ID A0A097RN11_CYNSE Unreviewed; 551 AA.
AC A0A097RN11;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|EMBL:AIU80157.1};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000001672.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|EMBL:AIU80157.1}
RP NUCLEOTIDE SEQUENCE.
RA Feng W., Ma Q., Liu S., Zhuang Z., Tang Q.;
RT "Quantitative change of mitochondrial DNA content in different tissues of
RT Cynoglossus semilaevis.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCSEP00000001672.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003551}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU000339}.
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DR EMBL; KJ813813; AIU80157.1; -; mRNA.
DR RefSeq; NP_001306746.1; NM_001319817.1.
DR Ensembl; ENSCSET00000001703.1; ENSCSEP00000001672.1; ENSCSEG00000001126.1.
DR GeneID; 103390430; -.
DR KEGG; csem:103390430; -.
DR CTD; 553755; -.
DR GeneTree; ENSGT00550000074846; -.
DR OMA; QDKCDSS; -.
DR OrthoDB; 1102723at2759; -.
DR Proteomes; UP000265120; Chromosome 14.
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; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_nt-bd_dom.
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 NCBIfam; TIGR00962; atpA; 1.
DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 2: Evidence at transcript level;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003551};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003551};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003551};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU000339};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000339}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003551};
KW Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT DOMAIN 68..134
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 191..414
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 421..545
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
SQ SEQUENCE 551 AA; 59822 MW; ACA988BD930BAD19 CRC64;
MLSVRVASTL VRTLPRRAGF VSKNVAAACV GVKNLHTSRP WLQKTGTAEV SSILEEKIMG
ADTSAELEET GRVLSIGDGI ARVYGLRNVQ AEEMVEFSSG LKGMSLNLEP DNVGVVVFGN
DKLIKEGDIV KRTGAIVDVP VGEELLGRVV DALGNAIDGK GPLGSSIRRR VGLKAPGIIP
RISVREPMQT GIKAVDSLVP IGRGQRELII GDRQTGKTAI AIDTIINQKR FNEGTDEKKK
LYCIYVAIGQ KRSTVAQLVK RLTDTDAMKY TIVVSATASD AAPLQYLAPY AGCSMGEYFR
DNGKHALIIY DDLSKHAVAY RQMSLLLRRP PGREAYPGDV FYLHSRLLER AAKMNDNFGG
GSLTALPVIE TQAGDVSAYI PTNVISITDG QIFLETELFY KGIRPAINVG LSVSRVGSAA
QTRAMKQVAG TMKLELAQYR EVAAFAQFGS DLDAATQQLL NRGVRLTELL KQGQYAPMAI
EEQVTVIYAG VRGYLDKMEP SKITKFEKAF LQHILSQQQD LLAAIKADGK ISEASDAKLK
QVVLNFLSSF E
//
