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 02-DEC-2020, entry version 130. DE RecName: Full=Guanylate-binding protein 7; 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). CC -!- FUNCTION: Hydrolyzes GTP to GMP in two consecutive cleavage reactions. CC Promotes oxidative killing and delivers antimicrobial peptides to CC autophagolysosomes, providing broad host protection against different CC pathogen classes (By similarity). {ECO:0000250}. 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}. 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 SMR; Q8N8V2; -. DR BioGRID; 132790; 4. 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; 58 antibodies. DR Ensembl; ENST00000294671; ENSP00000294671; ENSG00000213512. DR GeneID; 388646; -. DR KEGG; hsa:388646; -. DR UCSC; uc001dna.2; human. DR CTD; 388646; -. DR EuPathDB; HostDB:ENSG00000213512.1; -. 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 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 BioGRID-ORCS; 388646; 1 hit in 837 CRISPR screens. DR GenomeRNAi; 388646; -. DR Pharos; Q8N8V2; Tdark. DR PRO; PR:Q8N8V2; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8N8V2; protein. DR Bgee; ENSG00000213512; Expressed in liver and 23 other tissues. DR ExpressionAtlas; Q8N8V2; baseline and differential. DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. 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; IBA:GO_Central. DR CDD; cd16269; GBP_C; 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; GTP-binding; Membrane; Nucleotide-binding; Polymorphism; 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 NP_BIND 45..52 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 67..69 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 97..101 FT /note="GTP" FT /evidence="ECO:0000250" FT REGION 1..310 FT /note="GTPase domain (Globular)" FT /evidence="ECO:0000250" 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 //