MX1_MACMU
ID MX1_MACMU Reviewed; 661 AA.
AC A1E2I4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miller C.J., Dutra J.C.;
RL Submitted (NOV-2006) 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|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}.
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; EF101561; ABK97616.1; -; mRNA.
DR RefSeq; NP_001073161.1; NM_001079693.2.
DR RefSeq; XP_014988323.1; XM_015132837.1.
DR RefSeq; XP_014988324.1; XM_015132838.1.
DR RefSeq; XP_014988325.1; XM_015132839.1.
DR RefSeq; XP_014988326.1; XM_015132840.1.
DR AlphaFoldDB; A1E2I4; -.
DR SMR; A1E2I4; -.
DR STRING; 9544.ENSMMUP00000020103; -.
DR PRIDE; A1E2I4; -.
DR GeneID; 715186; -.
DR KEGG; mcc:715186; -.
DR CTD; 4599; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_8_0_1; -.
DR InParanoid; A1E2I4; -.
DR OMA; FHKWSAV; -.
DR OrthoDB; 494748at2759; -.
DR TreeFam; TF331484; -.
DR Proteomes; UP000006718; 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..661
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000382944"
FT DOMAIN 67..340
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 573..661
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 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..631
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 554..557
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 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 661 AA; 75431 MW; 80A98D43DC36FD60 CRC64;
MVLSEVDIVK ADPAAASQPL LLNGDADVAQ KSPGSVAENN LCSQYEEKVR PCIDLIDSLR
ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLVLK LKKLVNEDEW
RGKVSYQDYE IEILDASEVE KEINKAQNTI AGEGMGISHE LITLEISSRD VPDLTLIDLP
GITRVAVGNQ PPDIGYKIKT LIRKYIQRQE TINLVVVPSN VDIATTEALS MAQEVDPEGD
RTIGILTKPD LVDKGTEDKV VDVVRNLVFH LKKGYMIVKC RGQQEIQDQL SLSEALQREK
IFFEDHPHFR DLLEEGKATI PCLAEKLTSE LIAHICKSLP LLENQIKESH QGITEELQKY
GVDIPEDENE KMFFLIDKIN AFNQDITALI QGEETVGEDD SRLFTRLRRE FHKWGIIIEN
NLQEGHKITS RKMQKFENQY RGRELPGFVN YRTFETIVKQ QIKALEEPAV NMLHTVTDMV
RLAFTDVSMK NFEELFNLHR TAKSKIEDIR TEQEREGEKL IRLHFQMEQI VYCQDQVYRG
ALQKVREKEL EEEKKKKSWD IGTFQPSSTE SSMEEIFQHL MAYHQEASKR ISSHIPLVIQ
FFMLQMYGQQ LQKAMLQLLQ DKDTYSWLLK ERSDTSDKRK FLKERLARLT QARRRLAQFP
G
