Search Results
Overview
| Uniprot ID | A0A5G2Q9C7 |
|---|---|
| Protein Name | T-complex protein 1 subunit gamma |
| Gene Name | CCT3 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | DMISTLKKISTPVDT |
| 15 | LVLSQNTKRESGRKV |
| 184 | LRGVMINKDVTHPRM |
| 21 | TKRESGRKVQSGNIN |
| 210 | LDSSLEYKKGESQTD |
| 211 | DSSLEYKKGESQTDI |
| 332 | ITECKDPKACTILLR |
| 343 | ILLRGASKEILSEVE |
| 389 | HALTEKSKAMTGVEQ |
| 489 | DDIVSGHKKKGDDQS |
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
KVQSGNINAA
40
KIQVQHPAAK
50
SMIEISRTQD
60
EEVGDGTTSV
70
IILAGEMLSV
80
AEHFLEQQMH
90
PTVVISAYRK
100
ALDDMISTLK
110
KISTPVDTNN
120
RDMMLNIINS
130
SITTKVISRW
140
SSLACNIALD
150
AVKTVQFEEN
160
GRKEIDIKKY
170
ARVEKIPGGI
180
IEDSCVLRGV
190
MINKDVTHPR
200
MRRYIKNPRI
210
VLLDSSLEYK
220
KGESQTDIEI
230
TREEDFTRIL
240
QMEEEYIQQL
250
CEDIIHLKPD
260
VVITEKGISD
270
LAQHYLMRAN
280
ITAIRRVRKT
290
DNNRIARACG
300
ARIVSRPEEL
310
REEDIGTGAG
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
KHTQENCETW
450
GVNGETGTLV
460
DMKELGIWEP
470
LAVKLQTYKT
480
AVETAVLLLR
490
IDDIVSGHKK
500
KGDDQSRQGG
APDAGQE
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0044297 | cell body |
| Cellular Component | GO:0005832 | chaperonin-containing T-complex |
| Cellular Component | GO:0005874 | microtubule |
| Cellular Component | GO:0002199 | zona pellucida receptor 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 |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0050821 | protein stabilization |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.