ID   MX2_MACMU               Reviewed;         715 AA.
AC   A1E2I5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE   AltName: Full=Myxovirus resistance protein 2;
GN   Name=MX2;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Miller C.J., Dutra J.C.;
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- INDUCTION: By type I and type III interferons.
CC       {ECO:0000269|PubMed:18062906}.
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; EF101562; ABK97617.1; -; mRNA.
DR   RefSeq; NP_001073164.1; NM_001079696.1.
DR   RefSeq; XP_014988327.1; XM_015132841.1.
DR   RefSeq; XP_014988328.1; XM_015132842.1.
DR   RefSeq; XP_014988329.1; XM_015132843.1.
DR   AlphaFoldDB; A1E2I5; -.
DR   SMR; A1E2I5; -.
DR   Ensembl; ENSMMUT00000025665; ENSMMUP00000024010; ENSMMUG00000044257.
DR   Ensembl; ENSMMUT00000093227; ENSMMUP00000061903; ENSMMUG00000044257.
DR   Ensembl; ENSMMUT00000100424; ENSMMUP00000070693; ENSMMUG00000044257.
DR   Ensembl; ENSMMUT00000105314; ENSMMUP00000068364; ENSMMUG00000044257.
DR   GeneID; 780935; -.
DR   KEGG; mcc:780935; -.
DR   CTD; 4600; -.
DR   VEuPathDB; HostDB:ENSMMUG00000044257; -.
DR   VGNC; VGNC:81723; MX2.
DR   GeneTree; ENSGT00940000163266; -.
DR   InParanoid; A1E2I5; -.
DR   OrthoDB; 494748at2759; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000044257; Expressed in spleen and 21 other tissues.
DR   ExpressionAtlas; A1E2I5; baseline.
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:0005643; C:nuclear pore; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IEA:Ensembl.
DR   GO; GO:0035455; P:response to interferon-alpha; IEA:Ensembl.
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; Nucleus; Reference proteome.
FT   CHAIN           1..715
FT                   /note="Interferon-induced GTP-binding protein Mx2"
FT                   /id="PRO_0000319628"
FT   DOMAIN          115..387
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          623..714
FT                   /note="GED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..132
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          150..152
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          225..228
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          294..297
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          326..329
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   COMPBIAS        1..17
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         125..132
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         225..229
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         294..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   715 AA;  82123 MW;  894CB40E7890DD4F CRC64;
     MSKAHKSWPH RRRNQFSSQR SLKKEMNFFQ QQPPPFGTVP PQMTFPPNWQ GVEKDPAFLT
     KDFNLLTLNN QPLPGNTSQP RAKGPENNLH NQYEQKVRPY IDLIDSLRAL GVEQDLALPA
     IAVIGDQSSG KSSVLEALSG VALPRGSGIV TRCPLVLKLK KQPYKAWAGR ISYQNTEIEL
     QDPGQVEKEI HKAQNVMAGN GLGISHELIS LEITSPEVPD LTIIDLPGIA RVAVGNQPRD
     IGLQIKALIK RYIQRQQTIN LVVVPCNVDI ATTEALSMAH EVDPEGDRTI GILTKPDLMD
     RGTEKSIINV VRNLTYPLKK GYMIVKCRGQ QEIINRLSLA EATKKEITFF QTHPCFRVLL
     EEGSATVPRL AERLTAELIT HIQKSLPLLE EQIRESHQKA TEELRRCGAD IPSQDADKMF
     FLIEKIKMFN QDIEKLIEGE EVVRENETRL YNKIREDFKN WIGILATNTQ KVKNIIHEEV
     EKYEKQYRGK ELLGFVNYKT FETIVHQYIQ HLVEPALSML QKAVEIIRQA FVNMAKKHFG
     EFFNLNHTVQ SKIEDIKVRH TEKAENMIQL QFRMEQIVFC QDQIYSVVVK KVREEIFNPL
     GKPSQNMKLN SHFPINESSV SSFNEIGVHL NAYFSETSTR LANQIPFIIQ YFMLRENGDS
     LQKAMMQILQ EKNRYSWLLQ EQSETATKRR MLKERIYRLT QARHALCQFS SKEIH