GenomeNet

Database: UniProt
Entry: G7Q2V2_MACFA
LinkDB: G7Q2V2_MACFA
Original site: G7Q2V2_MACFA 
ID   G7Q2V2_MACFA            Unreviewed;       277 AA.
AC   G7Q2V2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000256|ARBA:ARBA00019294};
DE            EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN   ORFNames=EGM_18829 {ECO:0000313|EMBL:EHH60931.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1] {ECO:0000313|EMBL:EHH60931.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CE-4 {ECO:0000313|EMBL:EHH60931.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
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.
CC       {ECO:0000256|ARBA:ARBA00003086}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001296; EHH60931.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7Q2V2; -.
DR   Proteomes; UP000009130; Chromosome X.
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:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   SUPFAM; SSF47917; C-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   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          58..191
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   277 AA;  30193 MW;  0968EFB766B2F4BB CRC64;
     MNVIKEPDER GPIKTTQFAP VHAEAPEFME MSVEQEILVT DIKVTRSASS LCQDSAAIRQ
     MIEPPGARAQ VTLTGLIVVE YFTDQEGQDV LLFIDKICCF IQARAEVSAL SGGIHSAVGY
     QPTLTTDMST MQEIITTTKK GSITSVQAIY VPADDLTDPA SATTFAHLDV LSQVIAELGI
     CPAVDPLDST SCIIDPNIVG DEHYDVAHGV QKIPQDYKSL QGLIAILGMD ELSQDDKLTM
     SCAQKIRCYL SQPFQVVEVF TGHMRKLVPL KDTIKGF
//
DBGET integrated database retrieval system