ID   TCPD_ARATH              Reviewed;         536 AA.
AC   Q9LV21; Q8L994;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=T-complex protein 1 subunit delta {ECO:0000303|PubMed:11599560};
DE            Short=TCP-1-delta {ECO:0000303|PubMed:11599560};
DE   AltName: Full=CCT-delta {ECO:0000303|PubMed:11599560};
DE   AltName: Full=Chaperonin CCT4 {ECO:0000305};
GN   Name=CCT4 {ECO:0000305};
GN   OrderedLocusNames=At3g18190 {ECO:0000312|Araport:AT3G18190}; ORFNames=MRC8;
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
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   [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].
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.
RN   [5]
RP   GENE FAMILY, NOMENCLATURE, AND SUBUNIT.
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).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin. {ECO:0000305}.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter.
CC       {ECO:0000305|PubMed:11599560}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC       {ECO:0000255|RuleBase:RU004187}.
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DR   EMBL; AB020749; BAB02032.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76061.1; -; Genomic_DNA.
DR   EMBL; AY099877; AAM20728.1; -; mRNA.
DR   EMBL; BT003418; AAO30081.1; -; mRNA.
DR   EMBL; AY088570; AAM66101.1; -; mRNA.
DR   RefSeq; NP_188447.1; NM_112702.3.
DR   AlphaFoldDB; Q9LV21; -.
DR   SMR; Q9LV21; -.
DR   IntAct; Q9LV21; 4.
DR   STRING; 3702.AT3G18190.1; -.
DR   iPTMnet; Q9LV21; -.
DR   MetOSite; Q9LV21; -.
DR   PaxDb; Q9LV21; -.
DR   PRIDE; Q9LV21; -.
DR   ProteomicsDB; 234201; -.
DR   EnsemblPlants; AT3G18190.1; AT3G18190.1; AT3G18190.
DR   GeneID; 821346; -.
DR   Gramene; AT3G18190.1; AT3G18190.1; AT3G18190.
DR   KEGG; ath:AT3G18190; -.
DR   Araport; AT3G18190; -.
DR   TAIR; locus:2092697; AT3G18190.
DR   eggNOG; KOG0358; Eukaryota.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; Q9LV21; -.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 511484at2759; -.
DR   PhylomeDB; Q9LV21; -.
DR   BRENDA; 3.6.4.B10; 399.
DR   PRO; PR:Q9LV21; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LV21; baseline and differential.
DR   Genevisible; Q9LV21; AT.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03338; TCP1_delta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012717; Chap_CCT_delta.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
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   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02342; chap_CCT_delta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..536
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000431661"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        8
FT                   /note="M -> I (in Ref. 4; AAM66101)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   536 AA;  57775 MW;  68939F47760168D8 CRC64;
     MAAVAAPMAS KPRGSKAESF VDNKRREDIR FANINSARAV SDAVRTSLGP KGMDKMISTA
     NGEVIITNDG ATILNKMEVL QPAAKMLVEL SKSQDSAAGD GTTTVVVIAG ALLKECQSLL
     TNGIHPTVIS DSLHKACGKA IDILTAMAVP VELTDRDSLV KSASTSLNSK VVSQYSTLLA
     PLAVDAVLSV IDPEKPEIVD LRDIKIVKKL GGTVDDTHTV KGLVFDKKVS RAAGGPTRVE
     NAKIAVIQFQ ISPPKTDIEQ SIVVSDYTQM DRILKEERNY ILGMIKKIKA TGCNVLLIQK
     SILRDAVTDL SLHYLAKAKI MVIKDVERDE IEFVTKTLNC LPIANIEHFR AEKLGHADLV
     EEASLGDGKI LKITGIKDMG RTTSVLVRGS NQLVLDEAER SLHDALCVVR CLVSKRFLIA
     GGGAPEIELS RQLGAWAKVL HGMEGYCVKS FAEALEVIPY TLAENAGLNP IAIVTELRNK
     HAQGEINAGI NVRKGQITNI LEENVVQPLL VSTSAITLAT ECVRMILKID DIVTVR