ATP6V1A
entrez
523
canonical
uniprot
P38606
canonical
ensembl
ENSG00000114573
resolver
ensp
ENSP00000273398
resolver
ensp
ENSP00000515542
resolver
genesymbol
ATP6V1A
resolver
genesymbol_syn
ATP6A1
resolver
genesymbol_syn
ATP6V1A1
resolver
genesymbol_syn
VPP2
resolver
hgnc
HGNC:851
resolver
uniprot
B2RBR8
resolver
uniprot
B7Z1R5
resolver
uniprot
D3DN75
resolver
uniprot
Q53YD9
resolver
uniprot
Q96DY6
resolver
uniprot
Q9UHY3
resolver
uniprot_entry
VATA_HUMAN
resolver
uniprot_sec
B2RBR8
resolver
uniprot_sec
B7Z1R5
resolver
uniprot_sec
D3DN75
resolver
uniprot_sec
Q53YD9
resolver
uniprot_sec
Q96DY6
resolver
uniprot_sec
Q9UHY3
resolver
activity_regulation
ACTIVITY REGULATION: ATP hydrolysis occurs at the interface between the nucleotide-binding domains of subunits A and B (By similarity). ATP hydrolysis triggers a conformational change in the subunits D and F, which induces a shift of subunit d (By similarity). The c-ring is subsequently rotated and results in a continuous proton translocation across the membrane (By similarity). {ECO:0000250|UniProtKB:P31404}.
uniprot
proteins
amino_acid_sequence
MDFSKLPKILDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWDFTPCKNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGDILYKLSSMKFKDPLKDGEAKIKSDYAQLLEDMQNAFRSLED
uniprot
proteins
disease_involvement
DISEASE: Cutis laxa, autosomal recessive, 2D (ARCL2D) [MIM:617403]: A form of cutis laxa, a disorder characterized by an excessive congenital skin wrinkling, a large fontanelle with delayed closure, a typical facial appearance with downslanting palpebral fissures, and a general connective tissue weakness. Most ARCL2D patients exhibit severe hypotonia as well as cardiovascular and neurologic involvement. {ECO:0000269|PubMed:28065471}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Epileptic encephalopathy, infantile or early childhood, 3 (IECEE3) [MIM:618012]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. IECEE3 is an autosomal dominant form characterized by onset of seizures in the first years of life. The severity of the phenotype is highly variable: some patients may be non-verbal and non-ambulatory with spastic quadriparesis and poor eye contact, whereas others have moderate intellectual disability. {ECO:0000269|PubMed:29668857}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
7.1.2.2
uniprot
proteins
function
FUNCTION: Catalytic 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 (PubMed:8463241, PubMed:22053050). 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 (PubMed:32001091). 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:22053050). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). May play a role in neurite development and synaptic connectivity (PubMed:29668857). {ECO:0000250|UniProtKB:P50516, ECO:0000269|PubMed:22053050, ECO:0000269|PubMed:28296633, ECO:0000269|PubMed:29668857, ECO:0000269|PubMed:8463241, ECO:0000303|PubMed:32001091}.; FUNCTION: (Microbial infection) Plays an important role in virion uncoating during Rabies virus replication after membrane fusion. Specifically, participates in the dissociation of incoming viral matrix M proteins uncoating through direct interaction. {ECO:0000269|PubMed:33208464}.
uniprot
proteins
mass_dalton
68304
uniprot
proteins
mutagenesis
MUTAGEN 256; /note="K->Q: Complete loss of interaction with Rabies virus protein M; when associated with Q-279."; /evidence="ECO:0000269|PubMed:33208464"; MUTAGEN 279; /note="E->Q: Complete loss of interaction with Rabies virus protein M; when associated with Q-256."; /evidence="ECO:0000269|PubMed:33208464
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-384 by AMPK down-regulates its enzyme activity. {ECO:0000250|UniProtKB:P50516}.
uniprot
proteins
protein_family
ATPase alpha/beta chains family
uniprot
proteins
pubmed
10931946
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22053050
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23035048
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28065471
uniprot
proteins
pubmed
28296633
uniprot
proteins
pubmed
29668857
uniprot
proteins
pubmed
31786107
uniprot
proteins
pubmed
32001091
uniprot
proteins
pubmed
33065002
uniprot
proteins
pubmed
33208464
uniprot
proteins
pubmed
8463241
uniprot
proteins
sequence_length
617
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29668857, ECO:0000269|PubMed:33208464}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P50516}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:23035048}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P31404}; Peripheral membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000305|PubMed:22053050}; Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with WFS1 in the secretory granules in neuroblastoma cell lines. {ECO:0000269|PubMed:23035048}.
uniprot
proteins