TCPD_BOVIN
ID TCPD_BOVIN Reviewed; 542 AA.
AC Q2T9X2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=T-complex protein 1 subunit delta;
DE Short=TCP-1-delta;
DE AltName: Full=CCT-delta;
GN Name=CCT4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; BC111225; AAI11226.1; -; mRNA.
DR RefSeq; NP_001033283.1; NM_001038194.1.
DR PDB; 3IYG; EM; -; D=25-542.
DR PDB; 4B2T; X-ray; 5.50 A; D/d=1-542.
DR PDBsum; 3IYG; -.
DR PDBsum; 4B2T; -.
DR AlphaFoldDB; Q2T9X2; -.
DR SMR; Q2T9X2; -.
DR CORUM; Q2T9X2; -.
DR DIP; DIP-58619N; -.
DR IntAct; Q2T9X2; 1.
DR STRING; 9913.ENSBTAP00000042274; -.
DR PaxDb; Q2T9X2; -.
DR PeptideAtlas; Q2T9X2; -.
DR PRIDE; Q2T9X2; -.
DR GeneID; 613336; -.
DR KEGG; bta:613336; -.
DR CTD; 10575; -.
DR eggNOG; KOG0358; Eukaryota.
DR InParanoid; Q2T9X2; -.
DR OrthoDB; 511484at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:0051082; F:unfolded protein binding; IEA:InterPro.
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 3D-structure; Acetylation; ATP-binding; Cell projection; Chaperone; Cilium;
KW Cytoplasm; Cytoskeleton; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..542
FT /note="T-complex protein 1 subunit delta"
FT /id="PRO_0000236261"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80315"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 322
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
SQ SEQUENCE 542 AA; 58206 MW; 00610BF36473BB97 CRC64;
MPENVAPRTG PPAGAAGAAG GRGKSAYQDR DKPAQIRFSN ISAAKAVADA IRTSLGPKGM
DKMIQDGKGD VTITNDGATI LKQMQVLHPA ARMLVELSKA QDIEAGDGTT SVVIIAGSLL
DSCTKLLQKG IHPTIISESF QKALEKGIEI LTDMSRPEEL SDRETLLNSA ATSLNSKVVS
QYSSLLSPMS VDAVMKVIDP ATATSVDLRD IKIVKKLGGT IDDCELVEGL VLTQKVANSG
ITRVEKAKIG LIQFCLSAPK TDMDNQIVVS DYVQMDRVLR EERAYILNLV KQIKKTGCNV
LLIQKSILRD ALSDLALHFL NKMKIMVVKD IEREDIEFIC KTIGTKPVAH VDQFTADMLG
SAELAEEVSL NGSGKLIKIT GCASPGKTVT IVVRGSNKLV IEEAERSIHD ALCVIRCLVK
KRALIAGGGA PEIELALRLT EYSRTLSGME SYCIRAFADA MEVIPSTLAE NAGLNPISTV
TELRNRHAQG EKTTGINVRK GGISNILEEQ VVQPLLVSVS ALTLATETVR SILKIDDVVN
TR
