ATP7_SCHPO
ID ATP7_SCHPO Reviewed; 175 AA.
AC O94390;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP synthase subunit d, mitochondrial;
GN Name=atp7; ORFNames=SPBC29A10.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
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=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase d subunit family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22441.1; -; Genomic_DNA.
DR PIR; T40068; T40068.
DR RefSeq; NP_596058.1; NM_001021969.2.
DR AlphaFoldDB; O94390; -.
DR SMR; O94390; -.
DR BioGRID; 276974; 1.
DR IntAct; O94390; 2.
DR STRING; 4896.SPBC29A10.13.1; -.
DR MaxQB; O94390; -.
DR PaxDb; O94390; -.
DR PRIDE; O94390; -.
DR EnsemblFungi; SPBC29A10.13.1; SPBC29A10.13.1:pep; SPBC29A10.13.
DR GeneID; 2540446; -.
DR KEGG; spo:SPBC29A10.13; -.
DR PomBase; SPBC29A10.13; atp7.
DR VEuPathDB; FungiDB:SPBC29A10.13; -.
DR eggNOG; KOG3366; Eukaryota.
DR HOGENOM; CLU_080463_0_0_1; -.
DR InParanoid; O94390; -.
DR OMA; VSKGRWA; -.
DR PhylomeDB; O94390; -.
DR Reactome; R-SPO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SPO-8949613; Cristae formation.
DR PRO; PR:O94390; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; ISS:PomBase.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; ISS: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; ISS:PomBase.
DR Gene3D; 6.10.280.70; -; 1.
DR InterPro; IPR008689; ATP_synth_F0_dsu_mt.
DR InterPro; IPR036228; ATP_synth_F0_dsu_sf_mt.
DR PANTHER; PTHR12700; PTHR12700; 1.
DR Pfam; PF05873; Mt_ATP-synt_D; 1.
DR PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
DR SUPFAM; SSF161065; SSF161065; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..175
FT /note="ATP synthase subunit d, mitochondrial"
FT /id="PRO_0000071680"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 175 AA; 19138 MW; E50BF489F394A280 CRC64;
MSKVASAAGK AIDWASVASK LKLDAATASA IANFRSRHAQ AVAKLGTLRE QATTVDFATY
RSVLANKEIV NRIESSMKSF KPVKIDLNSQ LKAINAFEAK ASEGAKKNVE LVKAELQNLS
ATLKNIEQAR PTEEITIEDM KQAVPEIEKI VETMVTKGKW VIPGYREKFG DLSIM
