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Protein

T-complex protein 1 subunit theta

Gene

CCT8

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit theta
Short name:
TCP-1-theta
Alternative name(s):
CCT-theta
Gene namesi
Name:CCT8
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  • chaperonin-containing T-complex Source: UniProtKB
  • cilium Source: UniProtKB-KW
  • microtubule organizing center Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002362652 – 548T-complex protein 1 subunit thetaAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei23PhosphoserineBy similarity1
Modified residuei30PhosphotyrosineBy similarity1
Modified residuei162PhosphoserineBy similarity1
Modified residuei269PhosphoserineBy similarity1
Modified residuei317PhosphoserineBy similarity1
Modified residuei318N6-acetyllysineBy similarity1
Modified residuei400N6-acetyllysineBy similarity1
Cross-linki459Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei466N6-acetyllysineBy similarity1
Modified residuei505PhosphotyrosineBy similarity1
Cross-linki534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei537PhosphoserineBy similarity1
Cross-linki539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ3ZCI9.
PeptideAtlasiQ3ZCI9.
PRIDEiQ3ZCI9.

Expressioni

Gene expression databases

BgeeiENSBTAG00000014233.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8 (By similarity). Interacts with DYX1C1 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-58622N.
STRINGi9913.ENSBTAP00000018917.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IYGelectron microscopy-Q17-528[»]
4B2TX-ray5.50Q/q1-548[»]
ProteinModelPortaliQ3ZCI9.
SMRiQ3ZCI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0362. Eukaryota.
ENOG410XPXR. LUCA.
GeneTreeiENSGT00550000074783.
HOGENOMiHOG000226734.
HOVERGENiHBG103107.
InParanoidiQ3ZCI9.
KOiK09500.
OMAiKYGLMAV.
OrthoDBiEOG091G05WZ.
TreeFamiTF105699.

Family and domain databases

CDDicd03341. TCP1_theta. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012721. Chap_CCT_theta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02346. chap_CCT_theta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3ZCI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN
60 70 80 90 100
GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG
110 120 130 140 150
TNFVLVFAGA LLELAEELLR LGLSVSEVIE GYEIACKKAH EILPDLVCCS
160 170 180 190 200
AKNLRDVDEV SSLLHTSVMS KQYGNEVFLA KLIAQACVSI FPDSGHFNVD
210 220 230 240 250
NIRVCKILGS GVHSSSVLHG MVFKKETEGD VTSVKDAKIA VYSCPFDGMI
260 270 280 290 300
TETKGTVLIK SAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGRVADM
310 320 330 340 350
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLNPPV LEEMGHCDSV
360 370 380 390 400
YLSEVGDTQV VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK
410 420 430 440 450
VLTRDKRLVP GGGATEIELA KQITSYGETC PGLEQYAIKK FAEAFEAIPR
460 470 480 490 500
ALAENSGVKA NEVISKLYAV HQEGNKNVGL DIEAEVPAVK DMLEAGVLDT
510 520 530 540
YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK DWDEDQND
Length:548
Mass (Da):59,609
Last modified:January 23, 2007 - v3
Checksum:i4CA539F87FCDD06B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102169 mRNA. Translation: AAI02170.1.
RefSeqiNP_001028781.1. NM_001033609.1.
UniGeneiBt.49440.

Genome annotation databases

EnsembliENSBTAT00000018917; ENSBTAP00000018917; ENSBTAG00000014233.
GeneIDi281047.
KEGGibta:281047.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102169 mRNA. Translation: AAI02170.1.
RefSeqiNP_001028781.1. NM_001033609.1.
UniGeneiBt.49440.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IYGelectron microscopy-Q17-528[»]
4B2TX-ray5.50Q/q1-548[»]
ProteinModelPortaliQ3ZCI9.
SMRiQ3ZCI9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58622N.
STRINGi9913.ENSBTAP00000018917.

Proteomic databases

PaxDbiQ3ZCI9.
PeptideAtlasiQ3ZCI9.
PRIDEiQ3ZCI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000018917; ENSBTAP00000018917; ENSBTAG00000014233.
GeneIDi281047.
KEGGibta:281047.

Organism-specific databases

CTDi10694.

Phylogenomic databases

eggNOGiKOG0362. Eukaryota.
ENOG410XPXR. LUCA.
GeneTreeiENSGT00550000074783.
HOGENOMiHOG000226734.
HOVERGENiHBG103107.
InParanoidiQ3ZCI9.
KOiK09500.
OMAiKYGLMAV.
OrthoDBiEOG091G05WZ.
TreeFamiTF105699.

Enzyme and pathway databases

ReactomeiR-BTA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Gene expression databases

BgeeiENSBTAG00000014233.

Family and domain databases

CDDicd03341. TCP1_theta. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012721. Chap_CCT_theta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02346. chap_CCT_theta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTCPQ_BOVIN
AccessioniPrimary (citable) accession number: Q3ZCI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.