TCPE_ARATH
ID TCPE_ARATH Reviewed; 535 AA.
AC O04450; F4IAR7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=T-complex protein 1 subunit epsilon {ECO:0000303|PubMed:11599560};
DE Short=TCP-1-epsilon {ECO:0000303|PubMed:11599560};
DE AltName: Full=CCT-epsilon {ECO:0000303|PubMed:11599560};
DE AltName: Full=Chaperonin CCT5 {ECO:0000305};
GN Name=CCT5 {ECO:0000305};
GN OrderedLocusNames=At1g24510 {ECO:0000312|Araport:AT1G24510};
GN ORFNames=F21J9.12;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O04450-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O04450-2; Sequence=VSP_057339;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; AC000103; AAF97977.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30541.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30542.1; -; Genomic_DNA.
DR EMBL; AY075611; AAL91625.1; -; mRNA.
DR EMBL; BT000818; AAN33193.1; -; mRNA.
DR RefSeq; NP_173859.1; NM_102295.6. [O04450-1]
DR RefSeq; NP_973907.1; NM_202178.3. [O04450-2]
DR AlphaFoldDB; O04450; -.
DR SMR; O04450; -.
DR BioGRID; 24304; 66.
DR IntAct; O04450; 6.
DR STRING; 3702.AT1G24510.1; -.
DR iPTMnet; O04450; -.
DR PaxDb; O04450; -.
DR PRIDE; O04450; -.
DR ProteomicsDB; 234224; -. [O04450-1]
DR EnsemblPlants; AT1G24510.1; AT1G24510.1; AT1G24510. [O04450-1]
DR EnsemblPlants; AT1G24510.2; AT1G24510.2; AT1G24510. [O04450-2]
DR GeneID; 839066; -.
DR Gramene; AT1G24510.1; AT1G24510.1; AT1G24510. [O04450-1]
DR Gramene; AT1G24510.2; AT1G24510.2; AT1G24510. [O04450-2]
DR KEGG; ath:AT1G24510; -.
DR Araport; AT1G24510; -.
DR TAIR; locus:2024051; AT1G24510.
DR eggNOG; KOG0357; Eukaryota.
DR InParanoid; O04450; -.
DR OMA; QTGSNDM; -.
DR PhylomeDB; O04450; -.
DR BRENDA; 3.6.4.B10; 399.
DR PRO; PR:O04450; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04450; baseline and differential.
DR Genevisible; O04450; AT.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd03339; TCP1_epsilon; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012718; Chap_CCT_epsi.
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; TIGR02343; chap_CCT_epsi; 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 Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..535
FT /note="T-complex protein 1 subunit epsilon"
FT /id="PRO_0000128350"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform 2)"
FT /id="VSP_057339"
SQ SEQUENCE 535 AA; 59384 MW; 1CB56343A3AF1DC3 CRC64;
MALAFDEFGR PFIILREQDQ KTRLRGIDAQ KANIAAGKAV ARILRSSLGP KGMDKMLQGP
DGDITITNDG ATILEQMDVD NQIAKLMVEL SRSQDYEIGD GTTGVVVMAG ALLEQAERQL
DRGIHPIRIA EGYEMASRVA VEHLERIAQK FEFDVNNYEP LVQTCMTTLS SKIVNRCKRS
LAEIAVKAVL AVADLERRDV NLDLIKVEGK VGGKLEDTEL IYGILIDKDM SHPQMPKQIE
DAHIAILTCP FEPPKPKTKH KVDIDTVEKF ETLRKQEQQY FDEMVQKCKD VGATLVICQW
GFDDEANHLL MHRNLPAVRW VGGVELELIA IATGGRIVPR FQELTPEKLG KAGVVREKSF
GTTKERMLYI EHCANSKAVT VFIRGGNKMM IEETKRSIHD ALCVARNLIR NKSIVYGGGA
AEIACSLAVD AAADKYPGVE QYAIRAFAEA LDSVPMALAE NSGLQPIETL SAVKSQQIKE
NIPFYGIDCN DVGTNDMREQ NVFETLIGKQ QQILLATQVV KMILKIDDVI SNSEY
