TCPA_BOVIN
ID TCPA_BOVIN Reviewed; 556 AA.
AC Q32L40;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=T-complex protein 1 subunit alpha;
DE Short=TCP-1-alpha;
DE AltName: Full=CCT-alpha;
GN Name=TCP1; Synonyms=CCT1;
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 (NOV-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: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; BC109781; AAI09782.1; -; mRNA.
DR RefSeq; NP_001033175.1; NM_001038086.1.
DR PDB; 3IYG; EM; -; A=7-535.
DR PDB; 4B2T; X-ray; 5.50 A; A/a=1-556.
DR PDBsum; 3IYG; -.
DR PDBsum; 4B2T; -.
DR AlphaFoldDB; Q32L40; -.
DR SMR; Q32L40; -.
DR CORUM; Q32L40; -.
DR DIP; DIP-58617N; -.
DR IntAct; Q32L40; 2.
DR STRING; 9913.ENSBTAP00000003662; -.
DR PaxDb; Q32L40; -.
DR PeptideAtlas; Q32L40; -.
DR PRIDE; Q32L40; -.
DR GeneID; 512043; -.
DR KEGG; bta:512043; -.
DR CTD; 6950; -.
DR eggNOG; KOG0360; Eukaryota.
DR InParanoid; Q32L40; -.
DR OrthoDB; 335406at2759; -.
DR BRENDA; 3.6.4.B10; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..556
FT /note="T-complex protein 1 subunit alpha"
FT /id="PRO_0000236258"
FT REGION 536..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
SQ SEQUENCE 556 AA; 60206 MW; 161E9B04CFC5A1D7 CRC64;
MEGPLSVFGD RSTGEAIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT
ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG
YRLACKEAVR YISENLIINT DELGRDCLIN AAKTSMSSKV IGINGDFFAN LVVDAVLAIK
YTDIRGQPRY PVNSINVLKA HGRSQMESML INGYALNCVV GSQGMPKRIV NAKIACLDFS
LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF
VEAGAMAVRR VLKRDLKRIA KASGATVLST LANLEGEETF EASMLGQAEE VVQERICDDE
LILIKNTKAR TSASVILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS
IYLENYATSM GSREQLAIAE FARSLPVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
KNLKWIGLDL VNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD
KHGGYEDAVH SGALDA
