This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes 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, Fo, 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 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene is one of three genes that encode subunit c of the proton channel. Each of the three genes have distinct mitochondrial import sequences but encode the identical mature protein. Alternatively spliced transcript variants encoding the same protein have been identified.
Farrell LB, Nagley P (May 1987). "Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex". Biochemical and Biophysical Research Communications144 (3): 1257–64. doi:10.1016/0006-291X(87)91446-X. PMID2883974.
Yan WL, Lerner TJ, Haines JL, Gusella JF (Nov 1994). "Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3)". Genomics24 (2): 375–7. doi:10.1006/geno.1994.1631. PMID7698763.
Higuti T, Kawamura Y, Kuroiwa K, Miyazaki S, Tsujita H (Apr 1993). "Molecular cloning and sequence of two cDNAs for human subunit c of H(+)-ATP synthase in mitochondria". Biochimica et Biophysica Acta1173 (1): 87–90. doi:10.1016/0167-4781(93)90249-D. PMID8485160.
Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID8889548.
Wang HL, Zhu ZM, Yerle M, Wu X, Wang H, Yang SL, Li K (2005). "Full-length coding sequences and mapping of porcine ATP6VOE and ATP5G1 genes". Cytogenetic and Genome Research109 (4): 533. doi:10.1159/000084223. PMID15906478.