MX1B_MOUSE
ID MX1B_MOUSE Reviewed; 631 AA.
AC P09922;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Interferon-induced GTP-binding protein Mx1;
DE AltName: Full=Influenza resistance protein;
DE AltName: Full=Myxoma resistance protein 1;
DE AltName: Full=Myxovirus resistance protein 1;
GN Name=Mx1; Synonyms=Mx {ECO:0000303|PubMed:2903437};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3000619; DOI=10.1016/0092-8674(86)90493-9;
RA Staeheli P., Haller O., Boll W., Lindenmann J., Weissmann C.;
RT "Mx protein: constitutive expression in 3T3 cells transformed with cloned
RT Mx cDNA confers selective resistance to influenza virus.";
RL Cell 44:147-158(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2974922; DOI=10.1128/mcb.8.8.3065-3079.1988;
RA Hug H., Costas M., Staeheli P., Aebi M., Weissmann C.;
RT "Organization of the murine Mx gene and characterization of its
RT interferon- and virus-inducible promoter.";
RL Mol. Cell. Biol. 8:3065-3079(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERSTRAIN VARIABILITY IN MX1 GENE SEQUENCE.
RX PubMed=2903437; DOI=10.1128/mcb.8.10.4518-4523.1988;
RA Staeheli P., Grob R., Meier E., Sutcliffe J.G., Haller O.;
RT "Influenza virus-susceptible mice carry Mx genes with a large deletion or a
RT nonsense mutation.";
RL Mol. Cell. Biol. 8:4518-4523(1988).
RN [5]
RP MUTAGENESIS OF SER-47 AND LYS-49.
RX PubMed=8411374; DOI=10.1128/jvi.67.11.6726-6732.1993;
RA Pitossi F., Blank A., Schroeder A., Schwarz A., Huessi P., Schwemmle M.,
RA Pavlovic J., Staeheli P.;
RT "A functional GTP-binding motif is necessary for antiviral activity of Mx
RT proteins.";
RL J. Virol. 67:6726-6732(1993).
RN [6]
RP FUNCTION IN RESISTANCE TO INFLUENZA VIRUS.
RX PubMed=17652381; DOI=10.1128/jvi.01116-07;
RA Tumpey T.M., Szretter K.J., Van Hoeven N., Katz J.M., Kochs G., Haller O.,
RA Garcia-Sastre A., Staeheli P.;
RT "The Mx1 gene protects mice against the pandemic 1918 and highly lethal
RT human H5N1 influenza viruses.";
RL J. Virol. 81:10818-10821(2007).
RN [7]
RP REVIEW, AND INDUCTION.
RX PubMed=18062906; DOI=10.1016/j.micinf.2007.09.010;
RA Haller O., Stertz S., Kochs G.;
RT "The Mx GTPase family of interferon-induced antiviral proteins.";
RL Microbes Infect. 9:1636-1643(2007).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DDX39A AND DDX39B.
RX PubMed=21859714; DOI=10.1074/jbc.m111.251843;
RA Wisskirchen C., Ludersdorfer T.H., Mueller D.A., Moritz E., Pavlovic J.;
RT "Interferon-induced antiviral protein MxA interacts with the cellular RNA
RT helicases UAP56 and URH49.";
RL J. Biol. Chem. 286:34743-34751(2011).
RN [9]
RP FUNCTION.
RX PubMed=21651940; DOI=10.1016/j.vaccine.2011.05.069;
RA Frensing T., Seitz C., Heynisch B., Patzina C., Kochs G., Reichl U.;
RT "Efficient influenza B virus propagation due to deficient interferon-
RT induced antiviral activity in MDCK cells.";
RL Vaccine 29:7125-7129(2011).
RN [10]
RP RESISTANCE TO INFLUENZA VIRUS.
RX PubMed=22190720; DOI=10.1128/jvi.06156-11;
RA Cilloniz C., Pantin-Jackwood M.J., Ni C., Carter V.S., Korth M.J.,
RA Swayne D.E., Tumpey T.M., Katze M.G.;
RT "Molecular signatures associated with Mx1-mediated resistance to highly
RT pathogenic influenza virus infection: mechanisms of survival.";
RL J. Virol. 86:2437-2446(2012).
CC -!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
CC activity against influenza A virus, (IAV), influenza B virus (IBV) and
CC Thogoto virus (THOV). Inhibits FLUAV by interfering with the process of
CC primary transcription, probably by affecting the viral polymerase
CC function. {ECO:0000269|PubMed:17652381, ECO:0000269|PubMed:21651940}.
CC -!- SUBUNIT: Homooligomer. Oligomerizes into multimeric filamentous or
CC ring-like structures by virtue of its stalk domain. Oligomerization is
CC critical for GTPase activity, protein stability, and recognition of
CC viral target structures (By similarity). Interacts with TRPC1, TRPC3,
CC TRPC4, TRPC5, TRPC6 and TRPC7 (By similarity). Interacts with HSPA5 (By
CC similarity). Interacts with TUBB/TUBB5 (By similarity). Interacts with
CC DDX39A and DDX39B. {ECO:0000250, ECO:0000269|PubMed:21859714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21859714}. Nucleus
CC {ECO:0000269|PubMed:21859714}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively
CC charged phospholipids. Colocalizes with CCHFV protein N in the
CC perinuclear region. {ECO:0000250|UniProtKB:P20591}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:18062906}.
CC -!- DOMAIN: The C-terminal GTPase effector domain (GED) is involved in
CC oligomerization and viral target recognition. {ECO:0000250}.
CC -!- DOMAIN: The middle domain mediates self-assembly and oligomerization.
CC {ECO:0000250}.
CC -!- PTM: ISGylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- CAUTION: The sequence shown in this entry is that of the functional
CC protein expressed by the A2G strain, which is known for its unique
CC resistance to myxovirus (influenza) infections, or Czech II strain,
CC which derives from wild mice (PubMed:3000619, PubMed:15489334). Some
CC other strains also express fully active Mx1 protein, such as SL/NiA
CC (PubMed:2903437). In some inbred mouse strains however, including the
CC strain of the reference genome C57BL/6J, Mx1 gene contains a deletion
CC or a nonsense mutation that results in a non-functional gene product.
CC {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2903437,
CC ECO:0000269|PubMed:3000619, ECO:0000305}.
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DR EMBL; M12279; AAA39776.1; -; mRNA.
DR EMBL; M21117; AAA39777.1; -; Genomic_DNA.
DR EMBL; M21105; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21106; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21107; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21108; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21109; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21110; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21111; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21112; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21113; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21114; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21115; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; M21116; AAA39777.1; JOINED; Genomic_DNA.
DR EMBL; BC011113; AAH11113.1; -; mRNA.
DR PIR; A31203; A31203.
DR RefSeq; NP_034976.1; NM_010846.1.
DR AlphaFoldDB; P09922; -.
DR SMR; P09922; -.
DR IntAct; P09922; 1.
DR MINT; P09922; -.
DR iPTMnet; P09922; -.
DR PhosphoSitePlus; P09922; -.
DR jPOST; P09922; -.
DR MaxQB; P09922; -.
DR PRIDE; P09922; -.
DR ProteomicsDB; 293590; -.
DR DNASU; 17857; -.
DR GeneID; 17857; -.
DR KEGG; mmu:17857; -.
DR UCSC; uc008adf.1; mouse.
DR CTD; 4599; -.
DR MGI; MGI:97243; Mx1.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; P09922; -.
DR BioGRID-ORCS; 17857; 1 hit in 51 CRISPR screens.
DR PRO; PR:P09922; -.
DR RNAct; P09922; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; TAS:MGI.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Endoplasmic reticulum; GTP-binding; Immunity;
KW Innate immunity; Membrane; Nucleotide-binding; Nucleus; Ubl conjugation.
FT CHAIN 1..631
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000206593"
FT DOMAIN 33..306
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 543..631
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 43..50
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 68..70
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 144..147
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 213..216
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 245..248
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 307..332
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 332..499
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 333..601
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 520..522
FT /note="Critical for lipid-binding"
FT /evidence="ECO:0000250"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 144..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 213..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MUTAGEN 47
FT /note="S->C: No effect on viral infection."
FT /evidence="ECO:0000269|PubMed:8411374"
FT MUTAGEN 49
FT /note="K->A,M: Loss of protection against viral infection."
FT /evidence="ECO:0000269|PubMed:8411374"
SQ SEQUENCE 631 AA; 72038 MW; 7F0827668D190D68 CRC64;
MDSVNNLCRH YEEKVRPCID LIDTLRALGV EQDLALPAIA VIGDQSSGKS SVLEALSGVA
LPRGSGIVTR CPLVLKLRKL KEGEEWRGKV SYDDIEVELS DPSEVEEAIN KGQNFIAGVG
LGISDKLISL DVSSPNVPDL TLIDLPGITR VAVGNQPADI GRQIKRLIKT YIQKQETINL
VVVPSNVDIA TTEALSMAQE VDPEGDRTIG VLTKPDLVDR GAEGKVLDVM RNLVYPLKKG
YMIVKCRGQQ DIQEQLSLTE AFQKEQVFFK DHSYFSILLE DGKATVPCLA ERLTEELTSH
ICKSLPLLED QINSSHQSAS EELQKYGADI PEDDRTRMSF LVNKISAFNR NIMNLIQAQE
TVSEGDSRLF TKLRNEFLAW DDHIEEYFKK DSPEVQSKMK EFENQYRGRE LPGFVDYKAF
ESIIKKRVKA LEESAVNMLR RVTKMVQTAF VKILSNDFGD FLNLCCTAKS KIKEIRLNQE
KEAENLIRLH FQMEQIVYCQ DQVYKETLKT IREKEAEKEK TKALINPATF QNNSQFPQKG
LTTTEMTQHL KAYYQECRRN IGRQIPLIIQ YFILKTFGEE IEKMMLQLLQ DTSKCSWFLE
EQSDTREKKK FLKRRLLRLD EARQKLAKFS D
