ATP synthase subunit delta, mitochondrial precursor

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P05630 (ATPD_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATP synthase subunit delta, mitochondrial

Alternative name(s):
F-ATPase delta subunit

Gene names

Name:

ATP5D

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	168 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 turnover 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 ATPase epsilon chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC 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 proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	hydrogen ion transmembrane transporter activity Inferred from direct assay Ref.4. Source: MGI 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

Transit peptide

1 – 22

Mitochondrion Ref.3 Ref.4

Chain

23 – 168

146

ATP synthase subunit delta, mitochondrial

PRO_0000002660

Amino acid modifications

Cross-link

136

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

168

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P05630 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 7C47BBAD5A151608
Show »

FASTA

168

17,612

        10         20         30         40         50         60 
MLPSALLRRP GLGRLVRQVR LYAEAAAAQA PAAGPGQMSF TFASPTQVFF NSANVRQVDV 

        70         80         90        100        110        120 
PTQTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS SGSVTVNADS SVQLLAEEAV 

       130        140        150        160 
TLDMLDLGAA KANLEKAQSE LLGAADEATR AEIQIRIEAN EALVKALE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The delta-subunit of ATP synthase from bovine heart mitochondria. Complementary DNA sequence of its import precursor cloned with the aid of the polymerase chain reaction." Runswick M.J., Medd S.M., Walker J.E. Biochem. J. 266:421-426(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart muscle.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.
[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 23-168.
[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 23-31. 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 23-168 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5B; ATP5C1 AND ATP5E.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X17019 mRNA. Translation: CAA34885.1.
BC146208 mRNA. Translation: AAI46209.1.

IPI

IPI00707257.

PIR

PWBOD. S09202.

RefSeq

NP_788843.1. NM_176670.2.

UniGene

Bt.1426.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E79	X-ray	2.40	H	23-168	[»]
1H8E	X-ray	2.00	H	23-168	[»]
2CK3	X-ray	1.90	H	23-168	[»]
2JDI	X-ray	1.90	H	23-168	[»]
2V7Q	X-ray	2.10	H	23-168	[»]
2W6H	X-ray	5.00	H	1-168	[»]
2W6I	X-ray	4.00	H	1-168	[»]
2W6J	X-ray	3.84	H	1-168	[»]
2WSS	X-ray	3.20	H/Q	23-168	[»]
2XND	X-ray	3.50	H	37-167	[»]
4ASU	X-ray	2.60	H	23-168	[»]

ProteinModelPortal

P05630.

SMR

P05630. Positions 37-167.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39022N.

IntAct

P05630. 1 interaction.

MINT

MINT-5007030.

Proteomic databases

PaxDb

P05630.

PRIDE

P05630.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000000721; ENSBTAP00000000721; ENSBTAG00000000550.

GeneID

338081.

KEGG

bta:338081.

Organism-specific databases

CTD

513.

Phylogenomic databases

eggNOG

COG0355.

GeneTree

ENSGT00390000017576.

HOGENOM

HOG000216023.

HOVERGEN

HBG001856.

InParanoid

P05630.

K02134.

OMA

GILANHI.

OrthoDB

EOG4894NT.

Family and domain databases

Gene3D

2.60.15.10. 1 hit.

InterPro

IPR001469. ATPase_F1-cplx_dsu/esu.
IPR020547. ATPase_F1-cplx_dsu/esu_C.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
[Graphical view]

PANTHER

PTHR13822. PTHR13822. 1 hit.

Pfam

PF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]

ProDom

PD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF46604. ATPsynt_DE. 1 hit.
SSF51344. ATPsynt_DE. 1 hit.

TIGRFAMs

TIGR01216. ATP_synt_epsi. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P05630.

NextBio

20812529.

Entry information

Entry name

ATPD_BOVIN

Accession

Primary (citable) accession number: P05630
Secondary accession number(s): A6H7D8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents