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Overview

Uniprot ID	H0VDX5
Protein Name	T-complex protein 1 subunit gamma
Gene Name	CCT3
Organism	Cavia porcellus

Kla Sites from experimental identification

Position	Flanking peptide
343	ILLRGASKEILSEVE

Function

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia

Protein Sequence

10 MMGHRPVLVL 20 SQNTKRESGR 30 KVQSGNISAA 40 KIQVQHPAAK 50 SMIEISRTQD 60 EEVGDGTTSV 70 IILAGEMLSV 80 AEHFLEQQMH 90 PTVVISAYRK 100 ALDDMISTLK 110 KISTPVDINN 120 RDTMLNIINS 130 SITTKAISRW 140 SSLACNIALD 150 AVKTVQFEEN 160 GRKEIDIKKY 170 ARVEKIPGGI 180 IEDSCVLRGV 190 MINKDVTHSR 200 MRRYIKNPRI 210 VLLDSSLEYK 220 KGESQTDIEI 230 TREEDFARIL 240 QMEEEYIQQL 250 CEDIIQLKPD 260 VVITEKGISD 270 LAQHYLLRAN 280 ITAIRRVRKT 290 DNNRIARACG 300 ARIVSRPEEL 310 REDDVGTGAG 320 LLEIKKIGDE 330 YFTFITECKD 340 PKACTILLRG 350 ASKEILSEVE 360 RNLQDAMQVC 370 RNVLLDPQLV 380 PGGGASEMAV 390 AHALTEKSKA 400 MTGVEQWPYR 410 AVAQALEVIP 420 RTLIQNCGAS 430 TIRLLTSLRA 440 KHTQEGCETW 450 GVNGETGALV 460 DMKELGIWEP 470 LAVKLQTYKT 480 AVETAVLLLR 490 IDDIVSGHKK 500 KSDDQSRQGG APDAGQE

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005832	chaperonin-containing T-complex
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0016887	ATP hydrolysis activity
Molecular Function	GO:0140662	ATP-dependent protein folding chaperone
Molecular Function	GO:0051082	unfolded protein binding

Reference

[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.