MARCHF8
entrez
220972
canonical
uniprot
Q5T0T0
canonical
ensembl
ENSG00000165406
resolver
ensembl
ENSG00000278545
resolver
ensp
ENSP00000317087
resolver
ensp
ENSP00000379116
resolver
ensp
ENSP00000379118
resolver
ensp
ENSP00000411848
resolver
ensp
ENSP00000525487
resolver
ensp
ENSP00000525488
resolver
ensp
ENSP00000525489
resolver
ensp
ENSP00000525497
resolver
ensp
ENSP00000582332
resolver
enst
ENST00000395771
resolver
genesymbol
MARCHF8
resolver
genesymbol_syn
MARCH8
resolver
genesymbol_syn
MIR
resolver
genesymbol_syn
RNF178
resolver
hgnc
HGNC:23356
resolver
uniprot
B2R8E7
resolver
uniprot
H0Y7C6
resolver
uniprot
Q5T0S8
resolver
uniprot
Q8TC72
resolver
uniprot_entry
MARH8_HUMAN
resolver
uniprot_sec
B2R8E7
resolver
uniprot_sec
H0Y7C6
resolver
uniprot_sec
Q5T0S8
resolver
uniprot_sec
Q8TC72
resolver
amino_acid_sequence
MSMPLHQISAIPSQDAISARVYRSKTKEKEREEQNEKTLGHFMSHSSNISKAGSPPSASAPAPVSSFSRTSITPSSQDICRICHCEGDDESPLITPCHCTGSLHFVHQACLQQWIKSSDTRCCELCKYEFIMETKLKPLRKWEKLQMTSSERRKIMCSVTFHVIAITCVVWSLYVLIDRTAEEIKQGQATGILEWPFWTKLVVVAIGFTGGLLFMYVQCKVYVQLWKRLKAYNRVIYVQNCPETSKKNIFEKSPLTEPNFENKHGYGICHSDTNSSCCTEPEDTGAEIIHV
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that plays several important roles in innate immunity and adaptive immunity (PubMed:34285233, PubMed:35019698, PubMed:35503863). Mediates ubiquitination of CD86 and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies (PubMed:19117940, PubMed:19566897). Possesses a very broad antiviral activity by specifically inactivating different viral fusion proteins (PubMed:32934085). Targets and ubiquitinates cytoplasmic lysine residues of viral envelope glycoproteins with single transmembrane domains leading to their lysosomal degradation (PubMed:35019698). Therefore, shows broad-spectrum inhibition against many viruses including retroviruses, rhabdoviruses, arenaviruses, sarbecoviruses or influenzaviruses (PubMed:34285233, PubMed:35019698). Strongly blocks human immunodeficiency virus type 1 envelope glycoprotein incorporation into virions by down-regulating its cell surface expression. Also blocks ebola virus glycoprotein/GP incorporation via surface down-regulation (PubMed:32934085). Mediates 'Lys-63'-linked polyubiquitination of influenza M2 to target it to lysosome for degradation (PubMed:34285233). Mediates the regulation of constitutive ubiquitination and trafficking of the viral restriction factor BST2 within the endocytic pathway (PubMed:28320822). Plays a role in maintenance of immune tolerance to self by promoting the turnover and proteasomal degradation of PD-L1/CD274 via ubiquitination (PubMed:34183449). Catalyzes the 'Lys-63'-linked polyubiquitylation of cGAS thereby inhibiting its DNA binding ability and impairing its antiviral innate immunity (PubMed:35503863). Negatively regulates IL7-mediated T-cell homeostasis by mediating 'Lys-27'-linked polyubiquitination of IL7R, leading to its lysosomal degradation (PubMed:39311660). {ECO:0000269|PubMed:12582153, ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:18389477, ECO:0000269|PubMed:19117940, ECO:0000269|PubMed:19566897, ECO:0000269|PubMed:28320822, ECO:0000269|PubMed:32934085, ECO:0000269|PubMed:34183449, ECO:0000269|PubMed:34285233, ECO:0000269|PubMed:35019698, ECO:0000269|PubMed:35503863, ECO:0000269|PubMed:39311660}.; FUNCTION: (Microbial infection) Mediates 'Lys-63'-linked polyubiquitination of hepatitis C virus/HCV protein NS2 which allows its binding to HGS, an ESCRT-0 complex component, and this interaction is essential for HCV envelopment. {ECO:0000269|PubMed:30759391}.
uniprot
proteins
mass_dalton
32965
uniprot
proteins
mutagenesis
MUTAGEN 80; /note="C->S: Strong loss of catalytic activity; when associated with S-83, S-123 and S-126."; /evidence="ECO:0000269|PubMed:28320822"; MUTAGEN 83; /note="C->S: Strong loss of catalytic activity; when associated with S-80, S-123 and S-126."; /evidence="ECO:0000269|PubMed:28320822"; MUTAGEN 114; /note="W->A: Almost complete loss of ebolavirus restriction and IL7R degradation."; /evidence="ECO:0000269|PubMed:32934085, ECO:0000269|PubMed:39311660"; MUTAGEN 123; /note="C->S: Strong loss of catalytic activity; when associated with S-80, S-83 and S-126."; /evidence="ECO:0000269|PubMed:28320822"; MUTAGEN 126; /note="C->S: Strong loss of catalytic activity; when associated with S-80, S-83 and S-123."; /evidence="ECO:0000269|PubMed:28320822
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
pubmed
12582153
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14722266
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18389477
uniprot
proteins
pubmed
19117940
uniprot
proteins
pubmed
19566897
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
28320822
uniprot
proteins
pubmed
30759391
uniprot
proteins
pubmed
32934085
uniprot
proteins
pubmed
34183449
uniprot
proteins
pubmed
34285233
uniprot
proteins
pubmed
35019698
uniprot
proteins
pubmed
35503863
uniprot
proteins
pubmed
39311660
uniprot
proteins
sequence_length
291
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:32934085}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:30759391, ECO:0000269|PubMed:35503863}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19117940}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:35503863}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 157..177; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 197..217; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins