ID   ATPG_SCHPO              Reviewed;         301 AA.
AC   O74754; Q9USC2;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=ATP synthase subunit gamma, mitochondrial;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Flags: Precursor;
GN   Name=atp3; ORFNames=SPBC1734.13;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 27-125.
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).
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(1) domain and the central stalk which is part of the complex rotary
CC       element. The gamma subunit protrudes into the catalytic domain formed
CC       of alpha(3)beta(3). Rotation of the central stalk against the
CC       surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in
CC       three separate catalytic sites on the beta subunits.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA21307.1; -; Genomic_DNA.
DR   EMBL; AB027877; BAA87181.1; -; Genomic_DNA.
DR   PIR; T39660; T39660.
DR   RefSeq; NP_595430.1; NM_001021338.2.
DR   AlphaFoldDB; O74754; -.
DR   SMR; O74754; -.
DR   BioGRID; 276388; 9.
DR   STRING; 4896.SPBC1734.13.1; -.
DR   MaxQB; O74754; -.
DR   PaxDb; O74754; -.
DR   EnsemblFungi; SPBC1734.13.1; SPBC1734.13.1:pep; SPBC1734.13.
DR   GeneID; 2539839; -.
DR   KEGG; spo:SPBC1734.13; -.
DR   PomBase; SPBC1734.13; atp3.
DR   VEuPathDB; FungiDB:SPBC1734.13; -.
DR   eggNOG; KOG1531; Eukaryota.
DR   HOGENOM; CLU_050669_4_1_1; -.
DR   InParanoid; O74754; -.
DR   OMA; MQITSAM; -.
DR   PhylomeDB; O74754; -.
DR   Reactome; R-SPO-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-SPO-8949613; Cristae formation.
DR   PRO; PR:O74754; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR   GO; GO:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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   CDD; cd12151; F1-ATPase_gamma; 1.
DR   InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR   InterPro; IPR000131; ATP_synth_F1_gsu.
DR   InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR   PANTHER; PTHR11693; PTHR11693; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   PRINTS; PR00126; ATPASEGAMMA.
DR   SUPFAM; SSF52943; SSF52943; 1.
DR   TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR   PROSITE; PS00153; ATPASE_GAMMA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..301
FT                   /note="ATP synthase subunit gamma, mitochondrial"
FT                   /id="PRO_0000002690"
SQ   SEQUENCE   301 AA;  33577 MW;  8595039B8E2F2B32 CRC64;
     MLRQTLTQAS RMRPCISVVG FRGFHASSPC EATLKEIEQR LKSIKNIEKI TKTIKTVAQT
     KLTRAQRAME ASNKYYRVSD EVFKEAGTKA PEEGKTLMVA CSSDKGLCGG IHSSISRLIR
     RELHDPKTFE NTSLCILGEK VRTQLLRFCP ESFYLTFAHI GGASPSFEEA LQISSNILEH
     AKDYDRIVLV YNKFASAVSF ETVMKNLYTT KAINESPNLS AYEVSDEVHQ PLMEFAFANA
     IFSAMAEAHC SEMSSRRNAM ENASKSAGDM INKFSIQYNR QRQASITNEL IDIVTGANSL
     A