INGR1_HUMAN
ID INGR1_HUMAN Reviewed; 489 AA.
AC P15260; B4DFT7; E1P587; Q53Y96;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Interferon gamma receptor 1 {ECO:0000312|HGNC:HGNC:5439};
DE Short=IFN-gamma receptor 1;
DE Short=IFN-gamma-R1;
DE AltName: Full=CDw119;
DE AltName: Full=Interferon gamma receptor alpha-chain {ECO:0000303|PubMed:7615558, ECO:0000303|PubMed:9367779};
DE Short=IFN-gamma-R-alpha {ECO:0000303|PubMed:7615558};
DE AltName: CD_antigen=CD119;
DE Flags: Precursor;
GN Name=IFNGR1 {ECO:0000312|HGNC:HGNC:5439};
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 [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=2971451; DOI=10.1016/0092-8674(88)90050-5;
RA Aguet M., Dembic Z., Merlin G.;
RT "Molecular cloning and expression of the human interferon-gamma receptor.";
RL Cell 55:273-280(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-61; PRO-335 AND
RP PRO-467.
RG SeattleSNPs variation discovery resource;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [8]
RP DISULFIDE BONDS, PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS.
RX PubMed=8443182; DOI=10.1021/bi00060a038;
RA Stueber D., Friedlein A., Fountoulakis M., Lahm H.-W., Garotta G.;
RT "Alignment of disulfide bonds of the extracellular domain of the interferon
RT gamma receptor and investigation of their role in biological activity.";
RL Biochemistry 32:2423-2430(1993).
RN [9]
RP FUNCTION, INTERACTION WITH STAT1, AND PHOSPHORYLATION AT TYR-457.
RX PubMed=8156998; DOI=10.1002/j.1460-2075.1994.tb06422.x;
RA Greenlund A.C., Farrar M.A., Viviano B.L., Schreiber R.D.;
RT "Ligand-induced IFN gamma receptor tyrosine phosphorylation couples the
RT receptor to its signal transduction system (p91).";
RL EMBO J. 13:1591-1600(1994).
RN [10]
RP FUNCTION, INTERACTION WITH IFNGR2 AND JAK1, AND PHOSPHORYLATION.
RX PubMed=7615558; DOI=10.1074/jbc.270.29.17528;
RA Sakatsume M., Igarashi K., Winestock K.D., Garotta G., Larner A.C.,
RA Finbloom D.S.;
RT "The Jak kinases differentially associate with the alpha and beta
RT (accessory factor) chains of the interferon gamma receptor to form a
RT functional receptor unit capable of activating STAT transcription
RT factors.";
RL J. Biol. Chem. 270:17528-17534(1995).
RN [11]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=7673114; DOI=10.1074/jbc.270.36.20915;
RA Kotenko S.V., Izotova L.S., Pollack B.P., Mariano T.M., Donnelly R.J.,
RA Muthukumaran G., Cook J.R., Garotta G., Silvennoinen O., Ihle J.N.;
RT "Interaction between the components of the interferon gamma receptor
RT complex.";
RL J. Biol. Chem. 270:20915-20921(1995).
RN [12]
RP INVOLVEMENT IN SUSCEPTIBILITY TO SYSTEMIC LUPUS ERYTHEMATOSUS, AND VARIANT
RP MET-14.
RX PubMed=10079289; DOI=10.1007/s002510050492;
RA Tanaka Y., Nakashima H., Hisano C., Kohsaka T., Nemoto Y., Niiro H.,
RA Otsuka T., Otsuka T., Imamura T., Niho Y.;
RT "Association of the interferon-gamma receptor variant (Val14Met) with
RT systemic lupus erythematosus.";
RL Immunogenetics 49:266-271(1999).
RN [13]
RP INVOLVEMENT IN IMD27B.
RX PubMed=10192386; DOI=10.1038/7701;
RA Jouanguy E., Lamhamedi-Cherradi S., Lammas D., Dorman S.E.,
RA Fondaneche M.C., Dupuis S., Doeffinger R., Altare F., Girdlestone J.,
RA Emile J.F., Ducoulombier H., Edgar D., Clarke J., Oxelius V.A., Brai M.,
RA Novelli V., Heyne K., Fischer A., Holland S.M., Kumararatne D.S.,
RA Schreiber R.D., Casanova J.L.;
RT "A human IFNGR1 small deletion hotspot associated with dominant
RT susceptibility to mycobacterial infection.";
RL Nat. Genet. 21:370-378(1999).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION, UBIQUITINATION, MUTAGENESIS OF LYS-277; LYS-279 AND LYS-285, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28883123; DOI=10.1042/bcj20170548;
RA Londino J.D., Gulick D.L., Lear T.B., Suber T.L., Weathington N.M.,
RA Masa L.S., Chen B.B., Mallampalli R.K.;
RT "Post-translational modification of the interferon-gamma receptor alters
RT its stability and signaling.";
RL Biochem. J. 474:3543-3557(2017).
RN [16]
RP PHOSPHORYLATION, AND UBIQUITINATION.
RX PubMed=29343571; DOI=10.1128/jvi.00006-18;
RA Xia C., Wolf J.J., Vijayan M., Studstill C.J., Ma W., Hahm B.;
RT "Casein Kinase 1alpha Mediates the Degradation of Receptors for Type I and
RT Type II Interferons Caused by Hemagglutinin of Influenza A Virus.";
RL J. Virol. 92:0-0(2018).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-248, AND FUNCTION.
RX PubMed=7617032; DOI=10.1038/376230a0;
RA Walter M.R., Windsor W.T., Nagabhushan T.L., Lundell D.J., Lunn C.A.,
RA Zauodny P.J., Narula S.K.;
RT "Crystal structure of a complex between interferon-gamma and its soluble
RT high-affinity receptor.";
RL Nature 376:230-235(1995).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-122 IN COMPLEX WITH ANTIBODY.
RX PubMed=9367779; DOI=10.1006/jmbi.1997.1336;
RA Sogabe S., Stuart F., Henke C., Bridges A., Williams G., Birch A.,
RA Winkler F.K., Robinson J.A.;
RT "Neutralizing epitopes on the extracellular interferon gamma receptor
RT (IFNgammaR) alpha-chain characterized by homolog scanning mutagenesis and
RT X-ray crystal structure of the A6 fab-IFNgammaR1-108 complex.";
RL J. Mol. Biol. 273:882-897(1997).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF COMPLEX WITH IFNG, AND FUNCTION.
RX PubMed=10986460; DOI=10.1016/s0969-2126(00)00184-2;
RA Thiel D.J., le Du M.-H., Walter R.L., D'Arcy A., Chene C., Fountoulakis M.,
RA Garotta G., Winkler F.K., Ealick S.E.;
RT "Observation of an unexpected third receptor molecule in the crystal
RT structure of human interferon-gamma receptor complex.";
RL Structure 8:927-936(2000).
RN [20]
RP VARIANT IMD27A THR-87.
RX PubMed=9389728; DOI=10.1172/jci119810;
RA Jouanguy E., Lamhamedi-Cherradi S.-E., Altare F., Fondaneche M.-C.,
RA Tuerlinckx D., Blanche S., Emile J.-F., Gaillard J.-L., Schreiber R.,
RA Levin M., Fischer A., Hivroz C., Casanova J.-L.;
RT "Partial interferon-gamma receptor 1 deficiency in a child with tuberculoid
RT bacillus Calmette-Guerin infection and a sibling with clinical
RT tuberculosis.";
RL J. Clin. Invest. 100:2658-2664(1997).
RN [21]
RP REVIEW, VARIANT IMD27A THR-37, AND VARIANTS ARG-180 AND LYS-197.
RX PubMed=28744922; DOI=10.1002/humu.23302;
RA van de Vosse E., van Dissel J.T.;
RT "IFN-gammaR1 defects: Mutation update and description of the IFNGR1
RT variation database.";
RL Hum. Mutat. 38:1286-1296(2017).
RN [22]
RP VARIANTS IMD27A GLU-61; TYR-77; 99-TRP--VAL-102 DEL AND GLU-218 DEL, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10811850; DOI=10.1172/jci9166;
RA Jouanguy E., Dupuis S., Pallier A., Doffinger R., Fondaneche M.-C.,
RA Fieschi C., Lamhamedi-Cherradi S., Altare F., Emile J.-F., Lutz P.,
RA Bordigoni P., Cokugras H., Akcakaya N., Landman-Parker J., Donnadieu J.,
RA Camcioglu Y., Casanova J.-L.;
RT "In a novel form of IFN-gamma receptor 1 deficiency, cell surface receptors
RT fail to bind IFN-gamma.";
RL J. Clin. Invest. 105:1429-1436(2000).
RN [23]
RP VARIANT IMD27A GLY-63.
RX PubMed=11139207; DOI=10.1128/cdli.8.1.133-137.2001;
RA Allende L.M., Lopez-Goyanes A., Paz-Artal E., Corell A., Garcia-Perez M.A.,
RA Varela P., Scarpellini A., Negreira S., Palenque E., Arnaiz-Villena A.;
RT "A point mutation in a domain of gamma interferon receptor 1 provokes
RT severe immunodeficiency.";
RL Clin. Diagn. Lab. Immunol. 8:133-137(2001).
RN [24]
RP VARIANT MET-14.
RX PubMed=11240951; DOI=10.1067/mai.2001.113051;
RA Nakao F., Ihara K., Kusuhara K., Sasaki Y., Kinukawa N., Takabayashi A.,
RA Nishima S., Hara T.;
RT "Association of IFN-gamma and IFN regulatory factor 1 polymorphisms with
RT childhood atopic asthma.";
RL J. Allergy Clin. Immunol. 107:499-504(2001).
RN [25]
RP VARIANT IMD27B 278-GLU--SER-489 DEL.
RX PubMed=11335768; DOI=10.1542/peds.107.4.e47;
RA Villella A., Picard C., Jouanguy E., Dupuis S., Popko S., Abughali N.,
RA Meyerson H., Casanova J.L., Hostoffer R.W.;
RT "Recurrent Mycobacterium avium osteomyelitis associated with a novel
RT dominant interferon gamma receptor mutation.";
RL Pediatrics 107:E47-E47(2001).
RN [26]
RP INVOLVEMENT IN SUSCEPTIBILITY TO HELICOBACTER PYLORI INFECTION, AND
RP VARIANTS PRO-335 AND PRO-467.
RX PubMed=12516030; DOI=10.1086/367714;
RA Thye T., Burchard G.D., Nilius M., Mueller-Myhsok B., Horstmann R.D.;
RT "Genomewide linkage analysis identifies polymorphism in the human
RT interferon-gamma receptor affecting Helicobacter pylori infection.";
RL Am. J. Hum. Genet. 72:448-453(2003).
RN [27]
RP VARIANT PRO-467.
RX PubMed=12851715;
RA Aoki M., Matsui E., Kaneko H., Inoue R., Fukao T., Watanabe M.,
RA Teramoto T., Kato Z., Suzuki K., Suzuki Y., Kasahara K., Kondo N.;
RT "A novel single-nucleotide substitution, Leu 467 Pro, in the interferon-
RT gamma receptor 1 gene associated with allergic diseases.";
RL Int. J. Mol. Med. 12:185-191(2003).
RN [28]
RP VARIANTS IMD27A CYS-66 AND TYR-77.
RX PubMed=15589309; DOI=10.1016/s0140-6736(04)17552-1;
RA Dorman S.E., Picard C., Lammas D., Heyne K., van Dissel J.T., Baretto R.,
RA Rosenzweig S.D., Newport M., Levin M., Roesler J., Kumararatne D.,
RA Casanova J.L., Holland S.M.;
RT "Clinical features of dominant and recessive interferon gamma receptor 1
RT deficiencies.";
RL Lancet 364:2113-2121(2004).
RN [29]
RP VARIANT IMD27A PHE-77.
RX PubMed=16715106; DOI=10.1038/sj.bmt.1705399;
RA Chantrain C.F., Bruwier A., Brichard B., Largent V., Chapgier A.,
RA Feinberg J., Casanova J.L., Stalens J.P., Vermylen C.;
RT "Successful hematopoietic stem cell transplantation in a child with active
RT disseminated Mycobacterium fortuitum infection and interferon-gamma
RT receptor 1 deficiency.";
RL Bone Marrow Transplant. 38:75-76(2006).
RN [30]
RP VARIANT IMD27A THR-87.
RX PubMed=16195661; DOI=10.1159/000088682;
RA Remiszewski P., Roszkowska-Sliz B., Winek J., Chapgier A., Feinberg J.,
RA Langfort R., Bestry I., Augustynowicz-Kopec E., Ptak J., Casanova J.L.,
RA Rowinska-Zakrzewska E.;
RT "Disseminated Mycobacterium avium infection in a 20-year-old female with
RT partial recessive IFNgammaR1 deficiency.";
RL Respiration 73:375-378(2006).
RN [31]
RP VARIANT IMD27A TYR-85, AND CHARACTERIZATION OF VARIANT IMD27A TYR-85.
RX PubMed=17514500; DOI=10.1007/s10875-007-9097-8;
RA Noordzij J.G., Hartwig N.G., Verreck F.A., De Bruin-Versteeg S.,
RA De Boer T., Van Dissel J.T., De Groot R., Ottenhoff T.H., Van Dongen J.J.;
RT "Two patients with complete defects in interferon gamma receptor-dependent
RT signaling.";
RL J. Clin. Immunol. 27:490-496(2007).
RN [32]
RP VARIANT IMD27A 113-TYR--SER-489 DEL.
RX PubMed=20186794; DOI=10.1002/ajmg.a.33291;
RA Prando C., Boisson-Dupuis S., Grant A.V., Kong X.F., Bustamante J.,
RA Feinberg J., Chapgier A., Rose Y., Janniere L., Rizzardi E., Zhang Q.,
RA Shanahan C.M., Viollet L., Lyonnet S., Abel L., Ruga E.M., Casanova J.L.;
RT "Paternal uniparental isodisomy of chromosome 6 causing a complex syndrome
RT including complete IFN-gamma receptor 1 deficiency.";
RL Am. J. Med. Genet. A 152A:622-629(2010).
RN [33]
RP CHARACTERIZATION OF VARIANTS IMD27A GLU-61; GLY-63; CYS-66; PHE-77; TYR-77;
RP TYR-85 AND THR-87, CHARACTERIZATION OF VARIANTS MET-14; ILE-61; LEU-149;
RP PRO-335; MET-352 AND PRO-467, FUNCTION, AND MUTAGENESIS OF VAL-61.
RX PubMed=20015550; DOI=10.1016/j.molimm.2009.11.016;
RA van de Wetering D., de Paus R.A., van Dissel J.T., van de Vosse E.;
RT "Functional analysis of naturally occurring amino acid substitutions in
RT human IFN-gammaR1.";
RL Mol. Immunol. 47:1023-1030(2010).
RN [34]
RP VARIANT IMD27A PHE-485.
RX PubMed=22708048; DOI=10.4084/mjhid.2012.033;
RA Galal N., Boutros J., Marsafy A., Kong X.F., Feinberg J., Casanova J.L.,
RA Boisson-Dupuis S., Bustamante J.;
RT "Mendelian susceptibility to mycobacterial disease in egyptian children.";
RL Mediterr. J. Hematol. Infect. Dis. 4:E2012033-E2012033(2012).
RN [35]
RP VARIANT IMD27A ARG-219.
RX PubMed=25592983; DOI=10.1016/j.jaci.2014.11.030;
RA Tesi B., Sieni E., Neves C., Romano F., Cetica V., Cordeiro A.I.,
RA Chiang S., Schlums H., Galli L., Avenali S., Tondo A., Canessa C.,
RA Henter J.I., Nordenskjoeld M., Hsu A.P., Holland S.M., Neves J.F.,
RA Azzari C., Bryceson Y.T.;
RT "Hemophagocytic lymphohistiocytosis in 2 patients with underlying IFN-gamma
RT receptor deficiency.";
RL J. Allergy Clin. Immunol. 135:1638-1641(2015).
RN [36]
RP CHARACTERIZATION OF VARIANTS MET-14; ILE-61 AND CYS-397.
RX PubMed=26343451; DOI=10.1016/j.jaci.2015.06.047;
RA Gao L., Bin L., Rafaels N.M., Huang L., Potee J., Ruczinski I., Beaty T.H.,
RA Paller A.S., Schneider L.C., Gallo R., Hanifin J.M., Beck L.A., Geha R.S.,
RA Mathias R.A., Barnes K.C., Leung D.Y.M.;
RT "Targeted deep sequencing identifies rare loss-of-function variants in
RT IFNGR1 for risk of atopic dermatitis complicated by eczema herpeticum.";
RL J. Allergy Clin. Immunol. 136:1591-1600(2015).
RN [37]
RP VARIANT IMD27A 224-TRP--SER-489 DEL.
RX PubMed=27868075; DOI=10.1177/2324709616675463;
RA Gutierrez M.J., Kalra N., Horwitz A., Nino G.;
RT "Novel mutation of interferon-gamma receptor 1 gene presenting as early
RT life mycobacterial bronchial disease.";
RL J. Investig. Med. High Impact Case Rep.
RL 4:2324709616675463-2324709616675463(2016).
CC -!- FUNCTION: Receptor subunit for interferon gamma/INFG that plays crucial
CC roles in antimicrobial, antiviral, and antitumor responses by
CC activating effector immune cells and enhancing antigen presentation
CC (PubMed:20015550). Associates with transmembrane accessory factor
CC IFNGR2 to form a functional receptor (PubMed:7615558, PubMed:2971451,
CC PubMed:7617032, PubMed:10986460, PubMed:7673114). Upon ligand binding,
CC the intracellular domain of IFNGR1 opens out to allow association of
CC downstream signaling components JAK1 and JAK2. In turn, activated JAK1
CC phosphorylates IFNGR1 to form a docking site for STAT1. Subsequent
CC phosphorylation of STAT1 leads to dimerization, translocation to the
CC nucleus, and stimulation of target gene transcription
CC (PubMed:28883123). STAT3 can also be activated in a similar manner
CC although activation seems weaker. IFNGR1 intracellular domain
CC phosphorylation also provides a docking site for SOCS1 that regulates
CC the JAK-STAT pathway by competing with STAT1 binding to IFNGR1 (By
CC similarity). {ECO:0000250|UniProtKB:P15261,
CC ECO:0000269|PubMed:10986460, ECO:0000269|PubMed:20015550,
CC ECO:0000269|PubMed:28883123, ECO:0000269|PubMed:2971451,
CC ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7617032,
CC ECO:0000269|PubMed:7673114}.
CC -!- SUBUNIT: Monomer (PubMed:9367779). Heterodimer with IFNGR2, to form the
CC IFNG receptor complex (PubMed:7615558). Interacts with JAK1
CC (PubMed:7615558). Interacts (when phosphorylated) with STAT1
CC (PubMed:8156998). Interacts with SOCS1 (By similarity).
CC {ECO:0000250|UniProtKB:P15261, ECO:0000269|PubMed:7615558,
CC ECO:0000269|PubMed:8156998, ECO:0000269|PubMed:9367779}.
CC -!- INTERACTION:
CC P15260; Q13520: AQP6; NbExp=3; IntAct=EBI-1030755, EBI-13059134;
CC P15260; P01579: IFNG; NbExp=3; IntAct=EBI-1030755, EBI-1030767;
CC P15260; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-1030755, EBI-10317425;
CC P15260; Q96GQ5: RUSF1; NbExp=4; IntAct=EBI-1030755, EBI-8636004;
CC P15260; Q92581-2: SLC9A6; NbExp=3; IntAct=EBI-1030755, EBI-17198620;
CC P15260; P42224: STAT1; NbExp=4; IntAct=EBI-1030755, EBI-1057697;
CC P15260; Q13586: STIM1; NbExp=3; IntAct=EBI-1030755, EBI-448878;
CC P15260; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-1030755, EBI-8644968;
CC P15260; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-1030755, EBI-10982110;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10811850,
CC ECO:0000269|PubMed:28883123}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15260-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15260-2; Sequence=VSP_055589, VSP_055590, VSP_055591;
CC -!- PTM: Phosphorylated at Ser/Thr residues. Phosphorylation of Tyr-457 is
CC required for IFNG receptor signal transduction (PubMed:8156998).
CC Influenza virus infection leads to phosphorylation in a CSNK1A1-
CC dependent manner (PubMed:29343571). {ECO:0000269|PubMed:29343571,
CC ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7673114,
CC ECO:0000269|PubMed:8156998}.
CC -!- PTM: Ubiquitinated after phosphorylation in a CSNK1A1-dependent manner,
CC leading to the lysosome-dependent degradation (PubMed:29343571).
CC Proteasomally degraded through 'Lys-48'-mediated ubiquitination
CC (PubMed:28883123). Ubiquitination is necessary for efficient IFNGR1
CC signaling (PubMed:28883123). {ECO:0000269|PubMed:28883123,
CC ECO:0000269|PubMed:29343571}.
CC -!- POLYMORPHISM: A genetic variation in the IFNGR1 gene is associated with
CC susceptibility to Helicobacter pylori infection [MIM:600263].
CC -!- DISEASE: Immunodeficiency 27A (IMD27A) [MIM:209950]: A form of
CC Mendelian susceptibility to mycobacterial disease, a rare condition
CC caused by impairment of interferon-gamma mediated immunity. It is
CC characterized by predisposition to illness caused by moderately
CC virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG)
CC vaccine, environmental non-tuberculous mycobacteria, and by the more
CC virulent Mycobacterium tuberculosis. Other microorganisms rarely cause
CC severe clinical disease in individuals with susceptibility to
CC mycobacterial infections, with the exception of Salmonella which
CC infects less than 50% of these individuals. Clinical outcome severity
CC depends on the degree of impairment of interferon-gamma mediated
CC immunity. Some patients die of overwhelming mycobacterial disease with
CC lepromatous-like lesions in early childhood, whereas others develop,
CC later in life, disseminated but curable infections with tuberculoid
CC granulomas. {ECO:0000269|PubMed:10811850, ECO:0000269|PubMed:11139207,
CC ECO:0000269|PubMed:15589309, ECO:0000269|PubMed:16195661,
CC ECO:0000269|PubMed:16715106, ECO:0000269|PubMed:17514500,
CC ECO:0000269|PubMed:20015550, ECO:0000269|PubMed:20186794,
CC ECO:0000269|PubMed:22708048, ECO:0000269|PubMed:25592983,
CC ECO:0000269|PubMed:27868075, ECO:0000269|PubMed:28744922,
CC ECO:0000269|PubMed:9389728}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Immunodeficiency 27B (IMD27B) [MIM:615978]: A form of
CC Mendelian susceptibility to mycobacterial disease, a rare condition
CC caused by impairment of interferon-gamma mediated immunity. It is
CC characterized by predisposition to illness caused by moderately
CC virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG)
CC vaccine, environmental non-tuberculous mycobacteria, and by the more
CC virulent Mycobacterium tuberculosis. Other microorganisms rarely cause
CC severe clinical disease in individuals with susceptibility to
CC mycobacterial infections, with the exception of Salmonella which
CC infects less than 50% of these individuals. Clinical outcome severity
CC depends on the degree of impairment of interferon-gamma mediated
CC immunity. Some patients die of overwhelming mycobacterial disease with
CC lepromatous-like lesions in early childhood, whereas others develop,
CC later in life, disseminated but curable infections with tuberculoid
CC granulomas. IMD27B commonly presents with recurrent, moderately severe
CC infections with environmental mycobacteria or BCG. Salmonellosis is
CC present in about 5% of patients. {ECO:0000269|PubMed:10192386,
CC ECO:0000269|PubMed:11335768}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=IFNGR1base; Note=IFNGR1 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/IFNGR1base/";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ifngr1/";
CC ---------------------------------------------------------------------------
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DR EMBL; J03143; AAA52731.1; -; mRNA.
DR EMBL; AY594694; AAS89302.1; -; Genomic_DNA.
DR EMBL; BT006814; AAP35460.1; -; mRNA.
DR EMBL; AK294252; BAG57548.1; -; mRNA.
DR EMBL; AL050337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47931.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47932.1; -; Genomic_DNA.
DR EMBL; BC005333; AAH05333.1; -; mRNA.
DR CCDS; CCDS5185.1; -. [P15260-1]
DR PIR; A31555; A31555.
DR RefSeq; NP_000407.1; NM_000416.2. [P15260-1]
DR PDB; 1FG9; X-ray; 2.90 A; C/D/E=18-262.
DR PDB; 1FYH; X-ray; 2.04 A; B/E=18-246.
DR PDB; 1JRH; X-ray; 2.80 A; I=18-125.
DR PDB; 6E3K; X-ray; 3.25 A; C/D=18-246.
DR PDB; 6E3L; X-ray; 3.80 A; C/D=18-246.
DR PDBsum; 1FG9; -.
DR PDBsum; 1FYH; -.
DR PDBsum; 1JRH; -.
DR PDBsum; 6E3K; -.
DR PDBsum; 6E3L; -.
DR AlphaFoldDB; P15260; -.
DR SMR; P15260; -.
DR BioGRID; 109681; 94.
DR ComplexPortal; CPX-6015; Interferon gamma receptor-ligand complex.
DR DIP; DIP-47N; -.
DR IntAct; P15260; 34.
DR MINT; P15260; -.
DR STRING; 9606.ENSP00000356713; -.
DR BindingDB; P15260; -.
DR ChEMBL; CHEMBL2364171; -.
DR DrugBank; DB00033; Interferon gamma-1b.
DR GlyConnect; 294; 6 N-Linked glycans (1 site).
DR GlyGen; P15260; 6 sites, 10 N-linked glycans (5 sites).
DR iPTMnet; P15260; -.
DR PhosphoSitePlus; P15260; -.
DR SwissPalm; P15260; -.
DR BioMuta; IFNGR1; -.
DR DMDM; 124474; -.
DR EPD; P15260; -.
DR jPOST; P15260; -.
DR MassIVE; P15260; -.
DR MaxQB; P15260; -.
DR PaxDb; P15260; -.
DR PeptideAtlas; P15260; -.
DR PRIDE; P15260; -.
DR ProteomicsDB; 4077; -.
DR ProteomicsDB; 53122; -. [P15260-1]
DR ABCD; P15260; 10 sequenced antibodies.
DR Antibodypedia; 3840; 797 antibodies from 43 providers.
DR CPTC; P15260; 3 antibodies.
DR DNASU; 3459; -.
DR Ensembl; ENST00000367739.9; ENSP00000356713.5; ENSG00000027697.15. [P15260-1]
DR GeneID; 3459; -.
DR KEGG; hsa:3459; -.
DR MANE-Select; ENST00000367739.9; ENSP00000356713.5; NM_000416.3; NP_000407.1.
DR UCSC; uc003qho.3; human. [P15260-1]
DR CTD; 3459; -.
DR DisGeNET; 3459; -.
DR GeneCards; IFNGR1; -.
DR HGNC; HGNC:5439; IFNGR1.
DR HPA; ENSG00000027697; Low tissue specificity.
DR MalaCards; IFNGR1; -.
DR MIM; 107470; gene.
DR MIM; 209950; phenotype.
DR MIM; 600263; phenotype.
DR MIM; 615978; phenotype.
DR neXtProt; NX_P15260; -.
DR OpenTargets; ENSG00000027697; -.
DR Orphanet; 319581; Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR1 deficiency.
DR Orphanet; 319569; Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR1 deficiency.
DR Orphanet; 117; Behcet disease.
DR Orphanet; 99898; Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR1 deficiency.
DR PharmGKB; PA29675; -.
DR VEuPathDB; HostDB:ENSG00000027697; -.
DR eggNOG; ENOG502RXGW; Eukaryota.
DR GeneTree; ENSGT00510000048929; -.
DR HOGENOM; CLU_043814_0_0_1; -.
DR InParanoid; P15260; -.
DR OMA; NIMLPKS; -.
DR PhylomeDB; P15260; -.
DR TreeFam; TF338358; -.
DR PathwayCommons; P15260; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR Reactome; R-HSA-877312; Regulation of IFNG signaling.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P15260; -.
DR SIGNOR; P15260; -.
DR BioGRID-ORCS; 3459; 23 hits in 1092 CRISPR screens.
DR ChiTaRS; IFNGR1; human.
DR EvolutionaryTrace; P15260; -.
DR GeneWiki; Interferon_gamma_receptor_1; -.
DR GenomeRNAi; 3459; -.
DR Pharos; P15260; Tbio.
DR PRO; PR:P15260; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P15260; protein.
DR Bgee; ENSG00000027697; Expressed in lower lobe of lung and 211 other tissues.
DR ExpressionAtlas; P15260; baseline and differential.
DR Genevisible; P15260; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0004906; F:interferon-gamma receptor activity; TAS:ProtInc.
DR GO; GO:0048143; P:astrocyte activation; ISS:ARUK-UCL.
DR GO; GO:0098586; P:cellular response to virus; IC:ComplexPortal.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0001774; P:microglial cell activation; ISS:ARUK-UCL.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISS:ARUK-UCL.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:ARUK-UCL.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR021126; IFN_gamma_rc_D2_pox/mammal.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008355; Interferon_gamma_rcpt_asu.
DR PANTHER; PTHR20859:SF5; PTHR20859:SF5; 1.
DR Pfam; PF07140; IFNGR1; 1.
DR Pfam; PF01108; Tissue_fac; 1.
DR PRINTS; PR01777; INTERFERONGR.
DR SUPFAM; SSF49265; SSF49265; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..17
FT CHAIN 18..489
FT /note="Interferon gamma receptor 1"
FT /id="PRO_0000011009"
FT TOPO_DOM 18..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 329..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15261"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15261"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15261"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15261"
FT MOD_RES 457
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8156998"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..85
FT /evidence="ECO:0000269|PubMed:8443182"
FT DISULFID 122..167
FT /evidence="ECO:0000269|PubMed:8443182"
FT DISULFID 195..200
FT /evidence="ECO:0000269|PubMed:8443182"
FT DISULFID 214..235
FT /evidence="ECO:0000269|PubMed:8443182"
FT VAR_SEQ 1..28
FT /note="MALLFLLPLVMQGVSRAEMGTADLGPSS -> MLLKSPENSLLQFQFKYG
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055589"
FT VAR_SEQ 184..196
FT /note="QYKILTQKEDDCD -> KRSCAFSLFSFFI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055590"
FT VAR_SEQ 197..489
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055591"
FT VARIANT 14
FT /note="V -> M (may influence susceptibility to autoimmune
FT and inflammatory diseases such as systemic lupus
FT erythematosus, atopic asthma and atopic dermatitis
FT complicated by eczema herpeticum; no significant effect on
FT interferon-gamma-mediated signaling pathway;
FT dbSNP:rs11575936)"
FT /evidence="ECO:0000269|PubMed:10079289,
FT ECO:0000269|PubMed:11240951, ECO:0000269|PubMed:20015550,
FT ECO:0000269|PubMed:26343451"
FT /id="VAR_080058"
FT VARIANT 37
FT /note="I -> T (in IMD27A; dbSNP:rs945137618)"
FT /evidence="ECO:0000269|PubMed:28744922"
FT /id="VAR_080059"
FT VARIANT 61
FT /note="V -> E (in IMD27A; interferon-gamma-mediated
FT signaling pathway completely abrogated; dbSNP:rs121912715)"
FT /evidence="ECO:0000269|PubMed:10811850,
FT ECO:0000269|PubMed:20015550"
FT /id="VAR_080060"
FT VARIANT 61
FT /note="V -> I (may influence susceptibility to atopic
FT dermatitis complicated by eczema herpeticum; could be
FT detected on the cell surface; no significant effect on
FT interferon-gamma-mediated signaling pathway;
FT dbSNP:rs17175322)"
FT /evidence="ECO:0000269|PubMed:20015550,
FT ECO:0000269|PubMed:26343451, ECO:0000269|Ref.2"
FT /id="VAR_019281"
FT VARIANT 63
FT /note="V -> G (in IMD27A; interferon-gamma-mediated
FT signaling pathway severely reduced although not completely
FT abrogated)"
FT /evidence="ECO:0000269|PubMed:11139207,
FT ECO:0000269|PubMed:20015550"
FT /id="VAR_080062"
FT VARIANT 66
FT /note="Y -> C (in IMD27A; could be detected on the cell
FT surface; interferon-gamma-mediated signaling pathway
FT completely abrogated)"
FT /evidence="ECO:0000269|PubMed:15589309,
FT ECO:0000269|PubMed:20015550"
FT /id="VAR_080063"
FT VARIANT 77
FT /note="C -> F (in IMD27A; interferon-gamma-mediated
FT signaling pathway completely abrogated)"
FT /evidence="ECO:0000269|PubMed:16715106,
FT ECO:0000269|PubMed:20015550"
FT /id="VAR_080064"
FT VARIANT 77
FT /note="C -> Y (in IMD27A; fails to bind IFN-gamma; could be
FT detected on the cell surface; interferon-gamma-mediated
FT signaling pathway completely abrogated; dbSNP:rs104893974)"
FT /evidence="ECO:0000269|PubMed:10811850,
FT ECO:0000269|PubMed:15589309, ECO:0000269|PubMed:20015550"
FT /id="VAR_017577"
FT VARIANT 85
FT /note="C -> Y (in IMD27A; interferon-gamma-mediated
FT signaling pathway completely abrogated)"
FT /evidence="ECO:0000269|PubMed:17514500,
FT ECO:0000269|PubMed:20015550"
FT /id="VAR_080065"
FT VARIANT 87
FT /note="I -> T (in IMD27A; interferon-gamma-mediated
FT signaling pathway severely reduced; dbSNP:rs104893973)"
FT /evidence="ECO:0000269|PubMed:16195661,
FT ECO:0000269|PubMed:20015550, ECO:0000269|PubMed:9389728"
FT /id="VAR_017578"
FT VARIANT 99..102
FT /note="Missing (in IMD27A; fails to bind IFN-gamma)"
FT /evidence="ECO:0000269|PubMed:10811850"
FT /id="VAR_017579"
FT VARIANT 113..489
FT /note="Missing (in IMD27A)"
FT /evidence="ECO:0000269|PubMed:20186794"
FT /id="VAR_080066"
FT VARIANT 149
FT /note="S -> L (could be detected on the cell surface; does
FT not affect interferon-gamma-mediated signaling pathway;
FT dbSNP:rs387906572)"
FT /evidence="ECO:0000269|PubMed:20015550"
FT /id="VAR_080067"
FT VARIANT 180
FT /note="G -> R (in dbSNP:rs137854904)"
FT /evidence="ECO:0000269|PubMed:28744922"
FT /id="VAR_080068"
FT VARIANT 197
FT /note="E -> K (in dbSNP:rs55666220)"
FT /evidence="ECO:0000269|PubMed:28744922"
FT /id="VAR_080069"
FT VARIANT 218
FT /note="Missing (in IMD27A)"
FT /evidence="ECO:0000269|PubMed:10811850"
FT /id="VAR_080070"
FT VARIANT 219
FT /note="G -> R (in IMD27A; dbSNP:rs1311661488)"
FT /evidence="ECO:0000269|PubMed:25592983"
FT /id="VAR_080071"
FT VARIANT 224..489
FT /note="Missing (in IMD27A)"
FT /evidence="ECO:0000269|PubMed:27868075"
FT /id="VAR_080072"
FT VARIANT 278..489
FT /note="Missing (in IMD27B)"
FT /evidence="ECO:0000269|PubMed:11335768"
FT /id="VAR_080073"
FT VARIANT 335
FT /note="H -> P (associated with susceptibility to
FT Helicobacter pylori infection; no significant effect on
FT interferon-gamma-mediated signaling pathway;
FT dbSNP:rs17175350)"
FT /evidence="ECO:0000269|PubMed:12516030,
FT ECO:0000269|PubMed:20015550, ECO:0000269|Ref.2"
FT /id="VAR_019282"
FT VARIANT 352
FT /note="I -> M (no significant effect on interferon-gamma-
FT mediated signaling pathway; dbSNP:rs199641966)"
FT /evidence="ECO:0000269|PubMed:20015550"
FT /id="VAR_080074"
FT VARIANT 397
FT /note="Y -> C (associated with susceptibility to atopic
FT dermatitis complicated by eczema herpeticum; does not
FT affect completely interferon-gamma-mediated signaling
FT pathway; dbSNP:rs374787981)"
FT /evidence="ECO:0000269|PubMed:26343451"
FT /id="VAR_080075"
FT VARIANT 467
FT /note="L -> P (associated with susceptibility to
FT Helicobacter pylori infection; may influence susceptibility
FT to allergic diseases such as bronchial asthma and allergic
FT rhinitis; could be detected on the cell surface; no
FT significant effect on interferon-gamma-mediated signaling
FT pathway; dbSNP:rs1887415)"
FT /evidence="ECO:0000269|PubMed:12516030,
FT ECO:0000269|PubMed:12851715, ECO:0000269|PubMed:20015550,
FT ECO:0000269|Ref.2"
FT /id="VAR_019283"
FT VARIANT 485
FT /note="S -> F (in IMD27A; dbSNP:rs752113778)"
FT /evidence="ECO:0000269|PubMed:22708048"
FT /id="VAR_080076"
FT MUTAGEN 61
FT /note="V->Q: Loss of function in the interferon-gamma-
FT mediated signaling pathway."
FT /evidence="ECO:0000269|PubMed:20015550"
FT MUTAGEN 277
FT /note="K->R: Strong decreased level of ubiquitination; when
FT associated with R-279 and R-285."
FT /evidence="ECO:0000269|PubMed:28883123"
FT MUTAGEN 279
FT /note="K->R: Strong decreased level of ubiquitination; when
FT associated with R-277 and R-285."
FT /evidence="ECO:0000269|PubMed:28883123"
FT MUTAGEN 285
FT /note="K->R: Strong decreased level of ubiquitination; when
FT associated with R-277 and R-279."
FT /evidence="ECO:0000269|PubMed:28883123"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 74..86
FT /evidence="ECO:0007829|PDB:1FYH"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:1FYH"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:1FYH"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:1FYH"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:6E3K"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:1FYH"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1FYH"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1FYH"
SQ SEQUENCE 489 AA; 54405 MW; DCF9E574D8F47400 CRC64;
MALLFLLPLV MQGVSRAEMG TADLGPSSVP TPTNVTIESY NMNPIVYWEY QIMPQVPVFT
VEVKNYGVKN SEWIDACINI SHHYCNISDH VGDPSNSLWV RVKARVGQKE SAYAKSEEFA
VCRDGKIGPP KLDIRKEEKQ IMIDIFHPSV FVNGDEQEVD YDPETTCYIR VYNVYVRMNG
SEIQYKILTQ KEDDCDEIQC QLAIPVSSLN SQYCVSAEGV LHVWGVTTEK SKEVCITIFN
SSIKGSLWIP VVAALLLFLV LSLVFICFYI KKINPLKEKS IILPKSLISV VRSATLETKP
ESKYVSLITS YQPFSLEKEV VCEEPLSPAT VPGMHTEDNP GKVEHTEELS SITEVVTTEE
NIPDVVPGSH LTPIERESSS PLSSNQSEPG SIALNSYHSR NCSESDHSRN GFDTDSSCLE
SHSSLSDSEF PPNNKGEIKT EGQELITVIK APTSFGYDKP HVLVDLLVDD SGKESLIGYR
PTEDSKEFS
