ID   TCPH_CHICK              Reviewed;         553 AA.
AC   Q5ZJK8; P84166;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=T-complex protein 1 subunit eta;
DE            Short=TCP-1-eta;
DE   AltName: Full=CCT-eta;
GN   Name=CCT7 {ECO:0000250|UniProtKB:Q99832}; ORFNames=RCJMB04_17g3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAG32085.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAG32085.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG32085.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION, AND MASS SPECTROMETRY.
RC   TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX   PubMed=16287166; DOI=10.1002/pmic.200402056;
RA   Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA   Schneider J., Palomar M.A., Linares R.;
RT   "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT   development.";
RL   Proteomics 5:4946-4957(2005).
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. {ECO:0000250|UniProtKB:Q99832}.
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. {ECO:0000250|UniProtKB:Q99832}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P80313}.
CC   -!- MASS SPECTROMETRY: Mass=59367; Mass_error=2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16287166};
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000255}.
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DR   EMBL; AJ720426; CAG32085.1; -; mRNA.
DR   AlphaFoldDB; Q5ZJK8; -.
DR   SMR; Q5ZJK8; -.
DR   BioGRID; 687761; 1.
DR   STRING; 9031.ENSGALP00000036304; -.
DR   VEuPathDB; HostDB:geneid_428806; -.
DR   eggNOG; KOG0361; Eukaryota.
DR   HOGENOM; CLU_008891_7_1_1; -.
DR   InParanoid; Q5ZJK8; -.
DR   PhylomeDB; Q5ZJK8; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
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; cd03340; TCP1_eta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012720; Chap_CCT_eta.
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   PANTHER; PTHR11353:SF22; PTHR11353:SF22; 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; TIGR02345; chap_CCT_eta; 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   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..553
FT                   /note="T-complex protein 1 subunit eta"
FT                   /id="PRO_0000223484"
FT   REGION          523..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  60349 MW;  5849216B3413F698 CRC64;
     MMPTPVILLK EGTDTSQGIP QLVSNINACQ VIAEAVRTTL GPRGMDKLIV DDRGKATISN
     DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI
     IIRAFRTATQ LAVNKIKDIA VSVKKEDKDE QRSLLEKCAA TALSSKLISQ SKEFFSKMVV
     DAVMMLDDLL QLKMIGIKKV QGGALEDSQL VAGVAFKKTF SYAGFEMQPK KYQSPKIALL
     NVELELKAEK DNAEVRVNTV EDYQAIVDAE WNILYDKLDK IHKSGAKVVL SKLPIGDVAT
     QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSDD VLGRCELFEE IQIGGDRYNF
     FTGCPKAKTC TIILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL
     RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRAKHAQ GGMWYGVDVN
     NEDIADNFEA CVWEPAIVRI NALTAASEAA CLIVSVDETI KNPRSTVDAP PGGRGRGRGQ
     TPQPLRPRSV ALS