MX1_PHOVI
ID MX1_PHOVI Reviewed; 659 AA.
AC Q4ADG6;
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 Phoca vitulina (Harbor seal).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Phoca.
OX NCBI_TaxID=9720;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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; AB222181; BAE16332.1; -; mRNA.
DR AlphaFoldDB; Q4ADG6; -.
DR SMR; Q4ADG6; -.
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..659
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000319955"
FT DOMAIN 65..338
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 571..659
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..40
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..629
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 552..555
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 659 AA; 75288 MW; 27B32D11CA23B907 CRC64;
MVNSKGEITD SDPGSNHLLL NGLPDKAGKN QDTEPENSLC SQYEEKVRPC IDLIDSLRAL
GVEQDLALPA IAVIGDQSSG KSSVLEALSG VALPRGSGIV TRCPLVLKLK KLLNEDEWRG
KVSYQDFEME ISDPSEVEVE ISKAQNVIAG EGQGISHELI SLEVSSPHVP DLTLIDLPGI
TRVAVGNQPA DIGRQTKQLI RKYILKQETI NLVVVPCNVD IATTEALSMA QEVDPSGDRT
IGILTKPDLV DRGTESKVVD VAQNLVCHLK KGYMIVKCRG QQDIQDQVTL TEALQKERDF
FEDHPHFRVL LEEGRATVPC LADKLTSELI THICKTLPLL ENQIKENHEK ITEELKKYGS
DVPEEEHEKM FFLIEKINAF NHDINSLIEG EEFVGEDESR LFTKIRNEFH KWSCVIEKKF
QQGYKAIYKQ IEKFENRYRG RELPGFVNYK TFEIIIKQQI KELEEPAVYM LHMVTDMVQA
AFTDISEANF AEFFNLYRTT KSKIEDIKFE LEKEAEKSIR LHFQMEQIVY CQDQVYQRAL
QRVREKVADE EKNKKINSMS SEEVSSVNIS LSEIFEHLLA YRQEATNRIS SHIPLIIQYF
ILQAYGQKLQ KGMLQLLQDK DTYNWLLKER SDTSDKRKFL KERLSRLAQA RRRLAKFPG
