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 14-DEC-2022, entry version 138. 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}. 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; 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 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 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 type II interferon; 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; 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; 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 //