Overview
| Uniprot ID | Q9H9S5 |
|---|
| Protein Name | Ribitol 5-phosphate transferase FKRP |
|---|
| Gene Name | FKRP |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 291 |
LEWFGCNKETTRCFG |
Function
Catalyzes the transfer of a ribitol 5-phosphate from CDP-L-ribitol to the ribitol 5-phosphate previously attached by FKTN/fukutin to the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:26923585, PubMed:27194101, PubMed:29477842, PubMed:31949166). This constitutes the second step in the formation of the ribose 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1 (PubMed:25279699, PubMed:26923585, PubMed:27194101, PubMed:29477842, PubMed:31949166)
Protein Sequence
10
MRLTRCQAAL
20
AAAITLNLLV
30
LFYVSWLQHQ
40
PRNSRARGPR
50
RASAAGPRVT
60
VLVREFEAFD
70
NAVPELVDSF
80
LQQDPAQPVV
90
VAADTLPYPP
100
LALPRIPNVR
110
LALLQPALDR
120
PAAASRPETY
130
VATEFVALVP
140
DGARAEAPGL
150
LERMVEALRA
160
GSARLVAAPV
170
ATANPARCLA
180
LNVSLREWTA
190
RYGAAPAAPR
200
CDALDGDAVV
210
LLRARDLFNL
220
SAPLARPVGT
230
SLFLQTALRG
240
WAVQLLDLTF
250
AAARQPPLAT
260
AHARWKAERE
270
GRARRAALLR
280
ALGIRLVSWE
290
GGRLEWFGCN
300
KETTRCFGTV
310
VGDTPAYLYE
320
ERWTPPCCLR
330
ALRETARYVV
340
GVLEAAGVRY
350
WLEGGSLLGA
360
ARHGDIIPWD
370
YDVDLGIYLE
380
DVGNCEQLRG
390
AEAGSVVDER
400
GFVWEKAVEG
410
DFFRVQYSES
420
NHLHVDLWPF
430
YPRNGVMTKD
440
TWLDHRQDVE
450
FPEHFLQPLV
460
PLPFAGFVAQ
470
APNNYRRFLE
480
LKFGPGVIEN
490
PQYPNPALLS
LTGSG
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000139 |
Golgi membrane |
| Cellular Component |
GO:0005615 |
extracellular space |
| Cellular Component |
GO:0005794 |
Golgi apparatus |
| Cellular Component |
GO:0005791 |
rough endoplasmic reticulum |
| Cellular Component |
GO:0042383 |
sarcolemma |
| Cellular Component |
GO:0098723 |
skeletal muscle myofibril |
| Molecular Function |
GO:0002162 |
dystroglycan binding |
| Molecular Function |
GO:0042802 |
identical protein binding |
| Molecular Function |
GO:0043236 |
laminin binding |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0016780 |
phosphotransferase activity, for other substituted phosphate groups |
| Biological Process |
GO:0035269 |
protein O-linked glycosylation via mannose |
| Biological Process |
GO:0051262 |
protein tetramerization |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.