Atp6v1e1
entrez
11973
canonical
uniprot
P50518
canonical
ensembl
ENSMUSG00000019210
resolver
ensp
ENSMUSP00000019354
resolver
enst
ENSMUST00000019354
resolver
genesymbol
Atp6v1e1
resolver
genesymbol_syn
Atp6e
resolver
genesymbol_syn
Atp6e2
resolver
uniprot
Q3UK59
resolver
uniprot
Q8K5D6
resolver
uniprot
Q99LD0
resolver
uniprot_entry
VATE1_MOUSE
resolver
uniprot_sec
Q3UK59
resolver
uniprot_sec
Q8K5D6
resolver
uniprot_sec
Q99LD0
resolver
activity_regulation
ACTIVITY REGULATION: V-ATPase activity on lysosomes is inhibited in response to calorie restriction: deacetylated by SIRT1 downstream of TULP3, leading to (1) V-ATPase complex inhibition on lysosomes and (2) AMP-activated protein kinase (AMPK) activation via the AXIN1-STK11/LKB1 axis. {ECO:0000269|PubMed:39695235}.
uniprot
proteins
amino_acid_sequence
MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKIQMSNLMNQARLKVLRARDDLITDLLNEAKQRLSKVVKDTTRYQVLLDGLVLQGLYQLLEPRMIVRCRKQDFPLVKAAVQKAIPMYKIATKKDVDVQIDQEAYLPEEIAGGVEIYNGDRKIKVSNTLESRLDLIAQQMMPEVRGALFGANANRKFLD
uniprot
proteins
function
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 (By similarity). 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 promotes acidification of the extracellular environment (By similarity). The V-ATPase complex also acts as an activator for mTORC1 on lysosomal membrane by promoting the guanine nucleotide exchange factor (GEF) of the Ragulator complex, thereby enabling mTORC1 recruitment (PubMed:39695235). {ECO:0000250|UniProtKB:P36543, ECO:0000269|PubMed:39695235}.
uniprot
proteins
mass_dalton
26157
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="K->Q: In mutant 3KQ; mimics acetylation; abolished activation of AMPK downstream of litocholic acid and TULP3; when associated with Q-99 and Q-191."; /evidence="ECO:0000269|PubMed:39695235"; MUTAGEN 52; /note="K->R: In mutant 3KR; abolished ability to further activate AMPK downstream of litocholic acid and TULP3; when associated with R-99 and R-191."; /evidence="ECO:0000269|PubMed:39695235"; MUTAGEN 99; /note="K->Q: In mutant 3KQ; mimics acetylation; abolished activation of AMPK downstream of litocholic acid and TULP3; when associated with Q-52 and Q-191."; /evidence="ECO:0000269|PubMed:39695235"; MUTAGEN 99; /note="K->R: In mutant 3KR; abolished ability to further activate AMPK downstream of litocholic acid and TULP3; when associated with R-52 and R-191."; /evidence="ECO:0000269|PubMed:39695235"; MUTAGEN 191; /note="K->Q: In mutant 3KQ; mimics acetylation; abolished activation of AMPK downstream of litocholic acid and TULP3; when associated with Q-52 and Q-99."; /evidence="ECO:0000269|PubMed:39695235"; MUTAGEN 191; /note="K->R: In mutant 3KR; abolished ability to further activate AMPK downstream of litocholic acid and TULP3; when associated with R-52 and R-99."; /evidence="ECO:0000269|PubMed:39695235
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-52, Lys-99 and Lys-191 regulates the activity of the V-ATPase complex (PubMed:39695235). Deacetylation at Lys-52, Lys-99 and Lys-191 by SIRT1 in response to calorie restriction inhibits the V-ATPase complex on lysosomes and promotes AMPK activation via the AXIN1-STK11/LKB1 axis (PubMed:39695235). {ECO:0000269|PubMed:39695235}.
uniprot
proteins
protein_family
V-ATPase E subunit family
uniprot
proteins
pubmed
11872743
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23055941
uniprot
proteins
pubmed
29993276
uniprot
proteins
pubmed
39695235
uniprot
proteins
pubmed
8741845
uniprot
proteins
sequence_length
226
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P36543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36543}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36543}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36543}. Lysosome membrane {ECO:0000250|UniProtKB:P36543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36543}.
uniprot
proteins