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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: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Sitei143 – 1431Essential for proton translocationBy similarity

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: FlyBase
  • dsRNA transport Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • lysosomal lumen acidification Source: GO_Central
  • proton transport Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-DME-1222556. ROS, RNS production in response to bacteria.
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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0262736. Vha16-1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212LumenalSequence analysisAdd
BLAST
Transmembranei13 – 3523HelicalSequence analysisAdd
BLAST
Topological domaini36 – 5722CytoplasmicSequence analysisAdd
BLAST
Transmembranei58 – 7821HelicalSequence analysisAdd
BLAST
Topological domaini79 – 9618LumenalSequence analysisAdd
BLAST
Transmembranei97 – 11822HelicalSequence analysisAdd
BLAST
Topological domaini119 – 13012CytoplasmicSequence analysisAdd
BLAST
Transmembranei131 – 15626HelicalSequence analysisAdd
BLAST
Topological domaini157 – 1593LumenalSequence analysis

GO - Cellular componenti

  • fusome Source: FlyBase
  • integral component of membrane Source: GO_Central
  • plasma membrane proton-transporting V-type ATPase complex Source: FlyBase
  • vacuolar proton-transporting V-type ATPase, V0 domain Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 159159V-type proton ATPase 16 kDa proteolipid subunitPRO_0000071750Add
BLAST

Proteomic databases

PaxDbiP23380.
PRIDEiP23380.

Expressioni

Gene expression databases

BgeeiP23380.
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. 7 interactions.
DIPiDIP-19390N.
IntActiP23380. 151 interactions.
MINTiMINT-304429.
STRINGi7227.FBpp0085483.

Structurei

3D structure databases

ProteinModelPortaliP23380.
SMRiP23380. Positions 15-159.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00550000074873.
InParanoidiP23380.
KOiK02155.
OMAiTCAIVFT.
OrthoDBiEOG7FV3RW.
PhylomeDBiP23380.

Family and domain databases

HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP23380.
SMRiP23380. Positions 15-159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68967. 7 interactions.
DIPiDIP-19390N.
IntActiP23380. 151 interactions.
MINTiMINT-304429.
STRINGi7227.FBpp0085483.

Protein family/group databases

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

Proteomic databases

PaxDbiP23380.
PRIDEiP23380.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi44307.
FlyBaseiFBgn0262736. Vha16-1.

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00550000074873.
InParanoidiP23380.
KOiK02155.
OMAiTCAIVFT.
OrthoDBiEOG7FV3RW.
PhylomeDBiP23380.

Enzyme and pathway databases

ReactomeiR-DME-1222556. ROS, RNS production in response to bacteria.
R-DME-77387. Insulin receptor recycling.
R-DME-917977. Transferrin endocytosis and recycling.
R-DME-983712. Ion channel transport.

Miscellaneous databases

GenomeRNAii44307.
PROiP23380.

Gene expression databases

BgeeiP23380.
GenevisibleiP23380. DM.

Family and domain databases

HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a cDNA from Drosophila coding for the 16 kD proteolipid component of the vacuolar H(+)-ATPase."
    Meagher L., McLean P., Finbow M.E.
    Nucleic Acids Res. 18:6712-6712(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Larva.
  2. "Evidence that the 16 kDa proteolipid (subunit c) of the vacuolar H(+)- ATPase and ductin from gap junctions are the same polypeptide in Drosophila and Manduca: molecular cloning of the Vha16k gene from Drosophila."
    Finbow M.E., Goodwin S.F., Meagher L., Lane N.J., Keen J., Findlay J.B.C., Kaiser K.
    J. Cell Sci. 107:1817-1824(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiVATL_DROME
AccessioniPrimary (citable) accession number: P23380
Secondary accession number(s): A4UZ55
, Q0E9N6, Q53XD4, Q9V9D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: July 6, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.