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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
 
 
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