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Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)

 MX1_BOVIN               Reviewed;         648 AA.
P79135; O46623; Q17QZ1; Q53ZW3; Q867D5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 4.
12-SEP-2018, entry version 123.
RecName: Full=Interferon-induced GTP-binding protein Mx1;
AltName: Full=Myxoma resistance protein 1;
AltName: Full=Myxovirus resistance protein 1;
Name=MX1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALLELE MX1-A, AND
INDUCTION.
TISSUE=Endometrium;
PubMed=9781814; DOI=10.1089/jir.1998.18.745;
Ellinwood N.M., McCue J.M., Gordy P.W., Bowen R.A.;
"Cloning and characterization of cDNAs for a bovine (Bos taurus) Mx
protein.";
J. Interferon Cytokine Res. 18:745-755(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT MET-120, AND TISSUE
SPECIFICITY.
TISSUE=Endometrium;
PubMed=14994826; DOI=10.1023/B:BIGI.0000007773.15979.13;
Kojima T., Oshima K., Watanabe H., Komatsu M.;
"The bovine Mx1 gene: characterization of the gene structure,
alternative splicing, and promoter region.";
Biochem. Genet. 41:375-390(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Holstein;
PubMed=14729264; DOI=10.1016/j.gene.2003.10.006;
Gerardin J.A., Baise E.A., Pire G.A., Leroy M.P.-P., Desmecht D.J.-M.;
"Genomic structure, organisation, and promoter analysis of the bovine
(Bos taurus) Mx1 gene.";
Gene 326:67-75(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Hereford; TISSUE=Uterus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=16202617; DOI=10.1016/j.nbd.2005.08.015;
Leroy M., Pire G., Baise E., Desmecht D.;
"Expression of the interferon-alpha/beta-inducible bovine Mx1 dynamin
interferes with replication of rabies virus.";
Neurobiol. Dis. 21:515-521(2006).
[6]
REVIEW, AND INDUCTION.
PubMed=18062906; DOI=10.1016/j.micinf.2007.09.010;
Haller O., Stertz S., Kochs G.;
"The Mx GTPase family of interferon-induced antiviral proteins.";
Microbes Infect. 9:1636-1643(2007).
[7]
ALTERNATIVE SPLICING (ISOFORM 2), VARIANT MET-120, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=19951175; DOI=10.1089/vim.2009.0050;
Yamada K., Nakatsu Y., Onogi A., Ueda J., Watanabe T.;
"Specific intracellular localization and antiviral property of genetic
and splicing variants in bovine Mx1.";
Viral Immunol. 22:389-395(2009).
[8]
FUNCTION.
PubMed=22385204; DOI=10.1089/jir.2011.0123;
Dermine M., Desmecht D.;
"In vivo modulation of the innate response to pneumovirus by type-I
and -III interferon-induced bos taurus Mx1.";
J. Interferon Cytokine Res. 32:332-337(2012).
-!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
activity against rabies virus (RABV), vesicular stomatitis virus
(VSV) and murine pneumonia virus (MPV). Isoform 1 but not isoform
2 shows antiviral activity against vesicular stomatitis virus
(VSV). {ECO:0000269|PubMed:16202617, ECO:0000269|PubMed:19951175,
ECO:0000269|PubMed:22385204}.
-!- SUBUNIT: Homooligomer. Oligomerizes into multimeric filamentous or
ring-like structures by virtue of its stalk domain.
Oligomerization is critical for GTPase activity, protein
stability, and recognition of viral target structures (By
similarity). Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and
TRPC7 (By similarity). Interacts with HSPA5 (By similarity).
Interacts with TUBB/TUBB5 (By similarity). Interacts with DDX39A
and DDX39B (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19951175}.
Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591};
Peripheral membrane protein {ECO:0000250|UniProtKB:P20591};
Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm,
perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds
preferentially to negatively charged phospholipids. Colocalizes
with CCHFV protein N in the perinuclear region.
{ECO:0000250|UniProtKB:P20591}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus
{ECO:0000269|PubMed:19951175}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Mx1A;
IsoId=P79135-1; Sequence=Displayed;
Name=2; Synonyms=Mx1B;
IsoId=P79135-2; Sequence=VSP_031549;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:14994826}.
-!- INDUCTION: By type I and type III interferons.
{ECO:0000269|PubMed:18062906, ECO:0000269|PubMed:9781814}.
-!- DOMAIN: The C-terminal GTPase effector domain (GED) is involved in
oligomerization and viral target recognition. {ECO:0000250}.
-!- DOMAIN: The middle domain mediates self-assembly and
oligomerization. {ECO:0000250}.
-!- PTM: ISGylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
-----------------------------------------------------------------------
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EMBL; U88329; AAC18655.1; -; mRNA.
EMBL; AF047692; AAC13166.1; -; mRNA.
EMBL; AB060169; BAC56980.1; -; mRNA.
EMBL; AY251202; AAO74571.1; -; Genomic_DNA.
EMBL; AY251194; AAO74571.1; JOINED; Genomic_DNA.
EMBL; AY251195; AAO74571.1; JOINED; Genomic_DNA.
EMBL; AY251196; AAO74571.1; JOINED; Genomic_DNA.
EMBL; AY251197; AAO74571.1; JOINED; Genomic_DNA.
EMBL; AY251198; AAO74571.1; JOINED; Genomic_DNA.
EMBL; AY251199; AAO74571.1; JOINED; Genomic_DNA.
EMBL; AY251200; AAO74571.1; JOINED; Genomic_DNA.
EMBL; AY251201; AAO74571.1; JOINED; Genomic_DNA.
EMBL; BC118109; AAI18110.1; -; mRNA.
RefSeq; NP_776365.1; NM_173940.2. [P79135-1]
RefSeq; XP_005202046.1; XM_005201989.3. [P79135-2]
RefSeq; XP_015329109.1; XM_015473623.1. [P79135-2]
UniGene; Bt.4675; -.
ProteinModelPortal; P79135; -.
SMR; P79135; -.
STRING; 9913.ENSBTAP00000041289; -.
PaxDb; P79135; -.
PRIDE; P79135; -.
Ensembl; ENSBTAT00000012035; ENSBTAP00000012035; ENSBTAG00000030913. [P79135-1]
Ensembl; ENSBTAT00000043742; ENSBTAP00000041289; ENSBTAG00000030913. [P79135-2]
GeneID; 280872; -.
KEGG; bta:280872; -.
CTD; 4599; -.
VGNC; VGNC:31770; MX1.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00760000119213; -.
HOGENOM; HOG000063238; -.
HOVERGEN; HBG008788; -.
InParanoid; P79135; -.
KO; K14754; -.
OMA; AVDMLHT; -.
OrthoDB; EOG091G080G; -.
TreeFam; TF331484; -.
Reactome; R-BTA-1169408; ISG15 antiviral mechanism.
Proteomes; UP000009136; Chromosome 1.
Bgee; ENSBTAG00000030913; Expressed in 10 organ(s), highest expression level in lung.
ExpressionAtlas; P79135; baseline and differential.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0034340; P:response to type I interferon; TAS:UniProtKB.
GO; GO:0034342; P:response to type III interferon; TAS:UniProtKB.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
CDD; cd08771; DLP_1; 1.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11566; PTHR11566; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
2: Evidence at transcript level;
Acetylation; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; Endoplasmic reticulum; GTP-binding;
Immunity; Innate immunity; Membrane; Nucleotide-binding; Nucleus;
Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 648 Interferon-induced GTP-binding protein
Mx1.
/FTId=PRO_0000206590.
DOMAIN 56 329 Dynamin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
DOMAIN 560 648 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 66 73 GTP. {ECO:0000255}.
NP_BIND 167 171 GTP. {ECO:0000255}.
NP_BIND 236 239 GTP. {ECO:0000255}.
REGION 66 73 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 91 93 G2 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 167 170 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 236 239 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 268 271 G5 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 330 355 Bundle signaling element (BSE).
{ECO:0000250}.
REGION 355 522 Middle domain. {ECO:0000250}.
REGION 356 618 Stalk. {ECO:0000250}.
REGION 543 546 Critical for lipid-binding.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P20591}.
VAR_SEQ 1 25 MVHSDLGIEELDSPESSLNGSEDME -> MLGVMGGRRRRG
RRRMRCLDGITDSMDE (in isoform 2).
{ECO:0000303|PubMed:14994826}.
/FTId=VSP_031549.
VARIANT 24 24 M -> MVREHET (in allele Mx1-a).
VARIANT 120 120 I -> M. {ECO:0000269|PubMed:14994826,
ECO:0000269|PubMed:19951175}.
CONFLICT 364 364 L -> P (in Ref. 1; AAC13166).
{ECO:0000305}.
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


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