MX2_RAT
ID MX2_RAT Reviewed; 659 AA.
AC P18589;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE AltName: Full=Myxovirus resistance protein 2;
GN Name=Mx2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=2173790; DOI=10.1128/jvi.64.12.6263-6269.1990;
RA Meier E., Kunz G., Haller O., Arnheiter H.;
RT "Activity of rat Mx proteins against a rhabdovirus.";
RL J. Virol. 64:6263-6269(1990).
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 against vesicular stomatitis virus (VSV).
CC {ECO:0000269|PubMed:2173790}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2173790}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:18062906, ECO:0000269|PubMed:2173790}.
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; X52712; CAA36936.1; -; mRNA.
DR PIR; S11736; S11736.
DR AlphaFoldDB; P18589; -.
DR SMR; P18589; -.
DR PRIDE; P18589; -.
DR RGD; 628821; Mx2.
DR InParanoid; P18589; -.
DR Reactome; R-RNO-1169408; ISG15 antiviral mechanism.
DR PRO; PR:P18589; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; ISO:RGD.
DR GO; GO:0035455; P:response to interferon-alpha; ISO:RGD.
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..659
FT /note="Interferon-induced GTP-binding protein Mx2"
FT /id="PRO_0000206600"
FT DOMAIN 65..338
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 571..659
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 75..82
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 100..102
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 176..179
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 245..248
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 277..280
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 547..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 176..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 245..248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 659 AA; 75074 MW; 14F916C5F4117E12 CRC64;
MVLSTEENRS VDLVNLPSVP LPDGEAGVGE NNKDSLNNLC SQYEEKVRPC IDLIDSLRAL
GVEQDLALPA IAVIGDQSSG KSSVLEALSG VALPRGSGIV TRCPLVLKLK KLNQGEEWKG
KVTYDDIEVE LSDPSEVEEA INTGQNHIAG VGLGISDKLI SLDVSSPHVP DLTLIDLPGI
TRVAVGNQPA DIGRQIKRLI TNYIQKQETI NLVVVPSNVD IATTEALSMA QKVDPDGDRT
IGILTKPDLV DRGTEDKVVD VVRNLVCHLK KGYMIVKCRG QQDIQEQLSL AEALQKEQVF
FKEHPQFRAL LEDGKATVPC LAERLTMELI SHICKSLPLL ENQIKESHQS TSEELQKYGA
DIPEDENEKT LFLIEKINAF NQDITAIVEG EEIVREKECR LFTKLRKEFF LWSEEIERNF
QKGSDALYKE VYTFEMQYRG RELPGFVNYK TFENIIRRQI KTLEEPAMEM LHKVTEIVRA
AFTTVSEKNF SEFFNLHRTT KSKLEDIRLE QETEAEKSIR LHFQMEQIIY CQDQIYRKAL
QKVREEEAEE EERKHGKSRS SQSKNLQTSS MDEIFQHLNA YRQEAHNRIS SHIPLIIQYF
ILKMFAEKLQ KGMLQLLQDK DSCSWLLKEH SDTSEKRRFL KERLARLAQA QRRLAKFPG
