MX2_PIG
ID MX2_PIG Reviewed; 711 AA.
AC A7VK00;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE AltName: Full=Myxovirus resistance protein 2;
GN Name=MX2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=18977535; DOI=10.1016/j.molimm.2008.09.019;
RA Morozumi T., Naito T., Lan P.D., Nakajima E., Mitsuhashi T., Mikawa S.,
RA Hayashi T., Awata T., Uenishi H., Nagata K., Watanabe T., Hamasima N.;
RT "Molecular cloning and characterization of porcine Mx2 gene.";
RL Mol. Immunol. 46:858-865(2009).
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 influenza virus A (FLUAV).
CC {ECO:0000269|PubMed:18977535}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:18977535}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18977535}.
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; AB259856; BAF76735.1; -; Genomic_DNA.
DR AlphaFoldDB; A7VK00; -.
DR SMR; A7VK00; -.
DR STRING; 9823.ENSSSCP00000012857; -.
DR PaxDb; A7VK00; -.
DR PeptideAtlas; A7VK00; -.
DR PRIDE; A7VK00; -.
DR Ensembl; ENSSSCT00000060954; ENSSSCP00000055951; ENSSSCG00000012076.
DR Ensembl; ENSSSCT00015015781; ENSSSCP00015006145; ENSSSCG00015011655.
DR Ensembl; ENSSSCT00015015968; ENSSSCP00015006216; ENSSSCG00015011655.
DR Ensembl; ENSSSCT00025072779; ENSSSCP00025031534; ENSSSCG00025052147.
DR Ensembl; ENSSSCT00030057799; ENSSSCP00030026302; ENSSSCG00030041391.
DR Ensembl; ENSSSCT00035110112; ENSSSCP00035047932; ENSSSCG00035080268.
DR Ensembl; ENSSSCT00045047167; ENSSSCP00045032749; ENSSSCG00045027374.
DR Ensembl; ENSSSCT00050072275; ENSSSCP00050031078; ENSSSCG00050053075.
DR Ensembl; ENSSSCT00055012853; ENSSSCP00055010108; ENSSSCG00055006455.
DR Ensembl; ENSSSCT00065021442; ENSSSCP00065008683; ENSSSCG00065016129.
DR Ensembl; ENSSSCT00070018946; ENSSSCP00070015739; ENSSSCG00070009638.
DR Ensembl; ENSSSCT00070018958; ENSSSCP00070015751; ENSSSCG00070009638.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000163266; -.
DR InParanoid; A7VK00; -.
DR OMA; KETMFFQ; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Chromosome 13.
DR Bgee; ENSSSCG00000012076; Expressed in penis and 41 other tissues.
DR ExpressionAtlas; A7VK00; baseline and differential.
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; IDA:UniProtKB.
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_0000319959"
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..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..88
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 62..85
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 711 AA; 80327 MW; 04E23981962299FB CRC64;
MPKPRMSWPY QRHRQASSPP HPHKEMNFFP QQPLPLGAGP GQMTFPLNWQ MGGKDLTKGL
NMLTLSPQQP GGKSGQQTSK GPENNLYSPF EEKVRPCIDL IDSLRALGVE QDLALPTIAV
IGDQSSGKSS VLEALSGVPL PRGSGIITRC PLALRLKKKE CPWQGRISYR KVELQLQDPS
QVEREIRKAQ DAIAGSGVGI SHELISLEVT SPEVPDLTLI DLPGITRVAV GNQPQDIGLQ
IKALIRKYIQ EQQTINLVVV PCNVDIATTE ALRMAQEVDP EGDRTIGILT KPDLVDTGAE
KVVLNVMQNL TYHLKKGYMI VKCRGQQEIL NKLSLAEATK REIAFFHSHP HFRILLEEGK
ATVPRLAERL TVELIGHISK SLPLLFSQIK EIHQSATEEL RLCGASVPSN DADKMFFLIE
KIKVFNQDIE NLAEGEEIVK EKEARLYNKI REEFKSWIVT LDCNSKKVKN IIHEEVSKYD
RQYRGKELMG FVSYKTFESI VRQYLEELVD PALGMLQTVV EIVRQTFSDT AQKNFGEFSN
LNQTTQNKVD SIAARAAERA EGLIRLQFRM EQLVFCQDDI YRVDLKAVRE ELFNPVAEHP
QSLQLRLPFV NGPSPVSSIT EIGVHVNAYF MGTSQRLANQ IPFIIQYCVL QESRDHLQKA
MMQMLQGREQ YSWLLQEESH TSAKRHFLKE KIHRLAEARH TLSKFAQSLQ G
