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P38077 (ATPG_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene names
Name:ATP3
Synonyms:ATP3a, ATP3b
Ordered Locus Names:YBR039W
ORF Names:YBR0408
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Part of the complex F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. 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 structure

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.

Subcellular location

Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein.

Miscellaneous

Present with 28100 molecules/cell in log phase SD medium.

Ref.3 reports two tandemly repeated copies of ATP3 (ATP3a and ATP3b) on the right arm of chromosome II in several laboratory strains, including S288c. This has not been confirmed by the yeast genome sequencing project.

Sequence similarities

Belongs to the ATPase gamma chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion Ref.1
Chain34 – 311278ATP synthase subunit gamma, mitochondrial
PRO_0000002691

Natural variations

Natural variant2071S → I in strain: D273-10B/A1.
Natural variant3081S → F in allele ATP3a.

Experimental info

Mutagenesis2731A → V: Lower activity. Ref.1
Mutagenesis2971T → A in ATP3-5; dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. Ref.2
Mutagenesis3031I → T in ATP3-1; dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. Ref.2

Secondary structure

................................... 311
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38077 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: ADC71F3C1E0CDF91

FASTA31134,351
        10         20         30         40         50         60 
MLSRIVSNNA TRSVMCHQAQ VGILYKTNPV RTYATLKEVE MRLKSIKNIE KITKTMKIVA 

        70         80         90        100        110        120 
STRLSKAEKA KISAKKMDEA EQLFYKNAET KNLDVEATET GAPKELIVAI TSDKGLCGSI 

       130        140        150        160        170        180 
HSQLAKAVRR HLNDQPNADI VTIGDKIKMQ LLRTHPNNIK LSINGIGKDA PTFQESALIA 

       190        200        210        220        230        240 
DKLLSVMKAG TYPKISIFYN DPVSSLSFEP SEKPIFNAKT IEQSPSFGKF EIDTDANVPR 

       250        260        270        280        290        300 
DLFEYTLANQ MLTAMAQGYA AEISARRNAM DNASKNAGDM INRYSILYNR TRQAVITNEL 

       310 
VDIITGASSL G 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the yeast ATP3 gene coding for the gamma-subunit of F1 and characterization of atp3 mutants."
Paul M.-F., Ackermann S., Yue J., Arselin G., Velours J., Tzagoloff A.
J. Biol. Chem. 269:26158-26164(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-61; 77-86; 195-207; 220-240 AND 284-290, MUTAGENESIS OF ALA-273.
Strain: ATCC 201238 / W303-1B and D273-10B/A1.
[2]"Mutations in the mitochondrial ATP synthase gamma subunit suppress a slow-growth phenotype of yme1 yeast lacking mitochondrial DNA."
Weber E.R., Rooks R.S., Shafer K.S., Chase J.W., Thorsness P.E.
Genetics 140:435-442(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF THR-297 AND ILE-303.
[3]"Studies on the ATP3 gene of Saccharomyces cerevisiae: presence of two closely linked copies, ATP3a and ATP3b, on the right arm of chromosome II."
Ohnishi K., Ishibashi S., Kunihiro M., Satoh T., Matsubara K., Oku S., Ono B., Mabuchi T., Takeda M.
Yeast 20:943-954(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ATP3A AND ATP3B).
Strain: ATCC 64665 / S288c / DC5.
[4]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Molecular architecture of the rotary motor in ATP synthase."
Stock D., Leslie A.G., Walker J.E.
Science 286:1700-1705(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[9]"Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase."
Kabaleeswaran V., Puri N., Walker J.E., Leslie A.G.W., Mueller D.M.
EMBO J. 25:5433-5442(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 34-311.
[10]"Asymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides."
Kabaleeswaran V., Shen H., Symersky J., Walker J.E., Leslie A.G.W., Mueller D.M.
J. Biol. Chem. 284:10546-10551(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) OF 34-311.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09305 Genomic DNA. Translation: AAA62605.1.
U08318 Unassigned DNA. Translation: AAA88816.1.
AB036928 Genomic DNA. Translation: BAC97839.1.
AB036929 Genomic DNA. Translation: BAC97840.1.
Z35908 Genomic DNA. Translation: CAA84981.1.
AY557865 Genomic DNA. Translation: AAS56191.1.
BK006936 Genomic DNA. Translation: DAA07159.1.
PIRS55891.
RefSeqNP_009595.1. NM_001178387.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HLDX-ray2.80G/P/Y34-311[»]
2WPDX-ray3.43G34-311[»]
2XOKX-ray3.01G1-311[»]
3FKSX-ray3.59G/P/Y34-311[»]
3OE7X-ray3.19G/P/Y34-311[»]
3OEEX-ray2.74G/P/Y34-311[»]
3OEHX-ray3.00G/P/Y34-311[»]
3OFNX-ray3.20G/P/Y34-311[»]
3ZIAX-ray2.50G/Q34-311[»]
3ZRYX-ray6.50G34-311[»]
4B2Qelectron microscopy37.00G/g34-311[»]
ProteinModelPortalP38077.
SMRP38077. Positions 34-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32740. 48 interactions.
DIPDIP-3035N.
IntActP38077. 23 interactions.
MINTMINT-693544.

Protein family/group databases

TCDB3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

MaxQBP38077.
PaxDbP38077.
PeptideAtlasP38077.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR039W; YBR039W; YBR039W.
GeneID852327.
KEGGsce:YBR039W.

Organism-specific databases

CYGDYBR039w.
SGDS000000243. ATP3.

Phylogenomic databases

eggNOGCOG0224.
GeneTreeENSGT00390000006837.
HOGENOMHOG000215911.
KOK02136.
OMAMATLKDX.
OrthoDBEOG76QFTN.

Enzyme and pathway databases

BioCycYEAST:G3O-29013-MONOMER.

Gene expression databases

GenevestigatorP38077.

Family and domain databases

InterProIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERPTHR11693. PTHR11693. 1 hit.
PfamPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSPR00126. ATPASEGAMMA.
SUPFAMSSF52943. SSF52943. 1 hit.
TIGRFAMsTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38077.
NextBio971035.
PROP38077.

Entry information

Entry nameATPG_YEAST
AccessionPrimary (citable) accession number: P38077
Secondary accession number(s): D6VQ39, Q54AF5, Q76MT6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 14, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references