Search Results
Overview
| Uniprot ID | A0A287AJY2 |
|---|---|
| Protein Name | T-complex protein 1 subunit alpha |
| Gene Name | TCP1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | ADELVKQKIHPTSVI |
| 116 | SGYRLACKEAVRYIS |
| 189 | VNSINILKAHGRSQT |
| 262 | QRESDITKERIQKIL |
| 355 | DDELILIKNTKARTS |
| 489 | NGKPRDNKQAGVFEP |
| 500 | VFEPTIVKVKSLKFA |
| 522 | LRIDDLIKLHPESKD |
| 531 | HPESKDDKHGGYEDA |
| 99 | KNADELVKQKIHPTS |
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
MRCPHLSLVT
20
FVMAAASIAN
30
IVKSSLGPVG
40
LDKMLVDDIG
50
DVTITNDGAT
60
ILKLLEVEHP
70
AAKVLCELAD
80
LQDKEVGDGT
90
TSVVIIAAEL
100
LKNADELVKQ
110
KIHPTSVISG
120
YRLACKEAVR
130
YISENLIINT
140
DELGRDCLIN
150
AAKTSMSSKI
160
IGINGDFFAN
170
MVVDAVLAIK
180
YTDVRGQPRY
190
PVNSINILKA
200
HGRSQTESML
210
INGYALNCVV
220
GSQGMPKRIV
230
NAKIACLDFS
240
LQKTKMKLGV
250
QVVITDPEKL
260
DQIRQRESDI
270
TKERIQKILA
280
TGANVILTTG
290
GIDDMCLKYF
300
VETGAMAVRR
310
VLKRDLKRIA
320
KASGATILST
330
LANLEGEETF
340
EASMLGQAEE
350
VVQERICDDE
360
LILIKNTKAR
370
TSASIILRGA
380
NDFMCDEMER
390
SLHDALCVVR
400
RVLESKSVVP
410
GGGAVEAALS
420
IYLENYATSM
430
GSREQLAIAE
440
FARSLLVIPN
450
TLAVNAAQDS
460
TDLVAKLRAF
470
HNEAQVNPER
480
KNLKWIGLDL
490
VNGKPRDNKQ
500
AGVFEPTIVK
510
VKSLKFATEA
520
AITILRIDDL
530
IKLHPESKDD
540
KHGGYEDAVH
SGALDD
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| 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] 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.