Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP synthase subunit d, mitochondrial

Gene

ATP5H

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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 synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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 d, mitochondrial
Short name:
ATPase subunit d
Gene namesi
Name:ATP5H
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 161160ATP synthase subunit d, mitochondrialPRO_0000071672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei85 – 851N6-acetyllysineBy similarity
Modified residuei95 – 951N6-acetyllysineBy similarity
Modified residuei117 – 1171N6-acetyllysineBy similarity
Modified residuei149 – 1491N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP13620.
PeptideAtlasiP13620.
PRIDEiP13620.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. 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-39020N.
IntActiP13620. 2 interactions.
MINTiMINT-5006994.
STRINGi9913.ENSBTAP00000028282.

Structurei

Secondary structure

1
161
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 175Combined sources
Helixi22 – 243Combined sources
Helixi25 – 4420Combined sources
Helixi54 – 596Combined sources
Helixi66 – 749Combined sources
Helixi89 – 9911Combined sources
Helixi101 – 12222Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLYX-ray2.80B/E2-161[»]
2WSSX-ray3.20U2-119[»]
4B2Qelectron microscopy37.00U/u5-124[»]
5ARAelectron microscopy6.70U2-125[»]
5AREelectron microscopy7.40U2-125[»]
5ARHelectron microscopy7.20U2-125[»]
5ARIelectron microscopy7.40U2-125[»]
5FIJelectron microscopy7.40U2-125[»]
5FIKelectron microscopy6.40U2-125[»]
5FILelectron microscopy7.10U2-125[»]
ProteinModelPortaliP13620.
SMRiP13620. Positions 4-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13620.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase d subunit family.Curated

Phylogenomic databases

eggNOGiKOG3366. Eukaryota.
ENOG4111IHJ. LUCA.
GeneTreeiENSGT00390000003582.
HOGENOMiHOG000267023.
HOVERGENiHBG050612.
InParanoidiP13620.
KOiK02138.
OMAiKVKYPYW.
OrthoDBiEOG7673CC.
TreeFamiTF314031.

Family and domain databases

InterProiIPR008689. ATPase_F0-cplx_dsu_mt.
[Graphical view]
PANTHERiPTHR12700. PTHR12700. 1 hit.
PIRSFiPIRSF005514. ATPase_F0_D_mt. 1 hit.
SUPFAMiSSF161065. SSF161065. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P13620-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRKLALKT IDWVAFGEII PRNQKAVANS LKSWNETLTS RLATLPEKPP
60 70 80 90 100
AIDWAYYKAN VAKAGLVDDF EKKFNALKVP IPEDKYTAQV DAEEKEDVKS
110 120 130 140 150
CAEFLTQSKT RIQEYEKELE KMRNIIPFDQ MTIEDLNEVF PETKLDKKKY
160
PYWPHRPIET L
Length:161
Mass (Da):18,692
Last modified:January 23, 2007 - v2
Checksum:i60ED98258E57C7E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06089 mRNA. Translation: CAA29473.1.
BC104564 mRNA. Translation: AAI04565.1.
PIRiS00764.
RefSeqiNP_777149.1. NM_174724.4.
UniGeneiBt.5029.

Genome annotation databases

EnsembliENSBTAT00000028282; ENSBTAP00000028282; ENSBTAG00000021227.
GeneIDi282710.
KEGGibta:282710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06089 mRNA. Translation: CAA29473.1.
BC104564 mRNA. Translation: AAI04565.1.
PIRiS00764.
RefSeqiNP_777149.1. NM_174724.4.
UniGeneiBt.5029.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLYX-ray2.80B/E2-161[»]
2WSSX-ray3.20U2-119[»]
4B2Qelectron microscopy37.00U/u5-124[»]
5ARAelectron microscopy6.70U2-125[»]
5AREelectron microscopy7.40U2-125[»]
5ARHelectron microscopy7.20U2-125[»]
5ARIelectron microscopy7.40U2-125[»]
5FIJelectron microscopy7.40U2-125[»]
5FIKelectron microscopy6.40U2-125[»]
5FILelectron microscopy7.10U2-125[»]
ProteinModelPortaliP13620.
SMRiP13620. Positions 4-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39020N.
IntActiP13620. 2 interactions.
MINTiMINT-5006994.
STRINGi9913.ENSBTAP00000028282.

Proteomic databases

PaxDbiP13620.
PeptideAtlasiP13620.
PRIDEiP13620.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000028282; ENSBTAP00000028282; ENSBTAG00000021227.
GeneIDi282710.
KEGGibta:282710.

Organism-specific databases

CTDi10476.

Phylogenomic databases

eggNOGiKOG3366. Eukaryota.
ENOG4111IHJ. LUCA.
GeneTreeiENSGT00390000003582.
HOGENOMiHOG000267023.
HOVERGENiHBG050612.
InParanoidiP13620.
KOiK02138.
OMAiKVKYPYW.
OrthoDBiEOG7673CC.
TreeFamiTF314031.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP13620.

Family and domain databases

InterProiIPR008689. ATPase_F0-cplx_dsu_mt.
[Graphical view]
PANTHERiPTHR12700. PTHR12700. 1 hit.
PIRSFiPIRSF005514. ATPase_F0_D_mt. 1 hit.
SUPFAMiSSF161065. SSF161065. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ATP synthase from bovine mitochondria. The characterization and sequence analysis of two membrane-associated sub-units and of the corresponding cDNAs."
    Walker J.E., Runswick M.J., Poulter L.
    J. Mol. Biol. 197:89-100(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT ALA-2, PROTEIN SEQUENCE OF 2-161.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.
  3. "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.

Entry informationi

Entry nameiATP5H_BOVIN
AccessioniPrimary (citable) accession number: P13620
Secondary accession number(s): Q3SX10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 112 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.