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Protein

ATP synthase subunit delta, mitochondrial

Gene

Atp5d

Organism
Rattus norvegicus (Rat)
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

  • ATPase activity Source: RGD
  • protein complex binding Source: RGD
  • proton-transporting ATPase activity, rotational mechanism Source: InterPro
  • proton-transporting ATP synthase activity, rotational mechanism Source: RGD

GO - Biological processi

  • ATP biosynthetic process Source: RGD
  • ATP metabolic process Source: RGD
  • ATP synthesis coupled proton transport Source: RGD
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit delta, mitochondrial
Alternative name(s):
F-ATPase delta subunit
Gene namesi
Name:Atp5d
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621372. Atp5d.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: RGD
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
  • proton-transporting ATP synthase complex Source: RGD
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
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 – 2222Mitochondrion1 PublicationAdd
BLAST
Chaini23 – 168146ATP synthase subunit delta, mitochondrialPRO_0000002664Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP35434.
PRIDEiP35434.

2D gel databases

UCD-2DPAGEP35434.

PTM databases

iPTMnetiP35434.

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

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi251461. 1 interaction.
IntActiP35434. 2 interactions.
MINTiMINT-4590976.
STRINGi10116.ENSRNOP00000020670.

Structurei

3D structure databases

ProteinModelPortaliP35434.
SMRiP35434. Positions 37-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase epsilon chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1758. Eukaryota.
COG0355. LUCA.
HOGENOMiHOG000216023.
HOVERGENiHBG001856.
InParanoidiP35434.
KOiK02134.
PhylomeDBiP35434.

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.

P35434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPAALLRHP GLRRLVLQAR TYAQAAASPA PAAGPGQMSF TFASPTQVFF
60 70 80 90 100
DGANVRQVDV PTLTGAFGIL ASHVPTLQVL RPGLVMVHAE DGTTTKYFVS
110 120 130 140 150
SGSVTVNADS SVQLLAEEVV TLDMLDLGAA RANLEKAQSE LSGAADEAAR
160
AEIQIRIEAN EALVKALE
Length:168
Mass (Da):17,595
Last modified:February 1, 1996 - v2
Checksum:iC8628F8BF266F849
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241Q → E AA sequence (Ref. 3) Curated
Sequence conflicti28 – 281S → A AA sequence (Ref. 3) Curated
Sequence conflicti31 – 311P → S AA sequence (Ref. 3) Curated
Sequence conflicti51 – 511D → N AA sequence (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00926 mRNA. Translation: AAC28872.1.
PIRiB33160.
RefSeqiNP_620806.1. NM_139106.1.
UniGeneiRn.3879.

Genome annotation databases

GeneIDi245965.
KEGGirno:245965.
UCSCiRGD:621372. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00926 mRNA. Translation: AAC28872.1.
PIRiB33160.
RefSeqiNP_620806.1. NM_139106.1.
UniGeneiRn.3879.

3D structure databases

ProteinModelPortaliP35434.
SMRiP35434. Positions 37-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251461. 1 interaction.
IntActiP35434. 2 interactions.
MINTiMINT-4590976.
STRINGi10116.ENSRNOP00000020670.

PTM databases

iPTMnetiP35434.

2D gel databases

UCD-2DPAGEP35434.

Proteomic databases

PaxDbiP35434.
PRIDEiP35434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi245965.
KEGGirno:245965.
UCSCiRGD:621372. rat.

Organism-specific databases

CTDi513.
RGDi621372. Atp5d.

Phylogenomic databases

eggNOGiKOG1758. Eukaryota.
COG0355. LUCA.
HOGENOMiHOG000216023.
HOVERGENiHBG001856.
InParanoidiP35434.
KOiK02134.
PhylomeDBiP35434.

Miscellaneous databases

PROiP35434.

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.
ProtoNetiSearch...

Publicationsi

  1. Pan W., Pedersen P.L.
    Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Dunn M.J.
    Submitted (MAR-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-35.
    Tissue: Heart.
  3. Godinot C.
    Submitted (FEB-1991) to the PIR data bank
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 23-59.
  4. Lubec G., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 137-165, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Hippocampus.
  5. "Identification of two proteins associated with mammalian ATP synthase."
    Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.
    Mol. Cell. Proteomics 6:1690-1699(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.

Entry informationi

Entry nameiATPD_RAT
AccessioniPrimary (citable) accession number: P35434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 131 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.