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Protein

V-type proton ATPase catalytic subunit A isoform 2

Gene

Vha68-2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi247 – 2548ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: FlyBase
  • ATP metabolic process Source: InterPro
  • endosomal lumen acidification Source: FlyBase
  • endosomal transport Source: FlyBase
  • imaginal disc growth Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase catalytic subunit A isoform 2 (EC:3.6.3.14)
Short name:
V-ATPase subunit A 2
Alternative name(s):
V-ATPase 69 kDa subunit 2
Vacuolar proton pump subunit alpha 2
Gene namesi
Name:Vha68-2
Synonyms:VHAA2
ORF Names:CG3762
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0263598. Vha68-2.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: FlyBase
  • plasma membrane proton-transporting V-type ATPase complex Source: FlyBase
  • vacuolar proton-transporting V-type ATPase, V1 domain Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 614614V-type proton ATPase catalytic subunit A isoform 2PRO_0000144567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ27331.
PRIDEiQ27331.

PTM databases

iPTMnetiQ27331.

Expressioni

Gene expression databases

BgeeiQ27331.
ExpressionAtlasiQ27331. differential.
GenevisibleiQ27331. 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).

Protein-protein interaction databases

BioGridi69430. 42 interactions.
IntActiQ27331. 5 interactions.
MINTiMINT-1019493.
STRINGi7227.FBpp0079999.

Structurei

3D structure databases

ProteinModelPortaliQ27331.
SMRiQ27331. Positions 16-614.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiKOG1352. Eukaryota.
COG1155. LUCA.
GeneTreeiENSGT00550000074787.
InParanoidiQ27331.
KOiK02145.
OMAiEGYPPYL.
OrthoDBiEOG7Q8CMM.
PhylomeDBiQ27331.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00309. ATP_synth_A_arch.
InterProiIPR031686. ATP-synt_a_Xtn.
IPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR005725. ATPase_V1-cplx_asu.
IPR027417. P-loop_NTPase.
IPR022878. V-ATPase_asu.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
PF16886. ATP-synt_ab_Xtn. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01042. V-ATPase_V1_A. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27331-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNLKRFDDE ERESKYGRVF AVSGPVVTAE AMSGSAMYEL VRVGYYELVG
60 70 80 90 100
EIIRLEGDMA TIQVYEETSG VTVGDPVLRT GKPLSVELGP GIMGSIFDGI
110 120 130 140 150
QRPLKDINEL TESIYIPKGV NVPSLSRVAS WEFNPLNVKV GSHITGGDLY
160 170 180 190 200
GLVHENTLVK HKMIVNPRAK GTVRYIAPSG NYKVDDVVLE TEFDGEITKH
210 220 230 240 250
TMLQVWPVRQ PRPVTEKLPA NHPLLTGQRV LDSLFPCVQG GTTAIPGAFG
260 270 280 290 300
CGKTVISQAL SKYSNSDVII YVGCGERGNE MSEVLRDFPE LSVEIDGVTE
310 320 330 340 350
SIMKRTALVA NTSNMPVAAR EASIYTGITL SEYFRDMGYN VSMMADSTSR
360 370 380 390 400
WAEALREISG RLAEMPADSG YPAYLGARLA SFYERAGRVK CLGNPEREGS
410 420 430 440 450
VSIVGAVSPP GGDFSDPVTS ATLGIVQVFW GLDKKLAQRK HFPSINWLIS
460 470 480 490 500
YSKYMRALDD FYDKNFPEFV PLRTKVKEIL QEEEDLSEIV QLVGKASLAE
510 520 530 540 550
TDKITLEVAK LLKDDFLQQN SYSSYDRFCP FYKTVGMLRN IIDFYDMARH
560 570 580 590 600
SVESTAQSEN KITWNVIREA MGNIMYQLSS MKFKDPVKDG EAKIKADFEQ
610
LHEDLQQAFR NLED
Length:614
Mass (Da):68,302
Last modified:April 18, 2006 - v2
Checksum:i63DC9CA01CCDE275
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2123QPR → HHA in AAB02270 (PubMed:9050231).Curated
Sequence conflicti210 – 2123QPR → HHA in AAB02271 (PubMed:9050231).Curated
Sequence conflicti367 – 3671A → R in AAB02270 (PubMed:9050231).Curated
Sequence conflicti367 – 3671A → R in AAB02271 (PubMed:9050231).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59146 mRNA. Translation: AAB02270.1.
U59147 Genomic DNA. Translation: AAB02271.1.
AE014134 Genomic DNA. Translation: AAF53231.1.
AY084150 mRNA. Translation: AAL89888.1.
RefSeqiNP_001246015.1. NM_001259086.2.
NP_001260424.1. NM_001273495.1.
NP_001260425.1. NM_001273496.1.
NP_652004.2. NM_143747.3.
NP_723775.1. NM_165021.2.
NP_723776.1. NM_165022.2.
UniGeneiDm.6438.

Genome annotation databases

EnsemblMetazoaiFBtr0080418; FBpp0079999; FBgn0263598.
FBtr0080419; FBpp0080000; FBgn0263598.
FBtr0080420; FBpp0080001; FBgn0263598.
FBtr0305551; FBpp0294002; FBgn0263598.
FBtr0336613; FBpp0307596; FBgn0263598.
FBtr0336614; FBpp0307597; FBgn0263598.
GeneIDi45012.
KEGGidme:Dmel_CG3762.
UCSCiCG3762-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59146 mRNA. Translation: AAB02270.1.
U59147 Genomic DNA. Translation: AAB02271.1.
AE014134 Genomic DNA. Translation: AAF53231.1.
AY084150 mRNA. Translation: AAL89888.1.
RefSeqiNP_001246015.1. NM_001259086.2.
NP_001260424.1. NM_001273495.1.
NP_001260425.1. NM_001273496.1.
NP_652004.2. NM_143747.3.
NP_723775.1. NM_165021.2.
NP_723776.1. NM_165022.2.
UniGeneiDm.6438.

3D structure databases

ProteinModelPortaliQ27331.
SMRiQ27331. Positions 16-614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi69430. 42 interactions.
IntActiQ27331. 5 interactions.
MINTiMINT-1019493.
STRINGi7227.FBpp0079999.

PTM databases

iPTMnetiQ27331.

Proteomic databases

PaxDbiQ27331.
PRIDEiQ27331.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080418; FBpp0079999; FBgn0263598.
FBtr0080419; FBpp0080000; FBgn0263598.
FBtr0080420; FBpp0080001; FBgn0263598.
FBtr0305551; FBpp0294002; FBgn0263598.
FBtr0336613; FBpp0307596; FBgn0263598.
FBtr0336614; FBpp0307597; FBgn0263598.
GeneIDi45012.
KEGGidme:Dmel_CG3762.
UCSCiCG3762-RA. d. melanogaster.

Organism-specific databases

CTDi45012.
FlyBaseiFBgn0263598. Vha68-2.

Phylogenomic databases

eggNOGiKOG1352. Eukaryota.
COG1155. LUCA.
GeneTreeiENSGT00550000074787.
InParanoidiQ27331.
KOiK02145.
OMAiEGYPPYL.
OrthoDBiEOG7Q8CMM.
PhylomeDBiQ27331.

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

GenomeRNAii45012.
PROiQ27331.

Gene expression databases

BgeeiQ27331.
ExpressionAtlasiQ27331. differential.
GenevisibleiQ27331. DM.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00309. ATP_synth_A_arch.
InterProiIPR031686. ATP-synt_a_Xtn.
IPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR005725. ATPase_V1-cplx_asu.
IPR027417. P-loop_NTPase.
IPR022878. V-ATPase_asu.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
PF16886. ATP-synt_ab_Xtn. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01042. V-ATPase_V1_A. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular genetic analysis of V-ATPase function in Drosophila melanogaster."
    Dow J.A.T., Davies S.A., Guo Y., Graham S., Finbow M.E., Kaiser K.
    J. Exp. Biol. 200:237-245(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-S and Oregon-R.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiVATA2_DROME
AccessioniPrimary (citable) accession number: Q27331
Secondary accession number(s): Q8SXT2, Q9VK48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: April 18, 2006
Last modified: July 6, 2016
This is version 144 of the entry and version 2 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.