MXA_DANRE
ID MXA_DANRE Reviewed; 646 AA.
AC Q8JH68;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Interferon-induced GTP-binding protein MxA;
DE AltName: Full=IFN-inducible antiviral protein MxA;
DE AltName: Full=Interferon-inducible MxA protein;
GN Name=mxa;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14698216; DOI=10.1016/j.dci.2003.09.001;
RA Altmann S.M., Mellon M.T., Johnson M.C., Paw B.H., Trede N.S., Zon L.I.,
RA Kim C.H.;
RT "Cloning and characterization of an Mx gene and its corresponding promoter
RT from the zebrafish, Danio rerio.";
RL Dev. Comp. Immunol. 28:295-306(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12869211; DOI=10.1186/1471-2164-4-29;
RA Lutfalla G., Roest Crollius H., Stange-Thomann N., Jaillon O., Mogensen K.,
RA Monneron D.;
RT "Comparative genomic analysis reveals independent expansion of a lineage-
RT specific gene family in vertebrates: the class II cytokine receptors and
RT their ligands in mammals and fish.";
RL BMC Genomics 4:29-29(2003).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By interferons.
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; AF533769; AAN01189.1; -; mRNA.
DR EMBL; AJ544823; CAD67755.1; -; mRNA.
DR AlphaFoldDB; Q8JH68; -.
DR SMR; Q8JH68; -.
DR STRING; 7955.ENSDARP00000106285; -.
DR PaxDb; Q8JH68; -.
DR ZFIN; ZDB-GENE-030721-5; mxa.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; Q8JH68; -.
DR PhylomeDB; Q8JH68; -.
DR PRO; PR:Q8JH68; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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:0046685; P:response to arsenic-containing substance; IDA:ZFIN.
DR GO; GO:0009617; P:response to bacterium; IDA:ZFIN.
DR GO; GO:0009615; P:response to virus; IDA:ZFIN.
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 Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..646
FT /note="Interferon-induced GTP-binding protein MxA"
FT /id="PRO_0000292867"
FT DOMAIN 34..307
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 546..637
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 44..51
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 69..71
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 145..148
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 214..217
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 246..249
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 44..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 145..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 214..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 646 AA; 73262 MW; 3B7A764A2A126BFD CRC64;
MEKLSYTFSQ QYEEKIRPCI DTIDNLRSLG VEKDLALPAI AVIGDQSSGK SSVLEALSGV
PLPRGSGIVT RCPLELKMIR TKDQDRWHGR ISYKTCEEDF DDPAEVEKKI RQAQDEMAGA
GVGISEELIS LQITSADVPD LTLIDLPGIA RVAVKGQPEN IGDQIKRLIR KFVTRQETIN
LVVVPCNVDI ATTEALQMAQ AEDPDGERTL GILTKPDLVD KGTEGTVVDI VHNEVIHLTK
GYMIVRCRGQ KEIMDQVTLN EATETESAFF KDHPHFSKLY EEGFATIPKL AEKLTIELVH
HIQKSLPRLE EQIETKLAET QKELEAYGNG PPSEPAARLS FFIDKVTAFN QDMLNLTTGE
DVKCTTDLLL FPELRQEFAK WSHILDRSGD SFNKKIEKEV DNYEVKYRGR ELPGFINYKT
FEGLVRDQIK LLEEPALKTL KTVSDVVRKK FIQLAQCSFI GFPNLLKIAK TKIEGIKLNK
ESLAESMLKT QFKMELIVYS QDGTYSQSLK HAKDKLEEME KERPQPKIKL PLLSSFDLGT
DNHATLREMR LHLKSYYTIA SKRLADQIPM VIRYMLLQEA ALELQRNMLQ LLQDKDGVDN
LLKEDCDIGQ KRENLLSRQT RLIEGTQPLG HLLEVTFIDY CNILMQ
