MX2_MOUSE
ID MX2_MOUSE Reviewed; 655 AA.
AC Q9WVP9; Q922L4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE AltName: Full=Myxovirus resistance protein 2;
GN Name=Mx2;
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], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=NJL;
RX PubMed=10233954; DOI=10.1128/jvi.73.6.4925-4930.1999;
RA Jin H., Takada A., Kon Y., Haller O., Watanabe T.;
RT "Identification of the murine Mx2 gene: interferon-induced expression of
RT the Mx2 protein from the feral mouse gene confers resistance to vesicular
RT stomatitis virus.";
RL J. Virol. 73:4925-4930(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP FUNCTION.
RX PubMed=11266216; DOI=10.1007/s007050170189;
RA Jin H.K., Yoshimatsu K., Takada A., Ogino M., Asano A., Arikawa J.,
RA Watanabe T.;
RT "Mouse Mx2 protein inhibits hantavirus but not influenza virus
RT replication.";
RL Arch. Virol. 146:41-49(2001).
RN [4]
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).
CC -!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
CC activity against vesicular stomatitis virus (VSV) and Hantaan virus
CC (HNTV). {ECO:0000269|PubMed:10233954, ECO:0000269|PubMed:11266216}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10233954}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:10233954, ECO:0000269|PubMed:18062906}.
CC -!- MISCELLANEOUS: The Mx2 gene is non-functional in all laboratory mouse
CC strains examined. It is functional in feral strains.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; AB029920; BAA82593.1; -; mRNA.
DR EMBL; BC007127; AAH07127.1; -; mRNA.
DR RefSeq; NP_038634.1; NM_013606.1.
DR AlphaFoldDB; Q9WVP9; -.
DR SMR; Q9WVP9; -.
DR IntAct; Q9WVP9; 2.
DR MINT; Q9WVP9; -.
DR iPTMnet; Q9WVP9; -.
DR PhosphoSitePlus; Q9WVP9; -.
DR jPOST; Q9WVP9; -.
DR MaxQB; Q9WVP9; -.
DR PaxDb; Q9WVP9; -.
DR PRIDE; Q9WVP9; -.
DR ProteomicsDB; 286089; -.
DR DNASU; 17858; -.
DR Ensembl; ENSMUST00000024112; ENSMUSP00000024112; ENSMUSG00000023341.
DR GeneID; 17858; -.
DR KEGG; mmu:17858; -.
DR CTD; 4600; -.
DR MGI; MGI:97244; Mx2.
DR VEuPathDB; HostDB:ENSMUSG00000023341; -.
DR GeneTree; ENSGT00940000155686; -.
DR HOGENOM; CLU_008964_8_0_1; -.
DR InParanoid; Q9WVP9; -.
DR OMA; FHKWSAV; -.
DR PhylomeDB; Q9WVP9; -.
DR TreeFam; TF331484; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR BioGRID-ORCS; 17858; 0 hits in 19 CRISPR screens.
DR PRO; PR:Q9WVP9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9WVP9; protein.
DR Bgee; ENSMUSG00000023341; Expressed in small intestine Peyer's patch and 68 other tissues.
DR Genevisible; Q9WVP9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; TAS:MGI.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0034340; P:response to type I interferon; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA: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 2: Evidence at transcript level;
KW Antiviral defense; Cytoplasm; GTP-binding; Immunity; Innate immunity;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..655
FT /note="Interferon-induced GTP-binding protein Mx2"
FT /id="PRO_0000206599"
FT DOMAIN 60..333
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 567..655
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..77
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 95..97
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 171..174
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 240..243
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 272..275
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 542..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 171..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 240..243
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 326
FT /note="S -> L (in Ref. 1; BAA82593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 74292 MW; 9F58BD9D0E9349C5 CRC64;
MVLSTEENTG VDSVNLPSGE TGLGEKDQES VNNLCSQYEE KVRPCIDLID SLRALGVEQD
LALPAIAVIG DQSSGKSSVL EALSGVALPR GSGIVTRCPL VLKLRKLNEG EEWRGKVSYD
DIEVELSDPS EVEEAINKGQ NFIAGVGLGI SDKLISLDVS SPNVPDLTLI DLPGITRVAV
GNQPADIGRQ IKRLIKTYIQ KQETINLVVV PSNVDIATTE ALSMAQEVDP EGDRTIGILT
KPDLVDRGTE DKVVDVVRNL VYHLKKGYMI VKCRGQQDIQ EQLSLTEALQ NEQIFFKEHP
HFRVLLEDGK ATVPCLAERL TAELISHICK SLPLLENQIK ESHQSASEEL QKYGMDIPED
DSEKTFFLIE KINAFNQDIT ALVQGEENVA EGECRLFTRL RKEFLSWSKE IEKNFAKGYA
VLYNEVWAFE KQYRGRELPG FVNYKTFENI IRRQIKTLEE PAIEMLHTVT EIVRAAFTSV
SEKNFSEFYN LHRTTKSKLE DIRLEQEKEA EMSIRLHFKM EQIIYCQDQI YRGALQKVRE
EEAEEEKKTK HGTSSSSQSQ DLQTSSMAEI FQHLNAYRQE AHNRISSHVP LIIQYFILKM
FAERLQKGML QLLQDKDSCS WLLKEQSDTS EKRKFLKERL ARLAQARRRL AKFPG
