ATP synthase subunit alpha, mitochondrial
Details
- Name
- ATP synthase subunit alpha, mitochondrial
- Synonyms
- ATP5A
- ATP5AL2
- ATPM
- Gene Name
- ATP5A1
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0007361|ATP synthase subunit alpha, mitochondrial MLSVRVAAAVVRALPRRAGLVSRNALGSSFIAARNFHASNTHLQKTGTAEMSSILEERIL GADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFG NDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGII PRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKK KLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYF RDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFG GGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSA AQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMA IEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKL KEIVTNFLAGFEA
- Number of residues
- 553
- Molecular Weight
- 59750.06
- Theoretical pI
- 9.56
- GO Classification
- FunctionsATP binding / MHC class I protein binding / poly(A) RNA binding / proton-transporting ATP synthase activity, rotational mechanism / proton-transporting ATPase activity, rotational mechanism / transmembrane transporter activityProcessesATP biosynthetic process / ATP hydrolysis coupled proton transport / cellular metabolic process / embryo development / lipid metabolic process / mitochondrial ATP synthesis coupled proton transport / negative regulation of endothelial cell proliferation / respiratory electron transport chain / small molecule metabolic processComponentsextracellular exosome / membrane / mitochondrial inner membrane / mitochondrial matrix / mitochondrial proton-transporting ATP synthase complex / mitochondrion / myelin sheath / plasma membrane / proton-transporting ATP synthase complex, catalytic core F(1)
- General Function
- Transmembrane transporter activity
- 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. Subunits alpha and beta form the catalytic core in F(1). 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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Mitochondrion inner membrane
- Gene sequence
>lcl|BSEQ0021376|ATP synthase subunit alpha, mitochondrial (ATP5A1) ATGTCCTCTATTCTTGAAGAGCGTATTCTTGGAGCTGATACCTCTGTTGATCTTGAAGAA ACTGGGCGTGTCTTAAGTATTGGTGATGGTATTGCCCGCGTACATGGGCTGAGGAATGTT CAAGCAGAAGAAATGGTAGAGTTTTCTTCAGGCTTAAAGGGTATGTCCTTGAACTTGGAA CCTGACAATGTTGGTGTTGTCGTGTTTGGAAATGATAAACTAATTAAGGAAGGAGATATA GTGAAGAGGACAGGAGCCATTGTGGACGTTCCAGTTGGTGAGGAGCTGTTGGGTCGTGTA GTTGATGCCCTTGGTAATGCTATTGATGGAAAGGGTCCAATTGGTTCCAAGACGCGTAGG CGAGTTGGTCTGAAAGCCCCCGGTATCATTCCTCGAATTTCAGTGCGGGAACCAATGCAG ACTGGCATTAAGGCTGTGGATAGCTTGGTGCCAATTGGTCGTGGTCAGCGTGAACTGATT ATTGGTGACCGACAGACTGGGAAAACCTCAATTGCTATTGACACAATCATTAACCAGAAA CGTTTCAATGATGGATCTGATGAAAAGAAGAAGCTGTACTGTATTTATGTTGCTATTGGT CAAAAGAGATCCACTGTTGCCCAGTTGGTGAAGAGACTTACAGATGCAGATGCCATGAAG TACACCATTGTGGTGTCGGCTACGGCCTCGGATGCTGCCCCACTTCAGTACCTGGCTCCT TACTCTGGCTGTTCCATGGGAGAGTATTTTAGAGACAATGGCAAACATGCTTTGATCATC TATGACGACTTATCCAAACAGGCTGTTGCTTACCGTCAGATGTCTCTGTTGCTCCGCCGA CCCCCTGGTCGTGAGGCCTATCCTGGTGATGTGTTCTACCTACACTCCCGGTTGCTGGAG AGAGCAGCCAAAATGAACGATGCTTTTGGTGGTGGCTCCTTGACTGCTTTGCCAGTCATA GAAACACAGGCTGGTGATGTGTCTGCTTACATTCCAACAAATGTCATTTCCATCACTGAC GGACAGATCTTCTTGGAAACAGAATTGTTCTACAAAGGTATCCGCCCTGCAATTAACGTT GGTCTGTCTGTATCTCGTGTCGGATCCGCTGCCCAAACCAGGGCTATGAAGCAGGTAGCA GGTACCATGAAGCTGGAATTGGCTCAGTATCGTGAGGTTGCTGCTTTTGCCCAGTTCGGT TCTGACCTCGATGCTGCCACTCAACAACTTTTGAGTCGTGGCGTGCGTCTAACTGAGTTG CTGAAGCAAGGACAGTATTCTCCCATGGCTATTGAAGAACAAGTGGCTGTTATCTATGCG GGTGTAAGGGGATATCTTGATAAACTGGAGCCCAGCAAGATTACAAAGTTTGAGAATGCT TTCTTGTCTCATGTCGTCAGCCAGCACCAAGCCTTGTTGGGCACTATCAGGGCTGATGGA AAGATCTCAGAACAATCAGATGCAAAGCTGAAAGAGATTGTAACAAATTTCTTGGCTGGA TTTGAAGCTTAA
- Chromosome Location
- 18
- Locus
- 18q12-q21
- External Identifiers
Resource Link UniProtKB ID P25705 UniProtKB Entry Name ATPA_HUMAN GenBank Protein ID 28938 GenBank Gene ID X59066 HGNC ID HGNC:823 - General References
- Kataoka H, Biswas C: Nucleotide sequence of a cDNA for the alpha subunit of human mitochondrial ATP synthase. Biochim Biophys Acta. 1991 Jul 23;1089(3):393-5. [Article]
- Godbout R, Bisgrove DA, Honore LH, Day RS 3rd: Amplification of the gene encoding the alpha-subunit of the mitochondrial ATP synthase complex in a human retinoblastoma cell line. Gene. 1993 Jan 30;123(2):195-201. [Article]
- Akiyama S, Endo H, Inohara N, Ohta S, Kagawa Y: Gene structure and cell type-specific expression of the human ATP synthase alpha subunit. Biochim Biophys Acta. 1994 Sep 13;1219(1):129-40. [Article]
- 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. [Article]
- Nusbaum C, Zody MC, Borowsky ML, Kamal M, Kodira CD, Taylor TD, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Abouelleil A, Allen NR, Anderson S, Bloom T, Bugalter B, Butler J, Cook A, DeCaprio D, Engels R, Garber M, Gnirke A, Hafez N, Hall JL, Norman CH, Itoh T, Jaffe DB, Kuroki Y, Lehoczky J, Lui A, Macdonald P, Mauceli E, Mikkelsen TS, Naylor JW, Nicol R, Nguyen C, Noguchi H, O'Leary SB, O'Neill K, Piqani B, Smith CL, Talamas JA, Topham K, Totoki Y, Toyoda A, Wain HM, Young SK, Zeng Q, Zimmer AR, Fujiyama A, Hattori M, Birren BW, Sakaki Y, Lander ES: DNA sequence and analysis of human chromosome 18. Nature. 2005 Sep 22;437(7058):551-5. [Article]
- 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. [Article]
- Xu G, Shin SB, Jaffrey SR: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19310-5. doi: 10.1073/pnas.0908958106. Epub 2009 Nov 5. [Article]
- Kovalyov LI, Shishkin SS, Efimochkin AS, Kovalyova MA, Ershova ES, Egorov TA, Musalyamov AK: The major protein expression profile and two-dimensional protein database of human heart. Electrophoresis. 1995 Jul;16(7):1160-9. [Article]
- Moser TL, Stack MS, Asplin I, Enghild JJ, Hojrup P, Everitt L, Hubchak S, Schnaper HW, Pizzo SV: Angiostatin binds ATP synthase on the surface of human endothelial cells. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2811-6. [Article]
- Wang ZG, White PS, Ackerman SH: Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria. J Biol Chem. 2001 Aug 17;276(33):30773-8. Epub 2001 Jun 15. [Article]
- Ohta T, Ikemoto Y, Usami A, Koide T, Wakabayashi S: High affinity interaction between histidine-rich glycoprotein and the cell surface type ATP synthase on T-cells. Biochim Biophys Acta. 2009 May;1788(5):1099-107. doi: 10.1016/j.bbamem.2009.03.005. Epub 2009 Mar 12. [Article]
- 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. [Article]
- Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
- Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
- Scott I, Webster BR, Li JH, Sack MN: Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1. Biochem J. 2012 May 1;443(3):655-61. doi: 10.1042/BJ20120118. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
- Jonckheere AI, Renkema GH, Bras M, van den Heuvel LP, Hoischen A, Gilissen C, Nabuurs SB, Huynen MA, de Vries MC, Smeitink JA, Rodenburg RJ: A complex V ATP5A1 defect causes fatal neonatal mitochondrial encephalopathy. Brain. 2013 May;136(Pt 5):1544-54. doi: 10.1093/brain/awt086. Epub 2013 Apr 18. [Article]
- Lieber DS, Calvo SE, Shanahan K, Slate NG, Liu S, Hershman SG, Gold NB, Chapman BA, Thorburn DR, Berry GT, Schmahmann JD, Borowsky ML, Mueller DM, Sims KB, Mootha VK: Targeted exome sequencing of suspected mitochondrial disorders. Neurology. 2013 May 7;80(19):1762-70. doi: 10.1212/WNL.0b013e3182918c40. Epub 2013 Apr 17. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB07384 1-ACETYL-2-CARBOXYPIPERIDINE experimental unknown Details DB07394 AUROVERTIN B experimental unknown Details DB08399 Piceatannol experimental unknown Details DB04216 Quercetin experimental, investigational unknown Details DB08629 N1-(2-AMINO-4-METHYLPENTYL)OCTAHYDRO-PYRROLO[1,2-A] PYRIMIDINE experimental unknown Details DB11638 Artenimol approved, experimental, investigational unknown ligand Details DB01119 Diazoxide approved unknown inhibitor Details