Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

T-complex protein 1 subunit gamma

Gene

Cct3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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. Plays a role in the assembly of the von Hippel-Lindau ubiquitination complex (By similarity). Interacts with DYX1C1.By similarity

GO - Molecular functioni

GO - Biological processi

  • binding of sperm to zona pellucida Source: MGI
  • pore complex assembly Source: MGI
  • positive regulation of protein localization to Cajal body Source: MGI
  • positive regulation of telomerase RNA localization to Cajal body Source: MGI
  • positive regulation of telomere maintenance via telomerase Source: MGI
  • protein stabilization Source: MGI
  • toxin transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit gamma
Short name:
TCP-1-gamma
Alternative name(s):
CCT-gamma
Matricin
mTRiC-P5
Gene namesi
Name:Cct3
Synonyms:Cctg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:104708. Cct3.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: MGI
  • chaperonin-containing T-complex Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • microtubule Source: MGI
  • myelin sheath Source: UniProtKB
  • plasma membrane Source: MGI
  • zona pellucida receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 545545T-complex protein 1 subunit gammaPRO_0000128322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei170 – 1701PhosphoserineCombined sources
Modified residuei222 – 2221N6-acetyllysineBy similarity
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei252 – 2521PhosphoserineCombined sources
Disulfide bondi366 ↔ 372

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP80318.
PaxDbiP80318.
PRIDEiP80318.

2D gel databases

REPRODUCTION-2DPAGEIPI00116283.
P80318.

PTM databases

iPTMnetiP80318.
PhosphoSiteiP80318.
SwissPalmiP80318.

Expressioni

Gene expression databases

BgeeiP80318.
CleanExiMM_CCT3.
ExpressionAtlasiP80318. baseline and differential.
GenevisibleiP80318. MM.

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
gagP045913EBI-772361,EBI-10634977From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198565. 44 interactions.
DIPiDIP-32344N.
IntActiP80318. 53 interactions.
MINTiMINT-1870089.
STRINGi10090.ENSMUSP00000001452.

Structurei

Secondary structure

1
545
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi213 – 2219Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi238 – 2436Combined sources
Helixi264 – 28320Combined sources
Beta strandi288 – 2947Combined sources
Helixi298 – 3069Combined sources
Beta strandi310 – 3123Combined sources
Helixi317 – 32711Combined sources
Beta strandi331 – 3333Combined sources
Helixi335 – 3373Combined sources
Helixi340 – 3423Combined sources
Beta strandi347 – 3559Combined sources
Beta strandi358 – 36811Combined sources
Beta strandi373 – 3775Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GMLX-ray2.20A/B/C/D210-380[»]
1GN1X-ray2.80A/B/C/D/E/F/G/H210-380[»]
ProteinModelPortaliP80318.
SMRiP80318. Positions 7-526.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80318.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0364. Eukaryota.
COG0459. LUCA.
HOGENOMiHOG000226732.
HOVERGENiHBG104982.
InParanoidiP80318.
KOiK09495.
OMAiTQCGLFE.
OrthoDBiEOG7DJSKS.
PhylomeDBiP80318.
TreeFamiTF105649.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012719. Chap_CCT_gamma.
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]
PANTHERiPTHR11353:SF63. PTHR11353:SF63. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02344. chap_CCT_gamma. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML
60 70 80 90 100
LDPMGGIVMT NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII
110 120 130 140 150
LAGEMLSVAE HFLEQQMHPT VVISAYRMAL DDMISTLKKI STPVDVNNRE
160 170 180 190 200
MMLSIINSSI TTKVISRWSS LACNIALDAV KTVQFEENGR KEIDIKKYAR
210 220 230 240 250
VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL LDSSLEYKKG
260 270 280 290 300
ESQTDIEITR EEDFTRILQM EEEYIHQLCE DIIQLKPDVV ITEKGISDLA
310 320 330 340 350
QHYLMRANVT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL
360 370 380 390 400
EIKKIGDEYF TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN
410 420 430 440 450
VLLDPQLVPG GGASEMAVAH ALTEKSKAMT GVEQWPYRAV AQALEVIPRT
460 470 480 490 500
LIQNCGASTI RLLTSLRAKH TQESCETWGV NGETGTLVDM KELGIWEPLA
510 520 530 540
VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQNRQTGAP DAGQE
Length:545
Mass (Da):60,630
Last modified:June 1, 1994 - v1
Checksum:i492F9743C607FA1D
GO

Sequence cautioni

The sequence AAA19749.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241S → G in AAA19749 (PubMed:8110840).Curated
Sequence conflicti150 – 1501E → D in AAA19749 (PubMed:8110840).Curated
Sequence conflicti154 – 1541S → N in AAA19749 (PubMed:8110840).Curated
Sequence conflicti276 – 2761H → Q in AAA19749 (PubMed:8110840).Curated
Sequence conflicti365 – 3651D → E in AAA19749 (PubMed:8110840).Curated
Sequence conflicti474 – 4741S → N in AAA19749 (PubMed:8110840).Curated
Sequence conflicti534 – 5341N → S in AAA19749 (PubMed:8110840).Curated
Sequence conflicti537 – 5382TG → SS in AAA19749 (PubMed:8110840).Curated
Sequence conflicti542 – 5421A → G in AAA19749 (PubMed:8110840).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31556 mRNA. Translation: CAA83431.1.
L20509 mRNA. Translation: AAA19749.1. Different initiation.
CCDSiCCDS17468.1.
PIRiS42723.
S43062.
RefSeqiNP_033966.1. NM_009836.1.
UniGeneiMm.256034.

Genome annotation databases

EnsembliENSMUST00000001452; ENSMUSP00000001452; ENSMUSG00000001416.
GeneIDi12462.
KEGGimmu:12462.
UCSCiuc008puo.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31556 mRNA. Translation: CAA83431.1.
L20509 mRNA. Translation: AAA19749.1. Different initiation.
CCDSiCCDS17468.1.
PIRiS42723.
S43062.
RefSeqiNP_033966.1. NM_009836.1.
UniGeneiMm.256034.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GMLX-ray2.20A/B/C/D210-380[»]
1GN1X-ray2.80A/B/C/D/E/F/G/H210-380[»]
ProteinModelPortaliP80318.
SMRiP80318. Positions 7-526.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198565. 44 interactions.
DIPiDIP-32344N.
IntActiP80318. 53 interactions.
MINTiMINT-1870089.
STRINGi10090.ENSMUSP00000001452.

PTM databases

iPTMnetiP80318.
PhosphoSiteiP80318.
SwissPalmiP80318.

2D gel databases

REPRODUCTION-2DPAGEIPI00116283.
P80318.

Proteomic databases

EPDiP80318.
PaxDbiP80318.
PRIDEiP80318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001452; ENSMUSP00000001452; ENSMUSG00000001416.
GeneIDi12462.
KEGGimmu:12462.
UCSCiuc008puo.3. mouse.

Organism-specific databases

CTDi7203.
MGIiMGI:104708. Cct3.

Phylogenomic databases

eggNOGiKOG0364. Eukaryota.
COG0459. LUCA.
HOGENOMiHOG000226732.
HOVERGENiHBG104982.
InParanoidiP80318.
KOiK09495.
OMAiTQCGLFE.
OrthoDBiEOG7DJSKS.
PhylomeDBiP80318.
TreeFamiTF105649.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiCct3. mouse.
EvolutionaryTraceiP80318.
PROiP80318.
SOURCEiSearch...

Gene expression databases

BgeeiP80318.
CleanExiMM_CCT3.
ExpressionAtlasiP80318. baseline and differential.
GenevisibleiP80318. MM.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012719. Chap_CCT_gamma.
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]
PANTHERiPTHR11353:SF63. PTHR11353:SF63. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02344. chap_CCT_gamma. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin."
    Kubota H., Hynes G., Carne A., Ashworth A., Willison K.R.
    Curr. Biol. 4:89-99(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: 129/Sv.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 32-38; 128-138; 150-163; 204-216; 238-248; 428-461; 492-502 AND 508-518, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin."
    Pappenberger G., Wilsher J.A., Roe S.M., Counsell D.J., Willison K.R., Pearl L.H.
    J. Mol. Biol. 318:1367-1379(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 210-386.
  6. Cited for: INTERACTION WITH DYX1C1.

Entry informationi

Entry nameiTCPG_MOUSE
AccessioniPrimary (citable) accession number: P80318
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 8, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.