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P05630

- ATPD_BOVIN

UniProt

P05630 - ATPD_BOVIN

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Protein

ATP synthase subunit delta, mitochondrial

Gene
ATP5D
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: MGI
  2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP synthesis coupled proton transport Source: InterPro
  2. proton transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_212639. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit delta, mitochondrial
Alternative name(s):
F-ATPase delta subunit
Gene namesi
Name:ATP5D
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 7

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial envelope Source: MGI
  2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  3. proton-transporting ATP synthase complex Source: MGI
  4. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222Mitochondrion2 PublicationsAdd
BLAST
Chaini23 – 168146ATP synthase subunit delta, mitochondrialUniRule annotationPRO_0000002660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361N6-acetyllysine; alternate By similarity
Modified residuei136 – 1361N6-succinyllysine; alternate By similarity
Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei165 – 1651N6-acetyllysine; alternate By similarity
Modified residuei165 – 1651N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP05630.
PRIDEiP05630.

Interactioni

Subunit structurei

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 MP68.1 Publication

Protein-protein interaction databases

DIPiDIP-39022N.
IntActiP05630. 2 interactions.
MINTiMINT-5007030.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 436
Beta strandi48 – 503
Beta strandi56 – 605
Beta strandi62 – 654
Beta strandi66 – 705
Beta strandi76 – 805
Beta strandi82 – 898
Beta strandi92 – 998
Beta strandi101 – 1033
Beta strandi108 – 1103
Beta strandi114 – 1196
Beta strandi122 – 1243
Helixi129 – 14012
Beta strandi141 – 1433
Beta strandi147 – 1504
Helixi151 – 16414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP05630.
SMRiP05630. Positions 37-167.

Miscellaneous databases

EvolutionaryTraceiP05630.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0355.
GeneTreeiENSGT00390000017576.
HOGENOMiHOG000216023.
HOVERGENiHBG001856.
InParanoidiP05630.
KOiK02134.
OMAiLPHQAIF.
OrthoDBiEOG7RNK2T.
TreeFamiTF313029.

Family and domain databases

Gene3Di2.60.15.10. 1 hit.
HAMAPiMF_00530. ATP_synth_epsil_bac.
InterProiIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
IPR020547. ATPase_F1_dsu/esu_C.
[Graphical view]
PANTHERiPTHR13822. PTHR13822. 1 hit.
PfamiPF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomiPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46604. SSF46604. 1 hit.
SSF51344. SSF51344. 1 hit.
TIGRFAMsiTIGR01216. ATP_synt_epsi. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05630-1 [UniParc]FASTAAdd to Basket

« Hide

MLPSALLRRP GLGRLVRQVR LYAEAAAAQA PAAGPGQMSF TFASPTQVFF    50
NSANVRQVDV PTQTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS 100
SGSVTVNADS SVQLLAEEAV TLDMLDLGAA KANLEKAQSE LLGAADEATR 150
AEIQIRIEAN EALVKALE 168
Length:168
Mass (Da):17,612
Last modified:August 1, 1990 - v2
Checksum:i7C47BBAD5A151608
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17019 mRNA. Translation: CAA34885.1.
BC146208 mRNA. Translation: AAI46209.1.
PIRiS09202. PWBOD.
RefSeqiNP_788843.1. NM_176670.2.
UniGeneiBt.1426.

Genome annotation databases

EnsembliENSBTAT00000000721; ENSBTAP00000000721; ENSBTAG00000000550.
GeneIDi338081.
KEGGibta:338081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17019 mRNA. Translation: CAA34885.1 .
BC146208 mRNA. Translation: AAI46209.1 .
PIRi S09202. PWBOD.
RefSeqi NP_788843.1. NM_176670.2.
UniGenei Bt.1426.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P05630.
SMRi P05630. Positions 37-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-39022N.
IntActi P05630. 2 interactions.
MINTi MINT-5007030.

Chemistry

ChEMBLi CHEMBL612444.

Proteomic databases

PaxDbi P05630.
PRIDEi P05630.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000000721 ; ENSBTAP00000000721 ; ENSBTAG00000000550 .
GeneIDi 338081.
KEGGi bta:338081.

Organism-specific databases

CTDi 513.

Phylogenomic databases

eggNOGi COG0355.
GeneTreei ENSGT00390000017576.
HOGENOMi HOG000216023.
HOVERGENi HBG001856.
InParanoidi P05630.
KOi K02134.
OMAi LPHQAIF.
OrthoDBi EOG7RNK2T.
TreeFami TF313029.

Enzyme and pathway databases

Reactomei REACT_212639. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

EvolutionaryTracei P05630.
NextBioi 20812529.

Family and domain databases

Gene3Di 2.60.15.10. 1 hit.
HAMAPi MF_00530. ATP_synth_epsil_bac.
InterProi IPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
IPR020547. ATPase_F1_dsu/esu_C.
[Graphical view ]
PANTHERi PTHR13822. PTHR13822. 1 hit.
Pfami PF02823. ATP-synt_DE_N. 1 hit.
[Graphical view ]
ProDomi PD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF46604. SSF46604. 1 hit.
SSF51344. SSF51344. 1 hit.
TIGRFAMsi TIGR01216. ATP_synt_epsi. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiATPD_BOVIN
AccessioniPrimary (citable) accession number: P05630
Secondary accession number(s): A6H7D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: August 1, 1990
Last modified: September 3, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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