ATP synthase subunit gamma, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38077 (ATPG_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP synthesis coupled proton transport Inferred from direct assay PubMed 20691145. Source: SGD
Cellular_component	integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD mitochondrial proton-transporting ATP synthase, central stalk Inferred from direct assay Ref.9. Source: SGD
Molecular_function	proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAF4	P36130	1	EBI-3271,EBI-26394

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 33

Mitochondrion Ref.1

Chain

34 – 311

278

ATP synthase subunit gamma, mitochondrial

PRO_0000002691

Natural variations

Natural variant

207

S → I in strain: D273-10B/A1.

Natural variant

308

S → F in allele ATP3a.

Experimental info

Mutagenesis

273

A → V: Lower activity. Ref.1

Mutagenesis

297

T → A in ATP3-5; dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. Ref.2

Mutagenesis

303

I → 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

Length

Mass (Da)

Tools

P38077 [UniParc].

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

FASTA

311

34,351

        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' referencesShow '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. 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. 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.

PIR

S55891.

RefSeq

NP_009595.1. NM_001178387.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HLD	X-ray	2.80	G/P/Y	34-311	[»]
2WPD	X-ray	3.43	G	34-311	[»]
2XOK	X-ray	3.01	G	1-311	[»]
3FKS	X-ray	3.59	G/P/Y	34-311	[»]
3OE7	X-ray	3.19	G/P/Y	34-311	[»]
3OEE	X-ray	2.74	G/P/Y	34-311	[»]
3OEH	X-ray	3.00	G/P/Y	34-311	[»]
3OFN	X-ray	3.20	G/P/Y	34-311	[»]
3ZIA	X-ray	2.50	G/Q	34-311	[»]
3ZRY	X-ray	6.50	G	34-311	[»]
4B2Q	electron microscopy	37.00	G/g	34-311	[»]

ProteinModelPortal

P38077.

SMR

P38077. Positions 34-311.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3035N.

IntAct

P38077. 33 interactions.

MINT

MINT-693544.

Protein family/group databases

TCDB

3.A.2.1.3. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

Proteomic databases

PaxDb

P38077.

PeptideAtlas

P38077.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBR039W; YBR039W; YBR039W.

GeneID

852327.

KEGG

sce:YBR039W.

Organism-specific databases

CYGD

YBR039w.

SGD

S000000243. ATP3.

Phylogenomic databases

eggNOG

COG0224.

GeneTree

ENSGT00390000006837.

HOGENOM

HOG000215911.

K02136.

OMA

QQRGMAT.

OrthoDB

EOG4PVS7K.

Gene expression databases

Genevestigator

P38077.

GermOnline

YBR039W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]

PANTHER

PTHR11693. PTHR11693. 1 hit.

Pfam

PF00231. ATP-synt. 1 hit.
[Graphical view]

PRINTS

PR00126. ATPASEGAMMA.

SUPFAM

SSF52943. ATPase_gamma. 1 hit.

TIGRFAMs

TIGR01146. ATPsyn_F1gamma. 1 hit.

PROSITE

PS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P38077.

NextBio

971035.

Entry information

Entry name

ATPG_YEAST

Accession

Primary (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 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents