Reviewed, UniProtKB/Swiss-Prot Q06405 (ATPK_YEAST)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit f, mitochondrial

Gene names

Name:	ATP17
Ordered Locus Names:	YDR377W
ORF Names:	D9481.21

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	101 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. Minor subunit located with subunit a in the membrane.
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.
Subcellular location	Mitochondrion. Mitochondrion inner membrane.
Miscellaneous	Present with 14600 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the ATPase F chain family.
Mass spectrometry	Molecular mass is 10565±2 Da from positions 7 - 101. Determined by ESI. Ref.1

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Ref.1 Inferred from mutant phenotype. Source: SGD
Molecular function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-3285,EBI-3285
ATP18	P81450	1	EBI-3285,EBI-2045988
SET2	P46995	1	EBI-3285,EBI-16985
URN1	Q06525	1	EBI-3285,EBI-35138

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 6	6	Mitochondrion
	Chain	7 – 101	95	ATP synthase subunit f, mitochondrial		PRO_0000002637

Sequences

	Sequence		Length	Mass (Da)
	Q06405-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3DEF593AE4435551	FASTA	101	11,312
	10 20 30 40 50 60 MIFKRAVSTL IPPKVVSSKN IGSAPNAKRI ANVVHFYKSL PQGPAPAIKA NTRLARYKAK 70 80 90 100 YFDGDNASGK PLWHFALGII AFGYSMEYYF HLRHHKGAEE H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The subunit f of mitochondrial yeast ATP synthase -- characterization of the protein and disruption of the structural gene ATP17." Spannagel C., Vaillier J., Arselin G., Graves P.-V., Velours J. Eur. J. Biochem. 247:1111-1117(1997) [PubMed: 9288937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, MASS SPECTROMETRY. Strain: D273-10B/A/H/U.
[2]	"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.
[3]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U72652 Genomic DNA. Translation: AAB70108.1. U28373 Genomic DNA. Translation: AAB64813.1.
PIR	S61172.
RefSeq	NP_010665.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3033N.
IntAct	Q06405. 4 interactions.
Proteomic databases
PeptideAtlas	Q06405.
Genome annotation databases
Ensembl	YDR377W. Saccharomyces cerevisiae. [Contig view]
GeneID	851983.
GenomeReviews	Gene locus YDR377W in contig Z71256_GR.
KEGG	sce:YDR377W.
NMPDR	fig|4932.3.peg.1435.
Organism-specific databases
CYGD	YDR377w.
SGD	S000002785. ATP17.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q06405.
OMA	Q06405. LIPPKIA.
Gene expression databases
GermOnline	YDR377W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019727. ATPase_F0-cplx_fsu_mt_fun. [Graphical view]
Pfam	PF10791. F1F0-ATPsyn_F. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	970133.

Entry information

Entry name

ATPK_YEAST

Accession

Primary (citable) accession number: Q06405

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)