MX1_ONCMY
ID MX1_ONCMY Reviewed; 621 AA.
AC Q91192;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Interferon-induced GTP-binding protein Mx1;
DE Short=RBTMx1;
DE AltName: Full=Interferon-inducible Mx protein 1;
GN Name=mx1; Synonyms=mx;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gonad;
RX PubMed=8528941; DOI=10.1089/jir.1995.15.691;
RA Trobridge G.D., Leong J.-A.;
RT "Characterization of a rainbow trout Mx gene.";
RL J. Interferon Cytokine Res. 15:691-702(1995).
RN [2]
RP 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 [3]
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=Exhibits cytoplasmic staining in a large globular pattern
CC surrounding the nucleus.
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; U30253; AAA87839.1; -; mRNA.
DR RefSeq; NP_001165372.1; NM_001171901.1.
DR AlphaFoldDB; Q91192; -.
DR SMR; Q91192; -.
DR GeneID; 100335041; -.
DR KEGG; omy:100335041; -.
DR CTD; 100335041; -.
DR OrthoDB; 494748at2759; -.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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..621
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000206604"
FT DOMAIN 31..304
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 535..621
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 621 AA; 70641 MW; 3C7E2BB1AE348521 CRC64;
MNNTLNQHYE EKVRPCIDLI DSLRSLGVEK DLALPAIAVI GDQSSGKSSV LEALSGVALP
RGSGIVTRCP LELKMKRKKE GEEWHGKISY QDHEEEIEDP SDVEKKIREA QDEMAGVGVG
ISDDLISLEI GSPDVPDLTL IDLPGIARVA VKGQPENIGE QIKRLIRKFI MKQETISLVV
VPCNVDIATT EALKMAQEVD PEGERTLGIL TKPDLVDKGT EETVVDIVHN EVIHLTKGYM
IVKCRGQKEI MERVSLTEAT EREKAFFKEH AHLSTLYDEG HATIPKLAEK LTLELVHHIE
KSLPRLEEQI EAKLSETHAE LERYGTGPPE DSAERLYFLI DKVTAFTQDA INLSTGEEMK
SGVRLNVFST LRKEFGKWKL HLERSGEIFN QRIEGEVDDY EKTYRGRELP GFINYKTFEV
MVKDQIKQLE GPAVKKLKEI SDAVRKVFLL LAQSSFTGFP NLLKSAKTKI EAIKQVNEST
AESMLRTQFK MELIVYTQDS TYSHSLCERK REEDEDQPLT EIRSTIFSTD NHATLQEMML
HLKSYYWISS QRLADQIPMV IRYLVLQEFA SQLQREMLQT LQEKDNIEQL LKEDIDIGSK
RAALQSKLKR LMKARSYLVE F
