MX1_EUMJU
ID MX1_EUMJU Reviewed; 658 AA.
AC Q4ADG8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Interferon-induced GTP-binding protein Mx1;
DE AltName: Full=Myxoma resistance protein 1;
DE AltName: Full=Myxovirus resistance protein 1;
GN Name=MX1; Synonyms=MX;
OS Eumetopias jubatus (Steller sea lion) (Phoca jubata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Otariidae; Eumetopias.
OX NCBI_TaxID=34886;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Sakamoto A., Seyama T., Ueda J., Watanabe T.;
RT "Identification of Mx cDNAs in sea mammals.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Oligomerizes into multimeric filamentous or
CC ring-like structures by virtue of its stalk domain. Oligomerization is
CC critical for GTPase activity, protein stability, and recognition of
CC viral target structures (By similarity). Interacts with TRPC1, TRPC3,
CC TRPC4, TRPC5, TRPC6 and TRPC7 (By similarity). Interacts with HSPA5 (By
CC similarity). Interacts with TUBB/TUBB5 (By similarity). Interacts with
CC DDX39A and DDX39B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region
CC {ECO:0000250}. Note=Binds preferentially to negatively charged
CC phospholipids. {ECO:0000250}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:18062906}.
CC -!- DOMAIN: The C-terminal GTPase effector domain (GED) is involved in
CC oligomerization and viral target recognition. {ECO:0000250}.
CC -!- DOMAIN: The middle domain mediates self-assembly and oligomerization.
CC {ECO:0000250}.
CC -!- PTM: ISGylated. {ECO:0000250}.
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; AB222179; BAE16330.1; -; mRNA.
DR AlphaFoldDB; Q4ADG8; -.
DR SMR; Q4ADG8; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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 Acetylation; Antiviral defense; Cytoplasm; Endoplasmic reticulum;
KW GTP-binding; Immunity; Innate immunity; Membrane; Nucleotide-binding;
KW Ubl conjugation.
FT CHAIN 1..658
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000319952"
FT DOMAIN 65..338
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 570..658
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..82
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 100..102
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 176..179
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 245..248
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 277..280
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 339..364
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 364..531
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 365..628
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 551..554
FT /note="Critical for lipid-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 176..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 245..248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P20591"
SQ SEQUENCE 658 AA; 75103 MW; 1525251C4366C4FA CRC64;
MVNSKGKITD SDPGSSHLLL NGLADKAGKN QDTEPENSLC SQYEEKVRPC IDLIDSLRAL
GVEQDLALPA IAVIGDQSSG KSSVLEALSG VALPRGSGIV TRCPLVLKLK KLLNKDEWRG
KVSYQDFEME ISDPSEVEVE INKAQNAIAG EGQGISHELI SLEVSSPHVP DLTLIDLPGI
TRVAVGNQPA DIGHQTKKLI KKYILKQETI NLVVVPCNVD IATTEALSMA EEVDPDGDRT
IGILTKPDLV DRGTESKVVD VAQNLVCHLK KGYMIVKCRG QQDIQDQVTL TEALQKERDF
FEDHPHFRVL LEEGRATVPC LADRLTSELI THICKTLPLL ENQIKENYEK ITEELQKYGS
DVPEEEHEKM FFLIEKINAF NHDITSLTEG EEFVGEDECR LFTKIRNEFH KWSLVIEKRF
QRGYKAICKQ IERFENRYRG RELPGFVNYK TFEIIIKQQI KELEEPAVYM LHTITDMVQA
AFTDISEANF AEFFNLYRTT KSKIEDIKFE LEKEAEKSIR LHFQMEQIVY CQDQVYQCAL
QRVREESDKG KDRKINSMCS KEVSSVNISL SDIFEHLLAY RQEATNRISS HIPLIIQYFI
LQVYGQKLQK DMLLLLHDKD THNWLLKERS DTSDKRKLLK ERLARLAQAR RRLAKFPG
