Q9VQ79 · AIFM1_DROME

Function

function

Probable NADH oxidoreductase (By similarity).
Mitochondrial effector of cell death that plays roles in developmentally regulated cell death and normal mitochondrial function

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Features

Showing features for binding site.

1739100200300400500600700
TypeIDPosition(s)Description
Binding site261-265FAD (UniProtKB | ChEBI)
Binding site295FAD (UniProtKB | ChEBI)
Binding site300FAD (UniProtKB | ChEBI)
Binding site358FAD (UniProtKB | ChEBI)
Binding site410FAD (UniProtKB | ChEBI)
Binding site564FAD (UniProtKB | ChEBI)
Binding site580-581FAD (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentmitochondrial intermembrane space
Cellular Componentmitochondrion
Molecular FunctionDNA binding
Molecular FunctionFAD binding
Molecular FunctionNAD(P)H oxidase H2O2-forming activity
Molecular FunctionNADH dehydrogenase activity
Molecular Functionprotein dimerization activity
Biological Processapoptotic process
Biological Processdefense response to fungus
Biological Processmitochondrial ATP synthesis coupled electron transport
Biological Processmitochondrial respiratory chain complex assembly
Biological Processprogrammed cell death involved in cell development
Biological Processprotein import into mitochondrial intermembrane space

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Putative apoptosis-inducing factor 1, mitochondrial
  • EC number
  • Short names
    DmAIF

Gene names

    • Name
      AIF
    • ORF names
      CG7263

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VQ79
  • Secondary accessions
    • B5RIR8
    • Q95TL9
    • Q960F8

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Loss of zygotic expression results in decreased embryonic cell death and the persistence of differentiated neuronal cells along the ventral nerve cord at late embryonic stages. Embryos that do hatch undergo growth arrest at early larval stages, accompanied by mitochondrial respiratory dysfunction.

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-42Mitochondrion
ChainPRO_000002202943-739Putative apoptosis-inducing factor 1, mitochondrial

Proteomic databases

Expression

Developmental stage

Expressed both maternally and zygotically throughout development with slightly lower levels during pupation.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region257-564FAD-dependent oxidoreductase
Compositional bias644-673Polar residues
Region644-681Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q9VQ79-2

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    739
  • Mass (Da)
    81,217
  • Last updated
    2003-08-15 v2
  • Checksum
    71184B1721AB93AF
MSIWGVRCLTQRFIRQAYILANRRLLGPVPQRSPPAYAPLRPAHSSLYQMVKKRTLEARTKLQANKYPNHQVCVTKPSTTPPVEEYETAVEGAGVPAYANAQFQAHSQSEPLFKVGFADVKSVCSAKDVLKSDSAKLSTSQPVLDSCKATSPCEEFKRKRKETTCQPCDEDGTAPGGGDGGDEECECRMKDLRLKCLLGALAALLAGGFLAWFMTRDTDDSEAKKAEAEEEERKRRLVAGLATSPPSSEDLPKHVPYLIIGGGTAAFSAFRAIKSNDATAKVLMISNEFRKPYMRPPLSKELWYTPNPNEDPIKDYRFKQWTGSERSLFFEPDEFFIDPEDLDDNANGGIAVAQGFSVKKVDAQKRIVTLNDGYEISYDECLIATGCAPKNLPMLRDAPPSVLEKVMVYRTPDDFDRLRKLAAEKRSITIVGNGFIGSELACSLAHYSRENNGGKVYQVFQENANMSKVLPNYLSRWTTAKMEAQGVCVIPNASIRSAVRDETNLKLELNNGMTLMSDVVVVCVGCTPNTDLAGPSRLEVDRSLGGFVVNAELEARRNLYVAGDASCFFDPLLGRRRVEHHDHSVVSGRLAGENMTGAKKPYQHQSMFWSDLGPEIGYEGIGLVDSSLPTVGVFALPSESATRVDQLSESSDSDVPETSTSSSQSSKSDAGASQDGVTCDPDEAGNYGKGVIFYLKNDKIVGILLWNLFNRIGLARTIINQNKKYDDLNEVAKLFEIHA

Q9VQ79-1

  • Name
    A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
M9PBQ4M9PBQ4_DROMEAIF738

Sequence caution

The sequence AAL13925.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_00795151-115in isoform A
Sequence conflict639in Ref. 4; AAK93507
Compositional bias644-673Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014134
EMBL· GenBank· DDBJ
AAF51299.2
EMBL· GenBank· DDBJ
Genomic DNA
AE014134
EMBL· GenBank· DDBJ
AAN10444.2
EMBL· GenBank· DDBJ
Genomic DNA
AY052083
EMBL· GenBank· DDBJ
AAK93507.1
EMBL· GenBank· DDBJ
mRNA
AY058696
EMBL· GenBank· DDBJ
AAL13925.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BT044192
EMBL· GenBank· DDBJ
ACH92257.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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