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Protein

ATP synthase subunit a

Gene

MT-ATP6

Organism
Pelomedusa subrufa (African side-necked turtle)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit a
Alternative name(s):
F-ATPase protein 6
Gene namesi
Name:MT-ATP6
Synonyms:ATP6, ATPASE6, MTATP6
Encoded oniMitochondrion
OrganismiPelomedusa subrufa (African side-necked turtle)
Taxonomic identifieri44522 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaTestudinesPleurodiraPelomedusidaePelomedusa

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei13 – 33HelicalSequence analysisAdd BLAST21
Transmembranei69 – 89HelicalSequence analysisAdd BLAST21
Transmembranei98 – 118HelicalSequence analysisAdd BLAST21
Transmembranei139 – 159HelicalSequence analysisAdd BLAST21
Transmembranei194 – 214HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000821511 – 228ATP synthase subunit aAdd BLAST228

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.

Structurei

3D structure databases

ProteinModelPortaliO79675
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase A chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG016693

Family and domain databases

Gene3Di1.20.120.220, 1 hit
InterProiView protein in InterPro
IPR000568 ATP_synth_F0_asu
IPR035908 F0_ATP_A_sf
PfamiView protein in Pfam
PF00119 ATP-synt_A, 1 hit
PRINTSiPR00123 ATPASEA
SUPFAMiSSF81336 SSF81336, 1 hit
TIGRFAMsiTIGR01131 ATP_synt_6_or_A, 1 hit

Sequencei

Sequence statusi: Complete.

O79675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLTLFDQFS SPNILAIPLM TISLLMLTII FPMKHNRLLT NRLLSIQSKM
60 70 80 90 100
IHIFTKQLML PIPKSGHHWA LILTSLMTLL LTSNLLGLLP YTFTPTTQLS
110 120 130 140 150
MNLGFALPMW LATLLIGLRN QPTMSLAHLL PEGTPTPLIP TLILIESISL
160 170 180 190 200
MIRPLALGVR ISANLTAGHL LMQLTSSATL SLSSMPTLSF MTAILLFLLT
210 220
ILEMAVAMIQ ALVFVLLLSL YLQENTHN
Length:228
Mass (Da):25,250
Last modified:November 1, 1998 - v1
Checksum:iD483209845A7DDEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039066 Genomic DNA Translation: AAD05055.1
PIRiT11106
RefSeqiNP_008437.1, NC_001947.1

Genome annotation databases

GeneIDi808286

Similar proteinsi

Entry informationi

Entry nameiATP6_PELSU
AccessioniPrimary (citable) accession number: O79675
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: April 25, 2018
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health