Q9ERH6 · MOAP1_MOUSE

  • Protein
    Modulator of apoptosis 1
  • Gene
    Moap1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Retrotransposon-derived protein that forms virion-like capsids (PubMed:34413232).
Acts as an effector of BAX during apoptosis: enriched at outer mitochondria membrane and associates with BAX upon induction of apoptosis, facilitating BAX-dependent mitochondrial outer membrane permeabilization and apoptosis (By similarity).
Required for death receptor-dependent apoptosis (By similarity).
When associated with RASSF1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation (By similarity).
Also promotes autophagy: promotes phagophore closure via association with ATG8 proteins (PubMed:33783314).
Acts as an inhibitor of the NFE2L2/NRF2 pathway via interaction with SQSTM1: interaction promotes dissociation of SQSTM1 inclusion bodies that sequester KEAP1, relieving inactivation of the BCR(KEAP1) complex (By similarity).

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 Componentcytosol
Cellular Componentmitochondrial outer membrane
Cellular Componentnucleus
Molecular Functionubiquitin protein ligase binding
Biological Processapoptotic process
Biological Processautophagy
Biological Processextrinsic apoptotic signaling pathway in absence of ligand
Biological Processextrinsic apoptotic signaling pathway via death domain receptors
Biological Processintrinsic apoptotic signaling pathway in response to DNA damage
Biological Processpositive regulation of apoptotic process
Biological Processpositive regulation of autophagosome assembly
Biological Processpositive regulation of release of cytochrome c from mitochondria
Biological Processprotein insertion into mitochondrial membrane
Biological Processregulation of apoptotic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Modulator of apoptosis 1
  • Short names
    MAP-1
    ; MmMOAP1

Gene names

    • Name
      Moap1

Organism names

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

Accessions

  • Primary accession
    Q9ERH6

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
Note: Forms virion-like extracellular vesicles that are released from cells.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001552071-352Modulator of apoptosis 1

Post-translational modification

Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1, this modification is inhibited by TRIM39.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed, including in the brain. High expression levels in testis.

Gene expression databases

Interaction

Subunit

Homodimer. Under normal circumstances, held in an inactive conformation by an intramolecular interaction. Interacts with BAX. Binding to RASSF1 isoform A (RASSF1A) relieves this inhibitory interaction and allows further binding to BAX. Binds also to BCL2 and BCLX. Recruited to the TNFRSF1A and TNFRSF10A complexes in response to their respective cognate ligand, after internalization. Interacts with TRIM39 (By similarity).
Interacts with RASSF6 (PubMed:17404571).
Interacts with ATG8 proteins MAP1LC3A, MAP1LC3B and MAP1LC3C (By similarity).
Does not interact with ATG8 proteins GABARAPL1, GABARAPL2 and GABARAP (By similarity).
Interacts with SQSTM1; promoting dissociation of SQSTM1 inclusion bodies that sequester KEAP1 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif, region.

TypeIDPosition(s)Description
Motif49-52LIR
Region120-127BH3-like
Region204-207RASSF1-binding

Domain

The protein is evolutionarily related to retrotransposon Gag proteins: it contains the capsid (CA)subdomain of gag.
The BH3-like domain is required for association with BAX and for mediating apoptosis. The three BH domains (BH1, BH2, and BH3) of BAX are all required for mediating protein-protein interaction.
The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins MAP1LC3A, MAP1LC3B and MAP1LC3C.

Sequence similarities

Belongs to the PNMA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    352
  • Mass (Da)
    39,404
  • Last updated
    2001-03-01 v1
  • Checksum
    8F4630D080495D98
MTLRLLEDWCRGMDMNPRKALLVAGIPPTCGVADIEEALQAGLAPLGEHRLLGRMFRRDENKNVALIGLTVETGSALVPKEIPAKGGVWRVIFKPPDTDSDFLCRLNEFLKGEGMTMGELTRVLGNRNDPLGLDPGIMIPEIRAPMLAQALNEALKPTLQYLRYKKLSVFSGRDPPGPGEEEFESWMFHTSQVMKTWQVSDVEKRRRLIESLRGPAFEIIRVLKINNPFITVAECLKTLETIFGIIDNPRALQVKYLTTYQKTDEKLSAYVLRLEPLLQKLVQKGAIEKEVVNQARLDQVIAGAVHKSVRRELGLPEGSPAPGLLQLLTLIKDKEAEEEEVLLQAELEGYCT

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict57in Ref. 3; AAH55374

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF305551
EMBL· GenBank· DDBJ
AAG31787.1
EMBL· GenBank· DDBJ
mRNA
AK019599
EMBL· GenBank· DDBJ
BAB31810.1
EMBL· GenBank· DDBJ
mRNA
BC014715
EMBL· GenBank· DDBJ
AAH14715.1
EMBL· GenBank· DDBJ
mRNA
BC055374
EMBL· GenBank· DDBJ
AAH55374.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp