MX1_BOVIN
ID MX1_BOVIN Reviewed; 648 AA.
AC P79135; O46623; Q17QZ1; Q53ZW3; Q867D5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 4.
DT 03-AUG-2022, entry version 142.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALLELE MX1-A, AND
RP INDUCTION.
RC TISSUE=Endometrium;
RX PubMed=9781814; DOI=10.1089/jir.1998.18.745;
RA Ellinwood N.M., McCue J.M., Gordy P.W., Bowen R.A.;
RT "Cloning and characterization of cDNAs for a bovine (Bos taurus) Mx
RT protein.";
RL J. Interferon Cytokine Res. 18:745-755(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT MET-120, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Endometrium;
RX PubMed=14994826; DOI=10.1023/b:bigi.0000007773.15979.13;
RA Kojima T., Oshima K., Watanabe H., Komatsu M.;
RT "The bovine Mx1 gene: characterization of the gene structure, alternative
RT splicing, and promoter region.";
RL Biochem. Genet. 41:375-390(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein;
RX PubMed=14729264; DOI=10.1016/j.gene.2003.10.006;
RA Gerardin J.A., Baise E.A., Pire G.A., Leroy M.P.-P., Desmecht D.J.-M.;
RT "Genomic structure, organisation, and promoter analysis of the bovine (Bos
RT taurus) Mx1 gene.";
RL Gene 326:67-75(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=16202617; DOI=10.1016/j.nbd.2005.08.015;
RA Leroy M., Pire G., Baise E., Desmecht D.;
RT "Expression of the interferon-alpha/beta-inducible bovine Mx1 dynamin
RT interferes with replication of rabies virus.";
RL Neurobiol. Dis. 21:515-521(2006).
RN [6]
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 [7]
RP ALTERNATIVE SPLICING (ISOFORM 2), VARIANT MET-120, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19951175; DOI=10.1089/vim.2009.0050;
RA Yamada K., Nakatsu Y., Onogi A., Ueda J., Watanabe T.;
RT "Specific intracellular localization and antiviral property of genetic and
RT splicing variants in bovine Mx1.";
RL Viral Immunol. 22:389-395(2009).
RN [8]
RP FUNCTION.
RX PubMed=22385204; DOI=10.1089/jir.2011.0123;
RA Dermine M., Desmecht D.;
RT "In vivo modulation of the innate response to pneumovirus by type-I and
RT -III interferon-induced bos taurus Mx1.";
RL J. Interferon Cytokine Res. 32:332-337(2012).
CC -!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
CC activity against rabies virus (RABV), vesicular stomatitis virus (VSV)
CC and murine pneumonia virus (MPV). Isoform 1 but not isoform 2 shows
CC antiviral activity against vesicular stomatitis virus (VSV).
CC {ECO:0000269|PubMed:16202617, ECO:0000269|PubMed:19951175,
CC ECO:0000269|PubMed:22385204}.
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:19951175}.
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. Colocalizes with CCHFV protein N in the
CC perinuclear region. {ECO:0000250|UniProtKB:P20591}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:19951175}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Mx1A;
CC IsoId=P79135-1; Sequence=Displayed;
CC Name=2; Synonyms=Mx1B;
CC IsoId=P79135-2; Sequence=VSP_031549;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:14994826}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:18062906, ECO:0000269|PubMed:9781814}.
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; U88329; AAC18655.1; -; mRNA.
DR EMBL; AF047692; AAC13166.1; -; mRNA.
DR EMBL; AB060169; BAC56980.1; -; mRNA.
DR EMBL; AY251202; AAO74571.1; -; Genomic_DNA.
DR EMBL; AY251194; AAO74571.1; JOINED; Genomic_DNA.
DR EMBL; AY251195; AAO74571.1; JOINED; Genomic_DNA.
DR EMBL; AY251196; AAO74571.1; JOINED; Genomic_DNA.
DR EMBL; AY251197; AAO74571.1; JOINED; Genomic_DNA.
DR EMBL; AY251198; AAO74571.1; JOINED; Genomic_DNA.
DR EMBL; AY251199; AAO74571.1; JOINED; Genomic_DNA.
DR EMBL; AY251200; AAO74571.1; JOINED; Genomic_DNA.
DR EMBL; AY251201; AAO74571.1; JOINED; Genomic_DNA.
DR EMBL; BC118109; AAI18110.1; -; mRNA.
DR RefSeq; NP_776365.1; NM_173940.2. [P79135-1]
DR RefSeq; XP_005202046.1; XM_005201989.3. [P79135-2]
DR RefSeq; XP_015329109.1; XM_015473623.1. [P79135-2]
DR AlphaFoldDB; P79135; -.
DR SMR; P79135; -.
DR STRING; 9913.ENSBTAP00000041289; -.
DR PaxDb; P79135; -.
DR PRIDE; P79135; -.
DR Ensembl; ENSBTAT00000012035; ENSBTAP00000012035; ENSBTAG00000030913. [P79135-1]
DR Ensembl; ENSBTAT00000043742; ENSBTAP00000041289; ENSBTAG00000030913. [P79135-2]
DR GeneID; 280872; -.
DR KEGG; bta:280872; -.
DR CTD; 4599; -.
DR VEuPathDB; HostDB:ENSBTAG00000030913; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155686; -.
DR HOGENOM; CLU_008964_8_0_1; -.
DR InParanoid; P79135; -.
DR OMA; FHKWSAV; -.
DR OrthoDB; 494748at2759; -.
DR TreeFam; TF331484; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000030913; Expressed in abomasum and 105 other tissues.
DR ExpressionAtlas; P79135; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0034340; P:response to type I interferon; TAS:UniProtKB.
DR GO; GO:0034342; P:response to type III interferon; TAS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
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; Alternative splicing; Antiviral defense; Cytoplasm;
KW Endoplasmic reticulum; GTP-binding; Immunity; Innate immunity; Membrane;
KW Nucleotide-binding; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..648
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000206590"
FT DOMAIN 56..329
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 560..648
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..73
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 91..93
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 167..170
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 236..239
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 268..271
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 330..355
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 355..522
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 356..618
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 543..546
FT /note="Critical for lipid-binding"
FT /evidence="ECO:0000250"
FT BINDING 66..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 167..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 236..239
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 VAR_SEQ 1..25
FT /note="MVHSDLGIEELDSPESSLNGSEDME -> MLGVMGGRRRRGRRRMRCLDGIT
FT DSMDE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14994826"
FT /id="VSP_031549"
FT VARIANT 24
FT /note="M -> MVREHET (in allele Mx1-a)"
FT VARIANT 120
FT /note="I -> M"
FT /evidence="ECO:0000269|PubMed:14994826,
FT ECO:0000269|PubMed:19951175"
FT CONFLICT 364
FT /note="L -> P (in Ref. 1; AAC13166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 74805 MW; A27933696213EDDF CRC64;
MVHSDLGIEE LDSPESSLNG SEDMESKSNL YSQYEEKVRP CIDLIDSLRS LGVEQDLALP
AIAVIGDQSS GKSSVLEALS GVALPRGSGI VTRCPLVLRL KKLGNEDEWK GKVSFLDKEI
EIPDASQVEK EISEAQIAIA GEGTGISHEL ISLEVSSPHV PDLTLIDLPG ITRVAVGNQP
PDIEYQIKSL IRKYILRQET INLVVVPANV DIATTEALRM AQEVDPQGDR TIGILTKPDL
VDKGTEDKVV DVVRNLVFHL KKGYMIVKCR GQQDIKHRMS LDKALQRERI FFEDHAHFRD
LLEEGKATIP CLAERLTSEL IMHICKTLPL LENQIKETHQ RITEELQKYG KDIPEEESEK
MFCLIEKIDT FNKEIISTIE GEEFVEQYDS RLFTKVRAEF SKWSAVVEKN FEKGYEAIRK
EIKQFENRYR GRELPGFVNY KTFETIIKKQ VRVLEEPAVD MLHTVTDIIR NTFTDVSGKH
FNEFFNLHRT AKSKIEDIRL EQENEAEKSI RLHFQMEQLV YCQDQVYRRA LQQVREKEAE
EEKNKKSNHY FQSQVSEPST DEIFQHLTAY QQEVSTRISG HIPLIIQFFV LRTYGEQLKK
SMLQLLQDKD QYDWLLKERT DTRDKRKFLK ERLERLTRAR QRLAKFPG
