IRGM1_MOUSE
ID IRGM1_MOUSE Reviewed; 409 AA.
AC Q60766; Q3TJ73;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Immunity-related GTPase family M protein 1;
DE EC=3.6.5.-;
DE AltName: Full=Interferon-inducible GTPase 3;
DE AltName: Full=Interferon-inducible protein 1;
DE AltName: Full=LPS-stimulated RAW 264.7 macrophage protein 47;
DE Short=LRG-47;
GN Name=Irgm1; Synonyms=Ifi1, Iigp3, Irgm;
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] (ISOFORM 1), AND INDUCTION BY LPS AND IFNG.
RC STRAIN=BALB/cJ;
RX PubMed=7561525; DOI=10.1002/jlb.58.4.477;
RA Sorace J.M., Johnson R.J., Howard D.L., Drysdale B.E.;
RT "Identification of an endotoxin and IFN-inducible cDNA: possible
RT identification of a novel protein family.";
RL J. Leukoc. Biol. 58:477-484(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Placenta, 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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP CATALYTIC ACTIVITY.
RX PubMed=8702776; DOI=10.1074/jbc.271.34.20399;
RA Taylor G.A., Jeffers M., Largaespada D.A., Jenkins N.A., Copeland N.G.,
RA Vande Woude G.F.;
RT "Identification of a novel GTPase, the inducibly expressed GTPase, that
RT accumulates in response to interferon gamma.";
RL J. Biol. Chem. 271:20399-20405(1996).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=11457893; DOI=10.1084/jem.194.2.181;
RA Collazo C.M., Yap G.S., Sempowski G.D., Lusby K.C., Tessarollo L.,
RA Vande Woude G.F., Sher A., Taylor G.A.;
RT "Inactivation of LRG-47 and IRG-47 reveals a family of interferon gamma-
RT inducible genes with essential, pathogen-specific roles in resistance to
RT infection.";
RL J. Exp. Med. 194:181-188(2001).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14576437; DOI=10.1126/science.1088063;
RA MacMicking J.D., Taylor G.A., McKinney J.D.;
RT "Immune control of tuberculosis by IFN-gamma-inducible LRG-47.";
RL Science 302:654-659(2003).
RN [8]
RP FUNCTION.
RX PubMed=15607973; DOI=10.1016/j.cell.2004.11.038;
RA Gutierrez M.G., Master S.S., Singh S.B., Taylor G.A., Colombo M.I.,
RA Deretic V.;
RT "Autophagy is a defense mechanism inhibiting BCG and Mycobacterium
RT tuberculosis survival in infected macrophages.";
RL Cell 119:753-766(2004).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=14707092; DOI=10.4049/jimmunol.172.2.1163;
RA Feng C.G., Collazo-Custodio C.M., Eckhaus M., Hieny S., Belkaid Y.,
RA Elkins K., Jankovic D., Taylor G.A., Sher A.;
RT "Mice deficient in LRG-47 display increased susceptibility to mycobacterial
RT infection associated with the induction of lymphopenia.";
RL J. Immunol. 172:1163-1168(2004).
RN [10]
RP SUBCELLULAR LOCATION, TOPOLOGY, INDUCTION BY IFNG, AND MUTAGENESIS OF
RP SER-90.
RX PubMed=15294976; DOI=10.4049/jimmunol.173.4.2594;
RA Martens S., Sabel K., Lange R., Uthaiah R., Wolf E., Howard J.C.;
RT "Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-
RT 47 and IIGP1 on cellular membranes: retargeting to plasma membrane induced
RT by phagocytosis.";
RL J. Immunol. 173:2594-2606(2004).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15908352; DOI=10.1128/iai.73.6.3278-3286.2005;
RA Butcher B.A., Greene R.I., Henry S.C., Annecharico K.L., Weinberg J.B.,
RA Denkers E.Y., Sher A., Taylor G.A.;
RT "p47 GTPases regulate Toxoplasma gondii survival in activated
RT macrophages.";
RL Infect. Immun. 73:3278-3286(2005).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=16339555; DOI=10.4049/jimmunol.175.12.8165;
RA Santiago H.C., Feng C.G., Bafica A., Roffe E., Arantes R.M., Cheever A.,
RA Taylor G.A., Vieira L.Q., Aliberti J., Gazzinelli R.T., Sher A.;
RT "Mice deficient in LRG-47 display enhanced susceptibility to Trypanosoma
RT cruzi infection associated with defective hemopoiesis and intracellular
RT control of parasite growth.";
RL J. Immunol. 175:8165-8172(2005).
RN [13]
RP FUNCTION, AND INDUCTION BY LPS.
RX PubMed=17911638; DOI=10.4049/jimmunol.179.8.5514;
RA Bafica A., Feng C.G., Santiago H.C., Aliberti J., Cheever A., Thomas K.E.,
RA Taylor G.A., Vogel S.N., Sher A.;
RT "The IFN-inducible GTPase LRG47 (Irgm1) negatively regulates TLR4-triggered
RT proinflammatory cytokine production and prevents endotoxemia.";
RL J. Immunol. 179:5514-5522(2007).
RN [14]
RP FUNCTION.
RX PubMed=17982087; DOI=10.4049/jimmunol.179.10.6963;
RA Henry S.C., Daniell X., Indaram M., Whitesides J.F., Sempowski G.D.,
RA Howell D., Oliver T., Taylor G.A.;
RT "Impaired macrophage function underscores susceptibility to Salmonella in
RT mice lacking Irgm1 (LRG-47).";
RL J. Immunol. 179:6963-6972(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, 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 [17]
RP FUNCTION.
RX PubMed=19920210; DOI=10.1189/jlb.0509299;
RA Henry S.C., Traver M., Daniell X., Indaram M., Oliver T., Taylor G.A.;
RT "Regulation of macrophage motility by Irgm1.";
RL J. Leukoc. Biol. 87:333-343(2010).
RN [18]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-356; ILE-358; VAL-359;
RP PHE-362; PHE-363; LEU-365 AND LEU-366.
RX PubMed=20072621; DOI=10.1371/journal.pone.0008648;
RA Zhao Y.O., Konen-Waisman S., Taylor G.A., Martens S., Howard J.C.;
RT "Localisation and mislocalisation of the interferon-inducible immunity-
RT related GTPase, Irgm1 (LRG-47) in mouse cells.";
RL PLoS ONE 5:E8648-E8648(2010).
CC -!- FUNCTION: Putative GTPase which is required for IFNG-mediated clearance
CC of acute protozoan and bacterial infections. Functions in innate immune
CC response probably through regulation of autophagy. May regulate pro-
CC inflammatory cytokine production and prevent endotoxemia upon
CC infection. Required for macrophage motility and possibly also for
CC adhesion. {ECO:0000269|PubMed:11457893, ECO:0000269|PubMed:14576437,
CC ECO:0000269|PubMed:14707092, ECO:0000269|PubMed:15607973,
CC ECO:0000269|PubMed:15908352, ECO:0000269|PubMed:16339555,
CC ECO:0000269|PubMed:17911638, ECO:0000269|PubMed:17982087,
CC ECO:0000269|PubMed:19920210}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane. Cell membrane.
CC Cytoplasmic vesicle, phagosome membrane. Cytoplasmic vesicle,
CC autophagosome membrane. Lysosome membrane. Late endosome membrane. Cell
CC projection, phagocytic cup. Note=Behaves like an integral membrane
CC protein. Recruited to the plasma membrane around forming phagocytic
CC cups, it remains associated with maturing phagosomes. Association with
CC phagosomes is dependent on nucleotide-binding but is IFNG-independent.
CC Preferentially associated with cis- and medial-Golgi. Also detected in
CC late endosomes and lysosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60766-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60766-2; Sequence=VSP_032384;
CC -!- TISSUE SPECIFICITY: Expressed in lung and primary macrophages.
CC {ECO:0000269|PubMed:14576437}.
CC -!- INDUCTION: Up-regulated by LPS and IFNG (at protein level). Up-
CC regulated upon infection by various pathogens including T.cruzi,
CC T.gondii, L.monocytogenes, M.tuberculosis and murine cytomegalovirus.
CC {ECO:0000269|PubMed:11457893, ECO:0000269|PubMed:14576437,
CC ECO:0000269|PubMed:14707092, ECO:0000269|PubMed:15294976,
CC ECO:0000269|PubMed:16339555, ECO:0000269|PubMed:17911638,
CC ECO:0000269|PubMed:7561525}.
CC -!- DISRUPTION PHENOTYPE: Mice do not show obvious abnormalities except a
CC loss of resistance to infection by S.typhimurium, T.cruzi, T.gondii,
CC L.monocytogenes and M.tuberculosis. Upon infection, alterations of
CC blood elements occur including lymphopenia, anemia, and
CC thrombocytopenia. {ECO:0000269|PubMed:11457893,
CC ECO:0000269|PubMed:14576437}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. IRG family. {ECO:0000255|PROSITE-ProRule:PRU01053,
CC ECO:0000305}.
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DR EMBL; U19119; AAB48942.1; -; mRNA.
DR EMBL; AK002545; BAB22176.1; -; mRNA.
DR EMBL; AK167558; BAE39622.1; -; mRNA.
DR EMBL; AK171743; BAE42645.1; -; mRNA.
DR EMBL; AL645849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145957; AAI45958.1; -; mRNA.
DR CCDS; CCDS24588.1; -. [Q60766-1]
DR CCDS; CCDS88149.1; -. [Q60766-2]
DR RefSeq; NP_032352.1; NM_008326.1. [Q60766-1]
DR AlphaFoldDB; Q60766; -.
DR SMR; Q60766; -.
DR BioGRID; 200520; 4.
DR IntAct; Q60766; 1.
DR MINT; Q60766; -.
DR STRING; 10090.ENSMUSP00000050446; -.
DR iPTMnet; Q60766; -.
DR PhosphoSitePlus; Q60766; -.
DR SwissPalm; Q60766; -.
DR EPD; Q60766; -.
DR jPOST; Q60766; -.
DR MaxQB; Q60766; -.
DR PaxDb; Q60766; -.
DR PeptideAtlas; Q60766; -.
DR PRIDE; Q60766; -.
DR ProteomicsDB; 268995; -. [Q60766-1]
DR ProteomicsDB; 268996; -. [Q60766-2]
DR DNASU; 15944; -.
DR Ensembl; ENSMUST00000049519; ENSMUSP00000050446; ENSMUSG00000046879. [Q60766-1]
DR Ensembl; ENSMUST00000097271; ENSMUSP00000094870; ENSMUSG00000046879. [Q60766-2]
DR GeneID; 15944; -.
DR KEGG; mmu:15944; -.
DR UCSC; uc007ipg.1; mouse. [Q60766-1]
DR CTD; 15944; -.
DR MGI; MGI:107567; Irgm1.
DR VEuPathDB; HostDB:ENSMUSG00000046879; -.
DR eggNOG; ENOG502QS9R; Eukaryota.
DR GeneTree; ENSGT00950000183007; -.
DR InParanoid; Q60766; -.
DR OMA; KEEVCEP; -.
DR OrthoDB; 688334at2759; -.
DR PhylomeDB; Q60766; -.
DR TreeFam; TF331897; -.
DR BioGRID-ORCS; 15944; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Irgm1; mouse.
DR PRO; PR:Q60766; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60766; protein.
DR Bgee; ENSMUSG00000046879; Expressed in submandibular gland and 196 other tissues.
DR ExpressionAtlas; Q60766; baseline and differential.
DR Genevisible; Q60766; MM.
DR GO; GO:0044754; C:autolysosome; IDA:UniProtKB.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051434; F:BH3 domain binding; ISO:MGI.
DR GO; GO:0050700; F:CARD domain binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IDA:UniProtKB.
DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; ISO:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0098586; P:cellular response to virus; ISO:MGI.
DR GO; GO:0006952; P:defense response; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:MGI.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0061635; P:regulation of protein complex stability; ISO:MGI.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
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 Alternative splicing; Autophagy; Cell membrane; Cell projection;
KW Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding; Hydrolase;
KW Immunity; Innate immunity; Lysosome; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..409
FT /note="Immunity-related GTPase family M protein 1"
FT /id="PRO_0000325750"
FT DOMAIN 75..251
FT /note="IRG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01053"
FT REGION 75..289
FT /note="Mediates targeting to cell membrane and phagosomes"
FT REGION 350..374
FT /note="Mediates targeting to the Golgi"
FT BINDING 84..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 109..113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 191..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 232..234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032384"
FT MUTAGEN 90
FT /note="S->N: Loss of targeting to plasma membrane and
FT phagosomes."
FT /evidence="ECO:0000269|PubMed:15294976"
FT MUTAGEN 356
FT /note="C->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:20072621"
FT MUTAGEN 358
FT /note="I->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:20072621"
FT MUTAGEN 359
FT /note="V->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:20072621"
FT MUTAGEN 360
FT /note="N->A: No effect on subcellular location. Abolishes
FT Golgi and lysosomal localization; when associated with A-
FT 364."
FT MUTAGEN 362
FT /note="F->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:20072621"
FT MUTAGEN 362
FT /note="F->EF: Disrupts amphipathicity and abolishes Golgi
FT localization; when associated with Glu-367."
FT /evidence="ECO:0000269|PubMed:20072621"
FT MUTAGEN 363
FT /note="F->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:20072621"
FT MUTAGEN 364
FT /note="R->A: No effect on subcellular location. Abolishes
FT Golgi and lysosomal localization; when associated with A-
FT 360 or A-367."
FT MUTAGEN 365
FT /note="L->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:20072621"
FT MUTAGEN 366
FT /note="L->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:20072621"
FT MUTAGEN 367
FT /note="R->A: No effect on subcellular location. Abolishes
FT Golgi and lysosomal localization; when associated with A-
FT 364."
FT MUTAGEN 367
FT /note="R->ER: Disrupts amphipathicity and abolishes Golgi
FT localization; when associated with Glu-362."
FT CONFLICT 151
FT /note="M -> V (in Ref. 2; BAE39622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 46552 MW; E4913367193059B6 CRC64;
MKPSHSSCEA APLLPNMAET HYAPLSSAFP FVTSYQTGSS RLPEVSRSTE RALREGKLLE
LVYGIKETVA TLSQIPVSIF VTGDSGNGMS SFINALRVIG HDEDASAPTG VVRTTKTRTE
YSSSHFPNVV LWDLPGLGAT AQTVEDYVEE MKFSTCDLFI IIASEQFSSN HVKLSKIIQS
MGKRFYIVWT KLDRDLSTSV LSEVRLLQNI QENIRENLQK EKVKYPPVFL VSSLDPLLYD
FPKLRDTLHK DLSNIRCCEP LKTLYGTYEK IVGDKVAVWK QRIANESLKN SLGVRDDDNM
GECLKVYRLI FGVDDESVQQ VAQSMGTVVM EYKDNMKSQN FYTLRREDWK LRLMTCAIVN
AFFRLLRFLP CVCCCLRRLR HKRMLFLVAQ DTKNILEKIL RDSIFPPQI
