MOAP1_MACFA
ID MOAP1_MACFA Reviewed; 351 AA.
AC Q95KI4;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Modulator of apoptosis 1 {ECO:0000250|UniProtKB:Q96BY2};
DE Short=MAP-1 {ECO:0000250|UniProtKB:Q96BY2};
GN Name=MOAP1 {ECO:0000250|UniProtKB:Q96BY2};
GN ORFNames=QtrA-11392 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Retrotransposon-derived protein that forms virion-like
CC capsids (By similarity). Acts as an effector of BAX during apoptosis:
CC enriched at outer mitochondria membrane and associates with BAX upon
CC induction of apoptosis, facilitating BAX-dependent mitochondrial outer
CC membrane permeabilization and apoptosis. Required for death receptor-
CC dependent apoptosis. When associated with RASSF1, promotes BAX
CC conformational change and translocation to mitochondrial membranes in
CC response to TNF and TNFSF10 stimulation. Also promotes autophagy:
CC promotes phagophore closure via association with ATG8 proteins. Acts as
CC an inhibitor of the NFE2L2/NRF2 pathway via interaction with SQSTM1:
CC interaction promotes dissociation of SQSTM1 inclusion bodies that
CC sequester KEAP1, relieving inactivation of the BCR(KEAP1) complex (By
CC similarity). {ECO:0000250|UniProtKB:Q96BY2,
CC ECO:0000250|UniProtKB:Q9ERH6}.
CC -!- SUBUNIT: Homodimer. Under normal circumstances, held in an inactive
CC conformation by an intramolecular interaction. Interacts with BAX.
CC Binding to RASSF1 isoform A (RASSF1A) relieves this inhibitory
CC interaction and allows further binding to BAX. Binds also to BCL2 and
CC BCLX. Recruited to the TNFRSF1A and TNFRSF10A complexes in response to
CC their respective cognate ligand, after internalization. Interacts with
CC TRIM39 (By similarity). Interacts with RASSF6 (By similarity).
CC Interacts with ATG8 proteins MAP1LC3A, MAP1LC3B and MAP1LC3C. Does not
CC interact with ATG8 proteins GABARAPL1, GABARAPL2 and GABARAP. Interacts
CC with SQSTM1; promoting dissociation of SQSTM1 inclusion bodies that
CC sequester KEAP1 (By similarity). {ECO:0000250|UniProtKB:Q96BY2,
CC ECO:0000250|UniProtKB:Q9ERH6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96BY2}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96BY2}. Extracellular vesicle membrane
CC {ECO:0000250|UniProtKB:Q9ERH6}. Note=Forms virion-like extracellular
CC vesicles that are released from cells. {ECO:0000250|UniProtKB:Q9ERH6}.
CC -!- DOMAIN: The protein is evolutionarily related to retrotransposon Gag
CC proteins: it contains the capsid (CA)subdomain of gag.
CC {ECO:0000250|UniProtKB:Q96BY2}.
CC -!- DOMAIN: The BH3-like domain is required for association with BAX and
CC for mediating apoptosis. The three BH domains (BH1, BH2, and BH3) of
CC BAX are all required for mediating protein-protein interaction.
CC {ECO:0000250|UniProtKB:Q96BY2}.
CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC interaction with the ATG8 family proteins MAP1LC3A, MAP1LC3B and
CC MAP1LC3C. {ECO:0000250|UniProtKB:Q96BY2}.
CC -!- PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1, this
CC modification is inhibited by TRIM39. {ECO:0000250|UniProtKB:Q96BY2}.
CC -!- SIMILARITY: Belongs to the PNMA family. {ECO:0000305}.
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DR EMBL; AB060854; BAB46873.1; -; mRNA.
DR RefSeq; NP_001274595.1; NM_001287666.1.
DR AlphaFoldDB; Q95KI4; -.
DR STRING; 9541.XP_005595757.1; -.
DR PRIDE; Q95KI4; -.
DR Ensembl; ENSMFAT00000073431; ENSMFAP00000050942; ENSMFAG00000050773.
DR GeneID; 102133169; -.
DR CTD; 64112; -.
DR VEuPathDB; HostDB:ENSMFAG00000038233; -.
DR eggNOG; ENOG502SAVD; Eukaryota.
DR GeneTree; ENSGT01030000234522; -.
DR OMA; GMIPEIR; -.
DR OrthoDB; 820525at2759; -.
DR Proteomes; UP000233100; Chromosome 7.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
DR GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IEA:Ensembl.
DR InterPro; IPR026523; PNMA.
DR PANTHER; PTHR23095; PTHR23095; 1.
DR Pfam; PF14893; PNMA; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Autophagy; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..351
FT /note="Modulator of apoptosis 1"
FT /id="PRO_0000155206"
FT REGION 120..127
FT /note="BH3-like"
FT /evidence="ECO:0000250|UniProtKB:Q96BY2"
FT REGION 202..205
FT /note="RASSF1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q96BY2"
FT MOTIF 49..52
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:Q96BY2"
SQ SEQUENCE 351 AA; 39624 MW; C7530E4496A6FFB3 CRC64;
MTLRLLEDWC RGMDMNPRKA LLIAGISQSC SVAEIEEALQ AGLAPLGEYR LLGRMFRRDE
NRKVALVGLT AETSHALVPK EIPGKGGIWR VIFKPPDSDN TFLSRLNEFL AGEGMTVGEL
TRALAHENGS LDLEQGMIPE MWAPMLAQAL EALQPALQCL KYKKLRVFSG REPPEPGEEE
FGRWMFHTTQ MIKAWQVPDV EKRRRLLESL RGPALDVIRV LKINNPLITV DECLQALEEV
FGVTDNPREL QVKYLTTYQK DEEKLSAYVL RLEPLLQKLV QRGAIERDAV NQARLDQVIA
GAVHKTIRRE LNLPEDGPAP GFLQLLVLIK DYEAAEEEEA LLQEVLEGHF T
