TCPH_ARATH
ID TCPH_ARATH Reviewed; 557 AA.
AC Q9SF16; F4J7H2;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=T-complex protein 1 subunit eta {ECO:0000303|PubMed:11599560};
DE Short=TCP-1-eta {ECO:0000303|PubMed:11599560};
DE AltName: Full=CCT-eta {ECO:0000303|PubMed:11599560};
DE AltName: Full=Chaperonin CCT7 {ECO:0000303|PubMed:21868675};
GN Name=CCT7 {ECO:0000303|PubMed:21868675};
GN OrderedLocusNames=At3g11830 {ECO:0000312|Araport:AT3G11830};
GN ORFNames=F26K24.12 {ECO:0000312|EMBL:AAF23199.1};
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|Proteomes:UP000006548};
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;
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] (ISOFORM 1).
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 INTERACTION WITH KNAT1.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 (PubMed:11599560). Interacts
CC with KNAT1 (PubMed:21868675). {ECO:0000269|PubMed:21868675,
CC ECO:0000305|PubMed:11599560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SF16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SF16-2; Sequence=VSP_057340;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC {ECO:0000255|RuleBase:RU004187}.
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DR EMBL; AC016795; AAF23199.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75105.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75106.1; -; Genomic_DNA.
DR EMBL; AY070472; AAL49938.1; -; mRNA.
DR EMBL; AY102137; AAM26704.1; -; mRNA.
DR RefSeq; NP_001189863.1; NM_001202934.1. [Q9SF16-2]
DR RefSeq; NP_187789.1; NM_112016.5. [Q9SF16-1]
DR AlphaFoldDB; Q9SF16; -.
DR SMR; Q9SF16; -.
DR IntAct; Q9SF16; 11.
DR STRING; 3702.AT3G11830.1; -.
DR iPTMnet; Q9SF16; -.
DR PaxDb; Q9SF16; -.
DR PRIDE; Q9SF16; -.
DR ProteomicsDB; 234253; -. [Q9SF16-1]
DR EnsemblPlants; AT3G11830.1; AT3G11830.1; AT3G11830. [Q9SF16-1]
DR EnsemblPlants; AT3G11830.2; AT3G11830.2; AT3G11830. [Q9SF16-2]
DR GeneID; 820356; -.
DR Gramene; AT3G11830.1; AT3G11830.1; AT3G11830. [Q9SF16-1]
DR Gramene; AT3G11830.2; AT3G11830.2; AT3G11830. [Q9SF16-2]
DR KEGG; ath:AT3G11830; -.
DR Araport; AT3G11830; -.
DR TAIR; locus:2081491; AT3G11830.
DR eggNOG; KOG0361; Eukaryota.
DR HOGENOM; CLU_008891_7_1_1; -.
DR InParanoid; Q9SF16; -.
DR OMA; HRKGNTW; -.
DR PhylomeDB; Q9SF16; -.
DR BRENDA; 3.6.4.B10; 399.
DR PRO; PR:Q9SF16; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF16; baseline and differential.
DR Genevisible; Q9SF16; 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; cd03340; TCP1_eta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012720; Chap_CCT_eta.
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; TIGR02345; chap_CCT_eta; 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; Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..557
FT /note="T-complex protein 1 subunit eta"
FT /id="PRO_0000431664"
FT REGION 529..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 417..418
FT /note="Missing (in isoform 2)"
FT /id="VSP_057340"
SQ SEQUENCE 557 AA; 59776 MW; DC5840417FB62769 CRC64;
MASMMQPQII LLKEGTDTSQ GKAQLVSNIN ACTAVGDVVR TTLGPRGMDK LIHDDKGSVT
ISNDGATIMK LLDIVHPAAK ILVDIAKSQD SEVGDGTTTV VLLAAEFLKE AKPFIEDGVH
AQNLIRSYRT ASTLAIAKVK ELAVSIEGKS VEEKKGLLAK CAATTLSSKL IGGEKEFFAT
MVVDAVMAIG NDDRLNLIGI KKVPGGNMRD SFLVDGVAFK KTFSYAGFEQ QPKKFLNPKI
LLLNIELELK SEKENAEIRL SDPSQYQSIV DAEWNIIYDK LDKCVESGAK VVLSRLAIGD
LATQYFADRD IFCAGRVAEE DLNRVAAAAG GTVQTSVNNI IDEVLGTCEI FEEKQVGGER
FNIFSGCPSG RTATIVLRGG ADQFIEEAER SLHDAIMIVR RAVKNSTVVP GGGAIDMEIS
KYLRQHSRTI AGKSQLFINS YAKALEVIPR QLCDNAGFDA TDVLNKLRQK HAMQSGEGAS
YGVDINTGGI ADSFANFVWE PAVVKINAIN AATEAACLIL SVDETVKNPK SESAQGDAAG
AMGRGRGGGR GRGMRRR
