TCPG_PONAB
ID TCPG_PONAB Reviewed; 545 AA.
AC Q5NVF9; Q5R984;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
GN Name=CCT3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:P49368}.
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 (By similarity).
CC Interacts with DNAAF4 (By similarity). Interacts with DLEC1 (By
CC similarity). {ECO:0000250|UniProtKB:P49368,
CC ECO:0000250|UniProtKB:P80318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; CR859507; CAH91676.1; -; mRNA.
DR EMBL; CR926077; CAI29704.1; -; mRNA.
DR RefSeq; NP_001125981.1; NM_001132509.1.
DR AlphaFoldDB; Q5NVF9; -.
DR SMR; Q5NVF9; -.
DR STRING; 9601.ENSPPYP00000011901; -.
DR GeneID; 100172920; -.
DR KEGG; pon:100172920; -.
DR CTD; 7203; -.
DR eggNOG; KOG0364; Eukaryota.
DR InParanoid; Q5NVF9; -.
DR OrthoDB; 391677at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
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; IEA:InterPro.
DR CDD; cd03337; TCP1_gamma; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012719; Chap_CCT_gamma.
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; TIGR02344; chap_CCT_gamma; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Cytoplasm; Disulfide bond;
KW Isopeptide bond; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..545
FT /note="T-complex protein 1 subunit gamma"
FT /id="PRO_0000128324"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80318"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 247
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT DISULFID 366..372
FT /evidence="ECO:0000250"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT CONFLICT 81
FT /note="V -> I (in Ref. 1; CAH91676)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="I -> T (in Ref. 1; CAH91676)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="Q -> R (in Ref. 1; CAH91676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 60547 MW; 1A8B9BFEECA531CC CRC64;
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT
NDGNAILREI QVQHPAAKSM VEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT
VVISAYRKAL DDMISTLKKI SIPVDINDSD MMLNIINSSI TTKAISRWSS LACNIALDAV
KMVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL
LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA
QHYLMRANIT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF
TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH
ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQENCETWGV
NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQSRQGGAP
DAGQE
