ID   TCPA_MONDO              Reviewed;         557 AA.
AC   Q9XT06;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
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   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10353914; DOI=10.1093/genetics/152.2.743;
RA   Shintani S., O'Huigin C., Toyosawa S., Michalova V., Klein J.;
RT   "Origin of gene overlap: the case of TCP1 and ACAT2.";
RL   Genetics 152:743-754(1999).
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; AF143497; AAD34973.1; -; mRNA.
DR   RefSeq; NP_001028144.1; NM_001032972.2.
DR   AlphaFoldDB; Q9XT06; -.
DR   SMR; Q9XT06; -.
DR   STRING; 13616.ENSMODP00000009278; -.
DR   GeneID; 497250; -.
DR   KEGG; mdo:497250; -.
DR   CTD; 6950; -.
DR   eggNOG; KOG0360; Eukaryota.
DR   InParanoid; Q9XT06; -.
DR   OrthoDB; 335406at2759; -.
DR   Proteomes; UP000002280; 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; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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..557
FT                   /note="T-complex protein 1 subunit alpha"
FT                   /id="PRO_0000128303"
FT   REGION          538..557
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         552
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17987"
SQ   SEQUENCE   557 AA;  60579 MW;  06A525366697780C CRC64;
     MEGPLSVFGE RTTGESIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT
     ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSIIGG
     YRLACKEAVR YINENLIINT DELGKDCLIN AAKTSMSSKI IGIDGDFFAN MVVDAVLAVK
     YTDVKGQPRY PVNSINVLKA HGRSQKESML INGYALNCVV ASQGMPKRIV NAKIACLDFS
     LQKTKMKLGV QVVITDPEKL DQIRKREADI TKERIQKILA TGANVILTTG GIDDMCLKYF
     VESMTIAVRR VLKRDLKRIA KASGATILST LASLEGEESF EASMLGQAEE VVQERICDDE
     LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS
     IYLENYATSM GSREQLAIAE FARSLLIIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
     KNLKWIGLDL VNGKPRDNRQ TGVFEPTMVK VKSLKFATEA AITILRIDDL IKLHPESKDD
     KRGGTYEDAV HSGAIED