CH10_ARATH
ID CH10_ARATH Reviewed; 98 AA.
AC P34893; Q96249;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=10 kDa chaperonin, mitochondrial;
DE AltName: Full=Chaperonin 10;
DE Short=CPN10;
DE AltName: Full=Protein groES;
DE Flags: Precursor;
GN Name=CPN10; OrderedLocusNames=At1g14980; ORFNames=T15D22.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7906419; DOI=10.1104/pp.102.2.685;
RA Grellet F., Raynal M., Laudie M., Cooke R., Giraudat J., Delseny M.;
RT "cDNA encoding a putative 10-kilodalton chaperonin from Arabidopsis
RT thaliana.";
RL Plant Physiol. 102:685-685(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP INDUCTION BY HEAT SHOCK.
RC STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX PubMed=9011092; DOI=10.1046/j.1365-313x.1996.10061119.x;
RA Koumoto Y., Tsugeki R., Shimada T., Mori H., Kondo M., Hara-Nishimura I.,
RA Nishimura M.;
RT "Isolation and characterization of a cDNA encoding mitochondrial chaperonin
RT 10 from Arabidopsis thaliana by functional complementation of an
RT Escherichia coli groES mutant.";
RL Plant J. 10:1119-1125(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Seems to function only as a co-chaperone, along with CPN60,
CC and in certain cases is essential for the discharge of biologically
CC active proteins from CPN60. {ECO:0000305|PubMed:9011092}.
CC -!- SUBUNIT: Forms stable complexes with CPN60 in the presence of ATP.
CC {ECO:0000305|PubMed:9011092}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9011092}.
CC -!- INDUCTION: By heat shock treatment. {ECO:0000269|PubMed:9011092}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR EMBL; L02843; AAA32767.1; -; mRNA.
DR EMBL; D88314; BAA13588.2; -; mRNA.
DR EMBL; AC012189; AAF31020.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29249.1; -; Genomic_DNA.
DR EMBL; AY063928; AAL36284.1; -; mRNA.
DR EMBL; AY091252; AAM14191.1; -; mRNA.
DR EMBL; AY086708; AAM63762.1; -; mRNA.
DR PIR; S65597; S65597.
DR RefSeq; NP_563961.1; NM_101367.3.
DR AlphaFoldDB; P34893; -.
DR SMR; P34893; -.
DR BioGRID; 23303; 1.
DR STRING; 3702.AT1G14980.1; -.
DR iPTMnet; P34893; -.
DR PaxDb; P34893; -.
DR PRIDE; P34893; -.
DR ProteomicsDB; 224485; -.
DR EnsemblPlants; AT1G14980.1; AT1G14980.1; AT1G14980.
DR GeneID; 838063; -.
DR Gramene; AT1G14980.1; AT1G14980.1; AT1G14980.
DR KEGG; ath:AT1G14980; -.
DR Araport; AT1G14980; -.
DR TAIR; locus:2196189; AT1G14980.
DR eggNOG; KOG1641; Eukaryota.
DR HOGENOM; CLU_132825_0_2_1; -.
DR InParanoid; P34893; -.
DR OMA; KVFYRQW; -.
DR OrthoDB; 1580867at2759; -.
DR PhylomeDB; P34893; -.
DR PRO; PR:P34893; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P34893; baseline and differential.
DR Genevisible; P34893; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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:0005507; F:copper ion binding; HDA:TAIR.
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 GO; GO:0009408; P:response to heat; IEP:TAIR.
DR CDD; cd00320; cpn10; 1.
DR Gene3D; 2.30.33.40; -; 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; Reference proteome; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..98
FT /note="10 kDa chaperonin, mitochondrial"
FT /id="PRO_0000174923"
FT REGION 18..94
FT /note="Cpn-10 domain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 98 AA; 10812 MW; C405C7C342A99F27 CRC64;
MMKRLIPTFN RILVQRVIQP AKTESGILLP EKSSKLNSGK VIAVGPGSRD KDGKLIPVSV
KEGDTVLLPE YGGTQVKLGE NEYHLFRDED VLGTLHED
