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Protein

T-complex protein 1 subunit alpha

Gene

T-cp1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.

GO - Molecular functioni

  • ATP binding Source: FlyBase
  • hydrogen-exporting ATPase activity, phosphorylative mechanism Source: FlyBase

GO - Biological processi

  • hydrogen ion transmembrane transport Source: GOC
  • mitotic spindle assembly Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • phagocytosis Source: FlyBase
  • protein folding Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-390471. Association of TriC/CCT with target proteins during biosynthesis.

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:T-cp1
Synonyms:CCT-1, Tcp-1
ORF Names:CG5374
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003676. T-cp1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitochondrial proton-transporting ATP synthase complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 557557T-complex protein 1 subunit alphaPRO_0000128310Add
BLAST

Proteomic databases

PaxDbiP12613.
PRIDEiP12613.

Expressioni

Gene expression databases

BgeeiP12613.
ExpressionAtlasiP12613. differential.
GenevisibleiP12613. DM.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.

Protein-protein interaction databases

BioGridi67604. 21 interactions.
DIPiDIP-22081N.
MINTiMINT-993775.
STRINGi7227.FBpp0083683.

Structurei

3D structure databases

ProteinModelPortaliP12613.
SMRiP12613. Positions 7-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0360. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074878.
InParanoidiP12613.
KOiK09493.
OMAiHYLAQEG.
OrthoDBiEOG7K3TKJ.
PhylomeDBiP12613.

Family and domain databases

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.

P12613-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLASPLSI AGTRQSGASV RTQNVMAALS ISNIVKSSLG PVGLDKMLVD
60 70 80 90 100
DIGDVTVTND GATILRLLEV EHPAAKVLVE LAQLQDEEVG DGTTSVVILA
110 120 130 140 150
AELLKNADEL VKQKIHPTSI ISGYRIACKE ACKYISEHLT APVDELGRDS
160 170 180 190 200
LINIAKTSMS SKIIGADAEF FSAMVVDAAQ SVKITDPRGQ AAYSIKAINV
210 220 230 240 250
LKAHGKSARE SVLIPGYALN CTIASQQMPK KIVNAKIACL DFSLQKTKMK
260 270 280 290 300
MGVQVLINDP DKLEAIRARE LDITKERINM ILGTGVNVVL VSGGVDDLCM
310 320 330 340 350
KYFVEAGAMA VRRVKKSDLK IIAKATGAAF ITSLTNMDGE ESFDASMVGE
360 370 380 390 400
AAEVAQERIC DDELILIKGT KARAAASIIL RGPNDFYCDE MERSVHDALC
410 420 430 440 450
VVKRVLESKK VVAGGGCVEA ALSIYLENFA TSLASREQLA IAEFAKSLLV
460 470 480 490 500
IPKTLSVNAA KDATDLVAKL RSYHNSSQTK PERSDLKWTG LDLIEGVVRD
510 520 530 540 550
NKKAGVLEPA MSKIKSLKFA TEAAITILRI DDMIKLNPED KSGKSYADAC

AAGELDG
Length:557
Mass (Da):59,557
Last modified:May 4, 2001 - v2
Checksum:i6F4A28237456F3A2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 193GAS → RRI in AAA28927 (PubMed:3146529).Curated
Sequence conflicti192 – 1921A → V in AAA28927 (PubMed:3146529).Curated
Sequence conflicti198 – 1981I → V in AAA28927 (PubMed:3146529).Curated
Sequence conflicti240 – 2401L → H in AAA28927 (PubMed:3146529).Curated
Sequence conflicti413 – 4131A → R in AAA28927 (PubMed:3146529).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21159 mRNA. Translation: AAA28927.1.
AE014297 Genomic DNA. Translation: AAF56009.1.
AY118416 mRNA. Translation: AAM48445.1.
PIRiJT0367.
RefSeqiNP_524450.2. NM_079726.4.
NP_732748.1. NM_170016.2.
UniGeneiDm.1279.

Genome annotation databases

EnsemblMetazoaiFBtr0084290; FBpp0083683; FBgn0003676.
FBtr0084291; FBpp0083684; FBgn0003676.
GeneIDi42649.
KEGGidme:Dmel_CG5374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21159 mRNA. Translation: AAA28927.1.
AE014297 Genomic DNA. Translation: AAF56009.1.
AY118416 mRNA. Translation: AAM48445.1.
PIRiJT0367.
RefSeqiNP_524450.2. NM_079726.4.
NP_732748.1. NM_170016.2.
UniGeneiDm.1279.

3D structure databases

ProteinModelPortaliP12613.
SMRiP12613. Positions 7-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67604. 21 interactions.
DIPiDIP-22081N.
MINTiMINT-993775.
STRINGi7227.FBpp0083683.

Proteomic databases

PaxDbiP12613.
PRIDEiP12613.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084290; FBpp0083683; FBgn0003676.
FBtr0084291; FBpp0083684; FBgn0003676.
GeneIDi42649.
KEGGidme:Dmel_CG5374.

Organism-specific databases

CTDi42649.
FlyBaseiFBgn0003676. T-cp1.

Phylogenomic databases

eggNOGiKOG0360. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074878.
InParanoidiP12613.
KOiK09493.
OMAiHYLAQEG.
OrthoDBiEOG7K3TKJ.
PhylomeDBiP12613.

Enzyme and pathway databases

ReactomeiR-DME-390471. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

ChiTaRSiT-cp1. fly.
GenomeRNAii42649.
NextBioi829871.
PROiP12613.

Gene expression databases

BgeeiP12613.
ExpressionAtlasiP12613. differential.
GenevisibleiP12613. DM.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "A Drosophila melanogaster gene encodes a protein homologous to the mouse t complex polypeptide 1."
    Ursic D., Ganetzky B.
    Gene 68:267-274(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiTCPA_DROME
AccessioniPrimary (citable) accession number: P12613
Secondary accession number(s): Q9VCZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 4, 2001
Last modified: May 11, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.