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Showing Protein ATP synthase subunit alpha, mitochondrial (HMDBP01448)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 4 metabolites
Identification
HMDB Protein ID HMDBP01448
Secondary Accession Numbers
  • 6744
Name ATP synthase subunit alpha, mitochondrial
Synonyms Not Available
Gene Name ATP5A1
Protein Type Enzyme
Biological Properties
General Function Involved in ATP binding
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
Pathways
  • Oxidative phosphorylation
Reactions Not Available
GO Classification
Component
proton-transporting two-sector atpase complex
proton-transporting atp synthase complex, catalytic core f(1)
proton-transporting two-sector atpase complex, catalytic domain
macromolecular complex
protein complex
Function
binding
catalytic activity
hydrolase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
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
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
hydrolase activity, acting on acid anhydrides
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
purine nucleoside triphosphate metabolic process
purine ribonucleoside triphosphate metabolic process
atp metabolic process
hydrogen transport
proton transport
establishment of localization
transport
atp biosynthetic process
Cellular Location
  1. Mitochondrion inner membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 18q21
SNPs ATP5A1
Gene Sequence 
>1662 bp
ATGCTGTCCGTGCGCGTTGCTGCGGCCGTGGTCCGCGCCCTTCCTCGGCGGGCCGGACTG
GTCTCCAGAAATGCTTTGGGTTCATCTTTCATTGCTGCAAGGAACTTCCATGCCTCTAAC
ACTCATCTTCAAAAGACTGGGACTGCTGAGATGTCCTCTATTCTTGAAGAGCGTATTCTT
GGAGCTGATACCTCTGTTGATCTTGAAGAAACTGGGCGTGTCTTAAGTATTGGTGATGGT
ATTGCCCGCGTACATGGGCTGAGGAATGTTCAAGCAGAAGAAATGGTAGAGTTTTCTTCA
GGCTTAAAGGGTATGTCCTTGAACTTGGAACCTGACAATGTTGGTGTTGTCGTGTTTGGA
AATGATAAACTAATTAAGGAAGGAGATATAGTGAAGAGGACAGGAGCCATTGTGGACGTT
CCAGTTGGTGAGGAGCTGTTGGGTCGTGTAGTTGATGCCCTTGGTAATGCTATTGATGGA
AAGGGTCCAATTGGTTCCAAGACGCGTAGGCGAGTTGGTCTGAAAGCCCCCGGTATCATT
CCTCGAATTTCAGTGCGGGAACCAATGCAGACTGGCATTAAGGCTGTGGATAGCTTGGTG
CCAATTGGTCGTGGTCAGCGTGAACTGATTATTGGTGACCGACAGACTGGGAAAACCTCA
ATTGCTATTGACACAATCATTAACCAGAAACGTTTCAATGATGGATCTGATGAAAAGAAG
AAGCTGTACTGTATTTATGTTGCTATTGGTCAAAAGAGATCCACTGTTGCCCAGTTGGTG
AAGAGACTTACAGATGCAGATGCCATGAAGTACACCATTGTGGTGTCGGCTACGGCCTCG
GATGCTGCCCCACTTCAGTACCTGGCTCCTTACTCTGGCTGTTCCATGGGAGAGTATTTT
AGAGACAATGGCAAACATGCTTTGATCATCTATGACGACTTATCCAAACAGGCTGTTGCT
TACCGTCAGATGTCTCTGTTGCTCCGCCGACCCCCTGGTCGTGAGGCCTATCCTGGTGAT
GTGTTCTACCTACACTCCCGGTTGCTGGAGAGAGCAGCCAAAATGAACGATGCTTTTGGT
GGTGGCTCCTTGACTGCTTTGCCAGTCATAGAAACACAGGCTGGTGATGTGTCTGCTTAC
ATTCCAACAAATGTCATTTCCATCACTGACGGACAGATCTTCTTGGAAACAGAATTGTTC
TACAAAGGTATCCGCCCTGCAATTAACGTTGGTCTGTCTGTATCTCGTGTCGGATCCGCT
GCCCAAACCAGGGCTATGAAGCAGGTAGCAGGTACCATGAAGCTGGAATTGGCTCAGTAT
CGTGAGGTTGCTGCTTTTGCCCAGTTCGGTTCTGACCTCGATGCTGCCACTCAACAACTT
TTGAGTCGTGGCGTGCGTCTAACTGAGTTGCTGAAGCAAGGACAGTATTCTCCCATGGCT
ATTGAAGAACAAGTGGCTGTTATCTATGCGGGTGTAAGGGGATATCTTGATAAACTGGAG
CCCAGCAAGATTACAAAGTTTGAGAATGCTTTCTTGTCTCATGTCGTCAGCCAGCACCAA
GCCTTGTTGGGCACTATCAGGGCTGATGGAAAGATCTCAGAACAATCAGATGCAAAGCTG
AAAGAGATTGTAACAAATTTCTTGGCTGGATTTGAAGCTTAA
Protein Properties
Number of Residues 553
Molecular Weight 59750.1
Theoretical pI 9.56
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>ATP synthase subunit alpha, mitochondrial
MLSVRVAAAVVRALPRRAGLVSRNALGSSFIAARNFHASNTHLQKTGTAEMSSILEERIL
GADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFG
NDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGII
PRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKK
KLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYF
RDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFG
GGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSA
AQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMA
IEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKL
KEIVTNFLAGFEA
GenBank ID Protein 28938
UniProtKB/Swiss-Prot ID P25705
UniProtKB/Swiss-Prot Entry Name ATPA_HUMAN
PDB IDs
GenBank Gene ID X59066
GeneCard ID ATP5A1
GenAtlas ID ATP5A1
HGNC ID HGNC:823
References
General References
  1. 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 ]
  2. 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 ]
  3. 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. [PubMed:19892738 ]
  4. 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. [PubMed:7498159 ]
  5. 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. [PubMed:1830491 ]
  6. 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. [PubMed:8428659 ]
  7. 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. [PubMed:8086450 ]
  8. 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. [PubMed:11410595 ]