CH60A_ARATH
ID CH60A_ARATH Reviewed; 577 AA.
AC P29197; Q9LIQ8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Chaperonin CPN60, mitochondrial;
DE AltName: Full=HSP60;
DE Flags: Precursor;
GN Name=CPN60; OrderedLocusNames=At3g23990; ORFNames=F14O13.18;
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; TISSUE=Seed;
RX PubMed=1349837; DOI=10.1007/bf00019202;
RA Prasad T.K., Stewart C.R.;
RT "cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial
RT chaperonin HSP60 and gene expression during seed germination and heat
RT shock.";
RL Plant Mol. Biol. 18:873-885(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP TYR-31.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Implicated in mitochondrial protein import and macromolecular
CC assembly. May facilitate the correct folding of imported proteins. May
CC also prevent misfolding and promote the refolding and proper assembly
CC of unfolded polypeptides generated under stress conditions in the
CC mitochondrial matrix.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC ECO:0000305|PubMed:25732537}.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; Z11547; CAA77646.1; -; mRNA.
DR EMBL; AP001297; BAB03017.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76842.1; -; Genomic_DNA.
DR EMBL; AY099594; AAM20445.1; -; mRNA.
DR EMBL; BT010398; AAQ56841.1; -; mRNA.
DR PIR; S20876; S20876.
DR RefSeq; NP_189041.1; NM_113304.5.
DR AlphaFoldDB; P29197; -.
DR SMR; P29197; -.
DR BioGRID; 7315; 73.
DR STRING; 3702.AT3G23990.1; -.
DR iPTMnet; P29197; -.
DR MetOSite; P29197; -.
DR PaxDb; P29197; -.
DR PRIDE; P29197; -.
DR ProteomicsDB; 220391; -.
DR EnsemblPlants; AT3G23990.1; AT3G23990.1; AT3G23990.
DR GeneID; 821983; -.
DR Gramene; AT3G23990.1; AT3G23990.1; AT3G23990.
DR KEGG; ath:AT3G23990; -.
DR Araport; AT3G23990; -.
DR TAIR; locus:2076081; AT3G23990.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; P29197; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; P29197; -.
DR PRO; PR:P29197; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P29197; baseline and differential.
DR Genevisible; P29197; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IPI:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0000373; P:Group II intron splicing; IPI:TAIR.
DR GO; GO:0007005; P:mitochondrion organization; TAS:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 32..577
FT /note="Chaperonin CPN60, mitochondrial"
FT /id="PRO_0000005009"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 567
FT /note="A -> G (in Ref. 1; CAA77646)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..574
FT /note="GG -> VV (in Ref. 1; CAA77646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 61281 MW; 829ABEE93BFBB5DA CRC64;
MYRFASNLAS KARIAQNARQ VSSRMSWSRN YAAKEIKFGV EARALMLKGV EDLADAVKVT
MGPKGRNVVI EQSWGAPKVT KDGVTVAKSI EFKDKIKNVG ASLVKQVANA TNDVAGDGTT
CATVLTRAIF AEGCKSVAAG MNAMDLRRGI SMAVDAVVTN LKSKARMIST SEEIAQVGTI
SANGEREIGE LIAKAMEKVG KEGVITIQDG KTLFNELEVV EGMKLDRGYT SPYFITNQKT
QKCELDDPLI LIHEKKISSI NSIVKVLELA LKRQRPLLIV SEDVESDALA TLILNKLRAG
IKVCAIKAPG FGENRKANLQ DLAALTGGEV ITDELGMNLE KVDLSMLGTC KKVTVSKDDT
VILDGAGDKK GIEERCEQIR SAIELSTSDY DKEKLQERLA KLSGGVAVLK IGGASEAEVG
EKKDRVTDAL NATKAAVEEG ILPGGGVALL YAARELEKLP TANFDQKIGV QIIQNALKTP
VYTIASNAGV EGAVIVGKLL EQDNPDLGYD AAKGEYVDMV KAGIIDPLKV IRTALVDAAS
VSSLLTTTEA VVVDLPKDES ESGAAGAGMG GMGGMDY
