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ATPAM_ARATH
ID   ATPAM_ARATH             Reviewed;         507 AA.
AC   P92549; Q1NZ05; Q8S890;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN   Name=ATPA; Synonyms=ATP1; OrderedLocusNames=AtMg01190;
OS   Arabidopsis thaliana (Mouse-ear cress).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. C24;
RX   PubMed=8988169; DOI=10.1038/ng0197-57;
RA   Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT   "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT   366,924 nucleotides.";
RL   Nat. Genet. 15:57-61(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07698).
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-13, AND SUBCELLULAR LOCATION.
RC   TISSUE=Leaf, and Stem;
RX   PubMed=11743114; DOI=10.1104/pp.010474;
RA   Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT   "Proteomic approach to identify novel mitochondrial proteins in
RT   Arabidopsis.";
RL   Plant Physiol. 127:1694-1710(2001).
RN   [4]
RP   RNA EDITING.
RX   PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA   Giege P., Brennicke A.;
RT   "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT   ORFs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
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.
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 {ECO:0000269|PubMed:11743114,
CC       ECO:0000269|PubMed:14671022}. Mitochondrion inner membrane
CC       {ECO:0000305}. Note=Peripheral membrane protein. {ECO:0000305}.
CC   -!- RNA EDITING: Modified_positions=393 {ECO:0000269|PubMed:10611383}, 431
CC       {ECO:0000269|PubMed:10611383}, 472 {ECO:0000269|PubMed:10611383}, 495
CC       {ECO:0000269|PubMed:10611383};
CC   -!- MISCELLANEOUS: A stretch of 270 kb of the mitochondrial genome is
CC       duplicated within the centromere of chromosome 2 resulting in the
CC       duplication of the gene. The expression of this duplicated gene
CC       (At2g07698) is not demonstrated. It is also probably not RNA edited and
CC       therefore differs in all the positions known to be edited.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM15496.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Y08501; CAA69802.3; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC007729; AAM15496.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_085571.2; NC_001284.2.
DR   AlphaFoldDB; P92549; -.
DR   SMR; P92549; -.
DR   BioGRID; 566531; 6.
DR   IntAct; P92549; 1.
DR   MINT; P92549; -.
DR   STRING; 3702.ATMG01190.1; -.
DR   SWISS-2DPAGE; P92549; -.
DR   PaxDb; P92549; -.
DR   PeptideAtlas; P92549; -.
DR   PRIDE; P92549; -.
DR   ProteomicsDB; 246593; -.
DR   Araport; ATMG01190; -.
DR   eggNOG; KOG1353; Eukaryota.
DR   InParanoid; P92549; -.
DR   OrthoDB; 470054at2759; -.
DR   BioCyc; ARA:ATMG01190-MON; -.
DR   PRO; PR:P92549; -.
DR   Proteomes; UP000006548; Mitochondrion (cv. C24).
DR   ExpressionAtlas; P92549; baseline and differential.
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); IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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   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   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; Reference proteome;
KW   RNA editing; Transport.
FT   CHAIN           1..507
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000144395"
FT   BINDING         171..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            373
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        172
FT                   /note="G -> D (in Ref. 2; AAM15496)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   507 AA;  55045 MW;  1927B3B8E1EFF51E CRC64;
     MELSPRAAEL TNLFESRIRN FYANFQVDEI GRVVSVGDGI AQVYGLNEIQ AGEMVLFANG
     VKGMALNLEN ENVGIVVFGG DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DAMGVPIDGK
     GALSDHEQRR VEVKAPGILE RKSVHEPMQT GLKAVDSLVP IGRGQRELLI GGRQTGKTTI
     AIDTILNQKQ INSRATSESE TMYCVYVAIG QKRSTVGQLI QTLEEANALE YSILVAATAS
     DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
     VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF
     YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSLKLELAQY REVAAFAQFG SDLDAATQAL
     LNRGARLTEV LKQPQYAPLP IEKQILVIYA AVNGFCDRMP LDRISQYEKA ILNSVKPELL
     QALKGGLTNE RKMELDAFLK ERALALI
 
 
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