GBP1_MOUSE
ID GBP1_MOUSE Reviewed; 589 AA.
AC Q01514; Q32MT4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Guanylate-binding protein 1;
DE EC=3.6.5.- {ECO:0000269|PubMed:21551061};
DE AltName: Full=GTP-binding protein 1;
DE Short=GBP-1;
DE Short=mGBP-1;
DE Short=mGBP1;
DE AltName: Full=Guanine nucleotide-binding protein 1;
DE AltName: Full=Interferon-gamma-inducible protein MAG-1;
DE AltName: Full=Interferon-induced guanylate-binding protein 1;
GN Name=Gbp1; Synonyms=Gbp-1, Mag-1, Mpa1;
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.
RX PubMed=1753106;
RA Wynn T.A., Nicolet C.M., Paulnock D.M.;
RT "Identification and characterization of a new gene family induced during
RT macrophage activation.";
RL J. Immunol. 147:4384-4392(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1715024; DOI=10.1128/mcb.11.9.4717-4725.1991;
RA Cheng Y.-S.E., Patterson C.E., Staeheli P.;
RT "Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus
RT motif and bind GMP in addition to GDP and GTP.";
RL Mol. Cell. Biol. 11:4717-4725(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP ISOPRENYLATION AT CYS-586.
RX PubMed=10888661; DOI=10.1091/mbc.11.7.2191;
RA Stickney J.T., Buss J.E.;
RT "Murine guanylate-binding protein: incomplete geranylgeranyl isoprenoid
RT modification of an interferon-gamma-inducible guanosine triphosphate-
RT binding protein.";
RL Mol. Biol. Cell 11:2191-2200(2000).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP INTERACTION WITH SQSTM1, AND MUTAGENESIS OF ARG-48 AND SER-52.
RX PubMed=21551061; DOI=10.1126/science.1201711;
RA Kim B.H., Shenoy A.R., Kumar P., Das R., Tiwari S., MacMicking J.D.;
RT "A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial
RT infection.";
RL Science 332:717-721(2011).
CC -!- FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions
CC (PubMed:21551061). Confers protection to several pathogens, including
CC the bacterial pathogens Listeria monocytogenes and Mycobacterium bovis
CC BCG as well as the protozoan pathogen Toxoplasma gondii
CC (PubMed:21551061, PubMed:18025219). Promotes IFN-gamma-mediated host
CC defense against bacterial infections by regulating bacteriolytic
CC peptide generation through its interaction with ubiquitin-binding
CC protein SQSTM1, which delivers monoubiquitylated proteins to
CC autolysosomes for the generation of bacteriolytic peptides
CC (PubMed:21551061). Exhibits antiviral activity against influenza virus
CC (By similarity). {ECO:0000250|UniProtKB:P32455,
CC ECO:0000269|PubMed:21551061, ECO:0000303|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:0000269|PubMed:21551061};
CC -!- SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is
CC required for the second hydrolysis step from GDP to GMP. Heterodimer
CC with other family members, including GBP2, GBP3, GBP4 and GBP5.
CC Dimerization regulates subcellular location to membranous structures
CC (By similarity). Interacts with SQSTM1 (PubMed:21551061).
CC {ECO:0000250|UniProtKB:P32455, ECO:0000269|PubMed:21551061}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32455}. Golgi
CC apparatus membrane; Lipid-anchor {ECO:0000250|UniProtKB:P32455};
CC Cytoplasmic side. Cell membrane {ECO:0000250|UniProtKB:P32455}.
CC Secreted {ECO:0000250|UniProtKB:P32455}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:21551061}.
CC Note=Secreted from endothelial cells in the cerebrospinal fluid, upon
CC bacterial challenge and independently of IFNG induction. Golgi membrane
CC localization requires isoprenylation and the presence of another IFNG-
CC induced factor (By similarity).
CC -!- INDUCTION: By IFNG/IFN-gamma and CpG oligodeoxynucleotides
CC (PubMed:1753106, PubMed:18025219). Up-regulated upon infection by
CC T.gondii or L.monocytogenes (PubMed:18025219).
CC {ECO:0000269|PubMed:1753106, ECO:0000269|PubMed:18025219}.
CC -!- PTM: Isoprenylation of mouse GBP1 is incomplete. It persistently exists
CC in the cell as a mixture of C20-modified and (more predominantly)
CC unmodified form. Prenylation is required for proper subcellular
CC location (By similarity). {ECO:0000250|UniProtKB:P32455,
CC ECO:0000269|PubMed:10888661}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit normal T-cell, B-cell, and
CC phagocytic cell profiles in the spleen and Ly6G(+)neutrophils in
CC peripheral blood but macrophages show impaired killing activities
CC (PubMed:21551061). Infection of Gbp1-/- mice results in severe
CC listeriosis or M. bovis BCG-induced morbidity owing to massively
CC increased bacterial replication in the target organs, whereas wild-type
CC mice can control the infection (PubMed:21551061).
CC {ECO:0000269|PubMed:21551061}.
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; M63961; AAA39486.1; -; mRNA.
DR EMBL; M55544; AAA37666.1; -; mRNA.
DR EMBL; BC108990; AAI08991.1; -; mRNA.
DR CCDS; CCDS38658.1; -.
DR PIR; A46459; A46459.
DR AlphaFoldDB; Q01514; -.
DR SMR; Q01514; -.
DR STRING; 10090.ENSMUSP00000029936; -.
DR iPTMnet; Q01514; -.
DR PhosphoSitePlus; Q01514; -.
DR SwissPalm; Q01514; -.
DR MaxQB; Q01514; -.
DR PaxDb; Q01514; -.
DR PeptideAtlas; Q01514; -.
DR PRIDE; Q01514; -.
DR UCSC; uc008ror.1; mouse.
DR MGI; MGI:95666; Gbp1.
DR eggNOG; KOG2037; Eukaryota.
DR InParanoid; Q01514; -.
DR PhylomeDB; Q01514; -.
DR ChiTaRS; Gbp2b; mouse.
DR PRO; PR:Q01514; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q01514; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IDA:MGI.
DR GO; GO:0019002; F:GMP binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; 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:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; 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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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; Antiviral defense; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Hydrolase; Immunity;
KW Lipoprotein; Membrane; Nucleotide-binding; Prenylation; Reference proteome;
KW Secreted.
FT CHAIN 1..589
FT /note="Guanylate-binding protein 1"
FT /id="PRO_0000190965"
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 47..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:21551061"
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 LIPID 586
FT /note="S-geranylgeranyl cysteine; partial"
FT /evidence="ECO:0000269|PubMed:10888661"
FT MUTAGEN 48
FT /note="R->P: Loss of localization to cytoplasmic vesicle."
FT /evidence="ECO:0000269|PubMed:21551061"
FT MUTAGEN 52
FT /note="S->N: Loss of catalytic activity and localization to
FT cytoplasmic vesicle."
FT /evidence="ECO:0000269|PubMed:21551061"
SQ SEQUENCE 589 AA; 67712 MW; 1A2947DF443640CE CRC64;
MASEIHMSEP MCLIENTEAQ LVINQEALRI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG
KRTGFSLGST VQSHTKGIWM WCVPHPKKAG QTLVLLDTEG LEDVEKGDNQ 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
