ID   TCPZ_CHICK              Reviewed;         530 AA.
AC   Q5ZJ54; P84164;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=T-complex protein 1 subunit zeta;
DE            Short=TCP-1-zeta;
DE   AltName: Full=CCT-zeta;
GN   Name=CCT6 {ECO:0000250|UniProtKB:O77622}; ORFNames=RCJMB04_20k5;
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:0000305, ECO:0000312|EMBL:CAG32239.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAG32239.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG32239.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin (By similarity). {ECO:0000250|UniProtKB:P40227}.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40227}.
CC   -!- MASS SPECTROMETRY: Mass=58025; Mass_error=3; 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; AJ720580; CAG32239.1; -; mRNA.
DR   RefSeq; NP_001006216.1; NM_001006216.1.
DR   AlphaFoldDB; Q5ZJ54; -.
DR   SMR; Q5ZJ54; -.
DR   BioGRID; 678874; 1.
DR   STRING; 9031.ENSGALP00000003850; -.
DR   PaxDb; Q5ZJ54; -.
DR   Ensembl; ENSGALT00000003859; ENSGALP00000003850; ENSGALG00000002448.
DR   GeneID; 417541; -.
DR   KEGG; gga:417541; -.
DR   CTD; 908; -.
DR   VEuPathDB; HostDB:geneid_417541; -.
DR   eggNOG; KOG0359; Eukaryota.
DR   GeneTree; ENSGT00940000156339; -.
DR   HOGENOM; CLU_008891_3_1_1; -.
DR   InParanoid; Q5ZJ54; -.
DR   OMA; LHPRIMT; -.
DR   OrthoDB; 482152at2759; -.
DR   PhylomeDB; Q5ZJ54; -.
DR   PRO; PR:Q5ZJ54; -.
DR   Proteomes; UP000000539; Chromosome 19.
DR   Bgee; ENSGALG00000002448; Expressed in spermatid and 13 other tissues.
DR   ExpressionAtlas; Q5ZJ54; baseline and differential.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
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; cd03342; TCP1_zeta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012722; Chap_CCT_zeta.
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; TIGR02347; chap_CCT_zeta; 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   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..530
FT                   /note="T-complex protein 1 subunit zeta"
FT                   /id="PRO_0000223483"
SQ   SEQUENCE   530 AA;  57645 MW;  8B8F639A186F12EC CRC64;
     MAVKALNPKA EVARAQAALA VNISAARGLQ DVLRTNLGPK GTMKMLVSGA GDIKLTKDGN
     VLLQEMQIQH PTASLIAKVA TAQDDITGDG TTSNVLIIGE LLKQADLYIS EGLHPRIVAE
     GFEIAKEKAL EVLEQVKVTK EMDRETLIDV AKTSLRTKVH TELADILTEA VVDSVLAVRK
     PGEPIDLHMV EIMEMKHKSE TDTTLIRGLV LDHGARHPDM KKRVEDAYIL TCNVSLEYEK
     TEVSAGFFYK SAEEREKLVK AERKFIEDRV SKIIDLKRRV CGDSDKGFIV INQKGIDPFS
     LDALAKEGIV ALRRAKRRNM ERLTLACGGT AMNSVEDLTP DCLGHAGLVY EYTLGEEKYT
     FIEKCDNPRS VTLLIRGPNK HTLTQIKDAV RDGLRAVKNA IEDGCVIPGA GALEVAVANA
     LVKHKPNVKG RAQLGVQAFA DALLIIPKVL AQNSGYDPQE TLVKVQAEHA ESGQLTGVDL
     NTGEPMVAAA AGIWDNYNVK KQLLHSCTVI ASNILLVDEI MRAGMSSLKG