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Protein

T-complex protein 1 subunit alpha

Gene

Tcp1

Organism
Rattus norvegicus (Rat)
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 (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-RNO-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit alpha
Short name:
TCP-1-alpha
Alternative name(s):
CCT-alpha
Gene namesi
Name:Tcp1
Synonyms:Cct1, Ccta
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3832. Tcp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001283061 – 556T-complex protein 1 subunit alphaAdd BLAST556

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Modified residuei181PhosphotyrosineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei400N6-acetyllysineBy similarity1
Modified residuei494N6-acetyllysineBy similarity1
Modified residuei551PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP28480.
PRIDEiP28480.

2D gel databases

World-2DPAGE0004:P28480.

PTM databases

iPTMnetiP28480.
PhosphoSitePlusiP28480.
SwissPalmiP28480.

Expressioni

Gene expression databases

BgeeiENSRNOG00000014160.
ExpressionAtlasiP28480. baseline and differential.
GenevisibleiP28480. RN.

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

Protein-protein interaction databases

BioGridi246940. 4 interactors.
IntActiP28480. 3 interactors.
MINTiMINT-4568218.
STRINGi10116.ENSRNOP00000019531.

Structurei

3D structure databases

ProteinModelPortaliP28480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0360. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074878.
HOGENOMiHOG000226729.
HOVERGENiHBG001052.
InParanoidiP28480.
KOiK09493.
OMAiLRSCHHK.
OrthoDBiEOG091G04HL.
PhylomeDBiP28480.
TreeFamiTF106331.

Family and domain databases

CDDicd03335. TCP1_alpha. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012715. Chap_CCT_alpha.
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.
TIGRFAMsiTIGR02340. chap_CCT_alpha. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGPLSVFGD RSTGEAIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG
60 70 80 90 100
DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL
110 120 130 140 150
LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIINT DELGRDCLIN
160 170 180 190 200
AAKTSMSSKI IGINGDFFAN MVVDAVLAVK YTDIRGQPRY PVNSVNILKA
210 220 230 240 250
HGRSQIESML INGYALNCVV GSQGMLKRIV NAKIACLDFS LQKTKMKLGV
260 270 280 290 300
QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF
310 320 330 340 350
VEAGAMAVRR VLKRDLKRIA KASGASILST LANLEGEETF EATMLGQAEE
360 370 380 390 400
VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK
410 420 430 440 450
RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN
460 470 480 490 500
TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL VHGKPRDNKQ
510 520 530 540 550
AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGGYENAVH

SGALDD
Length:556
Mass (Da):60,360
Last modified:December 1, 1992 - v1
Checksum:i504F415F86EB7DA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90345 mRNA. Translation: BAA14357.1.
PIRiJQ0866.
RefSeqiNP_036802.1. NM_012670.1.
UniGeneiRn.7102.

Genome annotation databases

EnsembliENSRNOT00000019531; ENSRNOP00000019531; ENSRNOG00000014160.
GeneIDi24818.
KEGGirno:24818.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90345 mRNA. Translation: BAA14357.1.
PIRiJQ0866.
RefSeqiNP_036802.1. NM_012670.1.
UniGeneiRn.7102.

3D structure databases

ProteinModelPortaliP28480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246940. 4 interactors.
IntActiP28480. 3 interactors.
MINTiMINT-4568218.
STRINGi10116.ENSRNOP00000019531.

PTM databases

iPTMnetiP28480.
PhosphoSitePlusiP28480.
SwissPalmiP28480.

2D gel databases

World-2DPAGE0004:P28480.

Proteomic databases

PaxDbiP28480.
PRIDEiP28480.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000019531; ENSRNOP00000019531; ENSRNOG00000014160.
GeneIDi24818.
KEGGirno:24818.

Organism-specific databases

CTDi6950.
RGDi3832. Tcp1.

Phylogenomic databases

eggNOGiKOG0360. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074878.
HOGENOMiHOG000226729.
HOVERGENiHBG001052.
InParanoidiP28480.
KOiK09493.
OMAiLRSCHHK.
OrthoDBiEOG091G04HL.
PhylomeDBiP28480.
TreeFamiTF106331.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP28480.

Gene expression databases

BgeeiENSRNOG00000014160.
ExpressionAtlasiP28480. baseline and differential.
GenevisibleiP28480. RN.

Family and domain databases

CDDicd03335. TCP1_alpha. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012715. Chap_CCT_alpha.
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.
TIGRFAMsiTIGR02340. chap_CCT_alpha. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTCPA_RAT
AccessioniPrimary (citable) accession number: P28480
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 2, 2016
This is version 133 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.