GBP6_MOUSE
ID GBP6_MOUSE Reviewed; 611 AA.
AC A0A0G2JDV3; Q6PEN2; Q6ZQL8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Guanylate-binding protein 6;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P32455};
DE AltName: Full=GTP-binding protein 6;
DE Short=GBP-6;
DE AltName: Full=Guanine nucleotide-binding protein 6;
DE AltName: Full=Macrophage activation 2 like protein;
GN Name=Gbp6; Synonyms=Mpa2l;
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].
RA Kanehori K., Ishibashi T., Chiba Y., Fujimori K., Hiraoka S., Tanai H.,
RA Watanabe S., Ishida S., Ono Y., Hotuta T., Watanabe M., Sugiyama T.,
RA Irie R., Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J.,
RA Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Matsuo K.,
RA Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M.,
RA Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., Suzuki Y.,
RA Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.;
RT "NEDO cDNA sequencing project.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; 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 [4]
RP IDENTIFICATION, 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 [5]
RP FUNCTION.
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 (By
CC similarity). Confers protection to several pathogens, including the
CC bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG
CC as well as the protozoan pathogen Toxoplasma gondii (PubMed:21551061,
CC PubMed:18025219). {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:0000250|UniProtKB:P32455};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:18025219}.
CC -!- INDUCTION: By IFNG/IFN-gamma, IFNB1/IFN-beta, LPS and CpG
CC oligodeoxynucleotides (PubMed:18025219). Up-regulated upon infection by
CC T.gondii or L.monocytogenes (PubMed:18025219).
CC {ECO:0000269|PubMed:18025219}.
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; AK128993; BAC87667.1; -; mRNA.
DR EMBL; GL456119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057969; AAH57969.1; -; mRNA.
DR EMBL; BC115768; AAI15769.1; -; mRNA.
DR EMBL; BK005759; DAA05845.1; -; mRNA.
DR CCDS; CCDS19492.1; -.
DR RefSeq; NP_919317.2; NM_194336.2.
DR RefSeq; XP_006534750.1; XM_006534687.2.
DR AlphaFoldDB; A0A0G2JDV3; -.
DR EPD; A0A0G2JDV3; -.
DR PaxDb; A0A0G2JDV3; -.
DR ProteomicsDB; 351492; -.
DR DNASU; 100702; -.
DR GeneID; 100702; -.
DR KEGG; mmu:100702; -.
DR CTD; 163351; -.
DR MGI; MGI:2140937; Gbp6.
DR VEuPathDB; HostDB:ENSMUSG00000104713; -.
DR eggNOG; KOG2037; Eukaryota.
DR OMA; KESIEWD; -.
DR OrthoDB; 1027269at2759; -.
DR BioGRID-ORCS; 100702; 7 hits in 39 CRISPR screens.
DR ChiTaRS; Gbp6; mouse.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; A0A0G2JDV3; protein.
DR Bgee; ENSMUSG00000104713; Expressed in thymus and 66 other tissues.
DR ExpressionAtlas; A0A0G2JDV3; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Antimicrobial; Cytoplasmic vesicle; GTP-binding; Hydrolase; Immunity;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..611
FT /note="Guanylate-binding protein 6"
FT /id="PRO_0000454378"
FT DOMAIN 33..275
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..308
FT /note="GTPase domain (Globular)"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 65..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 95..99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT CONFLICT 130
FT /note="I -> N (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="P -> L (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="T -> I (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="R -> K (in Ref. 3; AAH57969)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="N -> D (in Ref. 3; AAH57969)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="D -> S (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="R -> S (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="A -> V (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="M -> I (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="E -> D (in Ref. 3; AAH57969)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="K -> R (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="L -> I (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="E -> D (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
FT CONFLICT 600..601
FT /note="LF -> VC (in Ref. 1; BAC87667 and 3; AAH57969/
FT AAI15769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 70443 MW; EE7A45391ECA71C1 CRC64;
MTQPQMAPIC LVENHNEQLS VNQEAIEILD KISQPVVVVA IVGLYRTGKS YLMNCLAGQN
HGFPLGSTVQ SQTKGIWMWC MPHPTKPEHT LVLLDTEGLG DVEKGDPKND LWIFALSVLL
SSTFIYNSMI TINHQALEQL QYVTELTELI RAKSSPNPAG IKNSTEFVSF FPDFVWTVRD
FMLELKLNGE DITSDDYLEN ALKLIPGDKP RMQASNSCRE CIRLFFPNRK CFVFDRPTHD
KELLQKLDSI TEDQLDPKFQ EVTKAFVSYI FTYAKIKTLK EGIKVTGNRL GILVTTYVNA
INSGAVPCLD DAVTTLAQRE NSVAVQKAAD HYSEQMAQRL RLPTETLQEL LDVHAACEKE
AMAVFMEHSF KDENQQFLKK LVELIGENKE LFLSKNEEAS NKYCQEELDR LSKDFMENIS
TFFVPCGHKL YMDKREKIEH DYWQVPRKGV KASEVFQSFL QSQAFIESSI LQADTALTAG
EKAIAEERAQ KVAAEKEQEL LRQKQKEQQE YMEAQEKSHK ENLEQLRRKL EQEREQDIKD
HDMMLKKLMK DQKAFLEEGF KKKAEEMNKE IQQLRDVIKD KKRNTDRIKE ALLNGFSTVL
FHYLVRYLKH L
