ID   TCPA_CAEEL              Reviewed;         549 AA.
AC   P41988; Q22228;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=T-complex protein 1 subunit alpha;
DE            Short=TCP-1-alpha;
DE   AltName: Full=CCT-alpha;
GN   Name=cct-1; Synonyms=tcp-1; ORFNames=T05C12.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7758963; DOI=10.1016/0378-1119(95)00025-2;
RA   Leroux M.R., Candido E.P.M.;
RT   "Molecular analysis of Caenorhabditis elegans tcp-1, a gene encoding a
RT   chaperonin protein.";
RL   Gene 156:241-246(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; U07941; AAB05072.1; -; Genomic_DNA.
DR   EMBL; Z66500; CAA91308.1; -; Genomic_DNA.
DR   PIR; JC4083; JC4083.
DR   PIR; T24508; T24508.
DR   RefSeq; NP_495722.1; NM_063321.4.
DR   AlphaFoldDB; P41988; -.
DR   SMR; P41988; -.
DR   BioGRID; 39647; 13.
DR   IntAct; P41988; 2.
DR   MINT; P41988; -.
DR   STRING; 6239.T05C12.7; -.
DR   EPD; P41988; -.
DR   PaxDb; P41988; -.
DR   PeptideAtlas; P41988; -.
DR   EnsemblMetazoa; T05C12.7.1; T05C12.7.1; WBGene00000377.
DR   GeneID; 174318; -.
DR   KEGG; cel:CELE_T05C12.7; -.
DR   UCSC; T05C12.7.1; c. elegans.
DR   CTD; 174318; -.
DR   WormBase; T05C12.7; CE02319; WBGene00000377; cct-1.
DR   eggNOG; KOG0360; Eukaryota.
DR   GeneTree; ENSGT00550000074878; -.
DR   HOGENOM; CLU_008891_7_3_1; -.
DR   InParanoid; P41988; -.
DR   OMA; KNYKNYG; -.
DR   OrthoDB; 335406at2759; -.
DR   PhylomeDB; P41988; -.
DR   BRENDA; 3.6.4.B10; 1045.
DR   Reactome; R-CEL-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-CEL-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P41988; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000377; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..549
FT                   /note="T-complex protein 1 subunit alpha"
FT                   /id="PRO_0000128309"
FT   CONFLICT        469
FT                   /note="K -> F (in Ref. 1; AAB05072)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   549 AA;  58803 MW;  DFA38B599F642407 CRC64;
     MASAGDSILA LTGKRTTGQG IRSQNVTAAV AIANIVKSSL GPVGLDKMLV DDVGDVIVTN
     DGATILKQLE VEHPAGKVLV ELAQLQDEEV GDGTTSVVIV AAELLKRADE LVKQKVHPTT
     IINGYRLACK EAVKYISENI SFTSDSIGRQ SVVNAAKTSM SSKIIGPDAD FFGELVVDAA
     EAVRVENNGK VTYPINAVNV LKAHGKSARE SVLVKGYALN CTVASQAMPL RVQNAKIACL
     DFSLMKAKMH LGISVVVEDP AKLEAIRREE FDITKRRIDK ILKAGANVVL TTGGIDDLCL
     KQFVESGAMA VRRCKKSDLK RIAKATGATL TVSLATLEGD EAFDASLLGH ADEIVQERIS
     DDELILIKGP KSRTASSIIL RGANDVMLDE MERSVHDSLC VVRRVLESKK LVAGGGAVET
     SLSLFLETYA QTLSSREQLA VAEFASALLI IPKVLASNAA RDSTDLVTKL RAYHSKAQLI
     PQLQHLKWAG LDLEEGTIRD NKEAGILEPA LSKVKSLKFA TEAAITILRI DDLIKLDKQE
     PLGGDDCHA