GBP2_MOUSE
ID GBP2_MOUSE Reviewed; 589 AA.
AC Q9Z0E6; Q4FK03; Q8CIC6; Q921N2; Q9R1I0;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Guanylate-binding protein 2;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P32456};
DE AltName: Full=GTP-binding protein 2;
DE Short=GBP-2;
DE Short=mGBP-2;
DE Short=mGBP2;
DE AltName: Full=Guanine nucleotide-binding protein 2;
DE AltName: Full=Interferon-induced guanylate-binding protein 2;
DE Flags: Precursor;
GN Name=Gbp2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=C57BL/6J;
RX PubMed=9862701;
RA Boehm U., Guethlein L., Klamp T., Ozbek K., Schaub A., Fuetterer A.,
RA Pfeffer K., Howard J.C.;
RT "Two families of GTPases dominate the complex cellular response to IFN-
RT gamma.";
RL J. Immunol. 161:6715-6723(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ISOPRENYLATION AT CYS-586.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=9858320; DOI=10.1089/jir.1998.18.977;
RA Vestal D.J., Buss J.E., McKercher S.R., Jenkins N.A., Copeland N.G.,
RA Kelner G.S., Asundi V.K., Maki R.A.;
RT "Murine GBP-2: a new IFN-gamma-induced member of the GBP family of GTPases
RT isolated from macrophages.";
RL J. Interferon Cytokine Res. 18:977-985(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=10386861; DOI=10.1089/107999099313938;
RA Anderson S.L., Carton J.M., Zhang X., Rubin B.Y.;
RT "Genomic organization and chromosomal localization of a new member of the
RT murine interferon-induced guanylate-binding protein family.";
RL J. Interferon Cytokine Res. 19:487-494(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18025219; DOI=10.4049/jimmunol.179.11.7729;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=31964735; DOI=10.1128/mbio.02993-19;
RA Steffens N., Beuter-Gunia C., Kravets E., Reich A., Legewie L., Pfeffer K.,
RA Degrandi D.;
RT "Essential Role of mGBP7 for Survival of Toxoplasma gondii Infection.";
RL MBio 11:0-0(2020).
CC -!- FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions,
CC but the major reaction product is GDP (By similarity). Exhibits
CC antiviral activity against influenza virus. Promotes oxidative killing
CC and delivers antimicrobial peptides to autophagolysosomes, providing
CC broad host protection against different pathogen classes (By
CC similarity). Confers protection to the protozoan pathogen Toxoplasma
CC gondii (PubMed:18025219). {ECO:0000250|UniProtKB:P32455,
CC ECO:0000250|UniProtKB:P32456, ECO:0000269|PubMed:18025219}.
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:0000250|UniProtKB:P32456};
CC -!- SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is
CC required for the association with membranous structures. Heterodimer
CC with other family members, including GBP1, GBP3, GBP4 and GBP5.
CC {ECO:0000250|UniProtKB:P32456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32456}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P32456}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P32456}. Membrane
CC {ECO:0000250|UniProtKB:P32456}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P32456}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:31964735}. Note=GBP2-
CC GBP5 dimers localize to the Golgi apparatus.
CC {ECO:0000250|UniProtKB:P32456}.
CC -!- INDUCTION: By IFNG/IFN-gamma and IFNB1/IFN-beta (PubMed:9862701,
CC PubMed:18025219). Up-regulated upon infection by T.gondii or
CC L.monocytogenes (PubMed:18025219). {ECO:0000269|PubMed:18025219,
CC ECO:0000269|PubMed:9862701}.
CC -!- PTM: Isoprenylation is required for proper subcellular location.
CC {ECO:0000250|UniProtKB:P32456}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR EMBL; AJ007970; CAA07797.1; -; mRNA.
DR EMBL; AF077007; AAC98287.1; -; mRNA.
DR EMBL; AF109168; AAD39746.1; -; mRNA.
DR EMBL; CT010249; CAJ18457.1; -; mRNA.
DR EMBL; BC011336; AAH11336.1; -; mRNA.
DR EMBL; BC032882; AAH32882.1; -; mRNA.
DR CCDS; CCDS17880.1; -.
DR RefSeq; NP_034390.1; NM_010260.1.
DR AlphaFoldDB; Q9Z0E6; -.
DR SMR; Q9Z0E6; -.
DR BioGRID; 199847; 18.
DR IntAct; Q9Z0E6; 2.
DR STRING; 10090.ENSMUSP00000132435; -.
DR iPTMnet; Q9Z0E6; -.
DR PhosphoSitePlus; Q9Z0E6; -.
DR SwissPalm; Q9Z0E6; -.
DR EPD; Q9Z0E6; -.
DR MaxQB; Q9Z0E6; -.
DR PaxDb; Q9Z0E6; -.
DR PeptideAtlas; Q9Z0E6; -.
DR PRIDE; Q9Z0E6; -.
DR ProteomicsDB; 272939; -.
DR DNASU; 14469; -.
DR Ensembl; ENSMUST00000165774; ENSMUSP00000132435; ENSMUSG00000028270.
DR GeneID; 14469; -.
DR KEGG; mmu:14469; -.
DR UCSC; uc008roy.1; mouse.
DR CTD; 2634; -.
DR MGI; MGI:102772; Gbp2.
DR VEuPathDB; HostDB:ENSMUSG00000028270; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000162297; -.
DR HOGENOM; CLU_018608_2_2_1; -.
DR InParanoid; Q9Z0E6; -.
DR OMA; TFVWTLR; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q9Z0E6; -.
DR TreeFam; TF331602; -.
DR BioGRID-ORCS; 14469; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Gbp2; mouse.
DR PRO; PR:Q9Z0E6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9Z0E6; protein.
DR Bgee; ENSMUSG00000028270; Expressed in subcutaneous adipose tissue and 180 other tissues.
DR ExpressionAtlas; Q9Z0E6; baseline and differential.
DR Genevisible; Q9Z0E6; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IDA:MGI.
DR GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0019955; F:cytokine binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISS:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0044406; P:adhesion of symbiont to host; IDA:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:MGI.
DR GO; GO:0042832; P:defense response to protozoan; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR CDD; cd16269; GBP_C; 1.
DR Gene3D; 3.40.50.300; -; 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 Antimicrobial; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW GTP-binding; Hydrolase; Immunity; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..586
FT /note="Guanylate-binding protein 2"
FT /id="PRO_0000190966"
FT PROPEP 587..589
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370783"
FT DOMAIN 35..276
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..309
FT /note="GTPase domain (Globular)"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 67..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 97..101
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT MOD_RES 586
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 586
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:9858320"
FT CONFLICT 163
FT /note="V -> I (in Ref. 4; CAJ18457 and 5; AAH11336/
FT AAH32882)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="S -> T (in Ref. 3; AAD39746)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="E -> D (in Ref. 5; AAH11336)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 66739 MW; 8E68B0A3BC5F3AE3 CRC64;
MASEIHMSEP MCLIENTEAQ LVINQEALRI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG
KRTGFSLGST VQSHTKGIWM WCVPHPKKAG QTLVLLDTEG LEDVEKGDNQ NDCWIFALAV
LLSSTFIYNS IGTINQQAMD QLHYVTELTD LIKSKSSPDQ SGVDDSANFV GFFPTFVWTL
RDFSLELEVN GKPVTSDEYL EHSLTLKKGA DKKTKSFNEP RLCIRKFFPK RKCFIFDRPA
QRKQLSKLET LREEELCGEF VEQVAEFTSY ILSYSSVKTL CGGIIVNGPR LKSLVQTYVG
AISNGSLPCM ESAVLTLAQI ENSAAVQKAI THYEEQMNQK IQMPTETLQE LLDLHRPIES
EAIEVFLKNS FKDVDQKFQT ELGNLLVAKR DAFIKKNMDV SSARCSDLLE DIFGPLEEEV
KLGTFSKPGG YYLFLQMRQE LEKKYNQAPG KGLQAEAMLK NYFDSKADVV ETLLQTDQSL
TEAAKEVEEE RTKAEAAEAA NRELEKKQKE FELMMQQKEK SYQEHVKKLT EKMKDEQKQL
LAEQENIIAA KLREQEKFLK EGFENESKKL IREIDTLKQN KSSGKCTIL
