TCPB_BOVIN
ID TCPB_BOVIN Reviewed; 535 AA.
AC Q3ZBH0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=T-complex protein 1 subunit beta;
DE Short=TCP-1-beta;
DE AltName: Full=CCT-beta;
GN Name=CCT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- INTERACTION:
CC Q3ZBH0; F1MWD3: CCT5; NbExp=6; IntAct=EBI-9014138, EBI-15839846;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78371}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; BC103298; AAI03299.1; -; mRNA.
DR RefSeq; NP_001029411.1; NM_001034239.1.
DR PDB; 3IYG; EM; -; B=14-526.
DR PDB; 3KTT; EM; -; B=14-526.
DR PDB; 4A0O; EM; 10.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=14-526.
DR PDB; 4A0V; EM; 10.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=14-526.
DR PDB; 4A0W; EM; 13.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=14-526.
DR PDB; 4A13; EM; 11.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=14-526.
DR PDB; 4B2T; X-ray; 5.50 A; B/b=1-535.
DR PDBsum; 3IYG; -.
DR PDBsum; 3KTT; -.
DR PDBsum; 4A0O; -.
DR PDBsum; 4A0V; -.
DR PDBsum; 4A0W; -.
DR PDBsum; 4A13; -.
DR PDBsum; 4B2T; -.
DR AlphaFoldDB; Q3ZBH0; -.
DR SMR; Q3ZBH0; -.
DR CORUM; Q3ZBH0; -.
DR DIP; DIP-58618N; -.
DR IntAct; Q3ZBH0; 3.
DR STRING; 9913.ENSBTAP00000025496; -.
DR PaxDb; Q3ZBH0; -.
DR PeptideAtlas; Q3ZBH0; -.
DR PRIDE; Q3ZBH0; -.
DR Ensembl; ENSBTAT00000025496; ENSBTAP00000025496; ENSBTAG00000019156.
DR GeneID; 505313; -.
DR KEGG; bta:505313; -.
DR CTD; 10576; -.
DR VEuPathDB; HostDB:ENSBTAG00000019156; -.
DR VGNC; VGNC:26995; CCT2.
DR eggNOG; KOG0363; Eukaryota.
DR GeneTree; ENSGT00550000074930; -.
DR HOGENOM; CLU_008891_6_2_1; -.
DR InParanoid; Q3ZBH0; -.
DR OMA; YCTGGEI; -.
DR OrthoDB; 335406at2759; -.
DR TreeFam; TF105645; -.
DR BRENDA; 3.6.4.B10; 908.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000019156; Expressed in spermatocyte and 105 other tissues.
DR ExpressionAtlas; Q3ZBH0; baseline and differential.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0002199; C:zona pellucida receptor complex; 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:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0051086; P:chaperone mediated protein folding independent of cofactor; IEA:Ensembl.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IEA:Ensembl.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IEA:Ensembl.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; IEA:Ensembl.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0090666; P:scaRNA localization to Cajal body; IEA:Ensembl.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd03336; TCP1_beta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 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; 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 PANTHER; PTHR11353:SF23; PTHR11353:SF23; 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; TIGR02341; chap_CCT_beta; 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 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW Isopeptide bond; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT CHAIN 2..535
FT /note="T-complex protein 1 subunit beta"
FT /id="PRO_0000236259"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 261
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78371"
SQ SEQUENCE 535 AA; 57475 MW; B21ED675C5EA4C7A CRC64;
MASLSLAPVN IFKAGADEER AETARLSSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS
LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK
IHPQTIIAGW REATKAARQA LLNSAVDHGS DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT
KLAVEAVLRL KGSGNLEAIH VIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA
NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP
EQLFGAAGVM AIEHADFVGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI
HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDSRTVYGG GCSEMLMAHA
VTQLASRTPG KEAVAMESYA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGKTTAGLDM
KEGTIGDMSV LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC
