TCPZB_ARATH
ID TCPZB_ARATH Reviewed; 535 AA.
AC Q8L7N0; Q9LFR8;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=T-complex protein 1 subunit zeta 2 {ECO:0000303|PubMed:11599560};
DE Short=TCP-1-zeta 2 {ECO:0000303|PubMed:11599560};
DE AltName: Full=CCT-zeta 2 {ECO:0000303|PubMed:11599560};
DE AltName: Full=Chaperonin CCT6B {ECO:0000305};
GN Name=CCT6B {ECO:0000305};
GN OrderedLocusNames=At5g16070 {ECO:0000312|Araport:AT5G16070};
GN ORFNames=F1N13.210 {ECO:0000312|EMBL:CAC01806.1};
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:AAM91565.1};
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;
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01806.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391145; CAC01806.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92243.1; -; Genomic_DNA.
DR EMBL; AY128362; AAM91565.1; -; mRNA.
DR EMBL; BT008893; AAP68332.1; -; mRNA.
DR PIR; T51390; T51390.
DR RefSeq; NP_197111.2; NM_121612.2.
DR AlphaFoldDB; Q8L7N0; -.
DR SMR; Q8L7N0; -.
DR IntAct; Q8L7N0; 4.
DR STRING; 3702.AT5G16070.1; -.
DR PaxDb; Q8L7N0; -.
DR PRIDE; Q8L7N0; -.
DR ProMEX; Q8L7N0; -.
DR ProteomicsDB; 234383; -.
DR EnsemblPlants; AT5G16070.1; AT5G16070.1; AT5G16070.
DR GeneID; 831464; -.
DR Gramene; AT5G16070.1; AT5G16070.1; AT5G16070.
DR KEGG; ath:AT5G16070; -.
DR Araport; AT5G16070; -.
DR TAIR; locus:2146082; AT5G16070.
DR eggNOG; KOG0359; Eukaryota.
DR HOGENOM; CLU_008891_3_1_1; -.
DR InParanoid; Q8L7N0; -.
DR OMA; LMEVANT; -.
DR OrthoDB; 482152at2759; -.
DR PhylomeDB; Q8L7N0; -.
DR PRO; PR:Q8L7N0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7N0; baseline and differential.
DR Genevisible; Q8L7N0; AT.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; 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; cd03342; TCP1_zeta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012722; Chap_CCT_zeta.
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; TIGR02347; chap_CCT_zeta; 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..535
FT /note="T-complex protein 1 subunit zeta 2"
FT /id="PRO_0000431663"
SQ SEQUENCE 535 AA; 58928 MW; 333A631870C99FF0 CRC64;
MSVRVLNPNA EVLNKSAALH MTINAAKGLQ DVLKSNLGPK GTIKMLVGGS GDIKLTKDGN
TLLKEMQIQN PTAIMIARTA VAQDDISGDG TTSTVIFIGE LMKQSERCID EGMHPRVLVD
GFEIAKRATL QFLDNFKTPV VMGDEVDKEI LKMVARTTLR TKLYEGLADQ LTDIVVNSVL
CIRKPEEAID LFMVEIMHMR HKFDVDTRLV EGLVLDHGSR HPDMKRRAEN CHILTCNVSL
EYEKSEINAG FFYSNAEQRE AMVTAERRSV DERVKKIIEL KKKVCGDNDN FVVINQKGID
PPSLDLLARE GIIGLRRAKR RNMERLVLAC GGEAVNSVDD LTPESLGWAG LVYEHVLGEE
KYTFVEQVKN PNSCTILIKG PNDHTIAQIK DAVRDGLRSV KNTIEDECVV LGAGAFEVAA
RQHLLNEVKK TVQGRAQLGV EAFANALLVV PKTLAENAGL DTQDVIISLT SEHDKGNVVG
LNLQDGEPID PQLAGIFDNY SVKRQLINSG PVIASQLLLV DEVIRAGRNM RKPTA