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Protein

ATP synthase subunit alpha, mitochondrial

Gene

blw

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

Functioni

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei412 – 4121Required for activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi211 – 2188ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • ATP synthesis coupled proton transport Source: FlyBase
  • electron transport chain Source: FlyBase
  • growth Source: FlyBase
  • lipid storage Source: FlyBase
  • phagocytosis Source: FlyBase
  • proton transport Source: FlyBase
  • regulation of choline O-acetyltransferase activity Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • spermatid development Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrial
Alternative name(s):
Protein bellwether
Gene namesi
Name:blw
Synonyms:ATPSYN-ALPHA
ORF Names:CG3612
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0011211. blw.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: FlyBase
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747MitochondrionSequence analysisAdd
BLAST
Chaini48 – 552505ATP synthase subunit alpha, mitochondrialPRO_0000002429Add
BLAST

Proteomic databases

PaxDbiP35381.
PRIDEiP35381.

Expressioni

Gene expression databases

BgeeiP35381.
GenevisibleiP35381. DM.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.

Protein-protein interaction databases

BioGridi63229. 44 interactions.
DIPiDIP-19192N.
IntActiP35381. 6 interactions.
MINTiMINT-925462.
STRINGi7227.FBpp0071794.

Structurei

3D structure databases

ProteinModelPortaliP35381.
SMRiP35381. Positions 66-543.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1353. Eukaryota.
COG0056. LUCA.
GeneTreeiENSGT00550000074846.
InParanoidiP35381.
KOiK02132.
OMAiLHASNTC.
OrthoDBiEOG773XFP.
PhylomeDBiP35381.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35381-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIFSARLAS SVARNLPKAA NQVACKAAYP AASLAARKLH VASTQRSAEI
60 70 80 90 100
SNILEERILG VAPKADLEET GRVLSIGDGI ARVYGLNNIQ ADEMVEFSSG
110 120 130 140 150
LKGMALNLEP DNVGVVVFGN DKLIKQGDIV KRTGAIVDVP VGDELLGRVV
160 170 180 190 200
DALGNAIDGK GAINTKDRFR VGIKAPGIIP RVSVREPMQT GIKAVDSLVP
210 220 230 240 250
IGRGQRELII GDRQTGKTAL AIDTIINQKR FNEAQDESKK LYCIYVAIGQ
260 270 280 290 300
KRSTVAQIVK RLTDSGAMGY SVIVSATASD AAPLQYLAPY SGCAMGEYFR
310 320 330 340 350
DKGKHALIIY DDLSKQAVAY RQMSLLLRRP PGREAYPGDV FYLHSRLLER
360 370 380 390 400
AAKMSPAMGG GSLTALPVIE TQAGDVSAYI PTNVISITDG QIFLETELFY
410 420 430 440 450
KGIRPAINVG LSVSRVGSAA QTKAMKQVAG SMKLELAQYR EVAAFAQFGS
460 470 480 490 500
DLDAATQQLL NRGVRLTELL KQGQYVPMAI EDQVAVIYCG VRGHLDKMDP
510 520 530 540 550
AKITKFEKEF LQHIKTSEQA LLDTIAKDGA ISEASDAKLK DIVAKFMSTF

QG
Length:552
Mass (Da):59,422
Last modified:December 15, 1998 - v2
Checksum:i68DB3E77A4726FEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07894 mRNA. Translation: CAA69202.1.
AE013599 Genomic DNA. Translation: AAF46903.1.
BT003592 mRNA. Translation: AAO39595.1.
RefSeqiNP_726243.1. NM_166554.3.
UniGeneiDm.7300.

Genome annotation databases

EnsemblMetazoaiFBtr0071883; FBpp0071794; FBgn0011211.
GeneIDi37617.
KEGGidme:Dmel_CG3612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07894 mRNA. Translation: CAA69202.1.
AE013599 Genomic DNA. Translation: AAF46903.1.
BT003592 mRNA. Translation: AAO39595.1.
RefSeqiNP_726243.1. NM_166554.3.
UniGeneiDm.7300.

3D structure databases

ProteinModelPortaliP35381.
SMRiP35381. Positions 66-543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63229. 44 interactions.
DIPiDIP-19192N.
IntActiP35381. 6 interactions.
MINTiMINT-925462.
STRINGi7227.FBpp0071794.

Proteomic databases

PaxDbiP35381.
PRIDEiP35381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071883; FBpp0071794; FBgn0011211.
GeneIDi37617.
KEGGidme:Dmel_CG3612.

Organism-specific databases

CTDi37617.
FlyBaseiFBgn0011211. blw.

Phylogenomic databases

eggNOGiKOG1353. Eukaryota.
COG0056. LUCA.
GeneTreeiENSGT00550000074846.
InParanoidiP35381.
KOiK02132.
OMAiLHASNTC.
OrthoDBiEOG773XFP.
PhylomeDBiP35381.

Miscellaneous databases

ChiTaRSiblw. fly.
GenomeRNAii37617.
NextBioi804568.
PROiP35381.

Gene expression databases

BgeeiP35381.
GenevisibleiP35381. DM.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of the nuclear gene encoding mitochondrial ATP synthase subunit alpha in early development of Drosophila and sea urchin."
    Talamillo A., Chisholm A.A.K., Garesse R., Jacobs H.T.
    Mol. Biol. Rep. 25:87-94(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
    Tissue: Testis.
  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: Head.
  5. "Identification of Drosophila wing imaginal disc proteins by two-dimensional gel analysis and microsequencing."
    Santaren J.F., van Damme J., Puype M., Vandekerckhove J., Garcia-Bellido A.
    Exp. Cell Res. 206:220-226(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 472-491.
    Strain: Vallecas.
    Tissue: Wing imaginal disk.

Entry informationi

Entry nameiATPA_DROME
AccessioniPrimary (citable) accession number: P35381
Secondary accession number(s): Q53YF5, Q94512, Q9W1Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: May 11, 2016
This is version 150 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, Direct protein sequencing, 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.