TCPQ_CHICK
ID TCPQ_CHICK Reviewed; 548 AA.
AC Q6EE31;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=T-complex protein 1 subunit theta;
DE Short=TCP-1-theta;
DE AltName: Full=CCT-theta;
GN Name=CCT8 {ECO:0000250|UniProtKB:P50990};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:AAS49611.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:AAS49611.1};
RX PubMed=15128875; DOI=10.1093/molbev/msh150;
RA Takezaki N., Figueroa F., Zaleska-Rutczynska Z., Takahata N., Klein J.;
RT "The phylogenetic relationship of tetrapod, coelacanth, and lungfish
RT revealed by the sequences of forty-four nuclear genes.";
RL Mol. Biol. Evol. 21:1512-1524(2004).
RN [2] {ECO:0000305}
RP IDENTIFICATION, AND MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX PubMed=16287166; DOI=10.1002/pmic.200402056;
RA Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA Schneider J., Palomar M.A., Linares R.;
RT "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT development.";
RL Proteomics 5:4946-4957(2005).
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:P50990}.
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:P50990}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50990}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:P42932}.
CC -!- MASS SPECTROMETRY: Mass=60153; Mass_error=4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287166};
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000255}.
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DR EMBL; AY393846; AAS49611.1; -; mRNA.
DR RefSeq; NP_001004389.2; NM_001004389.2.
DR BioGRID; 679712; 1.
DR STRING; 9031.ENSGALP00000025461; -.
DR PaxDb; Q6EE31; -.
DR PRIDE; Q6EE31; -.
DR GeneID; 418486; -.
DR KEGG; gga:418486; -.
DR CTD; 10694; -.
DR VEuPathDB; HostDB:geneid_418486; -.
DR eggNOG; KOG0362; Eukaryota.
DR InParanoid; Q6EE31; -.
DR PhylomeDB; Q6EE31; -.
DR PRO; PR:Q6EE31; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd03341; TCP1_theta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012721; Chap_CCT_theta.
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; TIGR02346; chap_CCT_theta; 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; Cytoplasm;
KW Cytoskeleton; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16287166"
FT CHAIN 2..548
FT /note="T-complex protein 1 subunit theta"
FT /id="PRO_0000223485"
FT REGION 529..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 505
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 548 AA; 59485 MW; D793C099B09C7A8C CRC64;
MALHVPKAPG FAQMLKEGAK HYSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL
EKLFVTNDAA TILRELEVQH PAAKMLVMAS HMQEQEVGDG TNFVLVFAGV LLELAEDLLR
MGLSVSEVIE GYEKACKKAL EILPDLVCCS AKNLRDVDEV ASLLHTSVMS KQYGNESFLS
KLIAQACVSI LPDSGHFNVD NIRVCKIVGA GVSASSVLHG MVFNKETEGD VTSVKDAKXA
VYSCPFDGMI TETKGTVLIK NAEELMNFSK GEENLMDLQV KAIADSGANV VVTGGKVADM
ALHYANKYNL MIVRLNSKWD LRRLCKTVGA TALPRLTPPT LEEMGHCNSV YLSEVGDTQV
VVFKHEKEDG AISTILIRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA
KQITSYGETC PGLDQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYAV HQEGNKNVGF
DIEAEAAAVK DMLEAGILDT YLGKYWGIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK
DWDEDQND
