MPEG1
entrez
219972
canonical
uniprot
Q2M385
canonical
ensembl
ENSG00000197629
resolver
ensp
ENSP00000354335
resolver
ensp
ENSP00000547901
resolver
enst
ENST00000361050
resolver
enst
ENST00000877842
resolver
genesymbol
MPEG1
resolver
hgnc
HGNC:29619
resolver
uniprot
Q2M1T6
resolver
uniprot
Q8TEF8
resolver
uniprot_entry
MPEG1_HUMAN
resolver
uniprot_sec
Q2M1T6
resolver
uniprot_sec
Q8TEF8
resolver
activity_regulation
ACTIVITY REGULATION: Forms arc- and ring-shaped pre-pores on top of the membrane at neutral to slightly acidic pH conditions and converts to pores upon acidification (PubMed:31537793). Undergoes transition from the pre-pore to the pore in a processive clockwise hand-over-hand process (By similarity). In the pore state, 2 alpha-helical regions refold into transmembrane hairpins (TMH1 and TMH2) in each protomer that form in the ensemble complex giant beta-barrel transmembrane pores (PubMed:31537793). {ECO:0000250|UniProtKB:A1L314, ECO:0000269|PubMed:31537793}.
uniprot
proteins
amino_acid_sequence
MNNFRATILFWAAAAWAKSGKPSGEMDEVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTYSNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANYQSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAITTRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQTRMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQDSQSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSNRTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLPLHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPGCTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLSGNRDVLLCQKLEQKNPLTGDFSCPSGYSPVHLLSQIHEEGYNHLECHRKCTLLVFCKTVCEDVFQVAKAEFRAFWCVASSQVPENSGLLFGGLFSSKSINPMTNAQSCPAGYFPLRLFENLKVCVSQDYELGSRFAVPFGGFFSCTVGNPLVDPAISRDLGAPSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPARLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWRLGEPIELRRAMNVIHGDGGGLSGGAAAGVTVGVTTILAVVITLAIYGTRKFKKKAYQAIEERQSLVPGTAATGDTTYQEQGQSPA
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 77 (IMD77) [MIM:619223]: An autosomal dominant disorder characterized by recurrent, persistent bacterial and fungal infections with multiple unusual organisms. Skin and pulmonary infections are the most common. Patient macrophages show impaired killing of intracellular bacteria and organisms, including non-tubercular mycobacteria, Pseudomonas, Candida, and Aspergillus. {ECO:0000269|PubMed:28422754, ECO:0000269|PubMed:33224153}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Pore-forming protein involved in both innate and adaptive immunity (PubMed:23753625, PubMed:26402460, PubMed:28422754, PubMed:30609079, PubMed:31537793, PubMed:33224153). Plays a central role in antigen cross-presentation in dendritic cells by forming a pore in antigen-containing compartments, thereby promoting delivery of antigens for cross-presentation (By similarity). Also involved in innate immune response following bacterial infection; shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23753625, PubMed:26402460, PubMed:28422754, PubMed:30609079, PubMed:33224153). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (By similarity). Required for the antibacterial activity of reactive oxygen species and nitric oxide (By similarity). {ECO:0000250|UniProtKB:A1L314, ECO:0000269|PubMed:23753625, ECO:0000269|PubMed:26402460, ECO:0000269|PubMed:28422754, ECO:0000269|PubMed:30609079, ECO:0000269|PubMed:31537793, ECO:0000269|PubMed:33224153}.; FUNCTION: [Macrophage-expressed gene 1 protein, processed form]: Pore-forming protein that plays a central role in antigen cross-presentation in dendritic cells by mediating delivery of antigens for cross-presentation (By similarity). Dendritic cells bridge innate and adaptive immunity by capturing exogenous antigens on MHC class-I molecules and presenting them to naive CD8(+) T-cells (By similarity). Acts by forming a pore in antigen-containing compartments, promoting the release of antigens into the cytosol, enabling generation of MHCI:peptide complexes and T-cell priming (By similarity). {ECO:0000250|UniProtKB:A1L314}.
uniprot
proteins
mass_dalton
78587
uniprot
proteins
post_translational_modification
PTM: Proteolytically processed in two steps to generate the Macrophage-expressed gene 1 protein, processed form: cleaved by trypsin in proximity of the helical transmembrane domain releases the ectodomain into the lysosomal lumen to orient the pore-forming domain toward the endogenous membranes, and processed by the asparagine endopeptidase (LGMN). {ECO:0000250|UniProtKB:A1L314}.; PTM: Monoubiquitinated in response to bacterial infection; ubiquitination is required for vesicular localization and antibacterial activity and can be blocked by bacterial cell cycle inhibiting factor (cif) (By similarity). {ECO:0000250|UniProtKB:A1L314}.
uniprot
proteins
protein_family
MPEG1 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
23753625
uniprot
proteins
pubmed
26402460
uniprot
proteins
pubmed
28422754
uniprot
proteins
pubmed
28705375
uniprot
proteins
pubmed
30609079
uniprot
proteins
pubmed
31537793
uniprot
proteins
pubmed
33224153
uniprot
proteins
pubmed
7888681
uniprot
proteins
sequence_length
716
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:28705375, ECO:0000269|PubMed:31537793}; Multi-pass membrane protein {ECO:0000255}. Note=Bacterial infection induces translocation of the cytoplasmic vesicles to bacterium-containing phagocytic vesicles and fusing of the vesicles. {ECO:0000269|PubMed:28705375}.; SUBCELLULAR LOCATION: [Macrophage-expressed gene 1 protein, processed form]: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:A1L314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A1L314}. Note=Proteolytically processed in lysosomes, leading to its maturation and forms pores in the membrane of antigen-containing phagosomes. {ECO:0000250|UniProtKB:A1L314}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:28705375}.
uniprot
proteins
transmembrane_region
TRANSMEM 113..120; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:A1L314"; TRANSMEM 127..132; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:A1L314"; TRANSMEM 235..244; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:A1L314"; TRANSMEM 248..256; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:A1L314"; TRANSMEM 656..676; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins