ID   TCPA_MESAU              Reviewed;         123 AA.
AC   P86208;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=T-complex protein 1 subunit alpha {ECO:0000250|UniProtKB:P17987};
DE            Short=TCP-1-alpha {ECO:0000250|UniProtKB:P17987};
DE   AltName: Full=CCT-alpha {ECO:0000250|UniProtKB:P17987};
DE   Flags: Fragments;
GN   Name=TCP1 {ECO:0000250|UniProtKB:P17987};
GN   Synonyms=CCT1 {ECO:0000250|UniProtKB:P17987};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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:0000255}.
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DR   AlphaFoldDB; P86208; -.
DR   SMR; P86208; -.
DR   Proteomes; UP000189706; 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.10.560.10; -; 1.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   PANTHER; PTHR11353; PTHR11353; 3.
DR   SUPFAM; SSF48592; SSF48592; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           <1..>123
FT                   /note="T-complex protein 1 subunit alpha"
FT                   /id="PRO_0000394300"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000305"
FT   NON_CONS        34..35
FT                   /evidence="ECO:0000305"
FT   NON_CONS        51..52
FT                   /evidence="ECO:0000305"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000305"
FT   NON_CONS        99..100
FT                   /evidence="ECO:0000305"
FT   NON_CONS        112..113
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         123
SQ   SEQUENCE   123 AA;  13411 MW;  9BED15DEBE076DD9 CRC64;
     IHPTSVISGY RYISENLIIN TDELGRDCLI NAAKLGVQVV ITDPEKLDQI RYFVEAGAMA
     VRSVVPGGGA VEAALSIYLE NYATSMGSRE QLAIAEFARA FHNEAQVNPE RKFATEAAIT
     ILR