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Protein

ATP synthase subunit delta, mitochondrial

Gene

ATP5D

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled proton transport Source: GO_Central
  • proton transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-163210. 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
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

  • mitochondrial envelope Source: MGI
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: GO_Central
  • proton-transporting ATP synthase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL612444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 22Mitochondrion2 PublicationsAdd BLAST22
ChainiPRO_000000266023 – 168ATP synthase subunit delta, mitochondrialAdd BLAST146

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei136N6-acetyllysine; alternateBy similarity1
Modified residuei136N6-succinyllysine; alternateBy similarity1
Modified residuei165N6-acetyllysine; alternateBy similarity1
Modified residuei165N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP05630.
PeptideAtlasiP05630.
PRIDEiP05630.

Expressioni

Gene expression databases

BgeeiENSBTAG00000000550.

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 MP68.2 Publications

Protein-protein interaction databases

DIPiDIP-39022N.
IntActiP05630. 2 interactors.
MINTiMINT-5007030.
STRINGi9913.ENSBTAP00000000721.

Chemistry databases

BindingDBiP05630.

Structurei

Secondary structure

1168
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 43Combined sources6
Beta strandi48 – 50Combined sources3
Beta strandi56 – 59Combined sources4
Beta strandi63 – 65Combined sources3
Beta strandi66 – 70Combined sources5
Beta strandi76 – 80Combined sources5
Beta strandi82 – 89Combined sources8
Beta strandi92 – 99Combined sources8
Beta strandi101 – 103Combined sources3
Beta strandi108 – 110Combined sources3
Beta strandi114 – 119Combined sources6
Beta strandi122 – 124Combined sources3
Helixi129 – 140Combined sources12
Beta strandi141 – 143Combined sources3
Beta strandi147 – 150Combined sources4
Helixi151 – 164Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4YXWX-ray3.10H23-168[»]
5ARAelectron microscopy6.70H23-168[»]
5AREelectron microscopy7.40H23-168[»]
5ARHelectron microscopy7.20H23-168[»]
5ARIelectron microscopy7.40H23-168[»]
5FIJelectron microscopy7.40H23-168[»]
5FIKelectron microscopy6.40H23-168[»]
5FILelectron microscopy7.10H23-168[»]
ProteinModelPortaliP05630.
SMRiP05630.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05630.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase epsilon chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1758. Eukaryota.
COG0355. LUCA.
GeneTreeiENSGT00390000017576.
HOGENOMiHOG000216023.
HOVERGENiHBG001856.
InParanoidiP05630.
KOiK02134.
OMAiPQMSFTF.
OrthoDBiEOG091G1AP6.
TreeFamiTF313029.

Family and domain databases

CDDicd12152. F1-ATPase_delta. 1 hit.
Gene3Di2.60.15.10. 1 hit.
HAMAPiMF_00530. ATP_synth_epsil_bac. 1 hit.
InterProiIPR001469. ATP_synth_F1_dsu/esu.
IPR020547. ATP_synth_F1_dsu/esu_C.
IPR020546. ATP_synth_F1_dsu/esu_N.
[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

        10         20         30         40         50
MLPSALLRRP GLGRLVRQVR LYAEAAAAQA PAAGPGQMSF TFASPTQVFF
60 70 80 90 100
NSANVRQVDV PTQTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS
110 120 130 140 150
SGSVTVNADS SVQLLAEEAV TLDMLDLGAA KANLEKAQSE LLGAADEATR
160
AEIQIRIEAN EALVKALE
Length:168
Mass (Da):17,612
Last modified:August 1, 1990 - v2
Checksum:i7C47BBAD5A151608
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X17019 mRNA. Translation: CAA34885.1.
BC146208 mRNA. Translation: AAI46209.1.
PIRiS09202. PWBOD.
RefSeqiNP_788843.1. NM_176670.2.
UniGeneiBt.1426.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4YXWX-ray3.10H23-168[»]
5ARAelectron microscopy6.70H23-168[»]
5AREelectron microscopy7.40H23-168[»]
5ARHelectron microscopy7.20H23-168[»]
5ARIelectron microscopy7.40H23-168[»]
5FIJelectron microscopy7.40H23-168[»]
5FIKelectron microscopy6.40H23-168[»]
5FILelectron microscopy7.10H23-168[»]
ProteinModelPortaliP05630.
SMRiP05630.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39022N.
IntActiP05630. 2 interactors.
MINTiMINT-5007030.
STRINGi9913.ENSBTAP00000000721.

Chemistry databases

BindingDBiP05630.
ChEMBLiCHEMBL612444.

Proteomic databases

PaxDbiP05630.
PeptideAtlasiP05630.
PRIDEiP05630.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi513.

Phylogenomic databases

eggNOGiKOG1758. Eukaryota.
COG0355. LUCA.
GeneTreeiENSGT00390000017576.
HOGENOMiHOG000216023.
HOVERGENiHBG001856.
InParanoidiP05630.
KOiK02134.
OMAiPQMSFTF.
OrthoDBiEOG091G1AP6.
TreeFamiTF313029.

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

EvolutionaryTraceiP05630.
PROiP05630.

Gene expression databases

BgeeiENSBTAG00000000550.

Family and domain databases

CDDicd12152. F1-ATPase_delta. 1 hit.
Gene3Di2.60.15.10. 1 hit.
HAMAPiMF_00530. ATP_synth_epsil_bac. 1 hit.
InterProiIPR001469. ATP_synth_F1_dsu/esu.
IPR020547. ATP_synth_F1_dsu/esu_C.
IPR020546. ATP_synth_F1_dsu/esu_N.
[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.
ProtoNetiSearch...

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: November 30, 2016
This is version 145 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.