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Protein

T-complex protein 1 subunit alpha

Gene

TCP1

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

Keywordsi

Molecular functionChaperone
LigandATP-binding, Nucleotide-binding

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002362581 – 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 residuei551PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ32L40.
PeptideAtlasiQ32L40.
PRIDEiQ32L40.

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

GO - Molecular functioni

Protein-protein interaction databases

CORUMiQ32L40.
DIPiDIP-58617N.
IntActiQ32L40. 2 interactors.
STRINGi9913.ENSBTAP00000003662.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IYGelectron microscopy-A7-535[»]
4B2TX-ray5.50A/a1-556[»]
ProteinModelPortaliQ32L40.
SMRiQ32L40.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0360. Eukaryota.
COG0459. LUCA.
HOGENOMiHOG000226729.
HOVERGENiHBG001052.
InParanoidiQ32L40.
KOiK09493.

Family and domain databases

CDDicd03335. TCP1_alpha. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
InterProiView protein in InterPro
IPR012715. Chap_CCT_alpha.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR037290. Cpn60/TCP-1_sf.
IPR027409. GroEL-like_apical_dom_sf.
IPR027413. GROEL-like_equatorial_sf.
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiView protein in Pfam
PF00118. Cpn60_TCP1. 1 hit.
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
SSF54849. SSF54849. 2 hits.
TIGRFAMsiTIGR02340. chap_CCT_alpha. 1 hit.
PROSITEiView protein in PROSITE
PS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.

Sequencei

Sequence statusi: Complete.

Q32L40-1 [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 YISENLIINT DELGRDCLIN
160 170 180 190 200
AAKTSMSSKV IGINGDFFAN LVVDAVLAIK YTDIRGQPRY PVNSINVLKA
210 220 230 240 250
HGRSQMESML INGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV
260 270 280 290 300
QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF
310 320 330 340 350
VEAGAMAVRR VLKRDLKRIA KASGATVLST LANLEGEETF EASMLGQAEE
360 370 380 390 400
VVQERICDDE LILIKNTKAR TSASVILRGA NDFMCDEMER SLHDALCVVK
410 420 430 440 450
RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLPVIPN
460 470 480 490 500
TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL VNGKPRDNKQ
510 520 530 540 550
AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGGYEDAVH

SGALDA
Length:556
Mass (Da):60,206
Last modified:December 6, 2005 - v1
Checksum:i161E9B04CFC5A1D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109781 mRNA. Translation: AAI09782.1.
RefSeqiNP_001033175.1. NM_001038086.1.
UniGeneiBt.4585.

Genome annotation databases

GeneIDi512043.
KEGGibta:512043.

Similar proteinsi

Entry informationi

Entry nameiTCPA_BOVIN
AccessioniPrimary (citable) accession number: Q32L40
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 6, 2005
Last modified: November 22, 2017
This is version 83 of the entry and version 1 of the sequence. See 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