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MX3_ONCMY
ID   MX3_ONCMY               Reviewed;         623 AA.
AC   Q91197;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Interferon-induced GTP-binding protein Mx3;
DE            Short=RBTMx3 {ECO:0000303|PubMed:9188599, ECO:0000312|EMBL:AAC60215.1};
GN   Name=mx3 {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:AAC60215.1}
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: Cytoplasm {ECO:0000269|PubMed:9188599}.
CC       Note=Displays diffuse uniform expression throughout the cytoplasm.
CC       {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; U47946; AAC60215.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q91197; -.
DR   SMR; Q91197; -.
DR   GO; GO:0005829; C:cytosol; 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.
FT   CHAIN           1..623
FT                   /note="Interferon-induced GTP-binding protein Mx3"
FT                   /id="PRO_0000430326"
FT   DOMAIN          31..304
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          537..623
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   623 AA;  70962 MW;  7EFA55728B3D8A94 CRC64;
     MNNTLNQHYE EKVRPCIDLI DSLRSLGVEK DLALPAIAVI GDQSSGKSSV LEALSGVALP
     RGSGIVTRCP LELKMKRKRE GEEWHGKISY QDHEEEIEDP SDVEKKIREA QDEMAGVGVG
     ISDDLISLEI GSPDVPDLTL IDLPGIARVA VKGQPENIGE QIKRLIRKFI MKQETINLVV
     VPCNVDIATT EALQMAQEVD PEGERTLGIL TKPDLVDKGT EETVVDIVHN EVIHLTKGYM
     IVKCRGQKEI MERVSLTEAT EREKAFFKEH AHLSTLYDEG HATIPKLAEK LTLELVHHIE
     KSLPRLEEQI EAKLSETHAE LERYGTGPPE DSAERIYFLI DKVTAFTQDA INLSTGEELK
     SGVRLNVFST LRQEFGKWKL HLDRSGENFN QRIEGEVSNY EKTYRGRELP GFINYKTFEV
     MVKDQIKQLE EPAVKKLKEI SDAVRKVFLL LAQSSFTGFP NLLKSAKTKI EAIKQVNEST
     AESMLRTQFK MEMIVYTQDS TYSHSLSERK REEEDDRPLP TPKIRSTIFS TDNHATLQEM
     MLHLKSYYRI SSQRLADQIP MVIRYLVLQE FASQLQREML QTLQEKDNIE QLLKEDFDIG
     SKRAALQNKL KRLMKARSYL VEF
 
 
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