ID   TCPD_TAKRU              Reviewed;         536 AA.
AC   P53451;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=cct4; Synonyms=cctd;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Testis;
RX   PubMed=8543170; DOI=10.1016/0378-1119(95)00604-4;
RA   Yoda T., Morita T., Kawatsu K., Sueki K., Shibata T., Hamano Y.;
RT   "Cloning and sequencing of the chaperonin-encoding Cctd gene from Fugu
RT   rubripes rubripes.";
RL   Gene 166:249-253(1995).
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. {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. {ECO:0000250|UniProtKB:P50991}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50991}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; D49483; BAA08447.1; -; mRNA.
DR   EMBL; D49484; BAA18913.1; -; Genomic_DNA.
DR   PIR; JC4521; JC4521.
DR   RefSeq; NP_001027851.1; NM_001032679.1.
DR   AlphaFoldDB; P53451; -.
DR   SMR; P53451; -.
DR   STRING; 31033.ENSTRUP00000004197; -.
DR   GeneID; 446052; -.
DR   KEGG; tru:446052; -.
DR   CTD; 10575; -.
DR   eggNOG; KOG0358; Eukaryota.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; P53451; -.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 511484at2759; -.
DR   TreeFam; TF106332; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; 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   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..536
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000128336"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  57716 MW;  B3ED3285FAC18D07 CRC64;
     MPEGKATSSA SNTGKNKGGA YQDRDKPAQI RYSNISAAKA VADAVRTSLG PKGMDKMIQD
     EKGDVTITND GATILKQMQV LHPSAKMLVE LSKAQDIEAG DGTTSVVVIA GALLDSCNRL
     LQRGIHPTII SESFQKAVDK GVEVLTAMSQ PVQLGDRETL LNSATTSLCS KVVSQYSSLL
     APMSVDAVMR VIDPATATSV DLHDIKIIKK LGGTIDDCEL VEGLVLTQRV ANSSVSRVEK
     AKIGLIQFCL SPPKTDMDNQ IVVSDYTQMD RVLREERAYI LNMVKQIKKA GCNVLFIQKS
     ILRDALSDLA LHFLNKMKIM VVKDIEREDI EFICKTIGTK PIAHIDHFTP EMLGTAELAE
     EVSLDGSGKL VKITGCASPG KTVSIVVRGS NKLVIEEAER SIHDALCVIR CLVKKRALIA
     GGGAPEIELA VRLAEYSRTL GGMEAYCVRA YSDALEVIPS TLAENAGLNP ISTVTELRNR
     HAQGDKMAGI NVRKGGISNI MEELVVQPLL VSISALTLAT ETVRSILKID DVVNAR