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 24-JUL-2024, entry version 147. DE RecName: Full=Guanylate-binding protein 7; DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q91Z40}; 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: Interferon (IFN)-inducible GTPase that plays important roles CC in innate immunity against a diverse range of bacterial, viral and CC protozoan pathogens (By similarity). Hydrolyzes GTP to GMP in two CC consecutive cleavage reactions and predominantly uses GTP and not GDP CC or GMP as the substrate (By similarity). Following infection, recruited CC to the pathogen-containing vacuoles or vacuole-escaped bacteria and CC acts as a positive regulator of inflammasome assembly by promoting the CC release of inflammasome ligands from bacteria (By similarity). Acts by CC promoting lysis of pathogen-containing vacuoles, releasing pathogens CC into the cytosol (By similarity). Following pathogen release in the CC cytosol, promotes recruitment of proteins that mediate bacterial CC cytolysis: this liberates ligands that are detected by inflammasomes, CC such as lipopolysaccharide (LPS) that activates the non-canonical CC CASP4/CASP11 inflammasome or double-stranded DNA (dsDNA) that activates CC the AIM2 inflammasome (By similarity). Also promotes IFN-gamma-mediated CC host defense against bacterial infections by regulating oxidative CC responses and bacteriolytic peptide generation (By similarity). May CC help to assemble NADPH oxidase on phagosomal membranes by acting as a CC bridging protein between NADPH oxidase cytosolic subunits NCF2-NCF4 and CC the membrane subunits CYBA-CYBB (By similarity). Participates along CC with GBP1 in trafficking monoubiquinated protein cargo to autolysosomes CC for generating ubiquitin-derived antimicrobial peptides (By CC similarity). Facilitates influenza A virus replication by inhibiting CC the activation of NF-kappaB and JAK-STAT signaling pathways and the CC expression of type I, type III interferons and pro-inflammatory CC cytokines (PubMed:33408175). Confers protection to several pathogens, CC including the bacterial pathogens Listeria monocytogenes and CC Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma CC gondii (By similarity). Required for disruption of the parasitophorous CC vacuole formed following T.gondii infection and subsequent killing of CC the parasite (By similarity). {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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:Q91Z40}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:Q91Z40}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; 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: Cytoplasmic vesicle membrane 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}. 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; 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; 5. DR MINT; Q8N8V2; -. DR STRING; 9606.ENSP00000294671; -. DR iPTMnet; Q8N8V2; -. DR PhosphoSitePlus; Q8N8V2; -. DR BioMuta; GBP7; -. DR DMDM; 311033384; -. DR MassIVE; Q8N8V2; -. DR PaxDb; 9606-ENSP00000294671; -. DR PeptideAtlas; 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 AGR; HGNC:29606; -. DR CTD; 388646; -. DR DisGeNET; 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; CDMDDQE; -. DR OrthoDB; 5309032at2759; -. 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 1135 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 33 other cell types or tissues. DR ExpressionAtlas; Q8N8V2; baseline and differential. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle 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 type II interferon; IBA:GO_Central. DR GO; GO:0051715; P:cytolysis in another organism; ISS:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB. 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 canonical NF-kappaB signal transduction; IMP:UniProtKB. 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:SF92; GUANYLATE-BINDING PROTEIN 7; 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 1: Evidence at protein level; KW Antimicrobial; Antiviral defense; Cytoplasmic vesicle; GTP-binding; KW Hydrolase; Immunity; Innate immunity; Membrane; Nucleotide-binding; KW 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 //