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Protein

V-type proton ATPase 16 kDa proteolipid subunit

Gene

Vha16-1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei143Essential for proton translocationBy similarity1

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: FlyBase
  • dsRNA transport Source: FlyBase
  • lysosomal lumen acidification Source: GO_Central

Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-DME-1222556 ROS, RNS production in phagocytes
R-DME-6798695 Neutrophil degranulation
R-DME-77387 Insulin receptor recycling
R-DME-917977 Transferrin endocytosis and recycling
R-DME-983712 Ion channel transport

Protein family/group databases

TCDBi9.B.16.1.1 the putative ductin channel (ductin) family

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase 16 kDa proteolipid subunit
Short name:
V-ATPase 16 kDa proteolipid subunit
Short name:
VHA16K
Alternative name(s):
Ductin
Vacuolar H+ ATPase subunit 16-1
Vacuolar proton pump 16 kDa proteolipid subunit
Gene namesi
Name:Vha16-1
Synonyms:VHA, Vha16
ORF Names:CG3161
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0262736 Vha16-1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12LumenalSequence analysisAdd BLAST12
Transmembranei13 – 35HelicalSequence analysisAdd BLAST23
Topological domaini36 – 57CytoplasmicSequence analysisAdd BLAST22
Transmembranei58 – 78HelicalSequence analysisAdd BLAST21
Topological domaini79 – 96LumenalSequence analysisAdd BLAST18
Transmembranei97 – 118HelicalSequence analysisAdd BLAST22
Topological domaini119 – 130CytoplasmicSequence analysisAdd BLAST12
Transmembranei131 – 156HelicalSequence analysisAdd BLAST26
Topological domaini157 – 159LumenalSequence analysis3

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000717501 – 159V-type proton ATPase 16 kDa proteolipid subunitAdd BLAST159

Proteomic databases

PaxDbiP23380
PRIDEiP23380

Expressioni

Gene expression databases

BgeeiFBgn0262736
ExpressionAtlasiP23380 differential
GenevisibleiP23380 DM

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein; which is present as a hexamer that forms the proton-conducting pore).

Protein-protein interaction databases

BioGridi68967, 8 interactors
DIPiDIP-19390N
IntActiP23380, 156 interactors
STRINGi7227.FBpp0085483

Structurei

3D structure databases

ProteinModelPortaliP23380
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0232 Eukaryota
COG0636 LUCA
GeneTreeiENSGT00550000074873
InParanoidiP23380
KOiK02155
OMAiDMFARGI
OrthoDBiEOG091G0U1Y
PhylomeDBiP23380

Family and domain databases

InterProiView protein in InterPro
IPR002379 ATPase_proteolipid_c-like_dom
IPR000245 ATPase_proteolipid_csu
IPR011555 ATPase_proteolipid_su_C_euk
IPR035921 F/V-ATP_Csub_sf
PfamiView protein in Pfam
PF00137 ATP-synt_C, 2 hits
PRINTSiPR00122 VACATPASE
SUPFAMiSSF81333 SSF81333, 2 hits
TIGRFAMsiTIGR01100 V_ATP_synt_C, 1 hit

Sequencei

Sequence statusi: Complete.

P23380-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEVSSDNP IYGPFFGVMG AASAIIFSAL GAAYGTAKSG TGIAAMSVMR
60 70 80 90 100
PELIMKSIIP VVMAGIIAIY GLVVAVLIAG ALEEPSKYSL YRGFIHLGAG
110 120 130 140 150
LAVGFSGLAA GFAIGIVGDA GVRGTAQQPR LFVGMILILI FAEVLGLYGL

IVAIYLYTK
Length:159
Mass (Da):16,267
Last modified:November 1, 1991 - v1
Checksum:i9F147F8D72C72123
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55979 mRNA Translation: CAA39449.1
X77936 Genomic DNA Translation: CAA54908.1
AE013599 Genomic DNA Translation: AAF57359.1
AE013599 Genomic DNA Translation: AAF57360.1
AE013599 Genomic DNA Translation: AAM68381.1
BT012440 mRNA Translation: AAS93711.1
PIRiS42878
RefSeqiNP_476801.1, NM_057453.5
NP_724474.1, NM_165474.3
NP_724475.1, NM_165475.3
NP_724476.1, NM_165476.3
UniGeneiDm.6911

Genome annotation databases

EnsemblMetazoaiFBtr0086150; FBpp0085483; FBgn0262736
FBtr0086151; FBpp0085484; FBgn0262736
FBtr0086152; FBpp0085485; FBgn0262736
FBtr0086153; FBpp0085486; FBgn0262736
GeneIDi44307
KEGGidme:Dmel_CG3161

Similar proteinsi

Entry informationi

Entry nameiVATL_DROME
AccessioniPrimary (citable) accession number: P23380
Secondary accession number(s): A4UZ55
, Q0E9N6, Q53XD4, Q9V9D2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: March 28, 2018
This is version 170 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health