UniProt:P38606 ATP6V1A

chain
  • chain:1-617
  • initiator methionine:1
checksum DB409A8731D772CB
comment
  • 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). 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 (PubMed:32001091). 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).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.CATALYTIC ACTIVITY ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)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).SUBUNIT V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (PubMed:33065002). The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (PubMed:33065002). The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002). Interacts with the V0 complex V-ATPase subunit a4 ATP6V0A4 (By similarity). Interacts with WFS1 (PubMed:23035048). Interacts with alpha-crystallin B chain/CRYAB and with MTOR, forming a ternary complex (PubMed:31786107).SUBUNIT (Microbial infection) Interacts with Rabies virus protein M; this interaction promotes virion uncoating.INTERACTION Co-localizes with WFS1 in the secretory granules in neuroblastoma cell lines.ALTERNATIVE PRODUCTS High expression in the skin.PTM Phosphorylation at Ser-384 by AMPK down-regulates its enzyme activity.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the ATPase alpha/beta chains family.
crossReference
databaseName UniProt
dbId 67076
description
  • recommendedName: V-type proton ATPase catalytic subunit A shortName: V-ATPase subunit A ecNumber evidence="2"7.1.2.2 alternativeName: V-ATPase 69 kDa subunit alternativeName: Vacuolar ATPase isoform VA68 alternativeName: Vacuolar proton pump subunit alpha
displayName UniProt:P38606 ATP6V1A
geneName
  • ATP6V1A
  • ATP6A1
  • ATP6V1A1
  • VPP2
identifier P38606
isSequenceChanged false
keyword
  • 3D-structure
  • Acetylation
  • Alternative splicing
  • ATP-binding
  • Cytoplasm
  • Cytoplasmic vesicle
  • Disease variant
  • Epilepsy
  • Hydrogen ion transport
  • Ion transport
  • Lysosome
  • Membrane
  • Nucleotide-binding
  • Phosphoprotein
  • Proteomics identification
  • Reference proteome
  • Translocase
  • Transport
modified [InstanceEdit:9963647] Weiser, Joel, 2025-08-15
moleculeType Protein
name
  • ATP6V1A
otherIdentifier
  • 11718120_at
  • 11718121_x_at
  • 11718122_a_at
  • 11751178_a_at
  • 11756924_s_at
  • 16944096
  • 201971_PM_s_at
  • 201971_s_at
  • 201972_PM_at
  • 201972_at
  • 2636590
  • 2636597
  • 2636598
  • 2636599
  • 2636601
  • 2636602
  • 2636603
  • 2636604
  • 2636606
  • 2636608
  • 2636609
  • 2636610
  • 2636611
  • 2636612
  • 2636615
  • 2636617
  • 2636618
  • 2636619
  • 2636620
  • 2636621
  • 2636622
  • 2636623
  • 34889_at
  • 34890_at
  • 3910773
  • 523
  • 8081740
  • A_23_P211965
  • A_24_P396994
  • GE88476
  • GO:0000139
  • GO:0000166
  • GO:0000221
  • GO:0005515
  • GO:0005524
  • GO:0005654
  • GO:0005737
  • GO:0005764
  • GO:0005765
  • GO:0005829
  • GO:0005886
  • GO:0005902
  • GO:0006811
  • GO:0006879
  • GO:0007035
  • GO:0007042
  • GO:0010008
  • GO:0016020
  • GO:0016241
  • GO:0016324
  • GO:0016469
  • GO:0016787
  • GO:0016887
  • GO:0030133
  • GO:0030141
  • GO:0030665
  • GO:0031410
  • GO:0033176
  • GO:0033180
  • GO:0036295
  • GO:0042592
  • GO:0046034
  • GO:0046961
  • GO:0048388
  • GO:0051452
  • GO:0055085
  • GO:0055086
  • GO:0061795
  • GO:0070062
  • GO:0097401
  • GO:0098850
  • GO:1901135
  • GO:1902495
  • GO:1902600
  • GO:1904949
  • HMNXSV003015498
  • ILMN_1711516
  • L09235_at
  • PH_hs_0024782
  • TC03000583.hg
  • g4502304_3p_a_at
  • g6523820_3p_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • VATA_HUMAN
  • B2RBR8
  • B7Z1R5
  • D3DN75
  • Q53YD9
  • Q96DY6
  • Q9UHY3
sequenceLength 617
species [Species:48887] Homo sapiens
stId uniprot:P38606
url http://purl.uniprot.org/uniprot/P38606
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