GBP7_MOUSE
ID GBP7_MOUSE Reviewed; 638 AA.
AC Q91Z40; Q6KAN1; Q78UK8; Q8BU48;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Guanylate-binding protein 7;
DE EC=3.6.5.- {ECO:0000269|PubMed:21551061, ECO:0000269|PubMed:31689351};
DE AltName: Full=GTP-binding protein 7;
DE Short=GBP-7;
DE AltName: Full=Guanine nucleotide-binding protein 7;
DE AltName: Full=Guanylate-binding protein 4-like;
GN Name=Gbp7; Synonyms=Gbp4l;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION, FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
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].
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, SUBCELLULAR LOCATION, INTERACTION WITH NCF2;
RP NCF2-NCF4 COMPLEX; CYBA; CYBA-CYBB COMPLEX AND ATG4B, AND MUTAGENESIS OF
RP 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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-51.
RX PubMed=31689351; DOI=10.1042/bcj20190364;
RA Legewie L., Loschwitz J., Steffens N., Prescher M., Wang X., Smits S.H.J.,
RA Schmitt L., Strodel B., Degrandi D., Pfeffer K.;
RT "Biochemical and structural characterization of murine GBP7, a guanylate
RT binding protein with an elongated C-terminal tail.";
RL Biochem. J. 476:3161-3182(2019).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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).
RN [10]
RP INDUCTION.
RX PubMed=33408175; DOI=10.1128/jvi.02038-20;
RA Feng M., Zhang Q., Wu W., Chen L., Gu S., Ye Y., Zhong Y., Huang Q.,
RA Liu S.;
RT "Inducible Guanylate-Binding Protein 7 Facilitates Influenza A Virus
RT Replication by Suppressing Innate Immunity via NF-kappaB and JAK-STAT
RT Signaling Pathways.";
RL J. Virol. 95:0-0(2021).
CC -!- FUNCTION: Hydrolyzes GTP to GMP in two consecutive cleavage reactions
CC and predominantly uses GTP and not GDP or GMP as the substrate
CC (PubMed:21551061, PubMed:31689351). Confers protection to several
CC pathogens, including the bacterial pathogens Listeria monocytogenes and
CC Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma
CC gondii (PubMed:21551061, PubMed:31964735, PubMed:18025219). Promotes
CC IFN-gamma-mediated host defense against bacterial infections by
CC regulating oxidative responses and bacteriolytic peptide generation
CC (PubMed:21551061). May help to assemble NADPH oxidase on phagosomal
CC membranes by acting as a bridging protein between NADPH oxidase
CC cytosolic subunits NCF2-NCF4 and the membrane subunits CYBA-CYBB
CC (PubMed:21551061). Participates along with GBP1 in trafficking
CC monoubiquinated protein cargo to autolysosomes for generating
CC ubiquitin-derived antimicrobial peptides (PubMed:21551061). Required
CC for disruption of the parasitophorous vacuole formed following T.gondii
CC infection and subsequent killing of the parasite (PubMed:31964735).
CC Facilitates influenza A virus replication by inhibiting the activation
CC of NF-kappaB and JAK-STAT signaling pathways and the expression of type
CC I, type III interferons and pro-inflammatory cytokines (By similarity).
CC {ECO:0000250|UniProtKB:Q8N8V2, ECO:0000269|PubMed:21551061,
CC ECO:0000269|PubMed:31689351, ECO:0000269|PubMed:31964735,
CC 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, ECO:0000269|PubMed:31689351};
CC -!- ACTIVITY REGULATION: Inhibited by orthovanadate, berylium fluoride and
CC aluminum flouride. {ECO:0000269|PubMed:31689351}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=207 uM for GTP {ECO:0000269|PubMed:31689351};
CC Vmax=278 nmol/min/mg enzyme toward GTP {ECO:0000269|PubMed:31689351};
CC -!- SUBUNIT: Monomer and dimer (PubMed:31689351). Interacts with CYBA,
CC CYBA-CYBB complex and ATG4B (PubMed:21551061). Interacts (via GB1/RHD3-
CC type G domain) with NCF2 and NCF2-NCF4 complex (PubMed:21551061).
CC {ECO:0000269|PubMed:21551061, ECO:0000269|PubMed:31689351}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N8V2}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:18025219,
CC ECO:0000269|PubMed:21551061, ECO:0000269|PubMed:31689351,
CC ECO:0000269|PubMed:31964735}.
CC -!- INDUCTION: By IFNG/IFN-gamma and IFNB1/IFN-beta (PubMed:18025219). Up-
CC regulated upon infection by T.gondii or L.monocytogenes
CC (PubMed:18025219). Up-regulated in response to influenza virus A
CC infection (PubMed:33408175). {ECO:0000269|PubMed:18025219,
CC ECO:0000269|PubMed:33408175}.
CC -!- DISRUPTION PHENOTYPE: Mice show a dramatic susceptibility to T. gondii
CC infection, resulting in rapid death of infected mice in the acute phase
CC of infection. A significantly increased parasite load seen in the
CC spleen, liver and the peritoneal fluid, with markedly elevated
CC production of pro-inflammatory cytokines and development of severe
CC ascites. {ECO:0000269|PubMed:31964735}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29526.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD21426.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK087751; BAC39989.1; -; mRNA.
DR EMBL; AK131176; BAD21426.1; ALT_INIT; mRNA.
DR EMBL; AK036666; BAC29526.1; ALT_INIT; mRNA.
DR EMBL; GL456099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010229; AAH10229.2; -; mRNA.
DR EMBL; BK005760; DAA05846.1; -; mRNA.
DR CCDS; CCDS38657.1; -.
DR RefSeq; NP_001076781.1; NM_001083312.2.
DR RefSeq; NP_663520.2; NM_145545.4.
DR AlphaFoldDB; Q91Z40; -.
DR SMR; Q91Z40; -.
DR STRING; 10090.ENSMUSP00000049104; -.
DR iPTMnet; Q6KAN1; -.
DR EPD; Q91Z40; -.
DR MaxQB; Q91Z40; -.
DR PaxDb; Q91Z40; -.
DR PRIDE; Q91Z40; -.
DR ProteomicsDB; 343543; -.
DR DNASU; 229900; -.
DR Ensembl; ENSMUST00000045097; ENSMUSP00000049104; ENSMUSG00000040253.
DR Ensembl; ENSMUST00000171263; ENSMUSP00000132970; ENSMUSG00000040253.
DR GeneID; 229900; -.
DR KEGG; mmu:229900; -.
DR UCSC; uc008ros.2; mouse.
DR CTD; 388646; -.
DR MGI; MGI:2444421; Gbp7.
DR VEuPathDB; HostDB:ENSMUSG00000040253; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000163522; -.
DR HOGENOM; CLU_018608_2_1_1; -.
DR InParanoid; Q91Z40; -.
DR OMA; DYTLLPR; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q91Z40; -.
DR TreeFam; TF331602; -.
DR BioGRID-ORCS; 229900; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Gbp7; mouse.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q91Z40; protein.
DR Bgee; ENSMUSG00000040253; Expressed in interventricular septum and 148 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IMP:UniProtKB.
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: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; IDA:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0034345; P:negative regulation of type III interferon production; ISS:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISS:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
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; Coiled coil; Cytoplasmic vesicle;
KW GTP-binding; Hydrolase; Immunity; Membrane; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..638
FT /note="Guanylate-binding protein 7"
FT /id="PRO_0000454379"
FT DOMAIN 35..277
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..310
FT /note="GTPase domain (Globular)"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT REGION 311..638
FT /note="Interaction with the CYBA-CYBB complex"
FT /evidence="ECO:0000269|PubMed:21551061"
FT REGION 590..638
FT /note="C-terminal tail; required for its localization to
FT cytoplasmic vesicle"
FT /evidence="ECO:0000269|PubMed:31689351"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:21551061,
FT ECO:0000305|PubMed:31689351"
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 MUTAGEN 48
FT /note="R->P: Loss of localization to cytoplasmic vesicle."
FT /evidence="ECO:0000269|PubMed:21551061"
FT MUTAGEN 51
FT /note="K->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:31689351"
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 638 AA; 72721 MW; E4827ED839A8A98D CRC64;
MASGPNMEAP VCLVENENEE LRVNSKAINI LERITQPVVV VAIVGLYRTG KSYLMNRLAG
QNHGFNLGTT VRSETKGIWM WCVPHPSKPK FTLVLLDTEG LGDVEKGDPK NDSWIFALAV
LLSSTFVYNS MSTINHQALE QLHYVTELTE RIRAKSTSRS EEVDDSDEFV SFFPDFIWTV
RDFVLELKLE GRVITADEYL ENALKLIPGM SIKAQKANLP RECIRHFFPR RKCFVFDRPT
KDKELLVHVE EMPEDQLDHS FQVQSKEFCS YIFSNSKAKT LKEGIVVNGN RLATLVTTYV
DAINSGDVPC LENAVTTLAQ RENSIAVQKA ADHYSEQMAQ RMRLPTDTLQ ELLTVHTACE
KEAIAVFMEH SFKDENQQFQ KNLVVTIEEK KEDFLRQNEA ASLSHCQAEL DKLSESLRES
ISRGVFSVPG GHRLYLEARK KVEQDYERVP RKGVKANHVL QSFLQSQISI EDSIMQSDKA
LTDGQKAMEA ERAQKEAAEK EQELLRQKQK ELQQVMEAQE RSYKENVAQL HEKMETERKN
ILREQEVKLE HKLKIQKDML NEGFKRKCEA MDLEISQLQK EIQLNKEKNS SLGAKILDGF
GDVLISVVPG SGKYFGLGLK ILSSQMNQTQ NSDKVRKL
