MX2_ONCMY
ID MX2_ONCMY Reviewed; 635 AA.
AC Q91196;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE Short=RBTMx2 {ECO:0000303|PubMed:9188599, ECO:0000312|EMBL:AAC60214.1};
GN Name=mx2 {ECO:0000303|PubMed:9188599};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC60214.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9188599; DOI=10.1128/jvi.71.7.5304-5311.1997;
RA Trobridge G.D., Chiou P.P., Leong J.A.;
RT "Cloning of the rainbow trout (Oncorhynchus mykiss) Mx2 and Mx3 cDNAs and
RT characterization of trout Mx protein expression in salmon cells.";
RL J. Virol. 71:5304-5311(1997).
RN [2] {ECO:0000305}
RP INDUCTION.
RX PubMed=17157032; DOI=10.1016/j.fsi.2006.10.009;
RA Tafalla C., Chico V., Perez L., Coll J.M., Estepa A.;
RT "In vitro and in vivo differential expression of rainbow trout
RT (Oncorhynchus mykiss) Mx isoforms in response to viral haemorrhagic
RT septicaemia virus (VHSV) G gene, poly I:C and VHSV.";
RL Fish Shellfish Immunol. 23:210-221(2007).
CC -!- FUNCTION: Does not inhibit strain RB-1 of the fish pathogen, infectious
CC hematopoietic necrosis virus (IHNV). {ECO:0000269|PubMed:9188599}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9188599}. Cytoplasm
CC {ECO:0000269|PubMed:9188599}. Note=Displays highly punctate staining of
CC the nucleus. In some cells, punctate staining is observed in both
CC nucleus and cytoplasm. {ECO:0000269|PubMed:9188599}.
CC -!- INDUCTION: By polyinosinic-polycytidylic acid (poly I:C) and viral
CC haemorrhagic septicaemia virus (VHSV) strain 07.71 in muscle, head
CC kidney, spleen and liver. {ECO:0000269|PubMed:17157032}.
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; U47945; AAC60214.1; -; mRNA.
DR RefSeq; NP_001118223.1; NM_001124751.1.
DR AlphaFoldDB; Q91196; -.
DR SMR; Q91196; -.
DR GeneID; 100137062; -.
DR KEGG; omy:100137062; -.
DR CTD; 4600; -.
DR OrthoDB; 494748at2759; -.
DR GO; GO:0005829; C:cytosol; IMP:AgBase.
DR GO; GO:0005634; C:nucleus; IMP:AgBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0034340; P:response to type I interferon; ISS:AgBase.
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 Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus.
FT CHAIN 1..635
FT /note="Interferon-induced GTP-binding protein Mx2"
FT /id="PRO_0000430325"
FT DOMAIN 31..304
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 549..635
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 41..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 66..68
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 142..145
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 211..214
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 243..246
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 41..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 142..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 211..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 72113 MW; 6868253BA6752D90 CRC64;
MNYTLNQHYE EKVRPSIDLI DSLRSLGVEK DLALPAIAVI GDQSSGKSSV LEALSGVALP
RGSGIVTRCP LELKMKRKKE GEEWHGKISY QDREEEIEDP SDVENKIRKA QDEMAGVGVG
ISDDLISLEI GSPDVPDLTL IDLPGIARVA VKGQPENIGE QIKRLIRKFI TKQETINLVV
VPCNVDIATT EALKMAQEVD PDGERTLGIL TKPDLVDKGT EETVVDIVHN EVIQLTKGYM
IVKCRGQKEI MERVSLTEAT EREKAFFKEH AHLSTLYDEG HATIPKLAEK LTLELVQHIE
KSMPRLKEQI EEKLEETRTA LEKCGTGPPE DPKERLYFLI DKVTLFTQDA INLSTGEELK
SGDINVFSTL RTEFGKWKAY VDRSGKNFNK KIEKEVADYE KRYRGRELPG FINYKTFEVI
VKDQIKQLEE PAVKKLKELS DAARKAFILL AQNSFTGFPI LLKTAKTKIE TIKQEKESTA
ESTLRTQFKM ELIVYTQDST YSSSLKKRKR EEEELEEGEL VKNNLGSWKG LPVVSVRSTV
NGLDTHATLR EMMLHLKSYY HIASQRLADQ IPMVIRYLVL QEFASQLQRE MLQTLQEKDN
IEQLLKEDID IGSKRAALQS KLKRLMKAHN YLVEF
