ATP3

ATP synthase subunit gamma, mitochondrial

311 amino acids

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. F-type ATPases 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. 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. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Belongs to the ATPase gamma chain family.

34.351 kDa

MLSRIVSNNATRSVMCHQAQVGILYKTNPVRTYATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKISAKKMDEAEQLFYKNAETKNLDVEATETGAPKELIVAITSDKGLCGSIHSQLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSINGIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDPVSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDLFEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRYSILYNRTRQAVITNELVDIITGASSLG

atp3

ATP synthase subunit gamma, mitochondrial

301 amino acids

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. F-type ATPases 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. 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. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Belongs to the ATPase gamma chain family.

33.577 kDa

MLRQTLTQASRMRPCISVVGFRGFHASSPCEATLKEIEQRLKSIKNIEKITKTIKTVAQTKLTRAQRAMEASNKYYRVSDEVFKEAGTKAPEEGKTLMVACSSDKGLCGGIHSSISRLIRRELHDPKTFENTSLCILGEKVRTQLLRFCPESFYLTFAHIGGASPSFEEALQISSNILEHAKDYDRIVLVYNKFASAVSFETVMKNLYTTKAINESPNLSAYEVSDEVHQPLMEFAFANAIFSAMAEAHCSEMSSRRNAMENASKSAGDMINKFSIQYNRQRQASITNELIDIVTGANSLA

ATP3

ATP synthase subunit gamma, mitochondrial

293 amino acids

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).

Belongs to the ATPase gamma chain family.

32.337 kDa

MFALRTAARPAARSVGATRNYATLREIEMRLKSIKNIEKITNTMKIVASTKLGKAQRAMATSKVYNEASEKVFENSETAVPENIEKRLWVVVSSDKGLCGSIHSQLARTVRRKLLDFESGEKLIDIVAVGEKIKAQLGRSNPEQMRLSFGGTGKEAPTFEEAAHIADEILALDTQYDDIEIVYNKVLSGISFEPIMKESYSAKAIEDAPKFGQYELEDDVVKNLADFSLANTIYAAMAEGHAAEISARRNAMDNASKNASDMINKYSILYNRTRQAVITNELVDIITGASSLE

ATP3

ATP synthase subunit gamma, mitochondrial

289 amino acids

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. F-type ATPases 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. 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. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Belongs to the ATPase gamma chain family.

31.591 kDa

MFVRNTASVVRGTSRNYATLREIETRLKSIKNIEKITKTMKIVASTRLSKAERAKNSAKEYALADAAFYKNAETVPLEDAEKKDLIIAITSDKGLCGSIHSQLAKAVRLQLKQTPNADVVAIGDKVKGQLLRTNSDNLKFAFNGVGKEAPTFEETSLIANKILEGGASNYKKVSIFWNDPISSLSFEPSNKPVFNAAAIEQSPSFSKFEIDADNNVSQDLFEFTLSNEILAAMAEGYAAEVSARRNAMDNASKNAGDMINSYSILYNRTRQAVITNELVDIITGASSLD

ATP3

ATP synthase subunit gamma, mitochondrial

269 amino acids

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:27791192). 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 (By similarity). Part of the complex F(1) domain and the central stalk which is part of the complex rotary element (By similarity). The gamma/ATP3 subunit protrudes into the catalytic domain formed of alpha/ATP1(3)beta/ATP2(3) (By similarity). 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 (By similarity).

Belongs to the ATPase gamma chain family.

29.385 kDa

ATLREIETRLKSIKNIEKITNTMKVVASTRMGRAQRAMASSRAFREGDSDFFATAETSTPETAEKTLIIAVSSDKGLCGSIHSQIAKATRAKLQETPNADVVTIGDKIKAQMLRTHSSNVVLSFNGVGKEAPTFWEASLIADEIRKLGDYDKIEVMYNKFVSGVAFEPSVFPSFSPISIEESPKLSEFELEEDQAIPTSLSQISLTNAILNAMAEGYASEISARRNAMDNASKNAGEMINKYSILYNRTRQAVITNELVDIITGASSLD