位置:首页 > 蛋白库 > MX1_OTABY
MX1_OTABY
ID   MX1_OTABY               Reviewed;         658 AA.
AC   Q4ADG7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
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; Synonyms=MX;
OS   Otaria byronia (South American sea lion).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Otariidae; Otaria.
OX   NCBI_TaxID=161932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sakamoto A., Seyama T., Ueda J., Watanabe T.;
RT   "Identification of Mx cDNAs in sea mammals.";
RL   Submitted (JUL-2005) 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}. Endoplasmic reticulum
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region
CC       {ECO:0000250}. Note=Binds preferentially to negatively charged
CC       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}.
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; AB222180; BAE16331.1; -; mRNA.
DR   AlphaFoldDB; Q4ADG7; -.
DR   SMR; Q4ADG7; -.
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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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   Ubl conjugation.
FT   CHAIN           1..658
FT                   /note="Interferon-induced GTP-binding protein Mx1"
FT                   /id="PRO_0000319954"
FT   DOMAIN          65..338
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          570..658
FT                   /note="GED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..82
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          100..102
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          176..179
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          245..248
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          277..280
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          339..364
FT                   /note="Bundle signaling element (BSE)"
FT                   /evidence="ECO:0000250"
FT   REGION          364..531
FT                   /note="Middle domain"
FT                   /evidence="ECO:0000250"
FT   REGION          365..628
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          551..554
FT                   /note="Critical for lipid-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         75..82
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         176..180
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         245..248
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   658 AA;  75201 MW;  CAEE0FC107513675 CRC64;
     MVNSKGKITD SDPGSSHLLL NGLADKAGKN QDTEPENSLC SQYEEKVRPC IDLIDSLRAL
     GVEQDLALPA IAVIGDQSSG KSSVLEALSG VALPRGSGIV TRCPLVLKLK KLLNKDEWRG
     KVSYQDFEME ISDPSEVEVE INKAQNAIAG EGQGISHELI SLEVSSPHVP DLTLIDLPGI
     TRVAVGNQPA DIGHQTKKLI KKYILKQETI NLVVVPCNVD IATTEALSMA QEVDPDGDRT
     IGILTKPDLV DRGTESKVVD VAQNLVCHLK KGYMIVKCRG QQDIQDQVTL TEALQKERDF
     FEDHPHFRVL LEEGRATVPC LADRLTSELI THICKTLPLL EKQIKENYEK ITEELQKYGS
     DVPEEEHEKM FFLIEKINAF NHDITSLTEG EEFVGEDECR LFTKIRNEFH KWSLVIEKRF
     QQGYKAICKQ IERFENRYRG RELPGFVNYK TFEIIIKQQI KELEEPAVYM LHTITDMVQA
     AFTDISEANF AEFFNLYRTT KSKIEDIKFE LEKEAEKSIR LHFQMEQIVY CQDQVYQCAL
     QRVREESDKE KDKKINSMCS KEVSSVNISL SDIFEHLLAY RQEATNRISS HIPLIIQYFI
     LQVYGQKLQK DMLLLLHDKD THNWLLKERS DTRDKRKLLK ERLARLAQAR RRLAKFPG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024