ID   ATPG3_SPIOL             Reviewed;          26 AA.
AC   P80084;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   07-OCT-2020, entry version 80.
DE   RecName: Full=ATP synthase subunit gamma, mitochondrial;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Flags: Fragment;
GN   Name=ATPC;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Medania; TISSUE=Leaf mesophyll;
RX   PubMed=1313368; DOI=10.1111/j.1432-1033.1992.tb16794.x;
RA   Hamasur B., Glaser E.;
RT   "Plant mitochondrial F0F1 ATP synthase. Identification of the individual
RT   subunits and properties of the purified spinach leaf mitochondrial ATP
RT   synthase.";
RL   Eur. J. Biochem. 205:409-416(1992).
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane;
CC       Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR   PIR; S21243; S21243.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR   SUPFAM; SSF52943; SSF52943; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transport.
FT   CHAIN           1..>26
FT                   /note="ATP synthase subunit gamma, mitochondrial"
FT                   /id="PRO_0000073429"
FT   NON_TER         26
SQ   SEQUENCE   26 AA;  2941 MW;  94CCC3A74C67DC0B CRC64;
     IGTQIVXNXM KSIKNIQKIT KAMKMV