Overview
| Uniprot ID | H0VFT3 |
|---|
| Protein Name | V-type proton ATPase subunit C |
|---|
| Gene Name | ATP6V1C1 |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 115 |
DMAKYPIKQSLKNIS |
Function
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity
Protein Sequence
10
MTEFWLISAP
20
GEKTCQQTWE
30
KLHAATTKNN
40
NLAATAKFNI
50
PDLKVGTLDV
60
LVGLSDELAK
70
LDAFVEGVVK
80
KVAQYMADVL
90
EDSRDKVQEN
100
LLANGVDLVT
110
YITRFQWDMA
120
KYPIKQSLKN
130
ISEIIAKGVT
140
QIDNDLKSRA
150
SAYNNLKGNL
160
QNLERKNAGS
170
LLTRSLAEIV
180
KKDDFVLDSE
190
YLVTLLVVVP
200
KLNHNDWIKQ
210
YETLVDMVVP
220
RSSNVLSEDQ
230
DSYLCNVTLF
240
RKAVDDFRHK
250
AREHKFIVRD
260
FQYNEVEMKA
270
DKEEMTRLST
280
DKKKQFGPLV
290
RWLKVNFSEA
300
FIAWIHVKAL
310
RVFVESVLRY
320
GLPVNFQAML
330
LQPNKKTMKK
340
LREVLHELYK
350
HLDSSAAAII
360
DAPVDIPGLN
370
LSQQEYYPYV
380
YYKIDCNLLE
FK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0030665 |
clathrin-coated vesicle membrane |
| Cellular Component |
GO:0005765 |
lysosomal membrane |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0030672 |
synaptic vesicle membrane |
| Cellular Component |
GO:0000221 |
vacuolar proton-transporting V-type ATPase, V1 domain |
| Molecular Function |
GO:0046961 |
proton-transporting ATPase activity, rotational mechanism |
| Biological Process |
GO:0097401 |
synaptic vesicle lumen acidification |
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.