MX1_SHEEP
ID MX1_SHEEP Reviewed; 654 AA.
AC P33237; Q95MD4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Interferon-induced GTP-binding protein Mx1;
DE AltName: Full=Myxoma resistance protein 1;
DE AltName: Full=Myxovirus resistance protein 1;
DE AltName: Full=Oligodendrocyte GTP-binding protein;
GN Name=MX1; Synonyms=MX;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Endometrium;
RX PubMed=7507876; DOI=10.1016/0378-1119(93)90029-3;
RA Charleston B., Stewart H.J.;
RT "An interferon-induced Mx protein: cDNA sequence and high-level expression
RT in the endometrium of pregnant sheep.";
RL Gene 137:327-331(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11754216; DOI=10.1002/glia.10027;
RA Szuchet S., Plachetzki D.C., Karialukas R.;
RT "Oligodendrocytes express an alpha/beta-interferon-susceptible Mx gene:
RT molecular characterization of the encoded protein.";
RL Glia 37:183-189(2002).
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).
RN [4]
RP INTERACTION WITH TUBB.
RX PubMed=20584010; DOI=10.1111/j.1600-0897.2010.00885.x;
RA Racicot K., Ott T.;
RT "The myxovirus resistance protein, MX1, interacts with tubulin beta in
RT uterine glandular epithelial cells.";
RL Am. J. Reprod. Immunol. 65:44-53(2011).
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 DDX39A and DDX39B (By similarity).
CC Interacts with TUBB/TUBB5. {ECO:0000250, ECO:0000269|PubMed:20584010}.
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:7507876}.
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; X66093; CAA46888.1; -; mRNA.
DR EMBL; AF399856; AAK94466.1; -; mRNA.
DR PIR; S21552; S21552.
DR RefSeq; NP_001009753.1; NM_001009753.1.
DR AlphaFoldDB; P33237; -.
DR SMR; P33237; -.
DR STRING; 9940.ENSOARP00000011035; -.
DR PRIDE; P33237; -.
DR GeneID; 443146; -.
DR KEGG; oas:443146; -.
DR CTD; 4599; -.
DR eggNOG; KOG0446; Eukaryota.
DR OrthoDB; 494748at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; GTP-binding; Immunity;
KW Innate immunity; Membrane; Nucleotide-binding; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..654
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000206596"
FT DOMAIN 62..335
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 566..654
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..79
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 97..99
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 173..176
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 242..245
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 274..277
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 336..361
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 361..528
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 362..624
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 544..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..552
FT /note="Critical for lipid-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 544..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 173..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 242..245
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 CONFLICT 45
FT /note="R -> L (in Ref. 2; AAK94466)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="C -> S (in Ref. 2; AAK94466)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="F -> I (in Ref. 2; AAK94466)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="L -> F (in Ref. 2; AAK94466)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="H -> L (in Ref. 2; AAK94466)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="S -> K (in Ref. 2; AAK94466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 75573 MW; CF06250CA7456E04 CRC64;
MVLSDLDIKE PDSPESGLNG SDDMVREHET ESKGNLYSQY EEKVRPCIDL IDSLRALGVE
QDLALPAIAV IGDQSSGKSS VLEALSGVAL PRGSGIVTRC PLVLRLKKLE KEGEWKGKVS
FLDREIEISD ASQVEKEISE AQIAIAGEGM GISHELISLE VSSPHVPDLT LIDLPGITRV
AVGNQPHDIE YQIKSLIRKY ILRQETINLV VVPANVDIAT TEALRMAQDV DPQGDRTIGI
LTKPDLVDKG TEDKVVDVVR NLVFHLKKGY MIVKCRGQQE IQHRLSLDKA LQRERIFFED
HTHFRDLLEE GRATIPCLAE RLTNELIMHI CKTLPLLENQ IKETHQRITE ELQKYGKDIP
EEESEKMFSL IEKIDTFNKE IISTIEGEEH VGQYDSRLFT KVRAEFCKWS AVVEKNFEKG
HEAIRKEIKQ FENRYRGREL PGFVNYKTFE IIIKKQVIVL EEPAVDMLHT VTDIIRNTFT
EVSGKHFSEF FNLHRTAKSK IEDIRLEQEN EAEKSIRLHF QMEQLVYCQD QVYRRALQQV
REKEAEEEKK KKSNHYYQSE DSEPSTAEIF QHLMAYHQEV STRISSHIPL IIQFFVLRTY
GEQLKKSMLQ LLQDKDQYDW LLKERTDTRD KRKFLKERLE RLSRARQRLA KFPG
