P09457 (ATPO_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit 5, mitochondrial
Short name=ATP synthase chain 5

Alternative name(s):
Oligomycin sensitivity conferral protein
Short name=OSCP

Gene names

Name:	ATP5
Synonyms:	OSCP
Ordered Locus Names:	YDR298C
ORF Names:	D9740.11

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	212 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 F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements.
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.
Miscellaneous	Present with 32400 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the ATPase delta chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from direct assay. Source: SGD
Cellular component	mitochondrial proton-transporting ATP synthase, stator stalk Inferred from mutant phenotype Ref.2. Source: SGD plasma membrane Inferred from electronic annotation. Source: InterPro
Molecular function	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 17	17	Mitochondrion
	Chain	18 – 212	195	ATP synthase subunit 5, mitochondrial		PRO_0000002656
Amino acid modifications
	Modified residue	48	1	Phosphoserine Ref.7
	Modified residue	139	1	Phosphothreonine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P09457 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: BD5F8EF4503E4D66	FASTA	212	22,814
	10 20 30 40 50 60 MFNRVFTRSF ASSLRAAASK AAAPPPVRLF GVEGTYATAL YQAAAKNSSI DAAFQSLQKV 70 80 90 100 110 120 ESTVKKNPKL GHLLLNPALS LKDRNSVIDA IVETHKNLDG YVVNLLKVLS ENNRLGCFEK 130 140 150 160 170 180 IASDFGVLND AHNGLLKGTV TSAEPLDPKS FKRIEKALSA SKLVGQGKSL KLENVVKPEI 190 200 210 KGGLIVELGD KTVDLSISTK IQKLNKVLED SI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of the yeast ATP5 gene." Lee M., Jones D., Mueller D.M. Nucleic Acids Res. 16:8181-8181(1988) [PubMed: 2971156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24657 / D273-10B.
[2]	"The gene coding for the yeast oligomycin sensitivity-conferring protein." Uh M., Jones D., Mueller D.M. J. Biol. Chem. 265:19047-19052(1990) [PubMed: 2146269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase." Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C. Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed: 17761666] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND THR-139, MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X12356 Genomic DNA. Translation: CAA30917.1. M32487 Genomic DNA. Translation: AAA34836.1. U28374 Genomic DNA. Translation: AAB64734.1. AY557732 Genomic DNA. Translation: AAS56058.1. BK006938 Genomic DNA. Translation: DAA12137.1.
PIR	PWBYD. S05726.
RefSeq	NP_010584.1. NM_001180606.1.
3D structure databases
ProteinModelPortal	P09457.
SMR	P09457. Positions 20-211.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3037N.
IntAct	P09457. 6 interactions.
MINT	MINT-688192.
STRING	P09457.
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.
2D gel databases
UCD-2DPAGE	P09457.
Proteomic databases
PeptideAtlas	P09457.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR298C; YDR298C; YDR298C.
GeneID	851892.
KEGG	sce:YDR298C.
NMPDR	fig|4932.3.peg.1346.
Organism-specific databases
CYGD	YDR298c.
SGD	S000002706. ATP5.
Phylogenomic databases
eggNOG	fuNOG08424.
GeneTree	EFGT00050000004814.
HOGENOM	HBG668108.
OMA	RCATARS.
OrthoDB	EOG4RFQ2Z.
Gene expression databases
ArrayExpress	P09457.
Genevestigator	P09457.
GermOnline	YDR298C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000711. ATPase_F1-cplx_OSCP/dsu. IPR020781. ATPase_F1-cplx_OSCP/dsu_CS. [Graphical view]
Gene3D	G3DSA:1.10.520.20. ATPase_F1_OSCP/d. 1 hit.
KO	K02137.
PANTHER	PTHR11910. ATPase_F1_OSCP/d. 1 hit.
Pfam	PF00213. OSCP. 1 hit. [Graphical view]
PRINTS	PR00125. ATPASEDELTA.
SUPFAM	SSF47928. ATPsynt_OSCP. 1 hit.
TIGRFAMs	TIGR01145. ATP_synt_delta. 1 hit.
PROSITE	PS00389. ATPASE_DELTA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	969880.

Entry information

Entry name

ATPO_YEAST

Accession

Primary (citable) accession number: P09457
Secondary accession number(s): D6VSS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	December 14, 2011
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program