TCPZ_RABIT
ID TCPZ_RABIT Reviewed; 531 AA.
AC O77622;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=T-complex protein 1 subunit zeta;
DE Short=TCP-1-zeta;
DE AltName: Full=CCT-zeta;
GN Name=CCT6;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand;
RX PubMed=10810232; DOI=10.1159/000020663;
RA Schwartz G.J., Kittelberger A.M., Segel G.B.;
RT "Cloning of rabbit Cct6 and the distribution of the Cct complex in
RT mammalian tissues.";
RL Exp. Nephrol. 8:152-160(2000).
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.
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 -!- INTERACTION:
CC O77622; Q9BUR4: WRAP53; Xeno; NbExp=2; IntAct=EBI-10714431, EBI-2563542;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; AF068483; AAC19379.1; -; mRNA.
DR RefSeq; NP_001075508.1; NM_001082039.1.
DR AlphaFoldDB; O77622; -.
DR SMR; O77622; -.
DR IntAct; O77622; 1.
DR STRING; 9986.ENSOCUP00000015180; -.
DR Ensembl; ENSOCUT00000017675; ENSOCUP00000015180; ENSOCUG00000017674.
DR GeneID; 100008688; -.
DR KEGG; ocu:100008688; -.
DR CTD; 908; -.
DR eggNOG; KOG0359; Eukaryota.
DR GeneTree; ENSGT00940000154631; -.
DR HOGENOM; CLU_008891_3_1_1; -.
DR InParanoid; O77622; -.
DR OMA; LHPRIMT; -.
DR OrthoDB; 482152at2759; -.
DR TreeFam; TF106333; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000017674; Expressed in embryo and 15 other tissues.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
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:0071987; F:WD40-repeat domain binding; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IEA:Ensembl.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
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 Acetylation; ATP-binding; Chaperone; Cytoplasm; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT CHAIN 2..531
FT /note="T-complex protein 1 subunit zeta"
FT /id="PRO_0000128359"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80317"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80317"
FT MOD_RES 365
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 377
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 388
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P40227"
SQ SEQUENCE 531 AA; 58024 MW; 2A5007DA986A5338 CRC64;
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIT
EGFEAAKEKA LQVLEQIKVS REMDRETLID VARTSLRTKV HAELADVLTE AVVDSILAIK
KQDEPIDLFM VEIMEMKHKS ETDTSLIRGL VLDHGARHPD MKKRVEDAYI LTCNVSLEYE
KTEVNSGFFY KSAEEREKLV KAERKFIEDR VKKIVELKKK VCGDSDKGFV VINQKGIDPF
SLDALAKEGI VALRRAKRRN MERLTLACGG VPLNSLDDLN PDCLGHAGLV YEYTLGEEKF
TFIEKCNNPR SVTLLVKGPN KHTLTQIKDA IRDGLRAVKN AIDDGCVVPG AGAVEVAMAE
ALIKYKSSVK GRAQLGVQAF ADALLIIPKV LAQNSGFDLQ ETLVKIRTEH SESGQLVGVD
LNTGEPMVAA EVGIWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK G
