
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 56
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 66
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 66
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61604"
FT MOD_RES 80
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 86
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 102 AA; 10963 MW; 08BEB5566DBE8A3D CRC64;
MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGGKGKSGEI
EPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDSDILGKY VD
