CH102_ARATH
ID CH102_ARATH Reviewed; 139 AA.
AC O80504; Q94F15;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=10 kDa chaperonin 2, chloroplastic {ECO:0000305};
DE AltName: Full=Chloroplast chaperonin 10 {ECO:0000303|PubMed:11402030};
DE Short=Chl-Cpn10 {ECO:0000303|PubMed:11402030};
DE Flags: Precursor;
GN Name=CPN10-2 {ECO:0000305}; Synonyms=CPN10 {ECO:0000303|PubMed:11402030};
GN OrderedLocusNames=At2g44650 {ECO:0000312|Araport:AT2G44650};
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11402030; DOI=10.1074/jbc.m102330200;
RA Koumoto Y., Shimada T., Kondo M., Hara-Nishimura I., Nishimura M.;
RT "Chloroplasts have a novel Cpn10 in addition to Cpn20 as co-chaperonins in
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 276:29688-29694(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=23783410; DOI=10.1007/s11103-013-0082-8;
RA Zhang X.F., Jiang T., Wu Z., Du S.Y., Yu Y.T., Jiang S.C., Lu K.,
RA Feng X.J., Wang X.F., Zhang D.P.;
RT "Cochaperonin CPN20 negatively regulates abscisic acid signaling in
RT Arabidopsis.";
RL Plant Mol. Biol. 83:205-218(2013).
CC -!- FUNCTION: Functions as co-chaperone for protein folding in
CC chloroplasts. {ECO:0000269|PubMed:11402030}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11402030}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and stems (PubMed:11402030).
CC Expressed at low levels in germinating seeds, seedlings, rosettes
CC leaves, flowers and siliques (PubMed:23783410).
CC {ECO:0000269|PubMed:11402030, ECO:0000269|PubMed:23783410}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR EMBL; AB051163; BAB55457.1; -; mRNA.
DR EMBL; AC003672; AAC27467.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10451.1; -; Genomic_DNA.
DR EMBL; AF386970; AAK62415.1; -; mRNA.
DR EMBL; AY072530; AAL66945.1; -; mRNA.
DR PIR; T01592; T01592.
DR RefSeq; NP_566022.1; NM_130029.4.
DR AlphaFoldDB; O80504; -.
DR SMR; O80504; -.
DR STRING; 3702.AT2G44650.1; -.
DR PaxDb; O80504; -.
DR PRIDE; O80504; -.
DR ProteomicsDB; 224476; -.
DR EnsemblPlants; AT2G44650.1; AT2G44650.1; AT2G44650.
DR GeneID; 819073; -.
DR Gramene; AT2G44650.1; AT2G44650.1; AT2G44650.
DR KEGG; ath:AT2G44650; -.
DR Araport; AT2G44650; -.
DR TAIR; locus:2042381; AT2G44650.
DR eggNOG; KOG1641; Eukaryota.
DR HOGENOM; CLU_119260_0_0_1; -.
DR InParanoid; O80504; -.
DR OMA; GCLRIKA; -.
DR OrthoDB; 1449075at2759; -.
DR PhylomeDB; O80504; -.
DR PRO; PR:O80504; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80504; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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:0019904; F:protein domain specific binding; IPI:CAFA.
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:0006457; P:protein folding; IDA: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; IPR011032; GroES-like_sf.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Chloroplast; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..139
FT /note="10 kDa chaperonin 2, chloroplastic"
FT /id="PRO_0000438194"
FT REGION 51..138
FT /note="Cpn-10 domain"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="N -> D (in Ref. 4; AAK62415/AAL66945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 139 AA; 15049 MW; 79D6CBD19E5C3CF0 CRC64;
MASTFVCSLP NPFFAFPVKA TTPSTANHTL LGSRRGCLRI KAISTKWEPT KVVPQADRVL
VRLEDLPIKS SGGVLLPKAA VKFERYLTGE IISVGSEVGQ QVGPGKRVLF SDVSAYEVDL
GTDARHCFCK ESDLLALVE
