TCPQ_ARATH
ID TCPQ_ARATH Reviewed; 549 AA.
AC Q94K05; Q9SQR6;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=T-complex protein 1 subunit theta {ECO:0000303|PubMed:11599560};
DE Short=TCP-1-theta {ECO:0000303|PubMed:11599560};
DE AltName: Full=CCT-theta {ECO:0000303|PubMed:11599560};
DE AltName: Full=Chaperonin CCT8 {ECO:0000303|PubMed:21868675};
DE AltName: Full=Chaperonin containing TCP1 8 {ECO:0000303|PubMed:21868675};
DE AltName: Full=TCP1-ring complex {ECO:0000303|PubMed:21868675};
GN Name=CCT8 {ECO:0000303|PubMed:21868675};
GN Synonyms=TRIC {ECO:0000303|PubMed:21868675};
GN OrderedLocusNames=At3g03960 {ECO:0000312|Araport:AT3G03960};
GN ORFNames=T11I18.7 {ECO:0000312|EMBL:AAF05855.1};
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|EMBL:AAK43867.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000312|Proteomes:UP000006548};
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 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).
RN [5]
RP FUNCTION, MUTAGENESIS OF ALA-512, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP INTERACTION WITH CCT3; KNAT1; STM AND TTG1, AND SUBCELLULAR LOCATION.
RX PubMed=21868675; DOI=10.1126/science.1205727;
RA Xu X.M., Wang J., Xuan Z., Goldshmidt A., Borrill P.G., Hariharan N.,
RA Kim J.Y., Jackson D.;
RT "Chaperonins facilitate KNOTTED1 cell-to-cell trafficking and stem cell
RT function.";
RL Science 333:1141-1144(2011).
RN [6]
RP FUNCTION.
RX PubMed=22476462; DOI=10.4161/psb.19152;
RA Fichtenbauer D., Xu X.M., Jackson D., Kragler F.;
RT "The chaperonin CCT8 facilitates spread of tobamovirus infection.";
RL Plant Signal. Behav. 7:318-321(2012).
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. Contributes to stem cell maintenance through its impact on
CC transcription factors trafficking through plasmodesmata
CC (PubMed:21868675). Probably involved in refolding translocated,
CC partially unfolded proteins, including viral movement proteins
CC (PubMed:21868675, PubMed:22476462). {ECO:0000269|PubMed:21868675,
CC ECO:0000305|PubMed:22476462}.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC two stacked rings, 12 to 16 nm in diameter (PubMed:11599560). Interacts
CC with CCT3, KNAT1, STM and TTG1 (PubMed:21868675).
CC {ECO:0000269|PubMed:21868675, ECO:0000305|PubMed:11599560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21868675}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot meristems, root tip, vasculature
CC and leaf epidermis. {ECO:0000269|PubMed:21868675}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000305|PubMed:21868675}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC {ECO:0000255|RuleBase:RU004187}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF05855.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011698; AAF05855.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74018.1; -; Genomic_DNA.
DR EMBL; AF370490; AAK43867.1; -; mRNA.
DR EMBL; BT010388; AAQ56831.1; -; mRNA.
DR RefSeq; NP_566219.1; NM_111267.5.
DR AlphaFoldDB; Q94K05; -.
DR SMR; Q94K05; -.
DR IntAct; Q94K05; 7.
DR STRING; 3702.AT3G03960.1; -.
DR iPTMnet; Q94K05; -.
DR MetOSite; Q94K05; -.
DR PaxDb; Q94K05; -.
DR PRIDE; Q94K05; -.
DR ProteomicsDB; 234225; -.
DR EnsemblPlants; AT3G03960.1; AT3G03960.1; AT3G03960.
DR GeneID; 819549; -.
DR Gramene; AT3G03960.1; AT3G03960.1; AT3G03960.
DR KEGG; ath:AT3G03960; -.
DR Araport; AT3G03960; -.
DR TAIR; locus:2095948; AT3G03960.
DR eggNOG; KOG0362; Eukaryota.
DR HOGENOM; CLU_008891_4_2_1; -.
DR InParanoid; Q94K05; -.
DR OMA; WGLKYAV; -.
DR OrthoDB; 617040at2759; -.
DR PhylomeDB; Q94K05; -.
DR BRENDA; 3.6.4.B10; 399.
DR PRO; PR:Q94K05; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94K05; baseline and differential.
DR Genevisible; Q94K05; AT.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051050; P:positive regulation of transport; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd03341; TCP1_theta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012721; Chap_CCT_theta.
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; TIGR02346; chap_CCT_theta; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..549
FT /note="T-complex protein 1 subunit theta"
FT /id="PRO_0000431665"
FT MUTAGEN 512
FT /note="A->V: In cct8-1; impaired KNAT1 trafficking."
FT /evidence="ECO:0000269|PubMed:21868675"
SQ SEQUENCE 549 AA; 58939 MW; 315C50C84DC719EC CRC64;
MVGMSMQPYG IQSMLKEGYR HLSGLDEAVI KNIEACKELS TITRTSLGPN GMNKMVINHL
DKLFVTNDAA TIVNELEIQH PAAKLLVLAA KAQQEEIGDG ANLTISFAGE LLQNAEELIR
MGLHPSEIIS GYTKAVSKAV EILEQLVETG SETMDVRNKD EVISRMRAAV ASKQFGQEEI
ICSLVTDACI QVCPKNPTNF NVDNVRVSKL LGGGLHNSCI VRGMVLKSDA VGSIKRMEKA
KVAVFAGGVD TTATETKGTV LIHSAEQLEN YAKTEEAKVE ELIKAVAESG AKVIVSGGSI
GEMALHFCER YKIMVLKISS KFELRRFCRT AGAVAHLKLS RPSPEDLGYV DSISVEEIGG
VTVTIARNEE GGNSISTVVL RGSTDSILDD LERAVDDGVN TYKAMCRDSR IVPGAAATEI
ELAQRLKEYA NAEIGLDKYA ITKYAESFEF VPKTLADNAG LNAMEIIAAL YTGHGSGNTK
LGIDLEEGAC KDVSETKVWD LFATKLFALK YASDAACTVL RVDQIIMAKP AGGPRRDAAQ
AAGAGAEED
