MX1_CANLF
ID MX1_CANLF Reviewed; 657 AA.
AC Q9N0Y3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Vice S.J., Gordy P.W., Bowen R.A.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=15767791; DOI=10.1089/jir.2005.25.169;
RA Nakamura T., Asano A., Okano S., Ko J.H., Kon Y., Watanabe T., Agui T.;
RT "Intracellular localization and antiviral property of canine Mx proteins.";
RL J. Interferon Cytokine Res. 25:169-173(2005).
RN [3]
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:0000269|PubMed:15767791}.
CC Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Note=Binds preferentially to
CC negatively charged phospholipids. {ECO:0000250}.
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; AF239823; AAF44684.1; -; mRNA.
DR RefSeq; NP_001003134.1; NM_001003134.1.
DR RefSeq; XP_005638792.1; XM_005638735.2.
DR AlphaFoldDB; Q9N0Y3; -.
DR SMR; Q9N0Y3; -.
DR STRING; 9612.ENSCAFP00000014941; -.
DR PaxDb; Q9N0Y3; -.
DR Ensembl; ENSCAFT00030043120; ENSCAFP00030037636; ENSCAFG00030023413.
DR Ensembl; ENSCAFT00040044953; ENSCAFP00040039278; ENSCAFG00040024049.
DR Ensembl; ENSCAFT00845053414; ENSCAFP00845041963; ENSCAFG00845030104.
DR GeneID; 403745; -.
DR KEGG; cfa:403745; -.
DR CTD; 4599; -.
DR VEuPathDB; HostDB:ENSCAFG00845030104; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000163266; -.
DR HOGENOM; CLU_008964_8_0_1; -.
DR InParanoid; Q9N0Y3; -.
DR OMA; FHKWSAV; -.
DR OrthoDB; 494748at2759; -.
DR TreeFam; TF331484; -.
DR Proteomes; UP000002254; Chromosome 31.
DR Bgee; ENSCAFG00000010167; Expressed in adrenal cortex and 48 other tissues.
DR ExpressionAtlas; Q9N0Y3; differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
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..657
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000206591"
FT DOMAIN 63..336
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 569..657
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 73..80
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 98..100
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 174..177
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 243..246
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 275..278
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 337..362
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 362..529
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 363..627
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 540..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..553
FT /note="Critical for lipid-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 540..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 174..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 243..246
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 657 AA; 74801 MW; 25EA43329BFF7C70 CRC64;
MVNSQGKITD SNPVPNHVLL NGLTDKAEKN QGIGNSLCSQ YEEKVRPCID LIDSLRALGV
EQDLALPAIA VIGDQSSGKS SVLEALSGVA LPRGSGIVTR CPLVLKLKKL INEDEWRGKV
SYQDTEMEIS DPSEVEVEIN KAQDAIAGEG QGISHELISL EVSSPHVPDL TLIDLPGITR
VAVGNQPADI GRQTKQLIRK YILKQETINL VVVPCNVDIA TTEALSMAQE VDPDGDRTIG
ILTKPDLVDR GTEGKVVDVA QNLVCHLKKG YMIVKCRGQQ DIQDQVSLAE ALQKEKDFFE
DHPHFRVLLE EGRATVPNLA EKLTSELITH ICKTLPLLEN QIKENHEKIT EELQKYGSDV
PEDEHEKMFF LIDKLNAFNQ DISSLIQGEE SVGEDESRLF TKIRNEFHKW SAVIEKKFQR
GYKAIYKQME KFENRYRGRE LPGFVNYKTF EIIIKQQIKE LEEPAVDMLH TITDMVQVAF
GDISKANFDE FFNLYRTTKS KIEDIKFELE KEAEKSIRLH FQMEQIVYCQ DHVYQRALQR
VREKDSDEEK KKKTSSMSHD EVSSVNISLS EILEHLLAYR QEATNRISSH IPLIIQYFIL
QVYGQKLQNG MLQLLQDKDT YSWLLKERSD TSDKRKFLKE RLARLAQARR RLAKFPG
