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
Functions
ATP 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 activity
Processes
ATP 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 process
Components
extracellular 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
ResourceLink
UniProtKB IDP25705
UniProtKB Entry NameATPA_HUMAN
GenBank Protein ID28938
GenBank Gene IDX59066
HGNC IDHGNC:823
General References
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB073841-ACETYL-2-CARBOXYPIPERIDINEexperimentalunknownDetails
DB07394AUROVERTIN BexperimentalunknownDetails
DB08399PiceatannolexperimentalunknownDetails
DB04216Quercetinexperimental, investigationalunknownDetails
DB08629N1-(2-AMINO-4-METHYLPENTYL)OCTAHYDRO-PYRROLO[1,2-A] PYRIMIDINEexperimentalunknownDetails
DB11638Artenimolapproved, experimental, investigationalunknownligandDetails
DB01119DiazoxideapprovedunknowninhibitorDetails