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MX2_SHEEP
ID   MX2_SHEEP               Reviewed;         714 AA.
AC   Q5I2P5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE   AltName: Full=Myxovirus resistance protein 2;
GN   Name=MX2;
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].
RC   TISSUE=Endometrium;
RA   Assiri A.M., Welker J.E., Ott T.L.;
RT   "Cloning and characterization of a second Mx gene (Mx2) from pregnant sheep
RT   endometrium.";
RL   Submitted (DEC-2004) 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   -!- 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; AY859475; AAW51454.1; -; mRNA.
DR   RefSeq; NP_001072120.1; NM_001078652.1.
DR   AlphaFoldDB; Q5I2P5; -.
DR   SMR; Q5I2P5; -.
DR   STRING; 9940.ENSOARP00000010974; -.
DR   PRIDE; Q5I2P5; -.
DR   GeneID; 780441; -.
DR   KEGG; oas:780441; -.
DR   CTD; 4600; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   OrthoDB; 494748at2759; -.
DR   Proteomes; UP000002356; Unplaced.
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   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; Reference proteome.
FT   CHAIN           1..714
FT                   /note="Interferon-induced GTP-binding protein Mx2"
FT                   /id="PRO_0000319960"
FT   DOMAIN          115..386
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          622..713
FT                   /note="GED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..132
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          150..152
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          224..227
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          293..296
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          325..328
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   COMPBIAS        47..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         125..132
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         224..228
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         293..296
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   714 AA;  81681 MW;  508911B89A61BC06 CRC64;
     MSMSYRALKF RRHAPTSTQH HPKEDMNFHQ QPPGLPGPAL GQTMSPPPWQ MGESNPDFLP
     NNFNQLNLDP QQPEADGGQQ RSKGSENNLY RKYEEKVRPC IDLIDSLRAL GVEQDLALPA
     IAVIGDQSSG KSSVLEALSG VALPRGSGII TRCPLVLKLT KRECEWTGKI TYRNVTQQLH
     NPSEVEREIR RAQNIIAGNG VGISHELINL EVTSPEVPDL TLIDLPGITR VAVENQPQDI
     GLQIKALIKT YIQRQETINL VVVPCNVDIA TTEALSMAQE VDPDGDRTIG ILTKPDLVDK
     GTEKGVLKVM QNLTYHLKKG YMIVKCRGQQ DITNKLSLAE ATRKEVMFFQ THPYFRVLLD
     EGKATVPLLA ERLTTELIWH INKSLPLLEN QIKEKHQRAT EELQQYGDDI PSNEGDKMFF
     LIEKIKLFNE DIEKLIEGEE IVIETESRLC NRIREEFTRW VLILTTNIEK VKSILNEEVS
     KYETKYRGKE LLGFVNYKTF ETVVKHYLGQ LIDPALKMLQ KAMEIIWQTF KDTAKKHFAE
     FCNLHQTVQN KIEDIKTKQM AEAANLIQLQ FRMEKLVFCQ DQIYGVVLNK VREEIFNSVG
     KASENPQSKH PFLNNQSSVS SIVEIGVHLN AYFTETSKRL ANQIPFIIQY FMLQENGDKV
     QKAMMQLLQE TQHYSWLLQE QSDTATKRKF LKEKIFRLTQ AQQALYEFPH FKSI
 
 
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