ATP6_SCHPO
ID ATP6_SCHPO Reviewed; 257 AA.
AC P21535; Q9UU41;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
DE Flags: Precursor;
GN Name=atp6; ORFNames=SPMIT.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD7-50;
RA Lang B.F.;
RT "The mitochondrial genome of Schizosaccharomyces pombe.";
RL (In) O'Brien S.J. (eds.);
RL Genetic Maps (6th edition), pp.3118-3119, Cold Spring Harbor Laboratory
RL Press, New York (1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-54.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-257.
RC STRAIN=EF1;
RX PubMed=2243789; DOI=10.1093/nar/18.21.6429;
RA Massardo D.R.;
RT "Nucleotide sequence of the genes encoding tRNA(his), tRNA(pro) and
RT tRNA(gln) in the mitochondrial genome of Schizosaccharomyces pombe strain
RT EF1.";
RL Nucleic Acids Res. 18:6429-6429(1990).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR EMBL; X54421; CAA38289.1; -; Genomic_DNA.
DR EMBL; AB027826; BAA87130.1; -; Genomic_DNA.
DR EMBL; X54552; CAA38422.1; -; Genomic_DNA.
DR PIR; S12171; S12171.
DR PIR; S78200; S78200.
DR RefSeq; NP_039504.1; NC_001326.1.
DR AlphaFoldDB; P21535; -.
DR SMR; P21535; -.
DR STRING; 4896.SPMIT.07.1; -.
DR SwissPalm; P21535; -.
DR MaxQB; P21535; -.
DR PaxDb; P21535; -.
DR EnsemblFungi; SPMIT.07.1; SPMIT.07.1:pep; SPMIT.07.
DR GeneID; 1669530; -.
DR KEGG; spo:ScpofMp06; -.
DR PomBase; SPMIT.07; atp6.
DR VEuPathDB; FungiDB:SPMIT.07; -.
DR eggNOG; KOG4665; Eukaryota.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; P21535; -.
DR OMA; FFDQFMS; -.
DR PhylomeDB; P21535; -.
DR Reactome; R-SPO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SPO-8949613; Cristae formation.
DR PRO; PR:P21535; -.
DR Proteomes; UP000002485; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:PomBase.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; ISO:PomBase.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:PomBase.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..4
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002620"
FT CHAIN 5..257
FT /note="ATP synthase subunit a"
FT /id="PRO_0000002621"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 257 AA; 28294 MW; 4BADCC0CBDCB4E0F CRC64;
MFITSPLEQF ELNNYFGFYL FNYHFDFSNF GFYLGLSALI AISLAIINLT PYGSGAKIVP
QKFGIAMEAI YFTMLNLVEN QIHSSKTVSG QSYFPFIWSL FVLILFSNLL RLIPYGYATT
AQLIFTLGLS ISILIGATIL GLQQHKAKVF GLFLPSGTPT PLIPLLVLIE FVSYIARGLS
LGIRLGANII AGHLTMSILG GLIFTFMGLN LITFIIGFLP ITVLVAISLL EFGIAFIQAY
VFAILTCGFI NDSLNLH
