ID A4UUI2_MOUSE Unreviewed; 589 AA. AC A4UUI2; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 03-MAY-2023, entry version 119. DE SubName: Full=Guanylate binding protein 1 {ECO:0000313|EMBL:ABO88215.1}; DE SubName: Full=Guanylate binding protein 2b {ECO:0000313|Ensembl:ENSMUSP00000029936.5}; GN Name=Gbp2b {ECO:0000313|Ensembl:ENSMUSP00000029936.5, 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:ENSMUSP00000029936.5, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000029936.5, 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:0007829|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:ENSMUSP00000029936.5} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000029936.5}; RG Ensembl; RL Submitted (JAN-2023) 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 GTPase family. {ECO:0000256|PROSITE- CC ProRule:PRU01052}. 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; EF494422; ABO88215.1; -; mRNA. DR RefSeq; NP_034389.2; NM_010259.2. DR ProteomicsDB; 330566; -. DR DNASU; 14468; -. DR Ensembl; ENSMUST00000029936.5; ENSMUSP00000029936.5; ENSMUSG00000040264.11. DR GeneID; 14468; -. DR KEGG; mmu:14468; -. DR UCSC; uc008rox.1; mouse. DR AGR; MGI:95666; -. DR CTD; 14468; -. DR MGI; MGI:95666; Gbp2b. DR VEuPathDB; HostDB:ENSMUSG00000040264; -. DR GeneTree; ENSGT00940000162297; -. DR HOGENOM; CLU_018608_2_2_1; -. DR OMA; TECTMER; -. DR OrthoDB; 5309032at2759; -. DR TreeFam; TF331602; -. DR BioGRID-ORCS; 14468; 6 hits in 77 CRISPR screens. DR ChiTaRS; Gbp2b; mouse. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000040264; Expressed in mesenteric lymph node and 50 other tissues. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProt. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:UniProt. DR GO; GO:0009617; P:response to bacterium; IEA:UniProt. DR CDD; cd01851; GBP; 1. DR CDD; cd16269; GBP_C; 1. DR Gene3D; 1.20.1000.10; Guanylate-binding protein, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR10751; GUANYLATE BINDING PROTEIN; 1. DR PANTHER; PTHR10751:SF112; GUANYLATE-BINDING PROTEIN 2; 1. DR Pfam; PF02263; GBP; 1. DR Pfam; PF02841; GBP_C; 1. DR SUPFAM; SSF48340; Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:0007829|MaxQB:A4UUI2, KW ECO:0007829|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..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 //