The human ATP5F1Cgene encodes the gamma subunit of an
enzyme called mitochondrial ATP synthase.[5][6][7]
This gene encodes a subunit of
mitochondrialATP synthase. Mitochondrial ATP synthase catalyzes
adenosine triphosphate (ATP) synthesis, utilizing an
electrochemical gradient of protons across the inner membrane during
oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising the
proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a
stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the gamma subunit of the catalytic core. Alternatively
splicedtranscript variants encoding different
isoforms have been identified. This gene also has a
pseudogene on
chromosome 14.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Jabs EW, Thomas PJ, Bernstein M, Coss C, Ferreira GC, Pedersen PL (Jun 1994). "Chromosomal localization of genes required for the terminal steps of oxidative metabolism: alpha and gamma subunits of ATP synthase and the phosphate carrier". Hum Genet. 93 (5): 600–2.
doi:
10.1007/bf00202832.
PMID8168843.
S2CID39597611.
Overview of all the structural information available in the
PDB for
UniProt: Q91VR2 (ATP synthase subunit gamma, mitochondrial) at the
PDBe-KB.
Further reading
Yoshida M, Muneyuki E, Hisabori T (2001). "ATP synthase--a marvellous rotary engine of the cell". Nat. Rev. Mol. Cell Biol. 2 (9): 669–77.
doi:
10.1038/35089509.
PMID11533724.
S2CID3926411.
Itoh H, Takahashi A, Adachi K, Noji H, Yasuda R, Yoshida M, et al. (2004). "Mechanically driven ATP synthesis by F1-ATPase". Nature. 427 (6973): 465–8.
doi:
10.1038/nature02212.
PMID14749837.
S2CID4428646.
The human ATP5F1Cgene encodes the gamma subunit of an
enzyme called mitochondrial ATP synthase.[5][6][7]
This gene encodes a subunit of
mitochondrialATP synthase. Mitochondrial ATP synthase catalyzes
adenosine triphosphate (ATP) synthesis, utilizing an
electrochemical gradient of protons across the inner membrane during
oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising the
proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a
stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the gamma subunit of the catalytic core. Alternatively
splicedtranscript variants encoding different
isoforms have been identified. This gene also has a
pseudogene on
chromosome 14.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Jabs EW, Thomas PJ, Bernstein M, Coss C, Ferreira GC, Pedersen PL (Jun 1994). "Chromosomal localization of genes required for the terminal steps of oxidative metabolism: alpha and gamma subunits of ATP synthase and the phosphate carrier". Hum Genet. 93 (5): 600–2.
doi:
10.1007/bf00202832.
PMID8168843.
S2CID39597611.
Overview of all the structural information available in the
PDB for
UniProt: Q91VR2 (ATP synthase subunit gamma, mitochondrial) at the
PDBe-KB.
Further reading
Yoshida M, Muneyuki E, Hisabori T (2001). "ATP synthase--a marvellous rotary engine of the cell". Nat. Rev. Mol. Cell Biol. 2 (9): 669–77.
doi:
10.1038/35089509.
PMID11533724.
S2CID3926411.
Itoh H, Takahashi A, Adachi K, Noji H, Yasuda R, Yoshida M, et al. (2004). "Mechanically driven ATP synthesis by F1-ATPase". Nature. 427 (6973): 465–8.
doi:
10.1038/nature02212.
PMID14749837.
S2CID4428646.