TGTP1_MOUSE
ID TGTP1_MOUSE Reviewed; 415 AA.
AC Q62293; Q60711; Q8BN19;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=T-cell-specific guanine nucleotide triphosphate-binding protein 1;
DE EC=3.6.5.- {ECO:0000269|PubMed:9725230};
DE AltName: Full=Interferon-gamma-inducible GTPase Ifggb5 {ECO:0000303|PubMed:22892676};
GN Name=Tgtp1;
GN Synonyms=Ifggb5 {ECO:0000303|PubMed:22892676},
GN Irgb6 {ECO:0000303|PubMed:22892676}, Mg21 {ECO:0000303|PubMed:7884320};
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], INDUCTION BY IFNG, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Peritoneal macrophage;
RX PubMed=7884320; DOI=10.1002/jlb.57.3.477;
RA Lafuse W.P., Brown D., Castle L., Zwilling B.S.;
RT "Cloning and characterization of a novel cDNA that is IFN-gamma-induced in
RT mouse peritoneal macrophages and encodes a putative GTP-binding protein.";
RL J. Leukoc. Biol. 57:477-483(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic stem cell, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; 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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=7836757;
RA Carlow D.A., Marth J., Clark-Lewis I., Teh H.S.;
RT "Isolation of a gene encoding a developmentally regulated T cell-specific
RT protein with a guanine nucleotide triphosphate-binding motif.";
RL J. Immunol. 154:1724-1734(1995).
RN [7]
RP FUNCTION, INDUCTION BY IFNG, AND CATALYTIC ACTIVITY.
RX PubMed=9725230;
RA Carlow D.A., Teh S.J., Teh H.S.;
RT "Specific antiviral activity demonstrated by TGTP, a member of a new family
RT of interferon-induced GTPases.";
RL J. Immunol. 161:2348-2355(1998).
RN [8]
RP GENOMIC ORGANIZATION OF P47 GTPASE CLUSTER.
RX PubMed=16277747; DOI=10.1186/gb-2005-6-11-r92;
RA Bekpen C., Hunn J.P., Rohde C., Parvanova I., Guethlein L., Dunn D.M.,
RA Glowalla E., Leptin M., Howard J.C.;
RT "The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of the
RT cell autonomous resistance mechanism in the human lineage.";
RL Genome Biol. 6:R92.1-R92.18(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION BY
RP TNF, AND TISSUE SPECIFICITY.
RX PubMed=19285957; DOI=10.1016/j.bbrc.2009.03.043;
RA Yamada K., Akimoto H., Ogawa Y., Kinumi T., Kamagata Y., Ohmiya Y.;
RT "Upregulation of immunity-related GTPase (IRG) proteins by TNF-alpha in
RT murine astrocytes.";
RL Biochem. Biophys. Res. Commun. 382:434-439(2009).
RN [10]
RP FUNCTION.
RX PubMed=19265156; DOI=10.4049/jimmunol.0804190;
RA Zhao Y., Ferguson D.J., Wilson D.C., Howard J.C., Sibley L.D., Yap G.S.;
RT "Virulent Toxoplasma gondii evade immunity-related GTPase-mediated parasite
RT vacuole disruption within primed macrophages.";
RL J. Immunol. 182:3775-3781(2009).
RN [11]
RP IDENTIFICATION, AND GENOMIC ANALYSIS.
RX PubMed=22892676; DOI=10.1007/s10142-012-0291-2;
RA Premzl M.;
RT "Comparative genomic analysis of eutherian interferon-gamma-inducible
RT GTPases.";
RL Funct. Integr. Genomics 12:599-607(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, 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).
RN [13]
RP FUNCTION, AND INDUCTION BY IFNG.
RX PubMed=24563254; DOI=10.4049/jimmunol.1302822;
RA Ohshima J., Lee Y., Sasai M., Saitoh T., Su Ma J., Kamiyama N.,
RA Matsuura Y., Pann-Ghill S., Hayashi M., Ebisu S., Takeda K., Akira S.,
RA Yamamoto M.;
RT "Role of mouse and human autophagy proteins in IFN-gamma-induced cell-
RT autonomous responses against Toxoplasma gondii.";
RL J. Immunol. 192:3328-3335(2014).
CC -!- FUNCTION: Involved in innate cell-autonomous resistance to
CC intracellular pathogens, such as Toxoplasma gondii. During avirulent
CC type II T. gondii infection, recruited to the parasitophorous vacuole
CC (PV) membrane, leading to PV vesiculation and rupture, and subsequent
CC digestion of the parasite within the cytosol (PubMed:19265156,
CC PubMed:24563254). Not recruited to virulent type I T. gondii PV
CC membrane (PubMed:19265156). May confer an antiviral state for vesicular
CC stomatitis virus (PubMed:9725230). {ECO:0000269|PubMed:19265156,
CC ECO:0000269|PubMed:24563254, ECO:0000269|PubMed:9725230}.
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:0000269|PubMed:9725230};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19285957}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:19285957}. Golgi apparatus
CC {ECO:0000269|PubMed:19285957}. Note=In astrocytes stimulated with IFNG
CC or TNF, diffuse cytoplasmic localization decreases and the protein
CC partially relocalizes to the endoplasmic reticulum and Golgi apparatus
CC (PubMed:19285957). Due to sequence similarity with Tgtp2, it is
CC impossible to assign unambiguously experimental data published in the
CC literature to Tgtp1 or Tgtp2 gene (Probable).
CC {ECO:0000269|PubMed:19285957, ECO:0000305|PubMed:22892676}.
CC -!- TISSUE SPECIFICITY: Expressed in thymus and lymph nodes, predominantly
CC T-cells. Not expressed by immature CD4(+) CD8(+) thymocytes (at protein
CC level) (PubMed:7836757). Expressed in IFNG-stimulated macrophages
CC (PubMed:7884320). Expressed at low levels in unstimulated astrocytes
CC (PubMed:19285957). Due to sequence similarity with Tgtp2, it is
CC impossible to assign unambiguously experimental data published in the
CC literature to Tgtp1 or Tgtp2 gene. {ECO:0000269|PubMed:19285957,
CC ECO:0000269|PubMed:7836757, ECO:0000269|PubMed:7884320}.
CC -!- INDUCTION: In macrophages, up-regulated by IFNG, but not by IL2, IL4,
CC IL10, nor TNF (PubMed:7884320). Up-regulated by IFNG in lymph node
CC cells and thymocytes and other cell types (PubMed:7836757,
CC PubMed:9725230, PubMed:24563254). In astrocytes, up-regulated by TNF
CC and IFNG; when both cytokines are combined, the effect is synergistic
CC (PubMed:19285957). Due to sequence similarity with Tgtp2, it is
CC impossible to assign unambiguously experimental data published in the
CC literature to Tgtp1 or Tgtp2 gene (Probable).
CC {ECO:0000269|PubMed:19285957, ECO:0000269|PubMed:24563254,
CC ECO:0000269|PubMed:7836757, ECO:0000269|PubMed:7884320,
CC ECO:0000269|PubMed:9725230, ECO:0000305|PubMed:22892676}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. IRG family. {ECO:0000255|PROSITE-ProRule:PRU01053,
CC ECO:0000305}.
CC -!- CAUTION: The gene Tgtp1 belongs to a large family of eutherian IFNG-
CC inducible GTPases, called immunity-related p47 GTPases, which comprises
CC a variable amount of paralogs depending upon the species studied. In
CC C57BL/6J mice, there is over 20 genes, whereas humans have only one
CC ortholog. Tgtp1 closest paralog is Tgtp2. Both genes encode identical
CC proteins. At the nucleotide sequence level, their CDSs differ at only 4
CC positions. Consequently it is almost impossible to assign unambiguously
CC to one gene or the other experimental data published in the literature.
CC {ECO:0000305|PubMed:16277747, ECO:0000305|PubMed:22892676}.
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; U15636; AAA66220.1; -; mRNA.
DR EMBL; AK089836; BAC40974.1; -; mRNA.
DR EMBL; AK163978; BAE37565.1; -; mRNA.
DR EMBL; AK172473; BAE43026.1; -; mRNA.
DR EMBL; AL627237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466575; EDL33781.1; -; Genomic_DNA.
DR EMBL; BC085259; AAH85259.1; -; mRNA.
DR EMBL; FR734025; CBY65988.1; -; Genomic_DNA.
DR CCDS; CCDS24593.1; -.
DR PIR; I56251; I56251.
DR RefSeq; NP_001138636.1; NM_001145164.1.
DR RefSeq; NP_035709.3; NM_011579.3.
DR AlphaFoldDB; Q62293; -.
DR SMR; Q62293; -.
DR IntAct; Q62293; 1.
DR STRING; 10090.ENSMUSP00000045025; -.
DR iPTMnet; Q62293; -.
DR PhosphoSitePlus; Q62293; -.
DR EPD; Q62293; -.
DR MaxQB; Q62293; -.
DR PaxDb; Q62293; -.
DR PRIDE; Q62293; -.
DR DNASU; 21822; -.
DR Ensembl; ENSMUST00000046745; ENSMUSP00000045025; ENSMUSG00000078921.
DR Ensembl; ENSMUST00000068063; ENSMUSP00000069914; ENSMUSG00000078922.
DR GeneID; 100039796; -.
DR GeneID; 21822; -.
DR KEGG; mmu:100039796; -.
DR KEGG; mmu:21822; -.
DR UCSC; uc007ipm.3; mouse.
DR CTD; 100039796; -.
DR CTD; 21822; -.
DR MGI; MGI:98734; Tgtp1.
DR VEuPathDB; HostDB:ENSMUSG00000078921; -.
DR VEuPathDB; HostDB:ENSMUSG00000078922; -.
DR eggNOG; ENOG502S70P; Eukaryota.
DR GeneTree; ENSGT00950000183007; -.
DR HOGENOM; CLU_015342_2_0_1; -.
DR InParanoid; Q62293; -.
DR OMA; LMANLKC; -.
DR OrthoDB; 688334at2759; -.
DR PhylomeDB; Q62293; -.
DR TreeFam; TF331897; -.
DR BioGRID-ORCS; 100039796; 1 hit in 37 CRISPR screens.
DR BioGRID-ORCS; 21822; 4 hits in 39 CRISPR screens.
DR ChiTaRS; Tgtp1; mouse.
DR PRO; PR:Q62293; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q62293; protein.
DR Bgee; ENSMUSG00000078921; Expressed in thymus and 70 other tissues.
DR ExpressionAtlas; Q62293; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0035455; P:response to interferon-alpha; IDA:MGI.
DR GO; GO:0034341; P:response to interferon-gamma; IDA:MGI.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030385; G_IRG_dom.
DR InterPro; IPR007743; Immunity-related_GTPase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF05049; IIGP; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51716; G_IRG; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Golgi apparatus; GTP-binding; Hydrolase;
KW Immunity; Innate immunity; Nucleotide-binding; Reference proteome.
FT CHAIN 1..415
FT /note="T-cell-specific guanine nucleotide triphosphate-
FT binding protein 1"
FT /id="PRO_0000437942"
FT DOMAIN 55..237
FT /note="IRG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01053"
FT BINDING 64..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 89..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 218..220
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 91
FT /note="A -> G (in Ref. 1; AAA66220)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="E -> G (in Ref. 2; BAC40974)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47121 MW; 3AFB5F940242952A CRC64;
MAWASSFDAF FKNFKRESKI ISEYDITLIM TYIEENKLQK AVSVIEKVLR DIESAPLHIA
VTGETGAGKS TFINTLRGVG HEEKGAAPTG AIETTMKRTP YPHPKLPNVT IWDLPGIGTT
NFTPQNYLTE MKFGEYDFFI IISATRFKEN DAQLAKAIAQ MGMNFYFVRT KIDSDLDNEQ
KFKPKSFNKE EVLKNIKDYC SNHLQESLDS EPPVFLVSNV DISKYDFPKL ETKLLQDLPA
HKRHVFSLSL QSLTEATINY KRDSLKQKVF LEAMKAGALA TIPLGGMISD ILENLDETFN
LYRSYFGLDD ASLENIAQDL NMSVDDFKVH LRFPHLFAEH NDESLEDKLF KYIKHISSVT
GGPVAAVTYY RMAYYLQNLF LDTAANDAIA LLNSKALFEK KVGPYISEPP EYWEA
