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Protein

ATP synthase subunit gamma, mitochondrial

Gene

ATP3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. 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.

GO - Molecular functioni

  1. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP synthesis coupled proton transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29013-MONOMER.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene namesi
Name:ATP3
Synonyms:ATP3a, ATP3b
Ordered Locus Names:YBR039W
ORF Names:YBR0408
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBR039w.
EuPathDBiFungiDB:YBR039W.
SGDiS000000243. ATP3.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial proton-transporting ATP synthase, central stalk Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi273 – 2731A → V: Lower activity. 1 Publication
Mutagenesisi297 – 2971T → A in ATP3-5; dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. 1 Publication
Mutagenesisi303 – 3031I → T in ATP3-1; dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333Mitochondrion1 PublicationAdd
BLAST
Chaini34 – 311278ATP synthase subunit gamma, mitochondrialPRO_0000002691Add
BLAST

Proteomic databases

MaxQBiP38077.
PaxDbiP38077.
PeptideAtlasiP38077.

Expressioni

Gene expression databases

GenevestigatoriP38077.

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

BioGridi32740. 49 interactions.
DIPiDIP-3035N.
IntActiP38077. 24 interactions.
MINTiMINT-693544.

Structurei

Secondary structure

1
311
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 7944Combined sources
Helixi83 – 875Combined sources
Beta strandi105 – 1106Combined sources
Helixi120 – 13415Combined sources
Beta strandi139 – 1446Combined sources
Helixi145 – 15410Combined sources
Helixi156 – 1583Combined sources
Beta strandi159 – 1657Combined sources
Beta strandi167 – 1693Combined sources
Helixi173 – 18614Combined sources
Helixi189 – 1913Combined sources
Beta strandi193 – 2019Combined sources
Beta strandi203 – 2064Combined sources
Beta strandi209 – 2157Combined sources
Helixi218 – 2225Combined sources
Helixi227 – 2293Combined sources
Beta strandi234 – 2363Combined sources
Helixi239 – 30870Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP38077.
SMRiP38077. Positions 34-311.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38077.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase gamma chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0224.
GeneTreeiENSGT00390000006837.
HOGENOMiHOG000215911.
InParanoidiP38077.
KOiK02136.
OMAiLYWALAE.
OrthoDBiEOG76QFTN.

Family and domain databases

InterProiIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERiPTHR11693. PTHR11693. 1 hit.
PfamiPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P38077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRIVSNNA TRSVMCHQAQ VGILYKTNPV RTYATLKEVE MRLKSIKNIE
60 70 80 90 100
KITKTMKIVA STRLSKAEKA KISAKKMDEA EQLFYKNAET KNLDVEATET
110 120 130 140 150
GAPKELIVAI TSDKGLCGSI HSQLAKAVRR HLNDQPNADI VTIGDKIKMQ
160 170 180 190 200
LLRTHPNNIK LSINGIGKDA PTFQESALIA DKLLSVMKAG TYPKISIFYN
210 220 230 240 250
DPVSSLSFEP SEKPIFNAKT IEQSPSFGKF EIDTDANVPR DLFEYTLANQ
260 270 280 290 300
MLTAMAQGYA AEISARRNAM DNASKNAGDM INRYSILYNR TRQAVITNEL
310
VDIITGASSL G
Length:311
Mass (Da):34,351
Last modified:October 1, 1994 - v1
Checksum:iADC71F3C1E0CDF91
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071S → I in strain: D273-10B/A1.
Natural varianti308 – 3081S → F in allele ATP3a.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS55891.
RefSeqiNP_009595.1. NM_001178387.1.

Genome annotation databases

EnsemblFungiiYBR039W; YBR039W; YBR039W.
GeneIDi852327.
KEGGisce:YBR039W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS55891.
RefSeqiNP_009595.1. NM_001178387.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP38077.
SMRiP38077. Positions 34-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32740. 49 interactions.
DIPiDIP-3035N.
IntActiP38077. 24 interactions.
MINTiMINT-693544.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

MaxQBiP38077.
PaxDbiP38077.
PeptideAtlasiP38077.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR039W; YBR039W; YBR039W.
GeneIDi852327.
KEGGisce:YBR039W.

Organism-specific databases

CYGDiYBR039w.
EuPathDBiFungiDB:YBR039W.
SGDiS000000243. ATP3.

Phylogenomic databases

eggNOGiCOG0224.
GeneTreeiENSGT00390000006837.
HOGENOMiHOG000215911.
InParanoidiP38077.
KOiK02136.
OMAiLYWALAE.
OrthoDBiEOG76QFTN.

Enzyme and pathway databases

BioCyciYEAST:G3O-29013-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38077.
NextBioi971035.
PROiP38077.

Gene expression databases

GenevestigatoriP38077.

Family and domain databases

InterProiIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERiPTHR11693. PTHR11693. 1 hit.
PfamiPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. 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.

Entry informationi

Entry nameiATPG_YEAST
AccessioniPrimary (citable) accession number: P38077
Secondary accession number(s): D6VQ39, Q54AF5, Q76MT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 29, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 28100 molecules/cell in log phase SD medium.1 Publication
PubMed:12898710 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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 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.