TCPH_PLAF7
ID TCPH_PLAF7 Reviewed; 539 AA.
AC O77323;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=T-complex protein 1 subunit eta;
DE Short=TCP-1-eta;
DE AltName: Full=CCT-eta;
GN ORFNames=MAL3P3.6, PFC0350c;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=10448855; DOI=10.1038/22964;
RA Bowman S., Lawson D., Basham D., Brown D., Chillingworth T., Churcher C.M.,
RA Craig A., Davies R.M., Devlin K., Feltwell T., Gentles S., Gwilliam R.,
RA Hamlin N., Harris D., Holroyd S., Hornsby T., Horrocks P., Jagels K.,
RA Jassal B., Kyes S., McLean J., Moule S., Mungall K.L., Murphy L.,
RA Oliver K., Quail M.A., Rajandream M.A., Rutter S., Skelton J., Squares R.,
RA Squares S., Sulston J.E., Whitehead S., Woodward J.R., Newbold C.,
RA Barrell B.G.;
RT "The complete nucleotide sequence of chromosome 3 of Plasmodium
RT falciparum.";
RL Nature 400:532-538(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC two stacked rings, 12 to 16 nm in diameter. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; AL844502; CAB11107.1; -; Genomic_DNA.
DR PIR; T18430; T18430.
DR RefSeq; XP_001351157.1; XM_001351121.1.
DR AlphaFoldDB; O77323; -.
DR SMR; O77323; -.
DR BioGRID; 1209650; 4.
DR IntAct; O77323; 4.
DR STRING; 5833.PFC0350c; -.
DR DrugBank; DB11638; Artenimol.
DR SwissPalm; O77323; -.
DR PRIDE; O77323; -.
DR EnsemblProtists; CAB11107; CAB11107; PF3D7_0308200.
DR GeneID; 814399; -.
DR KEGG; pfa:PF3D7_0308200; -.
DR VEuPathDB; PlasmoDB:PF3D7_0308200; -.
DR HOGENOM; CLU_008891_7_1_1; -.
DR InParanoid; O77323; -.
DR OMA; HRKGNTW; -.
DR PhylomeDB; O77323; -.
DR BRENDA; 3.6.4.B10; 4889.
DR Reactome; R-PFA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Proteomes; UP000001450; Chromosome 3.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:GeneDB.
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; ISS:GeneDB.
DR GO; GO:0006457; P:protein folding; ISS:GeneDB.
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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..539
FT /note="T-complex protein 1 subunit eta"
FT /id="PRO_0000128368"
SQ SEQUENCE 539 AA; 59577 MW; 51A18D81698AAE6B CRC64;
MSHLMSLPIV LLKEGTDTAQ GRSQIIRNIN ACQIIVDIVK TTLGPRGMDK LIYTERDVTI
TNDGATVMNL LNISHPAASI LVDIAKSQDD EVGDGTTSVV VVAGELLNEA KGLLNDGIEP
NMIIDGFRNA CNVAINKLNE LSLNFSNKNE EEKRSILLKC AQTALNSKLV SNHKEFFGEL
VVNAVYKLGD NLDKSNIGIK KVTGGSCLDT QLIYGVAFKK TFSYAGFEQQ PKKFINPKIL
LLNVELELKA EKENAEVRIE NPNEYNSIVQ AEWDIIFKKL NLIKDCGANI VLSKLPIGDI
ATQFFADHDI FCAGRVEDAD LKRTANATGA LVQTSLFNLN DDVLGTCGVF EEVQIGNERY
NIFKECLKTK SVTIILRGGA KQFIEEVERS INDAIMIVLR CITNSEIVPG AGSIEMQLSK
YLRIYSRSIC NKEQIVLFSF AKALESIPRH LSHNAGYDST DILNKLRKKH SEQTSDIWYG
VDCMEGDIIN AYDNCIFEVT KIKRNVIYSA TEAACLILSI DETIKNPSSA AGTQRSPYS