TCPE_MOUSE
ID TCPE_MOUSE Reviewed; 541 AA.
AC P80316; Q3TIE0; Q3U530; Q3UCU4; Q3UJK9; Q3UWA9; Q542K3; Q6ZQJ1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=T-complex protein 1 subunit epsilon;
DE Short=TCP-1-epsilon;
DE AltName: Full=CCT-epsilon;
GN Name=Cct5; Synonyms=Ccte, Kiaa0098;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RX PubMed=7953530; DOI=10.1016/s0960-9822(94)00024-2;
RA Kubota H., Hynes G., Carne A., Ashworth A., Willison K.R.;
RT "Identification of six Tcp-1-related genes encoding divergent subunits of
RT the TCP-1-containing chaperonin.";
RL Curr. Biol. 4:89-99(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10336634; DOI=10.1046/j.1432-1327.1999.00405.x;
RA Kubota H., Yokota S., Yanagi H., Yura T.;
RT "Structures and co-regulated expression of the genes encoding mouse
RT cytosolic chaperonin CCT subunits.";
RL Eur. J. Biochem. 262:492-500(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Bone marrow, Colon, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 28-35; 50-59; 203-210; 248-261; 264-275; 324-340;
RP 353-368; 382-388 AND 497-513, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH DNAAF4.
RX PubMed=23872636; DOI=10.1038/ng.2707;
RA Tarkar A., Loges N.T., Slagle C.E., Francis R., Dougherty G.W.,
RA Tamayo J.V., Shook B., Cantino M., Schwartz D., Jahnke C., Olbrich H.,
RA Werner C., Raidt J., Pennekamp P., Abouhamed M., Hjeij R., Kohler G.,
RA Griese M., Li Y., Lemke K., Klena N., Liu X., Gabriel G., Tobita K.,
RA Jaspers M., Morgan L.C., Shapiro A.J., Letteboer S.J., Mans D.A.,
RA Carson J.L., Leigh M.W., Wolf W.E., Chen S., Lucas J.S., Onoufriadis A.,
RA Plagnol V., Schmidts M., Boldt K., Roepman R., Zariwala M.A., Lo C.W.,
RA Mitchison H.M., Knowles M.R., Burdine R.D., Loturco J.J., Omran H.;
RT "DYX1C1 is required for axonemal dynein assembly and ciliary motility.";
RL Nat. Genet. 45:995-1003(2013).
CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC molecular chaperone complex that assists the folding of proteins upon
CC ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1,
CC thereby regulating telomere maintenance. As part of the TRiC complex
CC may play a role in the assembly of BBSome, a complex involved in
CC ciliogenesis regulating transports vesicles to the cilia. The TRiC
CC complex plays a role in the folding of actin and tubulin.
CC {ECO:0000250|UniProtKB:P48643}.
CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC rings, 12 to 16 nm in diameter. Interacts with PACRG (By similarity).
CC Interacts with DNAAF4 (PubMed:23872636). Interacts with DLEC1 (By
CC similarity). {ECO:0000250|UniProtKB:P48643,
CC ECO:0000269|PubMed:23872636}.
CC -!- INTERACTION:
CC P80316; Q9JMB1: Theg; NbExp=2; IntAct=EBI-772379, EBI-1390549;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48643}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P48643}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Ubiquitinated by the DCX(DCAF12) complex specifically recognizes
CC the diglutamate (Glu-Glu) at the C-terminus, leading to its
CC degradation. {ECO:0000250|UniProtKB:P48643}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97866.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z31555; CAA83430.1; -; mRNA.
DR EMBL; AB022158; BAA81876.1; -; Genomic_DNA.
DR EMBL; AK129056; BAC97866.1; ALT_INIT; mRNA.
DR EMBL; AK088184; BAC40194.1; -; mRNA.
DR EMBL; AK133857; BAE21891.1; -; mRNA.
DR EMBL; AK136493; BAE23007.1; -; mRNA.
DR EMBL; AK145445; BAE26441.1; -; mRNA.
DR EMBL; AK146405; BAE27146.1; -; mRNA.
DR EMBL; AK146425; BAE27159.1; -; mRNA.
DR EMBL; AK150390; BAE29518.1; -; mRNA.
DR EMBL; AK153911; BAE32250.1; -; mRNA.
DR EMBL; AK167895; BAE39906.1; -; mRNA.
DR EMBL; BC094427; AAH94427.1; -; mRNA.
DR CCDS; CCDS27411.1; -.
DR PIR; S43061; S43061.
DR RefSeq; NP_001334964.1; NM_001348035.1.
DR RefSeq; NP_031663.1; NM_007637.3.
DR AlphaFoldDB; P80316; -.
DR SMR; P80316; -.
DR BioGRID; 198568; 40.
DR CORUM; P80316; -.
DR IntAct; P80316; 14.
DR MINT; P80316; -.
DR STRING; 10090.ENSMUSP00000022842; -.
DR iPTMnet; P80316; -.
DR PhosphoSitePlus; P80316; -.
DR SwissPalm; P80316; -.
DR REPRODUCTION-2DPAGE; IPI00116279; -.
DR REPRODUCTION-2DPAGE; P80316; -.
DR SWISS-2DPAGE; P80316; -.
DR EPD; P80316; -.
DR jPOST; P80316; -.
DR MaxQB; P80316; -.
DR PaxDb; P80316; -.
DR PeptideAtlas; P80316; -.
DR PRIDE; P80316; -.
DR ProteomicsDB; 259363; -.
DR Antibodypedia; 1210; 340 antibodies from 34 providers.
DR DNASU; 12465; -.
DR Ensembl; ENSMUST00000022842; ENSMUSP00000022842; ENSMUSG00000022234.
DR GeneID; 12465; -.
DR KEGG; mmu:12465; -.
DR UCSC; uc007vkj.1; mouse.
DR CTD; 22948; -.
DR MGI; MGI:107185; Cct5.
DR VEuPathDB; HostDB:ENSMUSG00000022234; -.
DR eggNOG; KOG0357; Eukaryota.
DR GeneTree; ENSGT00550000074988; -.
DR HOGENOM; CLU_008891_7_2_1; -.
DR InParanoid; P80316; -.
DR OMA; QTGSNDM; -.
DR OrthoDB; 511484at2759; -.
DR PhylomeDB; P80316; -.
DR TreeFam; TF105638; -.
DR BRENDA; 3.6.4.B10; 3474.
DR Reactome; R-MMU-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 12465; 28 hits in 72 CRISPR screens.
DR ChiTaRS; Cct5; mouse.
DR PRO; PR:P80316; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P80316; protein.
DR Bgee; ENSMUSG00000022234; Expressed in primitive streak and 262 other tissues.
DR ExpressionAtlas; P80316; baseline and differential.
DR Genevisible; P80316; MM.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
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:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISS:CAFA.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
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 Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CHAIN 2..541
FT /note="T-complex protein 1 subunit epsilon"
FT /id="PRO_0000128347"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CROSSLNK 392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48643"
FT CONFLICT 27
FT /note="R -> H (in Ref. 4; BAE23007)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="M -> I (in Ref. 4; BAE27146)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="G -> D (in Ref. 4; BAE32250)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="D -> E (in Ref. 4; BAE27146)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="N -> D (in Ref. 4; BAE39906)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="C -> Y (in Ref. 4; BAE29518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 59624 MW; E05316785ADB7612 CRC64;
MASVGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM
MVDKDGDVTI TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA
EQLLDRGIHP IRIADGYEQA ARIAIQHLDK ISDKVLVDIN NPEPLIQTAK TTLGSKVINS
CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP
KKVVDAKIAI LTCPFEPPKP KTKHKLDVMS VEDYKALQKY EKEKFEEMIK QIKETGANLA
ICQWGFDDEA NHLLLQNGLP AVRWVGGPEI ELIAIATGGR IVPRFSELTS EKLGFAGVVQ
EISFGTTKDK MLVIEKCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY
GGGAAEISCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR
QVKESNPALG IDCLHKGSND MQYQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE
E
