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   27-MAR-2024, entry version 50.
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: Interferon (IFN)-inducible GTPase that plays important roles
CC       in innate immunity against a diverse range of bacterial, viral and
CC       protozoan pathogens, such as bacterial pathogens Listeria monocytogenes
CC       and Mycobacterium bovis BCG as well as the protozoan pathogen
CC       Toxoplasma gondii (PubMed:18025219, PubMed:21551061). Confers
CC       protection to several pathogens, including the bacterial pathogens
CC       Listeria monocytogenes and Mycobacterium bovis BCG as well as the
CC       protozoan pathogen Toxoplasma gondii (PubMed:18025219,
CC       PubMed:21551061). {ECO:0000269|PubMed:18025219,
CC       ECO:0000269|PubMed:21551061}.
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}.
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; 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   AlphaFoldDB; A0A0G2JDV3; -.
DR   SMR; A0A0G2JDV3; -.
DR   STRING; 10090.ENSMUSP00000142518; -.
DR   PhosphoSitePlus; A0A0G2JDV3; -.
DR   EPD; A0A0G2JDV3; -.
DR   PaxDb; 10090-ENSMUSP00000062528; -.
DR   ProteomicsDB; 351492; -.
DR   DNASU; 100702; -.
DR   AGR; MGI:2140937; -.
DR   MGI; MGI:2140937; Gbp6.
DR   VEuPathDB; HostDB:ENSMUSG00000104713; -.
DR   eggNOG; KOG2037; Eukaryota.
DR   InParanoid; A0A0G2JDV3; -.
DR   OrthoDB; 5309032at2759; -.
DR   BioGRID-ORCS; 100702; 7 hits in 44 CRISPR screens.
DR   ChiTaRS; Gbp6; mouse.
DR   PRO; PR:A0A0G2JDV3; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; A0A0G2JDV3; Protein.
DR   Bgee; ENSMUSG00000104713; Expressed in thymus and 66 other cell types or 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:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR   GO; GO:0071346; P:cellular response to type II interferon; 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; 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:SF126; GUANYLATE-BINDING PROTEIN 6; 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   2: Evidence at transcript level;
KW   Antimicrobial; Cytoplasmic vesicle; GTP-binding; Hydrolase; Immunity;
KW   Innate immunity; 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
//