ID   ATPAM_SPIOL             Reviewed;          25 AA.
AC   P80082;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
DE   Flags: Fragment;
GN   Name=ATPA;
OS   Spinacia oleracea (Spinach).
OG   Mitochondrion.
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. Subunits alpha and
CC       beta form the catalytic core in F(1). Rotation of the central stalk
CC       against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC       ATP in three separate catalytic sites on the beta subunits. Subunit
CC       alpha does not bear the catalytic high-affinity ATP-binding sites (By
CC       similarity). {ECO:0000250}.
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       Note=Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   PIR; S21204; S21204.
DR   AlphaFoldDB; P80082; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Transport.
FT   CHAIN           1..>25
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000144409"
FT   NON_TER         25
SQ   SEQUENCE   25 AA;  2904 MW;  1B1486EBBD1A650D CRC64;
     MEFSPRAAEL TTLLESRISN FYTNI