Search Results
Overview
| Uniprot ID | A0A286Y3B4 |
|---|---|
| Protein Name | T-complex protein 1 subunit theta |
| Gene Name | CCT8 |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 318 | MLVRLNSKWDLRRLC |
| 326 | WDLRRLCKTVGATAL |
| 7 | *MALHVPKAPGFAQM |
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
MALHVPKAPG
20
FAQMLKEGAK
30
HFSGLEEAVY
40
RNIQACKELA
50
QTTRTAYGPN
60
GMNKMVINHL
70
EKLFVTNDAA
80
TILRELEVQH
90
PAAKMIVMAS
100
HMQEQEVGDG
110
TNFVLVFAGA
120
LLELAEELLR
130
IGLSVSEVIE
140
GYEIACRKAH
150
EILPDLVCCS
160
AKNLRDVEEV
170
SSLLRTSIMS
180
KQYGNEAFLA
190
KLIARACVSI
200
FPDSGHFNVD
210
NIRVCKILGS
220
GIFSSSVLHG
230
MVFKKETEGD
240
VTSVKDAKIA
250
VYSCPFDGMI
260
TETKGTVLIK
270
TAEELMNFSK
280
GEENLMDAQV
290
KAIADTGANV
300
VVTGGKVADM
310
ALHYANKYNI
320
MLVRLNSKWD
330
LRRLCKTVGA
340
TALPRLTPPV
350
LEEMGHCDSV
360
YLSEVGDTQV
370
VVFKHEKEDG
380
AISTIVLRGS
390
TDNLMDDIER
400
AVDDGVNTFK
410
VLTRDKRLVP
420
GGGATEIELA
430
KQITSYGETC
440
PGLEQYAIKK
450
FAEAFEAIPR
460
ALAENSGVKA
470
NEIISKLYAV
480
HQEGNKNVGL
490
DIEAEVPAVK
500
DMLEAGVLDT
510
YLGKYWAIKL
520
ATNAAVTVLR
530
VDQIIVAKLA
540
GGPKAPKPQG
550
NWDKDGWQDD
AHV
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0044297 | cell body |
| Cellular Component | GO:0005813 | centrosome |
| 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:0050821 | protein stabilization |
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.