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Protein

ATP synthase subunit a

Gene

Mtatp6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_287909. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit a
Alternative name(s):
F-ATPase protein 6
Gene namesi
Name:Mtatp6
Synonyms:Atp6, Atpase6, mt-Atp6
Encoded oniMitochondrion
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Mitochondrion

Organism-specific databases

MGIiMGI:99927. mt-Atp6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei6 – 2621HelicalSequence AnalysisAdd
BLAST
Transmembranei68 – 8821HelicalSequence AnalysisAdd
BLAST
Transmembranei97 – 11721HelicalSequence AnalysisAdd
BLAST
Transmembranei138 – 15821HelicalSequence AnalysisAdd
BLAST
Transmembranei164 – 18421HelicalSequence AnalysisAdd
BLAST
Transmembranei189 – 20921HelicalSequence AnalysisAdd
BLAST

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
Chaini1 – 226226ATP synthase subunit aPRO_0000082139Add
BLAST

Proteomic databases

MaxQBiP00848.
PaxDbiP00848.
PRIDEiP00848.

Expressioni

Gene expression databases

BgeeiP00848.
ExpressionAtlasiP00848. baseline and differential.

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 has three main subunits: a, b and c. 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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000080996.

Structurei

3D structure databases

ProteinModelPortaliP00848.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase A chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0356.
GeneTreeiENSGT00390000005568.
HOGENOMiHOG000034185.
HOVERGENiHBG016693.
InParanoidiP00848.
KOiK02126.
OMAiTAGHLLM.
OrthoDBiEOG769ZND.
PhylomeDBiP00848.
TreeFamiTF343395.

Family and domain databases

Gene3Di1.20.120.220. 1 hit.
InterProiIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERiPTHR11410. PTHR11410. 1 hit.
PfamiPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSiPR00123. ATPASEA.
SUPFAMiSSF81336. SSF81336. 1 hit.
TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEiPS00449. ATPASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00848-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNENLFASFI TPTMMGFPIV VAIIMFPSIL FPSSKRLINN RLHSFQHWLV
60 70 80 90 100
KLIIKQMMLI HTPKGRTWTL MIVSLIMFIG STNLLGLLPH TFTPTTQLSM
110 120 130 140 150
NLSMAIPLWA GAVITGFRHK LKSSLAHFLP QGTPISLIPM LIIIETISLF
160 170 180 190 200
IQPMALAVRL TANITAGHLL MHLIGGATLV LMNISPPTAT ITFIILLLLT
210 220
ILEFAVALIQ AYVFTLLVSL YLHDNT
Length:226
Mass (Da):25,096
Last modified:July 21, 1986 - v1
Checksum:i9941E80F027C4DA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01420 Genomic DNA. Translation: AAB48649.1.
V00711 Genomic DNA. Translation: CAA24085.1.
AF093677 mRNA. Translation: AAC63375.1.
AY172335 Genomic DNA. Translation: AAN85127.1.
PIRiA01051. PWMS6.
RefSeqiNP_904333.1. NC_005089.1.

Genome annotation databases

EnsembliENSMUST00000082408; ENSMUSP00000080996; ENSMUSG00000064357.
GeneIDi17705.
KEGGimmu:17705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01420 Genomic DNA. Translation: AAB48649.1.
V00711 Genomic DNA. Translation: CAA24085.1.
AF093677 mRNA. Translation: AAC63375.1.
AY172335 Genomic DNA. Translation: AAN85127.1.
PIRiA01051. PWMS6.
RefSeqiNP_904333.1. NC_005089.1.

3D structure databases

ProteinModelPortaliP00848.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000080996.

Proteomic databases

MaxQBiP00848.
PaxDbiP00848.
PRIDEiP00848.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000082408; ENSMUSP00000080996; ENSMUSG00000064357.
GeneIDi17705.
KEGGimmu:17705.

Organism-specific databases

CTDi4508.
MGIiMGI:99927. mt-Atp6.

Phylogenomic databases

eggNOGiCOG0356.
GeneTreeiENSGT00390000005568.
HOGENOMiHOG000034185.
HOVERGENiHBG016693.
InParanoidiP00848.
KOiK02126.
OMAiTAGHLLM.
OrthoDBiEOG769ZND.
PhylomeDBiP00848.
TreeFamiTF343395.

Enzyme and pathway databases

ReactomeiREACT_287909. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

NextBioi292306.
PROiP00848.
SOURCEiSearch...

Gene expression databases

BgeeiP00848.
ExpressionAtlasiP00848. baseline and differential.

Family and domain databases

Gene3Di1.20.120.220. 1 hit.
InterProiIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERiPTHR11410. PTHR11410. 1 hit.
PfamiPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSiPR00123. ATPASEA.
SUPFAMiSSF81336. SSF81336. 1 hit.
TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEiPS00449. ATPASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and gene organization of mouse mitochondrial DNA."
    Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.
    Cell 26:167-180(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Sato M., Matsuki Y., Oguma T., Tadakuma T.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiATP6_MOUSE
AccessioniPrimary (citable) accession number: P00848
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.