Identification |
HMDB Protein ID
| CDBP01343 |
Secondary Accession Numbers
| Not Available |
Name
| ATP synthase subunit alpha, mitochondrial |
Description
| Not Available |
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 |
GO Classification
|
Component |
proton-transporting two-sector atpase complex, catalytic domain |
macromolecular complex |
protein complex |
proton-transporting two-sector atpase complex |
proton-transporting atp synthase complex, catalytic core f(1) |
Function |
cation transmembrane transporter activity |
inorganic cation transmembrane transporter activity |
monovalent inorganic cation transmembrane transporter activity |
hydrogen ion transmembrane transporter activity |
binding |
transporter activity |
catalytic activity |
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances |
hydrolase activity |
nucleoside binding |
hydrolase activity, acting on acid anhydrides |
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 |
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 |
purine nucleotide metabolic process |
establishment of localization |
purine nucleotide biosynthetic process |
transport |
purine nucleoside triphosphate biosynthetic process |
atp 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 |
|
Cellular Location
|
- Mitochondrion inner membrane
|
Pathways
|
Name | SMPDB/Pathwhiz | KEGG | Mitochondrial Electron Transport Chain | | |
|
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
|
|
Transmembrane Regions
|
|
Protein Sequence
|
>ATP synthase subunit alpha, mitochondrial
MLSVRVAAAVVRALPRRAGLVSRNALGSSFIAARNFHASNTHLQKTGTAEMSSILEERIL
GADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFG
NDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGII
PRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKK
KLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYF
RDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFG
GGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSA
AQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMA
IEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKL
KEIVTNFLAGFEA
|
External Links |
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
| Not Available |