UniProt functional annotation for Q6C338



	UniProt functional annotation for Q6C338

UniProt code: Q6C338.

Organism: Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.

Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27373333). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (PubMed:27373333). Part of the complex F(1) domain and the central stalk which is part of the complex rotary element (PubMed:27373333). The gamma/ATP3 subunit protrudes into the catalytic domain formed of alpha/ATP1(3)beta/ATP2(3) (PubMed:27373333). Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits (PubMed:27373333). {ECO:0000269|PubMed:25759169, ECO:0000269|PubMed:27373333}.

Subunit: F-type ATP synthases have 2 components, the catalytic core F(1) and the membrane-embedded component F(0), linked together by a central stalk and a peripheral stalk (PubMed:27373333). The central stalk, also called rotor shaft, is often seen as part of F(1) (PubMed:27373333). The peripheral stalk is seen as part of F(0) (PubMed:27373333). F(0) contains the membrane channel next to the rotor (PubMed:27373333). F-type ATP synthases form dimers but each monomer functions independently in ATP generation (PubMed:27373333). The dimer consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer, part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4 (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP, part of the peripheral stalk), ATP6 (subunit a, part of the peripheral stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit 8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor, 10 molecules per monomer), ATP14 (subunit h, part of the peripheral stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16 (subunit delta, part of the central stalk), ATP17 (subunit f, part of the peripheral stalk), ATP18 (subunit i/j, part of the peripheral stalk), ATP19 (subunit k, dimer-specific, at interface between monomers), ATP20 (subunit g, at interface between monomers), TIM11 (subunit e, at interface between monomers) (PubMed:27373333, PubMed:25759169). {ECO:0000269|PubMed:25759169, ECO:0000269|PubMed:27373333}.

Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:27373333}; Peripheral membrane protein {ECO:0000305|PubMed:27373333}; Matrix side {ECO:0000305|PubMed:27373333}. Note=The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix. {ECO:0000305|PubMed:27373333}.

Mass spectrometry: Mass=30077.2; Method=MALDI; Evidence={ECO:0000269|PubMed:25759169};

Similarity: Belongs to the ATPase gamma chain family. {ECO:0000255|RuleBase:RU004001}.

Annotations taken from UniProtKB at the EBI.


Organism:		Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.



Function:		Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27373333). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (PubMed:27373333). Part of the complex F(1) domain and the central stalk which is part of the complex rotary element (PubMed:27373333). The gamma/ATP3 subunit protrudes into the catalytic domain formed of alpha/ATP1(3)beta/ATP2(3) (PubMed:27373333). Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits (PubMed:27373333). {ECO:0000269\|PubMed:25759169, ECO:0000269\|PubMed:27373333}.


Subunit:		F-type ATP synthases have 2 components, the catalytic core F(1) and the membrane-embedded component F(0), linked together by a central stalk and a peripheral stalk (PubMed:27373333). The central stalk, also called rotor shaft, is often seen as part of F(1) (PubMed:27373333). The peripheral stalk is seen as part of F(0) (PubMed:27373333). F(0) contains the membrane channel next to the rotor (PubMed:27373333). F-type ATP synthases form dimers but each monomer functions independently in ATP generation (PubMed:27373333). The dimer consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer, part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4 (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP, part of the peripheral stalk), ATP6 (subunit a, part of the peripheral stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit 8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor, 10 molecules per monomer), ATP14 (subunit h, part of the peripheral stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16 (subunit delta, part of the central stalk), ATP17 (subunit f, part of the peripheral stalk), ATP18 (subunit i/j, part of the peripheral stalk), ATP19 (subunit k, dimer-specific, at interface between monomers), ATP20 (subunit g, at interface between monomers), TIM11 (subunit e, at interface between monomers) (PubMed:27373333, PubMed:25759169). {ECO:0000269\|PubMed:25759169, ECO:0000269\|PubMed:27373333}.
Subcellular location:		Mitochondrion inner membrane {ECO:0000305\|PubMed:27373333}; Peripheral membrane protein {ECO:0000305\|PubMed:27373333}; Matrix side {ECO:0000305\|PubMed:27373333}. Note=The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix. {ECO:0000305\|PubMed:27373333}.
Mass spectrometry:		Mass=30077.2; Method=MALDI; Evidence={ECO:0000269\|PubMed:25759169};
Similarity:		Belongs to the ATPase gamma chain family. {ECO:0000255\|RuleBase:RU004001}.