GBP4_MOUSE
ID GBP4_MOUSE Reviewed; 620 AA.
AC Q61107; Q8VEC5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Guanylate-binding protein 4;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q96PP9};
DE AltName: Full=GTP-binding protein 3;
DE Short=GBP-3;
DE AltName: Full=GTP-binding protein 4;
DE Short=GBP-4;
DE AltName: Full=Guanine nucleotide-binding protein 4;
DE AltName: Full=Guanylate-binding protein 3;
GN Name=Gbp4; Synonyms=Gbp3;
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], FUNCTION, GTPASE ACTIVITY, INDUCTION,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9659399; DOI=10.1016/s0167-4838(98)00034-x;
RA Han B.H., Park D.J., Lim R.W., Im J.H., Kim H.D.;
RT "Cloning, expression, and characterization of a novel guanylate-binding
RT protein, GBP3 in murine erythroid progenitor cells.";
RL Biochim. Biophys. Acta 1384:373-386(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; 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 [3]
RP INDUCTION.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, Pancreas, 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).
CC -!- FUNCTION: Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP
CC rather than GMP is the major reaction product. Plays a role in
CC erythroid differentiation. {ECO:0000269|PubMed:9659399}.
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:Q96PP9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77.0 uM for GTP {ECO:0000269|PubMed:9659399};
CC Vmax=21 pmol/min/ug enzyme {ECO:0000269|PubMed:9659399};
CC -!- SUBUNIT: Heterodimer with other family members, including GBP1, GBP2
CC and GBP5. Dimerization regulates subcellular location.
CC {ECO:0000250|UniProtKB:Q96PP9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96PP9}. Nucleus
CC {ECO:0000250|UniProtKB:Q96PP9}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q96PP9}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q96PP9}. Note=Heterodimers with GBP1, GBP2 and
CC GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a
CC vesicle-like compartment, with GBP2, around the nucleus and with GBP-5,
CC at the Golgi apparatus. {ECO:0000250|UniProtKB:Q96PP9}.
CC -!- TISSUE SPECIFICITY: Brain, lung, heart, spleen, kidney, liver and
CC intestine. {ECO:0000269|PubMed:9659399}.
CC -!- INDUCTION: By IFNG/IFN-gamma, IFNB1/IFN-beta and TNF-alpha
CC (PubMed:9659399, PubMed:18025219). Up-regulated upon infection by
CC T.gondii or L.monocytogenes (PubMed:18025219).
CC {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:9659399}.
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; U44731; AAA86645.1; -; mRNA.
DR EMBL; BC019195; AAH19195.1; -; mRNA.
DR CCDS; CCDS17879.1; -.
DR RefSeq; NP_001276421.1; NM_001289492.1.
DR RefSeq; NP_001276422.1; NM_001289493.1.
DR RefSeq; NP_061204.3; NM_018734.3.
DR RefSeq; XP_006501784.1; XM_006501721.2.
DR RefSeq; XP_006501787.1; XM_006501724.2.
DR AlphaFoldDB; Q61107; -.
DR SMR; Q61107; -.
DR BioGRID; 207732; 3.
DR STRING; 10090.ENSMUSP00000101828; -.
DR iPTMnet; Q61107; -.
DR PhosphoSitePlus; Q61107; -.
DR EPD; Q61107; -.
DR MaxQB; Q61107; -.
DR PaxDb; Q61107; -.
DR PeptideAtlas; Q61107; -.
DR PRIDE; Q61107; -.
DR ProteomicsDB; 267769; -.
DR DNASU; 55932; -.
DR Ensembl; ENSMUST00000029935; ENSMUSP00000029935; ENSMUSG00000028268.
DR Ensembl; ENSMUST00000106221; ENSMUSP00000101828; ENSMUSG00000028268.
DR Ensembl; ENSMUST00000106222; ENSMUSP00000101829; ENSMUSG00000028268.
DR GeneID; 55932; -.
DR KEGG; mmu:55932; -.
DR UCSC; uc008rou.2; mouse.
DR CTD; 2635; -.
DR MGI; MGI:1926263; Gbp3.
DR VEuPathDB; HostDB:ENSMUSG00000028268; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000163522; -.
DR HOGENOM; CLU_018608_2_1_1; -.
DR InParanoid; Q61107; -.
DR OMA; MQSDNFC; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q61107; -.
DR TreeFam; TF331602; -.
DR BioGRID-ORCS; 55932; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Gbp4; mouse.
DR PRO; PR:Q61107; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61107; protein.
DR Bgee; ENSMUSG00000028268; Expressed in peripheral lymph node and 197 other tissues.
DR ExpressionAtlas; Q61107; baseline and differential.
DR Genevisible; Q61107; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; ISO: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; ISS:MGI.
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:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
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 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 Coiled coil; Cytoplasm; Golgi apparatus; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..620
FT /note="Guanylate-binding protein 4"
FT /id="PRO_0000261160"
FT DOMAIN 29..271
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..304
FT /note="GTPase domain (Globular)"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT COILED 375..411
FT /evidence="ECO:0000255"
FT COILED 477..582
FT /evidence="ECO:0000255"
FT BINDING 39..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 61..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT CONFLICT 184
FT /note="N -> K (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="K -> R (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="Q -> P (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="L -> P (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="M -> V (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="I -> M (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="L -> P (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="I -> V (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="I -> T (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="I -> V (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="S -> N (in Ref. 2; AAH19195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 70801 MW; 62C73E7FD71D8885 CRC64;
MEAPICLVEN WKNQLTVNLE AIRILEQIAQ PLVVVAIVGL YRTGKSYLMN RLAGRNHGFS
LGSTVQSETK GIWMWCVPHP TKPTHTLVLL DTEGLGDVEK GDPKNDSWIF ALAVLLSSTF
VYNSMSTINQ QALEQLHFVT ELTQLIRAKS SPREDKVKDS SEFVGFFPDF IWAVRDFALE
LKLNGRPITE DEYLENALKL IQGDNLKVQQ SNMTRECIRY FFPVRKCFVF DRPTSDKRLL
LQIENVPENQ LERNFQVESE KFCSYIFTNG KTKTLRGGVI VTGNRLGTLV QTYVNAINSG
TVPCLENAVT TLAQRENSIA VQKAADHYSE QMAQRMRLPT DTLQELLTVH AACEKEAIAV
FMEHSFKDDE QEFQKKLVVT IEERKEEFIR QNEAASIRHC QAELERLSES LRKSISCGAF
SVPGGHSLYL EARKKIELGY QQVLRKGVKA KEVLKSFLQS QAIMEDSILQ SDKALTDGER
AIAAERTKKE VAEKELELLR QRQKEQEQVM EAQERSFREN IAKLQEKMES EKEMLLREQE
KMLEHKLKVQ EELLIEGFRE KSDMLKNEIS HLREEMERTR RKPSLFGQIL DTIGNAFIMI
LPGAGKLFGV GLKFLGSLSS
