GBP7_HUMAN
ID GBP7_HUMAN Reviewed; 638 AA.
AC Q8N8V2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Guanylate-binding protein 7;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q91Z40};
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-14.
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP FUNCTION, AND 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 (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 (By similarity).
CC Promotes IFN-gamma-mediated host defense against bacterial infections
CC by regulating oxidative responses and bacteriolytic peptide generation
CC (By similarity). 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 (By
CC similarity). Participates along with GBP1 in trafficking
CC monoubiquinated protein cargo to autolysosomes for generating
CC ubiquitin-derived antimicrobial peptides (By similarity). Required for
CC disruption of the parasitophorous vacuole formed following T.gondii
CC infection and subsequent killing of the parasite (By similarity).
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
CC (PubMed:33408175). {ECO:0000250|UniProtKB:Q91Z40,
CC ECO:0000269|PubMed:33408175}.
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:Q91Z40};
CC -!- SUBUNIT: Monomer and dimer (By similarity). Interacts with CYBA, CYBA-
CC CYBB complex and ATG4B (By similarity). Interacts (via GB1/RHD3-type G
CC domain) with NCF2 and NCF2-NCF4 complex (By similarity).
CC {ECO:0000250|UniProtKB:Q91Z40}.
CC -!- INTERACTION:
CC Q8N8V2; Q96FN4: CPNE2; NbExp=3; IntAct=EBI-21835810, EBI-7097057;
CC Q8N8V2; Q96AL5: PBX3; NbExp=3; IntAct=EBI-21835810, EBI-741171;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q91Z40}.
CC -!- INDUCTION: Up-regulated in response to influenza virus A infection.
CC {ECO:0000269|PubMed:33408175}.
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; AK096141; BAC04709.1; -; mRNA.
DR EMBL; AC104459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS720.1; -.
DR RefSeq; NP_997281.2; NM_207398.2.
DR AlphaFoldDB; Q8N8V2; -.
DR SMR; Q8N8V2; -.
DR BioGRID; 132790; 12.
DR IntAct; Q8N8V2; 4.
DR STRING; 9606.ENSP00000294671; -.
DR iPTMnet; Q8N8V2; -.
DR PhosphoSitePlus; Q8N8V2; -.
DR BioMuta; GBP7; -.
DR DMDM; 311033384; -.
DR MassIVE; Q8N8V2; -.
DR MaxQB; Q8N8V2; -.
DR PaxDb; Q8N8V2; -.
DR PeptideAtlas; Q8N8V2; -.
DR PRIDE; Q8N8V2; -.
DR ProteomicsDB; 72463; -.
DR Antibodypedia; 53266; 60 antibodies from 17 providers.
DR DNASU; 388646; -.
DR Ensembl; ENST00000294671.3; ENSP00000294671.2; ENSG00000213512.3.
DR GeneID; 388646; -.
DR KEGG; hsa:388646; -.
DR MANE-Select; ENST00000294671.3; ENSP00000294671.2; NM_207398.3; NP_997281.2.
DR UCSC; uc001dna.2; human.
DR CTD; 388646; -.
DR GeneCards; GBP7; -.
DR HGNC; HGNC:29606; GBP7.
DR HPA; ENSG00000213512; Tissue enriched (liver).
DR MIM; 612468; gene.
DR neXtProt; NX_Q8N8V2; -.
DR OpenTargets; ENSG00000213512; -.
DR PharmGKB; PA142671744; -.
DR VEuPathDB; HostDB:ENSG00000213512; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000164365; -.
DR HOGENOM; CLU_018608_2_1_1; -.
DR InParanoid; Q8N8V2; -.
DR OMA; DYTLLPR; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q8N8V2; -.
DR TreeFam; TF331602; -.
DR PathwayCommons; Q8N8V2; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q8N8V2; -.
DR BioGRID-ORCS; 388646; 5 hits in 1057 CRISPR screens.
DR GenomeRNAi; 388646; -.
DR Pharos; Q8N8V2; Tbio.
DR PRO; PR:Q8N8V2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N8V2; protein.
DR Bgee; ENSG00000213512; Expressed in right lobe of liver and 34 other tissues.
DR ExpressionAtlas; Q8N8V2; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0042832; P:defense response to protozoan; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IMP:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IMP:UniProtKB.
DR GO; GO:0034345; P:negative regulation of type III interferon production; IMP:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP: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; Cytoplasmic vesicle; GTP-binding;
KW Hydrolase; Immunity; Membrane; Nucleotide-binding; Reference proteome.
FT CHAIN 1..638
FT /note="Guanylate-binding protein 7"
FT /id="PRO_0000313654"
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:0000250|UniProtKB:Q91Z40"
FT REGION 590..638
FT /note="C-terminal tail; required for its localization to
FT cytoplasmic vesicle"
FT /evidence="ECO:0000250|UniProtKB:Q91Z40"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q91Z40"
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 VARIANT 14
FT /note="T -> I (in dbSNP:rs676913)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_037687"
FT VARIANT 618
FT /note="G -> R (in dbSNP:rs1886297)"
FT /id="VAR_037688"
SQ SEQUENCE 638 AA; 72513 MW; A9F86253BED61276 CRC64;
MASEIHMPGP VCLTENTKGH LVVNSEALEI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG
KNKGFPLGCT VKSETKGIWM WCVPHPSKPN HTLILLDTEG LGDMEKSDPK SDSWIFALAV
LLSSSFVYNS MGTINHQALE QLHYVTELTE LIRAKSCPRP DEVEDSSEFV SFFPDFIWTV
RDFTLELKLD GHPITEDEYL ENALKLISGK NPQIQNSNKP REWIRHFFPK QKCFVFDRPI
NDKKLLLHVE EVREDQLDSN FQMQSENFCS YIFTHAKTKT LREGILVTGN RLGMLVETYL
DAINSGATPC LENAMAVLAQ CENSAAVQRA ANHYSQQMAQ QVRFPTDTLQ ELLDVHAVCE
REAIAVFMEY SFKDKSQEFQ KKLVDTMEKK KEDFVLQNEE ASAKYCQAEL KRLSELLTES
ISRGTFFVPG GHNIYLEAKK KIEQDYTLVP RKGVKADEVL QSFLQSQVVI EESILQSDKA
LTAGEKAIAA KQAKKEAAEK EQELLRQKQK EQQQMMEAQE RSFQENIAQL KKKMEREREN
YMRELRKMLS HKMKVLEELL TEGFKEIFES LNEEINRLKE QIEAAENEEP SVFSQILDVA
GSIFIAALPG AAKLVDLGMK ILSSLCNRLR NPGKKIIS
