TCPA_ARATH
ID TCPA_ARATH Reviewed; 545 AA.
AC P28769; Q5E917; Q8H0U0; Q9LJZ6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=T-complex protein 1 subunit alpha {ECO:0000303|PubMed:11599560};
DE Short=TCP-1-alpha {ECO:0000303|PubMed:11599560};
DE AltName: Full=CCT-alpha {ECO:0000303|PubMed:11599560};
DE AltName: Full=Chaperonin CCT1 {ECO:0000305};
GN Name=CCT1 {ECO:0000305};
GN OrderedLocusNames=At3g20050 {ECO:0000312|Araport:AT3G20050};
GN ORFNames=MAL21.5 {ECO:0000312|EMBL:BAA21772.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1487154; DOI=10.1016/0378-1119(92)90231-d;
RA Mori M., Murata K., Kubota H., Yamamoto A., Matsushiro A., Morita T.;
RT "Cloning of a cDNA encoding the Tcp-1 (t complex polypeptide 1) homologue
RT of Arabidopsis thaliana.";
RL Gene 122:381-382(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Mori M., Kuno N., Murata K., Kubota H., Furuya M., Matsushiro A.,
RA Morita T.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(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. {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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01862.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D11351; BAA01955.1; -; mRNA.
DR EMBL; D11352; BAA21772.1; -; Genomic_DNA.
DR EMBL; AP000383; BAB01862.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76324.1; -; Genomic_DNA.
DR EMBL; BT002052; AAN72063.1; -; mRNA.
DR EMBL; BT021103; AAX12873.1; -; mRNA.
DR PIR; JN0448; JN0448.
DR RefSeq; NP_188640.1; NM_112896.4.
DR AlphaFoldDB; P28769; -.
DR SMR; P28769; -.
DR BioGRID; 6876; 74.
DR IntAct; P28769; 11.
DR STRING; 3702.AT3G20050.1; -.
DR iPTMnet; P28769; -.
DR PaxDb; P28769; -.
DR PRIDE; P28769; -.
DR ProteomicsDB; 233018; -.
DR EnsemblPlants; AT3G20050.1; AT3G20050.1; AT3G20050.
DR GeneID; 821544; -.
DR Gramene; AT3G20050.1; AT3G20050.1; AT3G20050.
DR KEGG; ath:AT3G20050; -.
DR Araport; AT3G20050; -.
DR TAIR; locus:2087605; AT3G20050.
DR eggNOG; KOG0360; Eukaryota.
DR HOGENOM; CLU_008891_7_3_1; -.
DR InParanoid; P28769; -.
DR OMA; KNYKNYG; -.
DR OrthoDB; 335406at2759; -.
DR PhylomeDB; P28769; -.
DR BRENDA; 3.6.4.B10; 399.
DR PRO; PR:P28769; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P28769; baseline and differential.
DR Genevisible; P28769; 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; cd03335; TCP1_alpha; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012715; Chap_CCT_alpha.
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; TIGR02340; chap_CCT_alpha; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..545
FT /note="T-complex protein 1 subunit alpha"
FT /id="PRO_0000128313"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 289
FT /note="I -> V (in Ref. 5; AAN72063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 59229 MW; 250686F991B78DDF CRC64;
MSISAQNPDI SGDRQSGQDV RTQNVMACQA VSNIVKTSLG PVGLDKMLVD DIGDVTITND
GATILRMLEV EHPAAKVLVE LAELQDREVG DGTTSVVIVA AELLKRANDL VRNKIHPTSI
ISGYRLAMRE SCKYIEEKLV TKVEKLGKVP LINCAKTSMS SKLISGDSDF FANLVVEAVL
SVKMTNQRGE IKYPIKGINI LKAHGQSARD SYLLNGYALN TGRAAQGMPL RVSPAKIACL
DFNLQKTKMQ LGVQVVVNDP RELEKIRQRE ADMTKERIEK LLKAGANVIL TTKGIDDMAL
KYFVEAGAIA VRRVRKEDMR HVAKATGATL VTTFADMEGE ETFDPAHLGS ADEVVEERIA
DDDVILIKGT KTSSAVSLIL RGANDYMLDE MERALHDALC IVKRTLESNT VVAGGGAVES
ALSVYLEHLA TTLGSREQLA IAEFADALLI IPKVLAVNAA KDATELVAKL RAYHHTAQTK
ADKKHYSSMG LDLVNGTIRN NLEAGVIEPA MSKVKIIQFA TEAAITILRI DDMIKLVKDE
SQGEE
