TCPH_BOVIN
ID TCPH_BOVIN Reviewed; 543 AA.
AC Q2NKZ1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=T-complex protein 1 subunit eta;
DE Short=TCP-1-eta;
DE AltName: Full=CCT-eta;
GN Name=CCT7;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-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. The TRiC complex plays a role
CC in the folding of actin and tubulin. {ECO:0000250|UniProtKB:Q99832}.
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 (By similarity).
CC Interacts with DLEC1 (By similarity). {ECO:0000250|UniProtKB:Q99832}.
CC -!- INTERACTION:
CC Q2NKZ1; F1MWD3: CCT5; NbExp=6; IntAct=EBI-9014155, EBI-15839846;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P80313}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; BC111332; AAI11333.1; -; mRNA.
DR RefSeq; NP_001039636.1; NM_001046171.2.
DR PDB; 3IYG; EM; -; H=10-524.
DR PDB; 4B2T; X-ray; 5.50 A; H/h=1-543.
DR PDBsum; 3IYG; -.
DR PDBsum; 4B2T; -.
DR AlphaFoldDB; Q2NKZ1; -.
DR SMR; Q2NKZ1; -.
DR CORUM; Q2NKZ1; -.
DR DIP; DIP-58621N; -.
DR IntAct; Q2NKZ1; 5.
DR STRING; 9913.ENSBTAP00000016954; -.
DR PaxDb; Q2NKZ1; -.
DR PRIDE; Q2NKZ1; -.
DR Ensembl; ENSBTAT00000016954; ENSBTAP00000016954; ENSBTAG00000012756.
DR GeneID; 514355; -.
DR KEGG; bta:514355; -.
DR CTD; 10574; -.
DR VEuPathDB; HostDB:ENSBTAG00000012756; -.
DR VGNC; VGNC:27000; CCT7.
DR eggNOG; KOG0361; Eukaryota.
DR GeneTree; ENSGT00550000074832; -.
DR HOGENOM; CLU_008891_7_1_1; -.
DR InParanoid; Q2NKZ1; -.
DR OMA; HRKGNTW; -.
DR OrthoDB; 335406at2759; -.
DR BRENDA; 3.6.4.B10; 908.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000012756; Expressed in spermatid and 106 other tissues.
DR ExpressionAtlas; Q2NKZ1; 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: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:0007339; P:binding of sperm to zona pellucida; 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:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd03340; TCP1_eta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012720; Chap_CCT_eta.
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:SF22; PTHR11353:SF22; 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; TIGR02345; chap_CCT_eta; 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; Methylation; Nucleotide-binding; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..543
FT /note="T-complex protein 1 subunit eta"
FT /id="PRO_0000236264"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80313"
FT MOD_RES 320
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
FT MOD_RES 535
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
SQ SEQUENCE 543 AA; 59443 MW; E5367265CFAC03EF CRC64;
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN
DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI
IIRAFRTATQ LAVNKIKEIA VTVKKEDKVE QRKLLEKCAM TALSSKLISQ QKAFFAKMVV
DAVMMLDDLL QLKMIGIKKV QGGALEESQL VAGVAFKKTF SYAGFEMQPK KYHNPMIALL
NVELELKAEK DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHHSGAKVVL SKLPIGDVAT
QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSSD VLGRCQVFEE TQIGGERYNF
FTGCPKAKTC TIILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL
RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRARHAQ GGMWYGVDIN
TEDIADNFEA FVWEPAMVRI NALTAASEAA CLIVSVDETI KNPRSTVDAS PAAGRGRGRG
RLH
