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Protein

ATP synthase subunit a

Gene

ATP6

Organism
Patiria pectinifera (Starfish) (Asterina pectinifera)
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:ATP6
Encoded oniMitochondrion
OrganismiPatiria pectinifera (Starfish) (Asterina pectinifera)
Taxonomic identifieri7594 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEchinodermataEleutherozoaAsterozoaAsteroideaValvataceaValvatidaAsterinidaePatiria

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
Transmembranei16 – 36HelicalSequence analysisAdd BLAST21
Transmembranei73 – 93HelicalSequence analysisAdd BLAST21
Transmembranei106 – 126HelicalSequence analysisAdd BLAST21
Transmembranei142 – 162HelicalSequence analysisAdd BLAST21
Transmembranei165 – 185HelicalSequence analysisAdd BLAST21
Transmembranei192 – 212HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000820911 – 230ATP synthase subunit aAdd BLAST230

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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ33823
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase A chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.120.220, 1 hit
InterProiView protein in InterPro
IPR000568 ATP_synth_F0_asu
IPR023011 ATP_synth_F0_asu_AS
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
PROSITEiView protein in PROSITE
PS00449 ATPASE_A, 1 hit

Sequencei

Sequence statusi: Complete.

Q33823-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLNLNSIFG QFSPDLVLFI PMTLTAVFLN LSWLSISNPS NWLPSRANLL
60 70 80 90 100
ILSFYQEVLK ILFQQTNPNT APWVSAFTAI FILIFSINVL GLLPYAFTST
110 120 130 140 150
SHISLTYSIG VPLWMSVNIL GFYLAFNSRL GHLVPQGTPS YLIPFMVIIE
160 170 180 190 200
TISLFAQPIA LGLRLAANLT AGHLLIFLLS TAIWTLSSSP SIASITLLIF
210 220 230
FFLFLLEIGV ACIQAYVFTA LVNFYLSQNL
Length:230
Mass (Da):25,506
Last modified:November 1, 1996 - v1
Checksum:i2191DCB090D93601
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16387 Genomic DNA Translation: BAA03884.1
PIRiS70601
RefSeqiNP_008172.1, NC_001627.1

Genome annotation databases

GeneIDi807819

Similar proteinsi

Entry informationi

Entry nameiATP6_PATPE
AccessioniPrimary (citable) accession number: Q33823
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 25, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health