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Interferon-induced GTP-binding protein Mx1 (Influenza resistance protein) (Myxoma resistance protein 1) (Myxovirus resistance protein 1)

 MX1_MOUSE               Reviewed;         631 AA.
P09922;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
05-JUL-2017, entry version 111.
RecName: Full=Interferon-induced GTP-binding protein Mx1;
AltName: Full=Influenza resistance protein;
AltName: Full=Myxoma resistance protein 1;
AltName: Full=Myxovirus resistance protein 1;
Name=Mx1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3000619; DOI=10.1016/0092-8674(86)90493-9;
Staeheli P., Haller O., Boll W., Lindenmann J., Weissmann C.;
"Mx protein: constitutive expression in 3T3 cells transformed with
cloned Mx cDNA confers selective resistance to influenza virus.";
Cell 44:147-158(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2974922; DOI=10.1128/MCB.8.8.3065;
Hug H., Costas M., Staeheli P., Aebi M., Weissmann C.;
"Organization of the murine Mx gene and characterization of its
interferon- and virus-inducible promoter.";
Mol. Cell. Biol. 8:3065-3079(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
MUTAGENESIS OF SER-47 AND LYS-49.
PubMed=8411374;
Pitossi F., Blank A., Schroeder A., Schwarz A., Huessi P.,
Schwemmle M., Pavlovic J., Staeheli P.;
"A functional GTP-binding motif is necessary for antiviral activity of
Mx proteins.";
J. Virol. 67:6726-6732(1993).
[5]
FUNCTION IN RESISTANCE TO INFLUENZA VIRUS.
PubMed=17652381; DOI=10.1128/JVI.01116-07;
Tumpey T.M., Szretter K.J., Van Hoeven N., Katz J.M., Kochs G.,
Haller O., Garcia-Sastre A., Staeheli P.;
"The Mx1 gene protects mice against the pandemic 1918 and highly
lethal human H5N1 influenza viruses.";
J. Virol. 81:10818-10821(2007).
[6]
REVIEW, AND INDUCTION.
PubMed=18062906; DOI=10.1016/j.micinf.2007.09.010;
Haller O., Stertz S., Kochs G.;
"The Mx GTPase family of interferon-induced antiviral proteins.";
Microbes Infect. 9:1636-1643(2007).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH DDX39A AND DDX39B.
PubMed=21859714; DOI=10.1074/jbc.M111.251843;
Wisskirchen C., Ludersdorfer T.H., Mueller D.A., Moritz E.,
Pavlovic J.;
"Interferon-induced antiviral protein MxA interacts with the cellular
RNA helicases UAP56 and URH49.";
J. Biol. Chem. 286:34743-34751(2011).
[8]
FUNCTION.
PubMed=21651940; DOI=10.1016/j.vaccine.2011.05.069;
Frensing T., Seitz C., Heynisch B., Patzina C., Kochs G., Reichl U.;
"Efficient influenza B virus propagation due to deficient interferon-
induced antiviral activity in MDCK cells.";
Vaccine 29:7125-7129(2011).
[9]
RESISTANCE TO INFLUENZA VIRUS.
PubMed=22190720; DOI=10.1128/JVI.06156-11;
Cilloniz C., Pantin-Jackwood M.J., Ni C., Carter V.S., Korth M.J.,
Swayne D.E., Tumpey T.M., Katze M.G.;
"Molecular signatures associated with Mx1-mediated resistance to
highly pathogenic influenza virus infection: mechanisms of survival.";
J. Virol. 86:2437-2446(2012).
-!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
activity against influenza A virus, (IAV), influenza B virus (IBV)
and Thogoto virus (THOV). Inhibits FLUAV by interfering with the
process of primary transcription, probably by affecting the viral
polymerase function. {ECO:0000269|PubMed:17652381,
ECO:0000269|PubMed:21651940}.
-!- SUBUNIT: Homooligomer. 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 (By
similarity). Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and
TRPC7 (By similarity). Interacts with HSPA5 (By similarity).
Interacts with TUBB/TUBB5 (By similarity). Interacts with DDX39A
and DDX39B. {ECO:0000250, ECO:0000269|PubMed:21859714}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21859714}.
Nucleus {ECO:0000269|PubMed:21859714}. Endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane
protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side
{ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to
negatively charged phospholipids. Colocalizes with CCHFV protein N
in the perinuclear region. {ECO:0000250|UniProtKB:P20591}.
-!- INDUCTION: By type I and type III interferons.
{ECO:0000269|PubMed:18062906}.
-!- DOMAIN: The C-terminal GTPase effector domain (GED) is involved in
oligomerization and viral target recognition. {ECO:0000250}.
-!- DOMAIN: The middle domain mediates self-assembly and
oligomerization. {ECO:0000250}.
-!- PTM: ISGylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M12279; AAA39776.1; -; mRNA.
EMBL; M21117; AAA39777.1; -; Genomic_DNA.
EMBL; M21105; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21106; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21107; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21108; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21109; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21110; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21111; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21112; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21113; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21114; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21115; AAA39777.1; JOINED; Genomic_DNA.
EMBL; M21116; AAA39777.1; JOINED; Genomic_DNA.
EMBL; BC011113; AAH11113.1; -; mRNA.
PIR; A31203; A31203.
RefSeq; NP_034976.1; NM_010846.1.
UniGene; Mm.33996; -.
ProteinModelPortal; P09922; -.
SMR; P09922; -.
iPTMnet; P09922; -.
PhosphoSitePlus; P09922; -.
MaxQB; P09922; -.
PRIDE; P09922; -.
GeneID; 17857; -.
KEGG; mmu:17857; -.
UCSC; uc008adf.1; mouse.
CTD; 4599; -.
MGI; MGI:97243; Mx1.
HOVERGEN; HBG008788; -.
InParanoid; P09922; -.
PRO; PR:P09922; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MX1; -.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; TAS:MGI.
GO; GO:0003924; F:GTPase activity; TAS:MGI.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:0009615; P:response to virus; IMP:UniProtKB.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11566; PTHR11566; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
1: Evidence at protein level;
Antiviral defense; Complete proteome; Cytoplasm;
Endoplasmic reticulum; GTP-binding; Immunity; Innate immunity;
Membrane; Nucleotide-binding; Nucleus; Reference proteome;
Ubl conjugation.
CHAIN 1 631 Interferon-induced GTP-binding protein
Mx1.
/FTId=PRO_0000206593.
DOMAIN 33 306 Dynamin-type G.
DOMAIN 543 631 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 43 50 GTP. {ECO:0000255}.
NP_BIND 144 148 GTP. {ECO:0000255}.
NP_BIND 213 216 GTP. {ECO:0000255}.
REGION 35 306 GTPase domain. {ECO:0000250}.
REGION 307 332 Bundle signaling element (BSE).
{ECO:0000250}.
REGION 332 499 Middle domain. {ECO:0000250}.
REGION 333 601 Stalk. {ECO:0000250}.
REGION 520 522 Critical for lipid-binding.
{ECO:0000250}.
MUTAGEN 47 47 S->C: No effect on viral infection.
{ECO:0000269|PubMed:8411374}.
MUTAGEN 49 49 K->A,M: Loss of protection against viral
infection. {ECO:0000269|PubMed:8411374}.
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


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