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 08-NOV-2023, entry version 106.
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 PaxDb; 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; Unassembled WGS sequence.
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; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 NCBIfam; TIGR02345; chap_CCT_eta; 1.
DR NCBIfam; NF041082; thermosome_alpha; 1.
DR NCBIfam; NF041083; thermosome_beta; 1.
DR PANTHER; PTHR11353; CHAPERONIN; 1.
DR PANTHER; PTHR11353:SF22; T-COMPLEX PROTEIN 1 SUBUNIT ETA; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 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
//
