Hmdb loader
Survey
Identification
HMDB Protein ID HMDBP01343
Secondary Accession Numbers
  • 6639
Name ATP synthase subunit gamma, mitochondrial
Synonyms
  1. F-ATPase gamma subunit
Gene Name ATP5C1
Protein Type Enzyme
Biological Properties
General Function Involved in hydrogen ion transporting ATP synthase activity, rotational mechanism
Specific 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. 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
Pathways
  • Oxidative phosphorylation
Reactions Not Available
GO Classification
Component
proton-transporting atp synthase complex, catalytic core f(1)
proton-transporting two-sector atpase complex, catalytic domain
macromolecular complex
protein complex
Function
proton-transporting atpase activity, rotational mechanism
hydrogen ion transporting atp synthase activity, rotational mechanism
transmembrane transporter activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
hydrogen ion transmembrane transporter activity
transporter activity
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
atp synthesis coupled proton transport
atp biosynthetic process
Cellular Location
  1. Mitochondrion
  2. Peripheral membrane protein
  3. Mitochondrion inner membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 10p15.1
SNPs ATP5C1
Gene Sequence
>897 bp
ATGTTCTCTCGCGCGGGTGTCGCTGGGCTGTCGGCCTGGACCTTGCAGCCGCAATGGATT
CAAGTTCGAAATATGGCAACTTTGAAAGATATCACCAGGAGACTAAAGTCCATCAAAAAC
ATCCAGAAAATTACCAAGTCTATGAAAATGGTAGCGGCAGCAAAATATGCCCGAGCTGAG
AGAGAGCTGAAACCAGCTCGAATATATGGATTGGGATCTTTAGCTCTGTATGAAAAAGCT
GATATCAAGGGGCCTGAAGACAAGAAGAAACACCTCCTTATTGGTGTGTCCTCAGATCGA
GGACTGTGTGGTGCTATTCATTCCTCCATTGCTAAACAGATGAAAAGCGAGGTTGCTACA
CTAACAGCAGCTGGGAAAGAAGTTATGCTTGTTGGAATTGGTGACAAAATCAGAGGCATA
CTTTATAGGACTCATTCTGACCAGTTTCTGGTGGCATTCAAAGAAGTGGGAAGAAAGCCC
CCCACTTTTGGAGATGCGTCAGTCATTGCCCTTGAATTACTAAATTCTGGATATGAATTT
GATGAAGGCTCCATCATCTTTAATAAATTCAGGTCTGTCATCTCCTATAAGACAGAAGAA
AAGCCCATCTTTTCCCTTAATACCGTTGCAAGTGCTGACAGCATGAGTATCTATGACGAT
ATTGATGCTGACGTGCTGCAAAATTACCAAGAATACAATCTGGCCAACATCATCTACTAC
TCTCTGAAGGAGTCCACCACTAGTGAGCAGAGTGCCAGGATGACAGCCATGGACAATGCC
AGCAAGAATGCTTCTGAGATGATTGACAAATTGACATTGACATTCAACCGTACCCGCCAA
GCTGTCATCACAAAAGAGTTGATTGAAATTATCTCTGGTGCTGCAGCTCTGGATTAA
Protein Properties
Number of Residues 298
Molecular Weight 32995.7
Theoretical pI 9.71
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>ATP synthase subunit gamma, mitochondrial
MFSRAGVAGLSAWTLQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAE
RELKPARIYGLGSLALYEKADIKGPEDKKKHLLIGVSSDRGLCGAIHSSIAKQMKSEVAT
LTAAGKEVMLVGIGDKIRGILYRTHSDQFLVAFKEVGRKPPTFGDASVIALELLNSGYEF
DEGSIIFNKFRSVISYKTEEKPIFSLNTVASADSMSIYDDIDADVLQNYQEYNLANIIYY
SLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P36542
UniProtKB/Swiss-Prot Entry Name ATPG_HUMAN
PDB IDs
GenBank Gene ID D16562
GeneCard ID ATP5C1
GenAtlas ID ATP5C1
HGNC ID HGNC:833
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed:15164054 ]
  5. Matsuda C, Endo H, Ohta S, Kagawa Y: Gene structure of human mitochondrial ATP synthase gamma-subunit. Tissue specificity produced by alternative RNA splicing. J Biol Chem. 1993 Nov 25;268(33):24950-8. [PubMed:8227057 ]