MX2_CANLF
ID MX2_CANLF Reviewed; 711 AA.
AC Q9N0Y2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE AltName: Full=Myxovirus resistance protein 2;
GN Name=MX2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Vice S.J., Gordy P.W., Bowen R.A.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15767791; DOI=10.1089/jir.2005.25.169;
RA Nakamura T., Asano A., Okano S., Ko J.H., Kon Y., Watanabe T., Agui T.;
RT "Intracellular localization and antiviral property of canine Mx proteins.";
RL J. Interferon Cytokine Res. 25:169-173(2005).
RN [3]
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:15767791}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15767791}. Nucleus
CC {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; AF239824; AAF44685.1; -; mRNA.
DR RefSeq; NP_001003133.1; NM_001003133.1.
DR AlphaFoldDB; Q9N0Y2; -.
DR SMR; Q9N0Y2; -.
DR STRING; 9615.ENSCAFP00000051654; -.
DR PaxDb; Q9N0Y2; -.
DR Ensembl; ENSCAFT00845053398; ENSCAFP00845041949; ENSCAFG00845030104.
DR GeneID; 403744; -.
DR CTD; 4600; -.
DR VEuPathDB; HostDB:ENSCAFG00845030104; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000163266; -.
DR HOGENOM; CLU_008964_8_0_1; -.
DR InParanoid; Q9N0Y2; -.
DR OMA; PCIRDEE; -.
DR OrthoDB; 494748at2759; -.
DR TreeFam; TF331484; -.
DR Reactome; R-CFA-1169408; ISG15 antiviral mechanism.
DR Proteomes; UP000002254; Chromosome 31.
DR Bgee; ENSCAFG00000010167; Expressed in adrenal cortex and 48 other tissues.
DR ExpressionAtlas; Q9N0Y2; differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
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; 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: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; Reference proteome.
FT CHAIN 1..711
FT /note="Interferon-induced GTP-binding protein Mx2"
FT /id="PRO_0000206597"
FT DOMAIN 115..387
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 623..711
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
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 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"
FT CONFLICT 705
FT /note="A -> T (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 81442 MW; EA143DBB520024D3 CRC64;
MSKAHGSRPY RRHNVVIPRQ QPEKEMNFVQ QQPPPSDAAA RQMMYPPNCQ VGVQDPVYLA
KEFNLLTLNP QQLEGSRHQQ MAKGPEKSLY SQYEQKVRPC IDLVDSLRAL GVEQDLALPA
IAVIGDQSSG KSSVLEALSG VALPRGSGIV TRCPLVLKLK RDPHKAWRGR ISYRKTELQF
QDPSQVEKEI RQAQNIIAGQ GLGISHELIS LEITSPEVPD LTLIDLPGIT RVAVGNQPQD
IGVQIKALIK NYIQKQETIN LVVVPCNVDI ATTEALSMAQ EVDPNGDRTI GVLTKPDLVD
RGTEKTVVNV AQNLTYHLQK GYMIVRCRGQ EEITNQLSLA EATEKERMFF QTHPYFRALL
EEGKATVPCL AERLTKELIL HINKSLPLLE KQIRESHQRA TDELHQCGDS IPSNEADKMF
FLIEKIKLFN QDIDKLIEGE EIVKKNETRL YNKIREEFEH WALVLTANTQ KVKNIVSEEV
SVYEKQYRGK ELLGFVNYKT FETIVHQYIE QLVEPALTML RKTIEIVWQA FTDTAKKHFS
VFSNLSQTIQ NKIEDIKTRQ AETAENLIRL QFRMEQLVYC QDQIYSVVLR KVRKEVFNPA
GKAAQDLQLK FPFPKDLPSM SSNDEIGVHL NAYFLETSKR LANQIPFIIQ YFVLQENGSC
LQKAMMQILQ EREQYSWLLQ EHADTSAKRR FLKEKIYRLA QARRALYMFF S
