ID A4UUI2_MOUSE Unreviewed; 589 AA. AC A4UUI2; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 12-AUG-2020, entry version 107. DE SubName: Full=Guanylate binding protein 1 {ECO:0000313|EMBL:ABO88215.1}; DE SubName: Full=Guanylate-binding protein 2b {ECO:0000313|Ensembl:ENSMUSP00000029936}; GN Name=Gbp2b {ECO:0000313|Ensembl:ENSMUSP00000029936, GN ECO:0000313|MGI:MGI:95666}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:ABO88215.1}; RN [1] {ECO:0000313|EMBL:ABO88215.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6 {ECO:0000313|EMBL:ABO88215.1}; RC TISSUE=Liver {ECO:0000313|EMBL:ABO88215.1}; RX PubMed=18025219; RA Degrandi D., Konermann C., Beuter-Gunia C., Kresse A., Wurthner J., RA Kurig S., Beer S., Pfeffer K.; RT "Extensive characterization of IFN-induced GTPases mGBP1 to mGBP10 involved RT in host defense."; RL J. Immunol. 179:7729-7740(2007). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000029936, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000029936, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [4] {ECO:0000313|Ensembl:ENSMUSP00000029936} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000029936}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000256|ARBA:ARBA00001270}; CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. GB1/RHD3-type GTPase family. GB1 subfamily. CC {ECO:0000256|ARBA:ARBA00008043}. 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; AC102108; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; EF494422; ABO88215.1; -; mRNA. DR RefSeq; NP_034389.2; NM_010259.2. DR Ensembl; ENSMUST00000029936; ENSMUSP00000029936; ENSMUSG00000040264. DR GeneID; 14468; -. DR KEGG; mmu:14468; -. DR UCSC; uc008rox.1; mouse. DR CTD; 14468; -. DR MGI; MGI:95666; Gbp2b. DR GeneTree; ENSGT00940000162297; -. DR HOGENOM; CLU_018608_2_2_1; -. DR KO; K20897; -. DR OMA; GKNMGFS; -. DR OrthoDB; 1027269at2759; -. DR TreeFam; TF331602; -. DR BioGRID-ORCS; 14468; 3 hits in 19 CRISPR screens. DR ChiTaRS; Gbp2b; mouse. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000040264; Expressed in mesenteric lymph node and 81 other tissues. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR CDD; cd16269; GBP_C; 1. DR InterPro; IPR030386; G_GB1_RHD3_dom. DR InterPro; IPR037684; GBP_C. DR InterPro; IPR003191; Guanylate-bd/ATL_C. DR InterPro; IPR036543; Guanylate-bd_C_sf. DR InterPro; IPR015894; Guanylate-bd_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF02263; GBP; 1. DR Pfam; PF02841; GBP_C; 1. DR SUPFAM; SSF48340; SSF48340; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51715; G_GB1_RHD3; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Proteomics identification {ECO:0000213|MaxQB:A4UUI2, KW ECO:0000213|PeptideAtlas:A4UUI2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT DOMAIN 35..276 FT /note="GB1/RHD3-type G" FT /evidence="ECO:0000259|PROSITE:PS51715" FT COILED 480..553 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 560..580 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 589 AA; 67841 MW; 9E3AC4C5D072C576 CRC64; MASEIHMKGP VCLIKNSGEQ LEVYQEALDI LSAIQNPVVV VAIVGFYHTG KSYLMNKLAG KQKGFSLGST VQSHTKGIWM WCMPHPEKPE HTLVLLDTEG LKDMQKGDNQ NDCWIFALAV LLSSTFIYNS IGTINQQAMD QLHYVTELTD LIKSKSSPDQ SDVDNSANFV GFFPIFVWTL RDFSLDLEFD GESITPDEYL ETSLALRKGT DENTKKFNMP RLCIRKFFPK RKCFIFDRPG DRKQLSKLEW IQEDQLNKEF VEQVAEFTSY IFSYSGVKTL SGGITVNGPR LKSLVQTYVS AICSGELPCM ENAVLTLAQI ENSAAVQKAI TYYEEQMNQK IHMPTETLQE LLDLHRTCER EAIEVFMKNS FKDVDQKFQE ELGAQLEAKR DAFVKKNMDM SSAHCSDLLE GLFAHLEEEV KQGTFYKPGG YYLFLQRKQE LEKKYIQTPG KGLQAEVMLR KYFESKEDLA DTLLKMDQSL TEKEKQIEME RIKAEAAEAA NRALAEMQKK HEMLMEQKEQ SYQEHMKQLT EKMEQERKEL MAEQQRIISL KLQEQERLLK QGFQNESLQL RQEIEKIKNM PPPRSCTIL //