TCPB_MESAU
ID TCPB_MESAU Reviewed; 150 AA.
AC P86245;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=T-complex protein 1 subunit beta {ECO:0000250|UniProtKB:P78371};
DE Short=TCP-1-beta {ECO:0000250|UniProtKB:P78371};
DE AltName: Full=CCT-beta {ECO:0000250|UniProtKB:P78371};
DE Flags: Fragments;
GN Name=CCT2 {ECO:0000250|UniProtKB:P78371};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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:P78371}.
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. Interacts with
CC FLCN (By similarity). Interacts with DLEC1 (By similarity).
CC {ECO:0000250|UniProtKB:P78371}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78371}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000255}.
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DR AlphaFoldDB; P86245; -.
DR SMR; P86245; -.
DR IntAct; P86245; 1.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
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 Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012716; Chap_CCT_beta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR PANTHER; PTHR11353; PTHR11353; 3.
DR PANTHER; PTHR11353:SF23; PTHR11353:SF23; 3.
DR SUPFAM; SSF48592; SSF48592; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN <1..>150
FT /note="T-complex protein 1 subunit beta"
FT /id="PRO_0000394423"
FT NON_CONS 27..28
FT /evidence="ECO:0000305"
FT NON_CONS 49..50
FT /evidence="ECO:0000305"
FT NON_CONS 68..69
FT /evidence="ECO:0000305"
FT NON_CONS 117..118
FT /evidence="ECO:0000305"
FT NON_CONS 129..130
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 150
SQ SEQUENCE 150 AA; 15887 MW; 2D3732E0BE4DC147 CRC64;
AGADEERAET ARLSSFIGAI AIGDLVKVQD DEVGDGTTSV TVLAAELLRL GGSLADSYLD
EGFLLDKKQL IYNYPEQLFG AAGVMAIEHA DFAGVERLAL VTGGEIASTF DHPELVKGAT
QQILDEAERQ VLLSAAEAAE VILRVDNIIK
