MX1_HORSE
ID MX1_HORSE Reviewed; 660 AA.
AC Q28379;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Interferon-induced GTP-binding protein Mx1;
DE AltName: Full=Interferon-regulated resistance GTP-binding protein MxA;
DE AltName: Full=Myxoma resistance protein 1;
DE AltName: Full=Myxovirus resistance protein 1;
GN Name=MX1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Blood;
RX PubMed=9254021; DOI=10.3109/10425179709034043;
RA Chesters P.M., Steele M., Purewal A., Edington N.;
RT "Nucleotide sequence of equine MxA cDNA.";
RL DNA Seq. 7:239-242(1997).
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|UniProtKB:P20591}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively
CC charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:18062906, ECO:0000269|PubMed:9254021}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U55216; AAC23906.1; -; mRNA.
DR RefSeq; NP_001075961.1; NM_001082492.1.
DR AlphaFoldDB; Q28379; -.
DR SMR; Q28379; -.
DR STRING; 9796.ENSECAP00000015078; -.
DR PaxDb; Q28379; -.
DR PRIDE; Q28379; -.
DR GeneID; 100034192; -.
DR KEGG; ecb:100034192; -.
DR CTD; 4599; -.
DR InParanoid; Q28379; -.
DR OrthoDB; 494748at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
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 Reference proteome; Ubl conjugation.
FT CHAIN 1..660
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000319953"
FT DOMAIN 67..340
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 572..660
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 178..181
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 247..250
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 279..282
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 341..366
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 366..533
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 367..630
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 554..557
FT /note="Critical for lipid-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 178..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 247..250
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 660 AA; 75566 MW; B49CD399714C89CB CRC64;
MVHSEAKMTR PDSASASKQQ LLNGNADIQE TNQKRSIEKN LCSQYEEKVR PCIDLIDSLR
ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLVLK LKRLVKEDEW
KGKVSYRDIE VEISNALDVE EQVRKAQNVL AGEGVGISQE LVTLEVSSPH VPDLTLIDLP
GITRVAVGNQ PADIGRQIKT LIRKYIQRQE TINLVVVPSN VDIATTEALS MAQEVDPEGD
RTIGILTKPD LVDKGTEEQV VDVVRNLICH LKKGYMIVKC RGQQDIQDRL SLAEALQREK
AFFEENPYFR GLLEEGRASV PCLAERLTTE LITHISKSLP LLENQIKESY QNLSDELQKY
GTDIPEDETE KTFFLIVKIT TFNQNITSFV QGEELVGPND TRLFNKIRQE FQKWSGVIEN
NFRKGGEAIR RQIWTFENQY RGRELPGFVN YRTFETIIKQ QIQLLEEPAI DMLHRISDLV
RDTFTKVSEK NFSEFFNLHR TTKSKLEDIK LEQENEAEKS IRLHFQMEKI VYCQDHVYRG
TLQKVRENEM EEEKKKKTIN VWGQNTSTES SMAEILEHLN AYQHEAGNRL STHIPLIIQF
FVLQTFGQQL QKSMLQLLQD RDTYDWLLKE RNDTCDKRKF LKERLARLAQ ARRRLAKFPG
