P05632 (ATP5E_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

ATP5E

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	51 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 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. Ref.5
Subcellular location	Mitochondrion. Mitochondrion inner membrane.
Sequence similarities	Belongs to the eukaryotic ATPase epsilon family.
Sequence caution	The sequence CAA34849.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrial proton-transporting ATP synthase complex Inferred from direct assay Ref.5. Source: UniProtKB mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: InterPro
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.3 Ref.4

Chain

2 – 51

50

ATP synthase subunit epsilon, mitochondrial

PRO_0000071661

Amino acid modifications

Modified residue

21

1

N6-acetyllysine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

51

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

12 – 24

13

Turn

29 – 31

3

Helix

33 – 36

4

Beta strand

44 – 46

3

Sequences

	Sequence		Length	Mass (Da)
	P05632 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: E0D70FA7C9191CAE	FASTA	51	5,783
	10 20 30 40 50 MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAMKTSG STIKIVKVKK E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The epsilon-subunit of ATP synthase from bovine heart mitochondria. Complementary DNA sequence, expression in bovine tissues and evidence of homologous sequences in man and rat." Vinas O., Powell S.J., Runswick M.J., Iacobazzi V., Walker J.E. Biochem. J. 265:321-326(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver.
[3]	"Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria." Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D., Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J. J. Mol. Biol. 184:677-701(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-51.
[4]	"Identification of the subunits of F1F0-ATPase from bovine heart mitochondria." Walker J.E., Lutter R., Dupuis A., Runswick M.J. Biochemistry 30:5369-5378(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-7. Tissue: Heart.
[5]	"Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria." Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E. FEBS Lett. 581:3145-3148(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
[6]	"Structure at 2.8-A resolution of F1-ATPase from bovine heart mitochondria." Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E. Nature 370:621-628(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[7]	"How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria." Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E. Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-50 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5B; ATP5C1 AND ATP5D.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16978 mRNA. Translation: CAA34849.1. Different initiation.
BC108146 mRNA. Translation: AAI08147.1.

IPI

IPI00692573.

PIR

PWBOE. S08239.

RefSeq

NP_001137213.1. NM_001143741.1.

UniGene

Bt.58312.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E79	X-ray	2.40	I	2-51	[»]
1H8E	X-ray	2.00	I	2-51	[»]
2CK3	X-ray	1.95	I	2-51	[»]
2JDI	X-ray	1.90	I	2-50	[»]
2V7Q	X-ray	2.10	I	2-50	[»]
2W6H	X-ray	5.00	I	1-51	[»]
2W6I	X-ray	4.00	I	1-51	[»]
2W6J	X-ray	3.84	I	1-51	[»]
2WSS	X-ray	3.20	I/R	2-51	[»]
2XND	X-ray	3.50	I	2-48	[»]
4ASU	X-ray	2.60	I	2-51	[»]

ProteinModelPortal

P05632.

SMR

P05632. Positions 2-48.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46312N.

MINT

MINT-5007161.

STRING

9913.ENSBTAP00000051455.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000035337; ENSBTAP00000035213; ENSBTAG00000032954.
ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208.

GeneID

617230.

KEGG

bta:617230.

Organism-specific databases

CTD

514.

Phylogenomic databases

eggNOG

NOG318665.

GeneTree

ENSGT00390000015470.

HOGENOM

HOG000214506.

HOVERGEN

HBG050611.

InParanoid

P05632.

KO

K02135.

OMA

RFSQICA.

OrthoDB

EOG43N7FH.

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

P05632.

NextBio

20900552.

Entry information

Entry name

ATP5E_BOVIN

Accession

Primary (citable) accession number: P05632
Secondary accession number(s): Q32PE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 121 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program