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MGP001990

UniProt Annotations

Entry Information
Gene NameMX dynamin-like GTPase 1
Protein EntryMX1_HUMAN
UniProt IDP20591
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P20591-1; Sequence=Displayed; Name=2; Synonyms=56-kda, varMxA; IsoId=P20591-2; Sequence=VSP_042904;
DomainThe C-terminal GTPase effector domain (GED) is involved in oligomerization and viral target recognition. {ECO:0000269|PubMed:20538602}.
DomainThe middle domain mediates self-assembly and oligomerization. {ECO:0000269|PubMed:20538602}.
FunctionInterferon-induced dynamin-like GTPase with antiviral activity against a wide range of RNA viruses and some DNA viruses. Its target viruses include negative-stranded RNA viruses and HBV through binding and inactivation of their ribonucleocapsid. May also antagonize reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV) replication by preventing the nuclear import of viral nucleocapsids. Inhibits La Crosse virus (LACV) replication by sequestering viral nucleoprotein in perinuclear complexes, preventing genome amplification, budding, and egress. Inhibits influenza A virus (IAV) replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Enhances ER stress-mediated cell death after influenza virus infection. May regulate the calcium channel activity of TRPCs. {ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:14687945, ECO:0000269|PubMed:14752052, ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16202617, ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:17374778, ECO:0000269|PubMed:18668195, ECO:0000269|PubMed:19109387, ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21992152}.
InductionBy type I and type III interferons. Isoform 2 is induced by HSV-1. {ECO:0000269|PubMed:18062906}.
InteractionQ13507:TRPC3; NbExp=2; IntAct=EBI-929476, EBI-520807; Q9UBN4:TRPC4; NbExp=2; IntAct=EBI-929476, EBI-929504; Q9Y210:TRPC6; NbExp=4; IntAct=EBI-929476, EBI-929362;
PtmISGylated. {ECO:0000269|PubMed:16009940}.
SimilarityBelongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
SimilarityContains 1 dynamin-type G (guanine nucleotide-binding) domain. {ECO:0000305}.
SimilarityContains 1 GED domain. {ECO:0000255|PROSITE- ProRule:PRU00720}.
Subcellular LocationCytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region. Note=Binds preferentially to negatively charged phospholipids. Colocalizes with CCHFV protein N in the perinuclear region.
Subcellular LocationIsoform 2: Cytoplasm {ECO:0000269|PubMed:20603636}. Nucleus {ECO:0000269|PubMed:20603636}. Note=Translocates into the nuclei of HSV-1 infected cells.
SubunitHomotetramer. Oligomerizes into multimeric filamentous or ring-like structures by virtue of its stalk domain. Oligomerization is critical for GTPase activity, protein stability, and recognition of viral target structures. Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7. Interacts with HSPA5. Interacts with DDX39A and DDX39B. Interacts with TUBB/TUBB5 (By similarity). The GTP-bound form interacts (via C-terminus) with THOV P5 protein. The GTP-bound form interacts with LACV protein N. Interacts with CCHFV protein N. {ECO:0000250, ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:20428112, ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21962493, ECO:0000269|PubMed:21992152, ECO:0000269|PubMed:9933640}.
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