ID   CPNA2_ARATH             Reviewed;         575 AA.
AC   Q56XV8;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Chaperonin 60 subunit alpha 2, chloroplastic;
DE            Short=CPN-60 alpha 2;
DE   AltName: Full=Protein EMBRYO DEFECTIVE 3007;
DE   Flags: Precursor;
GN   Name=CPN60A2; Synonyms=Cpn60-A(1), EMB3007; OrderedLocusNames=At5g18820;
GN   ORFNames=F17K4.70;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11599560; DOI=10.1379/1466-1268(2001)006<0190:attiai>2.0.co;2;
RA   Hill J.E., Hemmingsen S.M.;
RT   "Arabidopsis thaliana type I and II chaperonins.";
RL   Cell Stress Chaperones 6:190-200(2001).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=21483722; DOI=10.1371/journal.pbio.1001040;
RA   Peng L., Fukao Y., Myouga F., Motohashi R., Shinozaki K., Shikanai T.;
RT   "A chaperonin subunit with unique structures is essential for folding of a
RT   specific substrate.";
RL   PLoS Biol. 9:E1001040-E1001040(2011).
CC   -!- FUNCTION: Involved in protein assisted folding. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the Cpn60 complex composed of 7 alpha and 7 beta
CC       subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; AC068655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92616.1; -; Genomic_DNA.
DR   EMBL; AK221565; BAD94998.1; -; mRNA.
DR   RefSeq; NP_197383.1; NM_121887.3.
DR   AlphaFoldDB; Q56XV8; -.
DR   SMR; Q56XV8; -.
DR   BioGRID; 17276; 3.
DR   IntAct; Q56XV8; 2.
DR   STRING; 3702.AT5G18820.1; -.
DR   PaxDb; Q56XV8; -.
DR   PRIDE; Q56XV8; -.
DR   EnsemblPlants; AT5G18820.1; AT5G18820.1; AT5G18820.
DR   GeneID; 832000; -.
DR   Gramene; AT5G18820.1; AT5G18820.1; AT5G18820.
DR   KEGG; ath:AT5G18820; -.
DR   Araport; AT5G18820; -.
DR   TAIR; locus:2144955; AT5G18820.
DR   eggNOG; KOG0356; Eukaryota.
DR   HOGENOM; CLU_016503_1_1_1; -.
DR   InParanoid; Q56XV8; -.
DR   OMA; IIKVGAH; -.
DR   OrthoDB; 415781at2759; -.
DR   PhylomeDB; Q56XV8; -.
DR   PRO; PR:Q56XV8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q56XV8; baseline and differential.
DR   Genevisible; Q56XV8; AT.
DR   GO; GO:0009507; C:chloroplast; IDA: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   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; 2.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..575
FT                   /note="Chaperonin 60 subunit alpha 2, chloroplastic"
FT                   /id="PRO_0000413683"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  61193 MW;  2B21F1FDDBC96EB6 CRC64;
     MFAVSPSSFS PTTISPRRSG QRNEPRKFSV VRAGAKRILY GKDSREKLQA GIDKLADAVS
     ITLGPRGRNV VLAEKDTIKV INDGVTIAKS IELPDTIENA GATLIQEVAI KMNESAGDGT
     TTAIILAREM IKAGSLAIAF GANAVSVKNG MNKTVKELVR VLQMKSIPVQ GKNDIKAVAS
     ISAGNDEFVG NLIAETVEKI GPDGVISIES SSTSETSVIV EEGMKFDKGY MSPHFITNQE
     KSTVEFDKAK ILVTDQKITS AKELVPLLEK TSQLSVPLLI IAEDISAEVL EILVVNKKQG
     LINVAVVKCP GMLDGKKALL QDIALMTGAD YLSGDLGMSL MGATSDQLGV SRRVVITANS
     TTIVADASTK PEIQARIAQM KKDLAETDNS YLSKKIAERI AKLTGGVAVI KVGGHTETEL
     EDRKLRIEDA KNATFAAMRE GIVPGGGATY IHLLDEIPRI KKNLMEDSYE QIGADIVAMA
     LTAPAMAIAT NAGVDGSVVV QKTRELEWRS GYNAMSGKYE DLLNAGIADP CRVSRFALQN
     AVSVAGIILT TQAVLVEKIK QPKPAVPQVP GIPTS