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MX2_BUBBU
ID   MX2_BUBBU               Reviewed;         710 AA.
AC   A0MWD1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE   AltName: Full=Myxovirus resistance protein 2;
GN   Name=MX2;
OS   Bubalus bubalis (Domestic water buffalo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bubalus.
OX   NCBI_TaxID=89462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=17119954; DOI=10.1007/s00251-006-0167-5;
RA   Babiker H.A.E., Nakatsu Y., Yamada K., Yoneda A., Takada A., Ueda J.,
RA   Hata H., Watanabe T.;
RT   "Bovine and water buffalo Mx2 genes: polymorphism and antiviral activity.";
RL   Immunogenetics 59:59-67(2007).
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 against vesicular stomatitis virus (VSV).
CC       {ECO:0000269|PubMed:17119954}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- INDUCTION: By type I and type III interferons.
CC       {ECO:0000269|PubMed:18062906}.
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; EF052266; ABK41143.1; -; mRNA.
DR   RefSeq; NP_001277778.1; NM_001290849.1.
DR   AlphaFoldDB; A0MWD1; -.
DR   SMR; A0MWD1; -.
DR   GeneID; 102399001; -.
DR   KEGG; bbub:102399001; -.
DR   CTD; 4600; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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   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   Antiviral defense; Cytoplasm; GTP-binding; Immunity; Innate immunity;
KW   Nucleotide-binding; Nucleus.
FT   CHAIN           1..710
FT                   /note="Interferon-induced GTP-binding protein Mx2"
FT                   /id="PRO_0000319958"
FT   DOMAIN          112..383
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          619..710
FT                   /note="GED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..129
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          147..149
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          221..224
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          290..293
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          322..325
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   COMPBIAS        41..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         221..225
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         290..293
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   710 AA;  81335 MW;  6FEE13E2FB983097 CRC64;
     MSLSFRPLKY KRHTQTSTPH HPKQDIYFHE QPPGPPLGQT MSPPQWQVEE SNPGFLPNNF
     SQLNLDPQQP EANGGQQRSK GPENNLYRKY EEKVRPCIDL IDSLRALGVE QDLALPAIAV
     IGDQSSGKSS VLEALSGVAL PRGSGIITRC PLVLKLTKRE CEWTGKITYR NITQQLQNPS
     EVEWEIRRAQ NIIAGNGRGI SHELINLEVT SPDVPDLTLI DLPGITRVAV ENQPQDIGLQ
     IKALIIQRQE TINLVVVPCN VDIATKKYTE ALSMAQEVDP DGDRTIGILT KPDLVDKGTE
     KGVLKVMQNL TYHLKKGYMI VKCRGQQDIT NKLSLAEATR KETMFFETHP YFRVLLDEGK
     ATMPLLAERL TTELIWHINK SLPLLENQIK EKHQRATEEL QQYGDDIPSD EGDKMFFLIE
     KIKVFNEDIG KLIEGEEIVM ETESRLCNKI REEFTSWILI LTTNIEKVKS ILNEEVSKYE
     KKYRGKELLG FVNYKTFETV VKHYLGQLID PALKMLQKAM EIVWQTFKDT AKKHFAEFCN
     LHQTVQNKIE DIKTKQMAEA ANLIQLQFKM EKLVFCQDQI YGVVLNKVRE DIFNSMGKAS
     ETPQSKQPFL NDQSSISSIV EIGVHLNAYF METSKRLANQ IPFIIQYFML QENGDKVQKA
     MMQLLQDTQH YSWLLQEQSD TATKRKFLKE KIFRLTQAQQ ALYEFPHFKG
 
 
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