CH60C_ARATH
ID CH60C_ARATH Reviewed; 572 AA.
AC Q93ZM7; Q9LRW0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Chaperonin CPN60-like 2, mitochondrial;
DE AltName: Full=HSP60-like 2;
DE Flags: Precursor;
GN OrderedLocusNames=At3g13860; ORFNames=MCP4.9;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC ECO:0000305|PubMed:25732537}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL09728.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB028610; BAB02911.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75427.1; -; Genomic_DNA.
DR EMBL; AY056782; AAL09728.1; ALT_FRAME; mRNA.
DR EMBL; AY094453; AAM19824.1; -; mRNA.
DR EMBL; BT015923; AAU95459.1; -; mRNA.
DR RefSeq; NP_566466.1; NM_112240.4.
DR AlphaFoldDB; Q93ZM7; -.
DR SMR; Q93ZM7; -.
DR BioGRID; 5933; 18.
DR IntAct; Q93ZM7; 3.
DR STRING; 3702.AT3G13860.1; -.
DR MetOSite; Q93ZM7; -.
DR PaxDb; Q93ZM7; -.
DR PRIDE; Q93ZM7; -.
DR ProteomicsDB; 220612; -.
DR EnsemblPlants; AT3G13860.1; AT3G13860.1; AT3G13860.
DR GeneID; 820599; -.
DR Gramene; AT3G13860.1; AT3G13860.1; AT3G13860.
DR KEGG; ath:AT3G13860; -.
DR Araport; AT3G13860; -.
DR TAIR; locus:2087959; AT3G13860.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; Q93ZM7; -.
DR OMA; SSAMFDK; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; Q93ZM7; -.
DR PRO; PR:Q93ZM7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93ZM7; baseline and differential.
DR Genevisible; Q93ZM7; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
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;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 32..572
FT /note="Chaperonin CPN60-like 2, mitochondrial"
FT /id="PRO_0000045793"
FT CONFLICT 273..274
FT /note="SS -> KY (in Ref. 3; AAL09728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 60466 MW; 7CA7CAF188753805 CRC64;
MYRVLSKLSS SIGSSTSRKL VSGRIISSRN YAAKDISFGI GARAAMLQGV SEVAEAVKVT
MGPKGRNVII ESSYGGPKIT KDGVTVAKSI SFQAKAKNIG AELVKQVASA TNKVAGDGTT
CATVLTQAIL IEGCKSVAAG VNVMDLRVGI NMAIAAVVSD LKSRAVMIST PEEITQVATI
SANGEREIGE LIARAMEKVG KEGVITVADG NTLDNELEVV EGMKLARGYI SPYFITDEKT
QKCELENPII LIHEKKISDI NSLLKVLEAA VKSSRPLLIV AEDVESDALA MLILNKHHGG
LKVCAIKAPG FGDNRKASLD DLAVLTGAEV ISEERGLSLE KIRPELLGTA KKVTVTRDDT
IILHGGGDKK LIEERCEELR SANEKSTSTF DQEKTQERLS KLSGGVAVFK VGGASESEVG
ERKDRVTDAL NATRAAVEEG IIPGGGVALL YATKALDNLQ TENEDQRRGV QIVQNALKAP
AFTIAANAGY DGSLVVGKLL EQDDCNFGFD AAKGKYVDMV KAGIIDPVKV IRTALTDAAS
VSLLLTTTEA SVLVKADENT PNHVPDMASM GM
