ATPF_YARLI
ID ATPF_YARLI Reviewed; 217 AA.
AC Q6C105;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ATP synthase subunit 4, mitochondrial {ECO:0000250|UniProtKB:P05626};
DE AltName: Full=ATP synthase subunit b {ECO:0000303|PubMed:25759169};
DE Flags: Precursor;
GN Name=ATP4 {ECO:0000250|UniProtKB:P05626};
GN OrderedLocusNames=YALI0_F20306g {ECO:0000312|EMBL:CAG78466.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000312|Proteomes:UP000001300};
RN [1] {ECO:0000312|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2] {ECO:0000305}
RP IDENTIFICATION IN ATP SYNTHASE COMPLEX, FUNCTION OF ATP SYNTHASE COMPLEX,
RP SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=CLIB 122 / E 150 {ECO:0000303|PubMed:25759169};
RX PubMed=25759169; DOI=10.1042/bj20150197;
RA Liu S., Charlesworth T.J., Bason J.V., Montgomery M.G., Harbour M.E.,
RA Fearnley I.M., Walker J.E.;
RT "The purification and characterization of ATP synthase complexes from the
RT mitochondria of four fungal species.";
RL Biochem. J. 468:167-175(2015).
RN [3] {ECO:0000305}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.7 ANGSTROMS) OF DIMERIC ATP SYNTHASE
RP COMPLEX, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27373333; DOI=10.1016/j.molcel.2016.05.037;
RA Hahn A., Parey K., Bublitz M., Mills D.J., Zickermann V., Vonck J.,
RA Kuehlbrandt W., Meier T.;
RT "Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of
RT Inner Mitochondrial Membrane Morphology.";
RL Mol. Cell 63:445-456(2016).
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 (PubMed:25759169). F-type ATP synthases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a peripheral
CC stalk (PubMed:27373333). During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation (PubMed:27373333). Part
CC of the complex F(0) domain and the peripheral stalk, which acts as a
CC stator to hold the catalytic alpha/ATP1(3)beta/ATP2(3) subcomplex and
CC subunit a/ATP6 static relative to the rotary elements
CC (PubMed:27373333). {ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27373333}.
CC -!- SUBUNIT: F-type ATP synthases have 2 components, the catalytic core
CC F(1) and the membrane-embedded component F(0), linked together by a
CC central stalk and a peripheral stalk (PubMed:27373333). The central
CC stalk, also called rotor shaft, is often seen as part of F(1)
CC (PubMed:27373333). The peripheral stalk is seen as part of F(0)
CC (PubMed:27373333). F(0) contains the membrane channel next to the rotor
CC (PubMed:27373333). F-type ATP synthases form dimers but each monomer
CC functions independently in ATP generation (PubMed:27373333). The dimer
CC consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules
CC per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer,
CC part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4
CC (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP,
CC part of the peripheral stalk), ATP6 (subunit a, part of the peripheral
CC stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit
CC 8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor,
CC 10 molecules per monomer), ATP14 (subunit h, part of the peripheral
CC stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16
CC (subunit delta, part of the central stalk), ATP17 (subunit f, part of
CC the peripheral stalk), ATP18 (subunit i/j, part of the peripheral
CC stalk), ATP19 (subunit k, dimer-specific, at interface between
CC monomers), ATP20 (subunit g, at interface between monomers), TIM11
CC (subunit e, at interface between monomers) (PubMed:27373333,
CC PubMed:25759169). {ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27373333}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:27373333}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:27373333}. Note=The F-type ATP synthase complex is
CC anchored in the mitochondrial inner membrane via the F(0) domain with
CC the F(1) domain and the peripheral stalk extending into the
CC mitochondrial matrix. {ECO:0000305|PubMed:27373333}.
CC -!- MASS SPECTROMETRY: Mass=22444.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25759169};
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC {ECO:0000305}.
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DR EMBL; CR382132; CAG78466.1; -; Genomic_DNA.
DR RefSeq; XP_505657.1; XM_505657.1.
DR AlphaFoldDB; Q6C105; -.
DR SMR; Q6C105; -.
DR STRING; 4952.CAG78466; -.
DR EnsemblFungi; CAG78466; CAG78466; YALI0_F20306g.
DR GeneID; 2907796; -.
DR KEGG; yli:YALI0F20306g; -.
DR VEuPathDB; FungiDB:YALI0_F20306g; -.
DR HOGENOM; CLU_077208_0_0_1; -.
DR InParanoid; Q6C105; -.
DR OMA; IYAISNE; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IEA:EnsemblFungi.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR InterPro; IPR013837; ATP_synth_F0_suB.
DR PANTHER; PTHR12733; PTHR12733; 1.
DR Pfam; PF05405; Mt_ATP-synt_B; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25759169"
FT CHAIN 15..217
FT /note="ATP synthase subunit 4, mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445316"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 217 AA; 24003 MW; B8134F223E1F0EE1 CRC64;
MPFARVGALS ARHYSNQVDP KVKATSILDS IPGNNVLSKT GVLATGVLGS IYAISNELYI
VNDESIVLGV FAAFVVVVAK LGGPGYTSWA DGYIENMRNI LNTTRDKHTD AVKERIGDVS
KLKDVVKTTQ DLFAVSKDTV KLEAEVFETK QQVVLAAEAK SVLDSWVRYE NSVRQREQKL
LTETVISKIE KDLKDPKFQQ KILQQSVEDI EKLFAKA
