TCPA_CRIGR
ID TCPA_CRIGR Reviewed; 556 AA.
AC P18279;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=T-complex protein 1 subunit alpha;
DE Short=TCP-1-alpha;
DE AltName: Full=65 kDa antigen;
DE AltName: Full=CCT-alpha;
GN Name=TCP1; Synonyms=CCT1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1977474; DOI=10.1016/0167-4781(90)90214-m;
RA Ahmad S., Gupta R.S.;
RT "Cloning of a Chinese hamster protein homologous to the mouse t-complex
RT protein TCP-1: structural similarity to the ubiquitous 'chaperonin' family
RT of heat-shock proteins.";
RL Biochim. Biophys. Acta 1087:253-255(1990).
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:P17987}.
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 GBA (By similarity). Interacts with DLEC1 (By similarity).
CC {ECO:0000250|UniProtKB:P17987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P17987}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P17987}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; M34665; AAA37020.1; -; mRNA.
DR PIR; S13163; S13163.
DR RefSeq; NP_001233662.1; NM_001246733.1.
DR AlphaFoldDB; P18279; -.
DR SMR; P18279; -.
DR STRING; 10029.NP_001233662.1; -.
DR Ensembl; ENSCGRT00001008930; ENSCGRP00001005768; ENSCGRG00001007629.
DR GeneID; 100689476; -.
DR KEGG; cge:100689476; -.
DR CTD; 6950; -.
DR eggNOG; KOG0360; Eukaryota.
DR GeneTree; ENSGT00550000074878; -.
DR OMA; KNYKNYG; -.
DR OrthoDB; 335406at2759; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0000242; C:pericentriolar material; 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; IEA:InterPro.
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: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:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:2000109; P:regulation of macrophage apoptotic process; IEA:Ensembl.
DR GO; GO:0090666; P:scaRNA localization to Cajal body; IEA:Ensembl.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR GO; GO:0044053; P:translocation of peptides or proteins into host cell cytoplasm; IEA:Ensembl.
DR CDD; cd03335; TCP1_alpha; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012715; Chap_CCT_alpha.
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; TIGR02340; chap_CCT_alpha; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Nucleotide-binding; Phosphoprotein.
FT CHAIN 1..556
FT /note="T-complex protein 1 subunit alpha"
FT /id="PRO_0000128301"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11983"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
SQ SEQUENCE 556 AA; 60339 MW; FD1D028B0DC1C30C CRC64;
MEGPLSVFGD RSTGEAIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT
ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG
YRLACKEAVR YISENLIINT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAVK
YTDLRGQPRY PVNSVNILKA HGRSQVESML INGYALNCVV GSQGMPKRIV NAKIACLDFS
LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIEKILA TGANVILTTG GIDDMCLKYF
VEAGAMAVRR VLKRDLKRIA KASGASILST LANLEGEETF EATMLGQAEE VVQERICDDE
LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS
IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
KNLKWIGLDL INGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPETKDD
KHGSYENAVH SGALDD
