TCPD_RAT
ID TCPD_RAT Reviewed; 539 AA.
AC Q7TPB1;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=T-complex protein 1 subunit delta;
DE Short=TCP-1-delta;
DE AltName: Full=CCT-delta;
GN Name=Cct4;
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], AND VARIANT MF TYR-450.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=12874111; DOI=10.1093/hmg/ddg198;
RA Lee M.J., Stephenson D.A., Groves M.J., Sweeney M.G., Davis M.B., An S.F.,
RA Houlden H., Salih M.A.M., Timmerman V., De Jonghe P., Auer-Grumbach M.,
RA Di Maria E., Scaravilli F., Wood N.W., Reilly M.M.;
RT "Hereditary sensory neuropathy is caused by a mutation in the delta subunit
RT of the cytosolic chaperonin-containing T-complex peptide-1 (Cct4) gene.";
RL Hum. Mol. Genet. 12:1917-1925(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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:P50991}.
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 (By similarity).
CC Interacts with DNAAF4 (By similarity). Interacts with DLEC1 (By
CC similarity). {ECO:0000250|UniProtKB:P50991,
CC ECO:0000250|UniProtKB:P80315}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50991}.
CC Melanosome {ECO:0000250|UniProtKB:P50991}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P50991}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:P80315}.
CC -!- DISEASE: Note=Defects in Cct4 are a cause of an early onset sensory
CC neuropathy knowm as mutilated foot (mf). The main clinical features
CC include ataxia, insensitivity to pain and foot ulceration. The
CC pathological features include a severe reduction in the number of
CC sensory ganglia and fibers. {ECO:0000269|PubMed:12874111}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; AY223861; AAP46161.1; -; mRNA.
DR EMBL; BC079283; AAH79283.1; -; mRNA.
DR RefSeq; NP_877966.1; NM_182814.2.
DR AlphaFoldDB; Q7TPB1; -.
DR SMR; Q7TPB1; -.
DR BioGRID; 248027; 8.
DR IntAct; Q7TPB1; 6.
DR MINT; Q7TPB1; -.
DR STRING; 10116.ENSRNOP00000012847; -.
DR iPTMnet; Q7TPB1; -.
DR PhosphoSitePlus; Q7TPB1; -.
DR jPOST; Q7TPB1; -.
DR PaxDb; Q7TPB1; -.
DR PRIDE; Q7TPB1; -.
DR Ensembl; ENSRNOT00000012847; ENSRNOP00000012847; ENSRNOG00000009642.
DR GeneID; 29374; -.
DR KEGG; rno:29374; -.
DR UCSC; RGD:727937; rat.
DR CTD; 10575; -.
DR RGD; 727937; Cct4.
DR eggNOG; KOG0358; Eukaryota.
DR GeneTree; ENSGT00550000074956; -.
DR HOGENOM; CLU_008891_9_1_1; -.
DR InParanoid; Q7TPB1; -.
DR OMA; HPAANMI; -.
DR OrthoDB; 511484at2759; -.
DR PhylomeDB; Q7TPB1; -.
DR TreeFam; TF106332; -.
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:Q7TPB1; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000009642; Expressed in testis and 20 other tissues.
DR Genevisible; Q7TPB1; RN.
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:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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: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:0090666; P:scaRNA localization to Cajal body; ISO:RGD.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
DR CDD; cd03338; TCP1_delta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012717; Chap_CCT_delta.
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; TIGR02342; chap_CCT_delta; 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; Cell projection; Chaperone; Cilium; Cytoplasm;
KW Cytoskeleton; Disease variant; Methylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..539
FT /note="T-complex protein 1 subunit delta"
FT /id="PRO_0000128335"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80315"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 302
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT VARIANT 450
FT /note="C -> Y (in mf)"
FT /evidence="ECO:0000269|PubMed:12874111"
SQ SEQUENCE 539 AA; 58099 MW; 0BD821D08733CDF8 CRC64;
MPENVASRSG PPAAGPGNRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM
IQDGKGDVTI TNDGATILKQ MQVLHPAARM LVELSKAQDI EAGDGTTSVV IIAGSLLDSC
TKLLQKGIHP TIISESFQKA LEKGLEILTD MSRPVQLSDR ETLLNSATTS LNSKVVSQYS
SLLSPMSVNA VMKVIDPATA TSVDLRDIKI VKKLGGTIDD CELVEGLVLT QKVANSGITR
VEKAKIGLIQ FCLSAPKTDM DNQIVVSDYA QMDRVLREER AYILNLVKQI KKTGCNVLLI
QKSILRDALS DLALHFLNKM KIMVVKDIER EDIEFICKTI GTKPVAHIDQ FTPDMLGSAE
LAEEVSLNGS GKLFKITGCT SPGKTVTIVV RGSNKLVIEE AERSIHDALC VIRCLVKKRA
LIAGGGAPEI ELALRLTEYS RTLSGMESYC VRAFADAMEV IPSTLAENAG LNPISTVTEL
RNRHAQGEKT TGINVRKGGI SNILEEMVVQ PLLVSVSALT LATETVRSIL KIDDVVNTR
