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P05630 (ATPD_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit delta, mitochondrial
Alternative name(s):
F-ATPase delta subunit
Gene names
Name:ATP5D
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. HAMAP-Rule MF_00530

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 HAMAP-Rule MF_00530.

Sequence similarities

Belongs to the ATPase epsilon chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Ref.3 Ref.4
Chain23 – 168146ATP synthase subunit delta, mitochondrial HAMAP-Rule MF_00530
PRO_0000002660

Amino acid modifications

Modified residue1361N6-acetyllysine; alternate By similarity
Modified residue1361N6-succinyllysine; alternate By similarity
Modified residue1651N6-acetyllysine; alternate By similarity
Modified residue1651N6-succinyllysine; alternate By similarity
Cross-link136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Secondary structure

.............................. 168
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05630 [UniParc].

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

FASTA16817,612
        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' 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.
PIRPWBOD. S09202.
RefSeqNP_788843.1. NM_176670.2.
UniGeneBt.1426.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E79X-ray2.40H23-168[»]
1H8EX-ray2.00H23-168[»]
2CK3X-ray1.90H23-168[»]
2JDIX-ray1.90H23-168[»]
2V7QX-ray2.10H23-168[»]
2W6HX-ray5.00H1-168[»]
2W6IX-ray4.00H1-168[»]
2W6JX-ray3.84H1-168[»]
2WSSX-ray3.20H/Q23-168[»]
2XNDX-ray3.50H37-167[»]
4ASUX-ray2.60H23-168[»]
ProteinModelPortalP05630.
SMRP05630. Positions 37-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-39022N.
IntActP05630. 2 interactions.
MINTMINT-5007030.

Chemistry

ChEMBLCHEMBL612444.

Proteomic databases

PaxDbP05630.
PRIDEP05630.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000000721; ENSBTAP00000000721; ENSBTAG00000000550.
GeneID338081.
KEGGbta:338081.

Organism-specific databases

CTD513.

Phylogenomic databases

eggNOGCOG0355.
GeneTreeENSGT00390000017576.
HOGENOMHOG000216023.
HOVERGENHBG001856.
InParanoidP05630.
KOK02134.
OMALPHQAIF.
OrthoDBEOG7RNK2T.
TreeFamTF313029.

Family and domain databases

Gene3D2.60.15.10. 1 hit.
HAMAPMF_00530. ATP_synth_epsil_bac.
InterProIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
IPR020547. ATPase_F1_dsu/esu_C.
[Graphical view]
PANTHERPTHR13822. PTHR13822. 1 hit.
PfamPF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF46604. SSF46604. 1 hit.
SSF51344. SSF51344. 1 hit.
TIGRFAMsTIGR01216. ATP_synt_epsi. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP05630.
NextBio20812529.

Entry information

Entry nameATPD_BOVIN
AccessionPrimary (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: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references