ID   TCPA_MACFA              Reviewed;         556 AA.
AC   Q4R5G2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=T-complex protein 1 subunit alpha;
DE            Short=TCP-1-alpha;
DE   AltName: Full=CCT-alpha;
GN   Name=TCP1; Synonyms=CCT1; ORFNames=QnpA-12515;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-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; AB169581; BAE01663.1; -; mRNA.
DR   RefSeq; NP_001272198.1; NM_001285269.1.
DR   AlphaFoldDB; Q4R5G2; -.
DR   SMR; Q4R5G2; -.
DR   STRING; 9541.XP_005551571.1; -.
DR   GeneID; 101866990; -.
DR   CTD; 6950; -.
DR   eggNOG; KOG0360; Eukaryota.
DR   OrthoDB; 335406at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; ISS: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   2: Evidence at transcript level;
KW   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_0000273198"
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;  60256 MW;  2F05E36E39B7A130 CRC64;
     MEGPLSVFGD RSTGEAIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT
     ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELGKQ KIHPTSVISG
     YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK
     YTDTRGQPRY PVNSVNILKA HGRSQMESKL ISGYALNCVV GSQGMPKRIV NAKIACLDFS
     LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF
     VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE
     LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS
     IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
     KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD
     KHGSYEDAVH SGALND