P21306 (ATP5E_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit epsilon, mitochondrial
Short name=ATPase subunit epsilon

Gene names

Name:	ATP15
Ordered Locus Names:	YPL271W
ORF Names:	P0345

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	62 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 of the central stalk which is part of the complex rotary element. 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.
Miscellaneous	Present with 4280 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the eukaryotic ATPase epsilon family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay PubMed 18722382. Source: GOC 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 PubMed 17082766. 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 62

61

ATP synthase subunit epsilon, mitochondrial

PRO_0000071667

Amino acid modifications

Modified residue

52

1

Phosphothreonine Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

62

Helix Strand Turn

Details...

Turn

4 – 6

3

Helix

11 – 24

14

Helix

28 – 30

3

Helix

33 – 37

5

Beta strand

44 – 47

4

Sequences

	Sequence		Length	Mass (Da)
	P21306 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0CD754A9DEFFD08C	FASTA	62	6,743
	10 20 30 40 50 60 MSAWRKAGIS YAAYLNVAAQ AIRSSLKTEL QTASVLNRSQ TDAFYTQYKN GTAASEPTPI TK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ATP synthase of yeast mitochondria. Isolation and disruption of the ATP epsilon gene." Guelin E., Chevallier J., Rigoulet M., Guerin B., Velours J. J. Biol. Chem. 268:161-167(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: D273-10B/A/H/U.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Isolation and complete amino acid sequence of the mitochondrial ATP synthase epsilon-subunit of the yeast Saccharomyces cerevisiae." Arselin G., Gandar J.-C., Guerin B., Velours J. J. Biol. Chem. 266:723-727(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-62. Strain: ATCC 60782 / S / NCYC 232 / American yeast foam.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52, MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X64767 Genomic DNA. Translation: CAA46014.1.
Z73627 Genomic DNA. Translation: CAA98007.1.
AY558140 Genomic DNA. Translation: AAS56466.1.
BK006949 Genomic DNA. Translation: DAA11165.1.

PIR

A45315.

RefSeq

NP_015052.1. NM_001184085.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HLD	X-ray	2.80	1/I/R	2-61	[»]
2WPD	X-ray	3.43	I	2-62	[»]
3FKS	X-ray	3.59	1/I/R	2-62	[»]
3OE7	X-ray	3.19	1/I/R	2-62	[»]
3OEE	X-ray	2.74	1/I/R	2-62	[»]
3OEH	X-ray	3.00	1/I/R	2-62	[»]
3OFN	X-ray	3.20	I/R	2-62	[»]
3ZIA	X-ray	2.50	I/S	2-62	[»]
4B2Q	electron microscopy	37.00	I/i	2-60	[»]

ProteinModelPortal

P21306.

SMR

P21306. Positions 2-60.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3031N.

MINT

MINT-547186.

STRING

4932.YPL271W.

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

P21306.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL271W; YPL271W; YPL271W.

GeneID

855857.

KEGG

sce:YPL271W.

Organism-specific databases

SGD

S000006192. ATP15.

Phylogenomic databases

eggNOG

NOG294695.

HOGENOM

HOG000214506.

KO

K02135.

OMA

MSAWRKA.

OrthoDB

EOG4GXJXQ.

Gene expression databases

ArrayExpress

P21306.

Genevestigator

P21306.

GermOnline

YPL271W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.1620.20. 1 hit.

InterPro

IPR006721. ATPase_F1-cplx_esu_mt.
[Graphical view]

Pfam

PF04627. ATP-synt_Eps. 1 hit.
[Graphical view]

SUPFAM

SSF48690. ATP_synth_E. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P21306.

NextBio

980466.

Entry information

Entry name

ATP5E_YEAST

Accession

Primary (citable) accession number: P21306
Secondary accession number(s): D6W399

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program