MX1_PIG
ID MX1_PIG Reviewed; 663 AA.
AC P27594; Q1AHC4; Q75PY7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 122.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=1578186; DOI=10.1089/jir.1992.12.119;
RA Mueller M., Brem G.;
RT "Molecular cloning of porcine Mx cDNAs: new members of a family of
RT interferon-inducible proteins with homology to GTP-binding proteins.";
RL J. Interferon Res. 12:119-129(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS, AND SUBCELLULAR LOCATION.
RX PubMed=17203407; DOI=10.1007/s10528-006-9045-y;
RA Nakajima E., Morozumi T., Tsukamoto K., Watanabe T., Plastow G.,
RA Mitsuhashi T.;
RT "A naturally occurring variant of porcine Mx1 associated with increased
RT susceptibility to influenza virus in vitro.";
RL Biochem. Genet. 45:11-24(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16738935; DOI=10.1007/s00251-006-0109-2;
RA Thomas A.V., Palm M., Broers A.D., Zezafoun H., Desmecht D.J.;
RT "Genomic structure, promoter analysis, and expression of the porcine (Sus
RT scrofa) Mx1 gene.";
RL Immunogenetics 58:383-389(2006).
RN [4]
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).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19109387; DOI=10.1128/jvi.00781-08;
RA Netherton C.L., Simpson J., Haller O., Wileman T.E., Takamatsu H.H.,
RA Monaghan P., Taylor G.;
RT "Inhibition of a large double-stranded DNA virus by MxA protein.";
RL J. Virol. 83:2310-2320(2009).
RN [6]
RP FUNCTION.
RX PubMed=20167191; DOI=10.1051/vetres/2010001;
RA Palm M., Garigliany M.M., Cornet F., Desmecht D.;
RT "Interferon-induced Sus scrofa Mx1 blocks endocytic traffic of incoming
RT influenza A virus particles.";
RL Vet. Res. 41:29-29(2010).
CC -!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
CC activity against influenza A virus, (IAV). Inhibits IAV replication by
CC decreasing or delaying NP synthesis and by blocking endocytic traffic
CC of incoming virus particles. {ECO:0000269|PubMed:20167191}.
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:0000269|PubMed:17203407,
CC ECO:0000269|PubMed:19109387}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}.
CC Note=Binds preferentially to negatively charged phospholipids.
CC {ECO:0000250|UniProtKB:P20591}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:1578186, 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; M65087; AAA31090.1; -; mRNA.
DR EMBL; AB164037; BAD11809.1; -; mRNA.
DR EMBL; DQ095779; AAZ30034.1; -; mRNA.
DR PIR; I46611; I46611.
DR RefSeq; NP_999226.1; NM_214061.1.
DR AlphaFoldDB; P27594; -.
DR SMR; P27594; -.
DR STRING; 9823.ENSSSCP00000029166; -.
DR PaxDb; P27594; -.
DR PeptideAtlas; P27594; -.
DR PRIDE; P27594; -.
DR GeneID; 397128; -.
DR KEGG; ssc:397128; -.
DR CTD; 4599; -.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; P27594; -.
DR OrthoDB; 494748at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IMP:AgBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IMP:AgBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0071357; P:cellular response to type I interferon; IMP:AgBase.
DR GO; GO:0051607; P:defense response to virus; IMP:AgBase.
DR GO; GO:0016197; P:endosomal transport; IMP:AgBase.
DR GO; GO:1901253; P:negative regulation of intracellular transport of viral material; IMP:AgBase.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP: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 Acetylation; Antiviral defense; Cytoplasm; Endoplasmic reticulum;
KW GTP-binding; Immunity; Innate immunity; Membrane; Nucleotide-binding;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..663
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000206594"
FT DOMAIN 67..341
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 575..663
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 77..84
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 102..104
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 179..182
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 248..251
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 280..283
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 342..367
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 367..534
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 368..633
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 551..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..558
FT /note="Critical for lipid-binding"
FT /evidence="ECO:0000250"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 179..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 248..251
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"
FT VARIANT 566
FT /note="Missing (in strain: Meishan; no effect)"
FT VARIANT 656..663
FT /note="RRLAKFPG -> QVPRLNRTLQAARGLQGTSPGNEDQPPSLTD (in
FT strain: Landrace; loss of function)"
FT CONFLICT 5
FT /note="S -> N (in Ref. 3; AAZ30034)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="E -> D (in Ref. 3; AAZ30034)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="A -> G (in Ref. 3; AAZ30034)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="R -> K (in Ref. 3; AAZ30034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 75587 MW; DA4FACC050B12E4B CRC64;
MVYSSCESKE PDSVSASNHL LLNGNDELVE KSHKTGPENN LYSQYEEKVR PCIDLIDSLR
ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLVLK LKKLVNEEDE
WKGKVSYRDS EIELSDASQV EKEVSAAQIA IAGEGVGISH ELISLEVSSP HVPDLTLIDL
PGITRVAVGN QPYDIEYQIK SLIKKYICKQ ETINLVVVPC NVDIATTEAL RMAQEVDPEG
DRTIGILTKP DLVDKGTEDK IVDVARNLVF HLKKGYMIVK CRGQQDIQEQ LSLAKALQKE
QAFFENHAHF RDLLEEGRAT IPCLAERLTS ELIMHICKTL PLLENQIKES HQKITEELQK
YGSDIPEDES GKMFFLIDKI DAFNSDITAL IQGEELVVEY ECRLFTKMRN EFCRWSAVVE
KNFKNGYDAI CKQIQLFENQ YRGRELPGFV NYKTFETIIK KQVSVLEEPA VDMLHTVTDL
VRLAFTDVSE TNFNEFFNLH RTAKSKIEDI KLEQEKEAET SIRLHFQMEQ IVYCQDQVYR
GALQKVREKE AEEEKNRKSN QYFLSSPAPS SDPSIAEIFQ HLIAYHQEVG KRISSHIPLI
IQFFILRTFG QQLQKSMLQL LQNKDQYDWL LRERSDTSDK RKFLKERLMR LTQARRRLAK
FPG
