MX2_BUBBU
ID MX2_BUBBU Reviewed; 710 AA.
AC A0MWD1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE AltName: Full=Myxovirus resistance protein 2;
GN Name=MX2;
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=17119954; DOI=10.1007/s00251-006-0167-5;
RA Babiker H.A.E., Nakatsu Y., Yamada K., Yoneda A., Takada A., Ueda J.,
RA Hata H., Watanabe T.;
RT "Bovine and water buffalo Mx2 genes: polymorphism and antiviral activity.";
RL Immunogenetics 59:59-67(2007).
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:17119954}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF052266; ABK41143.1; -; mRNA.
DR RefSeq; NP_001277778.1; NM_001290849.1.
DR AlphaFoldDB; A0MWD1; -.
DR SMR; A0MWD1; -.
DR GeneID; 102399001; -.
DR KEGG; bbub:102399001; -.
DR CTD; 4600; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; Nucleus.
FT CHAIN 1..710
FT /note="Interferon-induced GTP-binding protein Mx2"
FT /id="PRO_0000319958"
FT DOMAIN 112..383
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 619..710
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..129
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 147..149
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 221..224
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 290..293
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 322..325
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COMPBIAS 41..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 221..225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 290..293
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 710 AA; 81335 MW; 6FEE13E2FB983097 CRC64;
MSLSFRPLKY KRHTQTSTPH HPKQDIYFHE QPPGPPLGQT MSPPQWQVEE SNPGFLPNNF
SQLNLDPQQP EANGGQQRSK GPENNLYRKY EEKVRPCIDL IDSLRALGVE QDLALPAIAV
IGDQSSGKSS VLEALSGVAL PRGSGIITRC PLVLKLTKRE CEWTGKITYR NITQQLQNPS
EVEWEIRRAQ NIIAGNGRGI SHELINLEVT SPDVPDLTLI DLPGITRVAV ENQPQDIGLQ
IKALIIQRQE TINLVVVPCN VDIATKKYTE ALSMAQEVDP DGDRTIGILT KPDLVDKGTE
KGVLKVMQNL TYHLKKGYMI VKCRGQQDIT NKLSLAEATR KETMFFETHP YFRVLLDEGK
ATMPLLAERL TTELIWHINK SLPLLENQIK EKHQRATEEL QQYGDDIPSD EGDKMFFLIE
KIKVFNEDIG KLIEGEEIVM ETESRLCNKI REEFTSWILI LTTNIEKVKS ILNEEVSKYE
KKYRGKELLG FVNYKTFETV VKHYLGQLID PALKMLQKAM EIVWQTFKDT AKKHFAEFCN
LHQTVQNKIE DIKTKQMAEA ANLIQLQFKM EKLVFCQDQI YGVVLNKVRE DIFNSMGKAS
ETPQSKQPFL NDQSSISSIV EIGVHLNAYF METSKRLANQ IPFIIQYFML QENGDKVQKA
MMQLLQDTQH YSWLLQEQSD TATKRKFLKE KIFRLTQAQQ ALYEFPHFKG