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Showing Protein ATP synthase subunit e, mitochondrial (HMDBP01338)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 4 metabolites
Identification
HMDB Protein ID HMDBP01338
Secondary Accession Numbers
  • 6634
Name ATP synthase subunit e, mitochondrial
Synonyms
  1. ATPase subunit e
Gene Name ATP5I
Protein Type Enzyme
Biological Properties
General Function Involved in hydrogen ion 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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
membrane part
mitochondrial proton-transporting atp synthase complex, coupling factor f(o)
mitochondrial membrane part
Function
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. Mitochondrion inner membrane
Gene Properties
Chromosome Location Chromosome:4
Locus 4p16.3
SNPs ATP5I
Gene Sequence 
>210 bp
ATGGTGCCACCGGTGCAGGTCTCTCCGCTCATCAAGCTCGGCCGCTACTCCGCCCTGTTC
CTCGGTGTGGCCTACGGAGCCACGCGCTACAATTACCTAAAACCTCGGGCAGAAGAGGAG
AGGAGGATAGCAGCAGAAGAGAAGAAGAAGCAGGATGAACTGAAACGGATTGCCAGAGAA
TTGGCAGAAGATGACAGCATATTAAAGTGA
Protein Properties
Number of Residues 69
Molecular Weight 7933.1
Theoretical pI 9.82
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>ATP synthase subunit e, mitochondrial
MVPPVQVSPLIKLGRYSALFLGVAYGATRYNYLKPRAEEERRIAAEEKKKQDELKRIARE
LAEDDSILK
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P56385
UniProtKB/Swiss-Prot Entry Name ATP5I_HUMAN
PDB IDs Not Available
GenBank Gene ID D50371
GeneCard ID ATP5I
GenAtlas ID ATP5I
HGNC ID HGNC:846
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. 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 ]