ID T2HWL0_PIG Unreviewed; 711 AA.
AC T2HWL0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Interferon-induced GTP-binding protein Mx2 {ECO:0000256|ARBA:ARBA00039835};
DE AltName: Full=Myxovirus resistance protein 2 {ECO:0000256|ARBA:ARBA00042030};
GN Name=MX2 {ECO:0000313|EMBL:BAN84466.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:BAN84466.1};
RN [1] {ECO:0000313|EMBL:BAN84466.1}
RP NUCLEOTIDE SEQUENCE.
RA Sasaki K., Tungtrakoolsub P., Morozumi T., Uenishi H., Kawahara M.,
RA Watanabe T.;
RT "A single nucleotide polymorphism of porcine MX2 gene provides antiviral
RT activity against vesicular stomatitis virus.";
RL Immunogenetics 66:25-32(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR EMBL; AB854070; BAN84466.1; -; mRNA.
DR AlphaFoldDB; T2HWL0; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF46; INTERFERON-INDUCED GTP-BINDING PROTEIN MX2; 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; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00023118};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU003932};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003932}; Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 112..383
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 619..710
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
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 COMPBIAS 62..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 80286 MW; 9C8F0084C3D1D531 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 EQQAINLVVV PCNVDIATTE ALRMAQEVDP EGDRTIGILT KPDLVDTGAE
KVVLNVMQNL TYHLKKGYMI VKCRGQQEIL NKLSLAEATK REIAFFHSHP HFRILLEEGK
ATVPRLAERL TVELIGRISK SLPLLFSQIK EIHQSATEEL RLCGASVPSN DADKMFFLIE
KIKVFNQDIE NLAEGEEIVK EKEARLYNKI REEFKSWIVT LDCNSKKVKN IIHEEVSKYD
RQYRGKELMG FVSYKTFESI VRQYLEELVD PALGMLQAVV EIVRQTFSDT AQKNFGEFSN
LNQTTQNKVD SIAARAAERA EGLIRLQFRM EQLVFCQDDI YRVDLKAVRE ELFNPVAEHP
QSLQLRLPFV NGPSPVSSIT EIGVHVNAYF MGTSQRLANQ IPFIIQYCVL QESRDHLQKA
MMQMLQGREQ YSWLLQEESH TSAKRHFLKE KIHRLAEARH TLSKFAQSLQ G
//