TCPA_RAT
ID TCPA_RAT Reviewed; 556 AA.
AC P28480;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=T-complex protein 1 subunit alpha;
DE Short=TCP-1-alpha;
DE AltName: Full=CCT-alpha;
GN Name=Tcp1; Synonyms=Cct1, Ccta;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1937024; DOI=10.1016/0378-1119(91)90162-5;
RA Kubota H., Morita T., Nagata T., Takemoto Y., Nozaki M., Gachelin G.,
RA Matsushiro A.;
RT "Nucleotide sequence of mouse Tcp-1a cDNA.";
RL Gene 105:269-273(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1756183; DOI=10.1016/0167-4781(91)90219-c;
RA Morita T., Kubota H., Gachelin G., Nozaki M., Matsushiro A.;
RT "Cloning of cDNA encoding rat TCP-1.";
RL Biochim. Biophys. Acta 1129:96-99(1991).
RN [3]
RP PROTEIN SEQUENCE OF 131-145; 485-496 AND 516-526, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (DEC-2006) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC molecular chaperone complex that assists the folding of proteins upon
CC ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1,
CC thereby regulating telomere maintenance. As part of the TRiC complex
CC may play a role in the assembly of BBSome, a complex involved in
CC ciliogenesis regulating transports vesicles to the cilia. The TRiC
CC complex plays a role in the folding of actin and tubulin.
CC {ECO:0000250|UniProtKB:P17987}.
CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC rings, 12 to 16 nm in diameter. Interacts with PACRG. Interacts with
CC GBA (By similarity). Interacts with DLEC1 (By similarity).
CC {ECO:0000250|UniProtKB:P17987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P17987}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P17987}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; D90345; BAA14357.1; -; mRNA.
DR PIR; JQ0866; JQ0866.
DR RefSeq; NP_036802.1; NM_012670.1.
DR AlphaFoldDB; P28480; -.
DR SMR; P28480; -.
DR BioGRID; 246940; 7.
DR IntAct; P28480; 4.
DR MINT; P28480; -.
DR STRING; 10116.ENSRNOP00000019531; -.
DR iPTMnet; P28480; -.
DR PhosphoSitePlus; P28480; -.
DR SwissPalm; P28480; -.
DR World-2DPAGE; 0004:P28480; -.
DR jPOST; P28480; -.
DR PaxDb; P28480; -.
DR PRIDE; P28480; -.
DR Ensembl; ENSRNOT00000019531; ENSRNOP00000019531; ENSRNOG00000014160.
DR GeneID; 24818; -.
DR KEGG; rno:24818; -.
DR CTD; 6950; -.
DR RGD; 3832; Tcp1.
DR eggNOG; KOG0360; Eukaryota.
DR GeneTree; ENSGT00550000074878; -.
DR HOGENOM; CLU_008891_5_1_1; -.
DR InParanoid; P28480; -.
DR OMA; KNYKNYG; -.
DR OrthoDB; 335406at2759; -.
DR PhylomeDB; P28480; -.
DR TreeFam; TF106331; -.
DR BRENDA; 3.6.4.B10; 5301.
DR Reactome; R-RNO-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-RNO-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:P28480; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014160; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; P28480; baseline and differential.
DR Genevisible; P28480; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000792; C:heterochromatin; IDA:RGD.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0000242; C:pericentriolar material; ISO:RGD.
DR GO; GO:0002199; C:zona pellucida receptor complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0044183; F:protein folding chaperone; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:RGD.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:RGD.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; ISO:RGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:2000109; P:regulation of macrophage apoptotic process; ISO:RGD.
DR GO; GO:0090666; P:scaRNA localization to Cajal body; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; TAS:RGD.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
DR GO; GO:0044053; P:translocation of peptides or proteins into host cell cytoplasm; ISO:RGD.
DR CDD; cd03335; TCP1_alpha; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012715; Chap_CCT_alpha.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02340; chap_CCT_alpha; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..556
FT /note="T-complex protein 1 subunit alpha"
FT /id="PRO_0000128306"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11983"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 556 AA; 60360 MW; 504F415F86EB7DA1 CRC64;
MEGPLSVFGD RSTGEAIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT
ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG
YRLACKEAVR YINENLIINT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAVK
YTDIRGQPRY PVNSVNILKA HGRSQIESML INGYALNCVV GSQGMLKRIV NAKIACLDFS
LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF
VEAGAMAVRR VLKRDLKRIA KASGASILST LANLEGEETF EATMLGQAEE VVQERICDDE
LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS
IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
KNLKWIGLDL VHGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD
KHGGYENAVH SGALDD
