ID   TCPG_XENLA              Reviewed;         547 AA.
AC   P50143; Q5D0A0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=T-complex protein 1 subunit gamma;
DE            Short=TCP-1-gamma;
DE   AltName: Full=CCT-gamma;
GN   Name=cct3; Synonyms=cctg;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8901050;
RX   DOI=10.1002/(sici)1097-0177(199604)205:4<387::aid-aja3>3.0.co;2-e;
RA   Dunn M.K., Mercola M.;
RT   "Cloning and expression of Xenopus CCT gamma, a chaperonin subunit
RT   developmentally regulated in neural-derived and myogenic lineages.";
RL   Dev. Dyn. 205:387-394(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8950171; DOI=10.1016/s0167-4781(96)88918-4;
RA   Walkley N.A., Page R.A., Malik A.N.;
RT   "Molecular characterisation of the Xenopus laevis chaperonin gene Cctg.";
RL   Biochim. Biophys. Acta 1309:25-30(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2003) 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. {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. {ECO:0000250|UniProtKB:P49368}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U37062; AAC59783.1; -; mRNA.
DR   EMBL; X84990; CAA59350.1; -; mRNA.
DR   EMBL; BC048365; AAH48365.1; -; mRNA.
DR   PIR; S54210; S54210.
DR   RefSeq; NP_001080812.1; NM_001087343.1.
DR   RefSeq; XP_018089033.1; XM_018233544.1.
DR   AlphaFoldDB; P50143; -.
DR   SMR; P50143; -.
DR   BioGRID; 98748; 1.
DR   MaxQB; P50143; -.
DR   DNASU; 380506; -.
DR   GeneID; 108700399; -.
DR   GeneID; 380506; -.
DR   KEGG; xla:380506; -.
DR   CTD; 380506; -.
DR   Xenbase; XB-GENE-6250719; cct3.S.
DR   OrthoDB; 391677at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 108700399; Expressed in testis and 19 other tissues.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IEA:UniProt.
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   ATP-binding; Chaperone; Cytoplasm; Disulfide bond; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..547
FT                   /note="T-complex protein 1 subunit gamma"
FT                   /id="PRO_0000128325"
FT   REGION          525..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        365..371
FT                   /evidence="ECO:0000250"
FT   CONFLICT        45
FT                   /note="M -> V (in Ref. 1; AAC59783)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  60636 MW;  CEFA1C85D6DD6700 CRC64;
     MMGRPVLVLS QNMKRESGRK VQSGNINAAK TIADIIRTCL GPRAMMKMLL DPMGGIVMTN
     DGNAILREIQ VQHPAAKSMI EISRTQDEEV GDGTTSVIIL AGEMLSVAEQ FLEQQMHPTV
     IISAYRKALD DMVNTLKEIS TPVDTNDREL MLKIINSAIN TKAIKLWADM ACGIALDAVK
     TVELEENGRK EIDIKKYAKV EKIPGGIIED SCVLRGVMVN KDVTHPKMRR LIKNPRIILL
     DCSLEYKKGE SQTEIEITRE EDFARILQME EEYIQQVCED IIRLKPDVVI TEKGISDLAQ
     HYLVKANITA VRRVRKTDNN RIARACGARI ASRTDELREE DVGTGAGLFE IKKIGDEYFT
     FITDCKDPKA CTIVLRGASK EILAEVERNL QDAMQVCRNV VIDPYLVPGG GASEMSVAHI
     LTEKSKTMTG VEQWPYRAVA QALEVIPRTL IQNCGASTIR ILTSLRAKHT QEGCQTWGVD
     GEAGVLADMK ELGIWEPLAV KLQTYKTAVE TAILLLRIDD IVSGHKKKGE DHGRQPAAAP
     EAPQQAE