ATPA_XENLA
ID ATPA_XENLA Reviewed; 545 AA.
AC P08428;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit alpha {ECO:0000250|UniProtKB:P25705};
DE Flags: Precursor;
GN Name=atp5f1a {ECO:0000250|UniProtKB:P25705}; Synonyms=an2, atp5a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2953029; DOI=10.1073/pnas.84.9.2798;
RA Weeks D.L., Melton D.A.;
RT "A maternal mRNA localized to the animal pole of Xenopus eggs encodes a
RT subunit of mitochondrial ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2798-2802(1987).
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 inner membrane
CC {ECO:0000250|UniProtKB:P19483}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P19483}; Matrix side
CC {ECO:0000250|UniProtKB:P19483}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; M16259; AAA49646.1; -; mRNA.
DR PIR; A29865; A29865.
DR AlphaFoldDB; P08428; -.
DR SMR; P08428; -.
DR Proteomes; UP000186698; Genome assembly.
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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 2: Evidence at transcript level;
KW ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..545
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000002428"
FT BINDING 214..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19483"
FT BINDING 465..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19483"
FT SITE 405
FT /note="Required for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 545 AA; 58983 MW; 672528340639F38D CRC64;
MLSVRVAAAL ARALPRQSGL VSKKALGAAF VATRNIHASG VWPPEKSGTA EVSSILEERI
LGADTTADLE ETGRVLSIGD GIARVYGLRN VQAEEMVEFS SGLKGMSLNL EPDNVGVVGL
ANDKLIKEGD IVKRTGAIVD VPVGDELLGR VVDALGNTID GKGPIGSKTR RRVGLKAPGI
IPRISVREPM QTGIKAVDSL VPIGRGQREL IIGDRQTGKT SIAIDTIINQ KRFNDGTDEK
KKLYCIYVAI GQKRLTDADA MKYTIVVSRT ASDAAPLQYL APYSGCSMGE YFRDNGTHAL
IIYDDLSKQA VAYRQMSLLL RRPPGREAYP GDVFYLHSRL LERAAKMNDH FGGGSLTALP
VIETQAGDVS AYIPTNVISI TDGQIFLETE LFYKGIRPAI NVGLSVSRVG SAAQTRAMKQ
VAGTMKLELA QYREVAAFAQ FGSDLDAATQ QLLNRGVRLT ELLKQGQYVP MAIEEQVTVI
YAGVRGHLDK MEPSKITKFE SAFLAHVKSQ HQELLATIRA DGKISEQADA KLKEIVLNFL
STFEA
