Reviewed, UniProtKB/Swiss-Prot Q96253 (ATP5E_ARATH)

Names and origin

Protein names

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

Gene names

Ordered Locus Names:	At1g51650
ORF Names:	F19C24.25

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	70 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 Ref.4.
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
Technical term	Complete 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, catalytic core F(1) Inferred from electronic annotation. Source: InterPro
Molecular function	hydrogen ion 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 By similarity
	Chain	2 – 70	69	ATP synthase subunit epsilon, mitochondrial		PRO_0000071668

Sequences

	Sequence		Length	Mass (Da)
	Q96253-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 13CA2441550ED5A5	FASTA	70	7,832
	10 20 30 40 50 60 MASNAAVPFW RAAGMTYISY SNICANIVRN CLKEPHKAEA LTREKVHFSL SKWADGKPQK 70 PVLRSDTPEV

References

[1]	"Nucleotide sequence of cDNAs encoding gamma, delta, delta-prime, and epsilon subunits of mitochondrial F1-ATPase in Arabidopsis thaliana." Sakamoto W., Wintz H. Plant Gene Register PGR96-125 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D88377 mRNA. Translation: BAA13602.1. AC025294 Genomic DNA. Translation: AAG50890.1. AY072309 mRNA. Translation: AAL61916.1. AY114540 mRNA. Translation: AAM47859.1.
IPI	IPI00538260.
PIR	C96555.
RefSeq	NP_175576.1.
UniGene	At.25226 Rra.9050
3D structure databases
SMR	Q96253. Positions 7-52.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96253. 2 interactions.
STRING	Q96253.
Proteomic databases
PRIDE	Q96253.
Genome annotation databases
GeneID	841590.
GenomeReviews	Gene locus AT1G51650 in contig CT485782_GR.
KEGG	ath:AT1G51650.
NMPDR	fig|3702.1.peg.4639.
Organism-specific databases
GeneFarm	3311.
TAIR	At1g51650.
Phylogenomic databases
eggNOG	KOG3495.
HOGENOM	HBG601799.
InParanoid	Q96253.
OMA	ISYSNIC.
Gene expression databases
ArrayExpress	Q96253.
Genevestigator	Q96253.
GermOnline	AT1G51650. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR006721. ATPase_F1-cplx_esu_mt. [Graphical view]
Gene3D	G3DSA:1.10.1620.20. ATPase_F1_e_mt. 1 hit.
Pfam	PF04627. ATP-synt_Eps. 1 hit. [Graphical view]
SUPFAM	SSF48690. ATP_synth_E. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ATP5E_ARATH

Accession

Primary (citable) accession number: Q96253

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	March 2, 2010
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)