O35143 · ATIF1_MOUSE

  • Protein
    ATPase inhibitor, mitochondrial
  • Gene
    Atp5if1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Endogenous F1F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F1F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F1F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity).
Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme (PubMed:23135403).

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 Componentcell surface
Cellular Componentmitochondrion
Cellular Componentprotein-containing complex
Molecular Functionangiostatin binding
Molecular FunctionATPase binding
Molecular FunctionATPase inhibitor activity
Molecular Functioncalmodulin binding
Molecular Functionidentical protein binding
Molecular Functionmitochondrial proton-transporting ATP synthase complex binding
Biological Processerythrocyte differentiation
Biological Processheme biosynthetic process
Biological Processmitochondrial depolarization
Biological Processnegative regulation of ATP-dependent activity
Biological Processnegative regulation of endothelial cell proliferation
Biological Processnegative regulation of hydrolase activity
Biological Processnegative regulation of mitochondrial ATP synthesis coupled proton transport
Biological Processpositive regulation of autophagy of mitochondrion in response to mitochondrial depolarization
Biological Processpositive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway
Biological Processpositive regulation of proteolysis involved in protein catabolic process
Biological Processreactive oxygen species metabolic process
Biological Processregulation of protein targeting to mitochondrion

Names & Taxonomy

Protein names

  • Recommended name
    ATPase inhibitor, mitochondrial
  • Alternative names
    • ATP synthase F1 subunit epsilon
    • Inhibitor of F(1)F(o)-ATPase (IF(1); IF1)

Gene names

    • Name
      Atp5if1
    • Synonyms
      Atpi, Atpif1
      , If1

Organism names

  • Taxonomic identifier
  • Strains
    • DBA/1
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O35143
  • Secondary accessions
    • Q9D879

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-25Mitochondrion
ChainPRO_000000254826-106ATPase inhibitor, mitochondrial
Modified residue39Phosphoserine
Modified residue103N6-succinyllysine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homodimer; represents the active form and is present at a pH value below 6.5. Homotetramer; represents the inactive form and is present at a pH value above 7.0 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, coiled coil.

TypeIDPosition(s)Description
Region26-52N-terminal inhibitory region
Region26-58Disordered
Coiled coil60-106
Region74-106Antiparallel alpha-helical coiled coil region

Domain

Forms an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 74-106, leaving each N-terminal inhibitory region (residues 26-52) accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region (residues 26-52) binds the alpha(ADP-bound)-beta(ADP-bound) (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also contact the central gamma subunit (ATP5F1C). This dimeric state is favored by pH values below 7.0, and at higher values the dimers associate to form inactive homotetramer, where the inhibitory region is occluded, masking its inhibitory activity (By similarity).

Sequence similarities

Belongs to the ATPase inhibitor family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    106
  • Mass (Da)
    12,159
  • Last updated
    2012-10-03 v2
  • Checksum
    78C0FE0CD04FA2D3
MAGSALAVRARFGVWGMKVLQTRGFVSDSSDSMDTGAGSIREAGGAFGKREKAEEDRYFREKTKEQLAALRKHHEDEIDHHSKEIERLQKQIERHKKKIQQLKNNH

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
E9PV44E9PV44_MOUSEAtp5if174

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict93in Ref. 1; AAB69647

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF002718
EMBL· GenBank· DDBJ
AAB69647.1
EMBL· GenBank· DDBJ
mRNA
AK008346
EMBL· GenBank· DDBJ
BAB25618.1
EMBL· GenBank· DDBJ
mRNA
AK152389
EMBL· GenBank· DDBJ
BAE31177.1
EMBL· GenBank· DDBJ
mRNA
AL805897
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH466552
EMBL· GenBank· DDBJ
EDL30101.1
EMBL· GenBank· DDBJ
Genomic DNA
BC012680
EMBL· GenBank· DDBJ
AAH12680.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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