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Interferon gamma receptor 1 (IFN-gamma receptor 1) (IFN-gamma-R1) (CDw119) (Interferon gamma receptor alpha-chain) (IFN-gamma-R-alpha) (CD antigen CD119)

 INGR1_HUMAN             Reviewed;         489 AA.
P15260; B4DFT7; E1P587; Q53Y96;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 197.
RecName: Full=Interferon gamma receptor 1 {ECO:0000312|HGNC:HGNC:5439};
Short=IFN-gamma receptor 1;
Short=IFN-gamma-R1;
AltName: Full=CDw119;
AltName: Full=Interferon gamma receptor alpha-chain {ECO:0000303|PubMed:7615558, ECO:0000303|PubMed:9367779};
Short=IFN-gamma-R-alpha {ECO:0000303|PubMed:7615558};
AltName: CD_antigen=CD119;
Flags: Precursor;
Name=IFNGR1 {ECO:0000312|HGNC:HGNC:5439};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=2971451; DOI=10.1016/0092-8674(88)90050-5;
Aguet M., Dembic Z., Merlin G.;
"Molecular cloning and expression of the human interferon-gamma
receptor.";
Cell 55:273-280(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-61; PRO-335 AND
PRO-467.
SeattleSNPs variation discovery resource;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
DISULFIDE BONDS, PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS.
PubMed=8443182; DOI=10.1021/bi00060a038;
Stueber D., Friedlein A., Fountoulakis M., Lahm H.-W., Garotta G.;
"Alignment of disulfide bonds of the extracellular domain of the
interferon gamma receptor and investigation of their role in
biological activity.";
Biochemistry 32:2423-2430(1993).
[9]
FUNCTION, INTERACTION WITH IFNGR2 AND JAK1, AND PHOSPHORYLATION.
PubMed=7615558; DOI=10.1074/jbc.270.29.17528;
Sakatsume M., Igarashi K., Winestock K.D., Garotta G., Larner A.C.,
Finbloom D.S.;
"The Jak kinases differentially associate with the alpha and beta
(accessory factor) chains of the interferon gamma receptor to form a
functional receptor unit capable of activating STAT transcription
factors.";
J. Biol. Chem. 270:17528-17534(1995).
[10]
FUNCTION, AND PHOSPHORYLATION.
PubMed=7673114; DOI=10.1074/jbc.270.36.20915;
Kotenko S.V., Izotova L.S., Pollack B.P., Mariano T.M., Donnelly R.J.,
Muthukumaran G., Cook J.R., Garotta G., Silvennoinen O., Ihle J.N.;
"Interaction between the components of the interferon gamma receptor
complex.";
J. Biol. Chem. 270:20915-20921(1995).
[11]
INVOLVEMENT IN IMD27B.
PubMed=10192386; DOI=10.1038/7701;
Jouanguy E., Lamhamedi-Cherradi S., Lammas D., Dorman S.E.,
Fondaneche M.C., Dupuis S., Doeffinger R., Altare F., Girdlestone J.,
Emile J.F., Ducoulombier H., Edgar D., Clarke J., Oxelius V.A.,
Brai M., Novelli V., Heyne K., Fischer A., Holland S.M.,
Kumararatne D.S., Schreiber R.D., Casanova J.L.;
"A human IFNGR1 small deletion hotspot associated with dominant
susceptibility to mycobacterial infection.";
Nat. Genet. 21:370-378(1999).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-248, AND FUNCTION.
PubMed=7617032; DOI=10.1038/376230a0;
Walter M.R., Windsor W.T., Nagabhushan T.L., Lundell D.J., Lunn C.A.,
Zauodny P.J., Narula S.K.;
"Crystal structure of a complex between interferon-gamma and its
soluble high-affinity receptor.";
Nature 376:230-235(1995).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-122 IN COMPLEX WITH
ANTIBODY.
PubMed=9367779; DOI=10.1006/jmbi.1997.1336;
Sogabe S., Stuart F., Henke C., Bridges A., Williams G., Birch A.,
Winkler F.K., Robinson J.A.;
"Neutralizing epitopes on the extracellular interferon gamma receptor
(IFNgammaR) alpha-chain characterized by homolog scanning mutagenesis
and X-ray crystal structure of the A6 fab-IFNgammaR1-108 complex.";
J. Mol. Biol. 273:882-897(1997).
[15]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF COMPLEX WITH IFNG, AND
FUNCTION.
PubMed=10986460; DOI=10.1016/S0969-2126(00)00184-2;
Thiel D.J., le Du M.-H., Walter R.L., D'Arcy A., Chene C.,
Fountoulakis M., Garotta G., Winkler F.K., Ealick S.E.;
"Observation of an unexpected third receptor molecule in the crystal
structure of human interferon-gamma receptor complex.";
Structure 8:927-936(2000).
[16]
VARIANT IMD27A THR-87.
PubMed=9389728; DOI=10.1172/JCI119810;
Jouanguy E., Lamhamedi-Cherradi S.-E., Altare F., Fondaneche M.-C.,
Tuerlinckx D., Blanche S., Emile J.-F., Gaillard J.-L., Schreiber R.,
Levin M., Fischer A., Hivroz C., Casanova J.-L.;
"Partial interferon-gamma receptor 1 deficiency in a child with
tuberculoid bacillus Calmette-Guerin infection and a sibling with
clinical tuberculosis.";
J. Clin. Invest. 100:2658-2664(1997).
[17]
VARIANTS IMD27A TYR-77 AND 99-TRP--VAL-102 DEL, AND SUBCELLULAR
LOCATION.
PubMed=10811850; DOI=10.1172/JCI9166;
Jouanguy E., Dupuis S., Pallier A., Doffinger R., Fondaneche M.-C.,
Fieschi C., Lamhamedi-Cherradi S., Altare F., Emile J.-F., Lutz P.,
Bordigoni P., Cokugras H., Akcakaya N., Landman-Parker J.,
Donnadieu J., Camcioglu Y., Casanova J.-L.;
"In a novel form of IFN-gamma receptor 1 deficiency, cell surface
receptors fail to bind IFN-gamma.";
J. Clin. Invest. 105:1429-1436(2000).
[18]
INVOLVEMENT IN SUSCEPTIBILITY TO HELICOBACTER PYLORI INFECTION, AND
VARIANTS PRO-335 AND PRO-467.
PubMed=12516030; DOI=10.1086/367714;
Thye T., Burchard G.D., Nilius M., Mueller-Myhsok B., Horstmann R.D.;
"Genomewide linkage analysis identifies polymorphism in the human
interferon-gamma receptor affecting Helicobacter pylori infection.";
Am. J. Hum. Genet. 72:448-453(2003).
-!- FUNCTION: Associates with IFNGR2 to form a receptor for the
cytokine interferon gamma (IFNG) (PubMed:7615558, PubMed:2971451,
PubMed:7617032, PubMed:10986460). Ligand binding stimulates
activation of the JAK/STAT signaling pathway (PubMed:7673114).
{ECO:0000269|PubMed:10986460, ECO:0000269|PubMed:2971451,
ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7617032,
ECO:0000269|PubMed:7673114}.
-!- SUBUNIT: Monomer (PubMed:9367779). Heterodimer with IFNGR2, to
form the IFNG receptor complex (PubMed:7615558). Interacts with
JAK1 (PubMed:7615558). {ECO:0000269|PubMed:7615558,
ECO:0000269|PubMed:9367779}.
-!- INTERACTION:
P01579:IFNG; NbExp=2; IntAct=EBI-1030755, EBI-1030767;
P42224:STAT1; NbExp=4; IntAct=EBI-1030755, EBI-1057697;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10811850};
Single-pass type I membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P15260-1; Sequence=Displayed;
Name=2;
IsoId=P15260-2; Sequence=VSP_055589, VSP_055590, VSP_055591;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated at Ser/Thr residues.
{ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7673114}.
-!- POLYMORPHISM: A genetic variation in the IFNGR1 gene is associated
with susceptibility to Helicobacter pylori infection [MIM:600263].
-!- DISEASE: Immunodeficiency 27A (IMD27A) [MIM:209950]: A form of
Mendelian susceptibility to mycobacterial disease, a rare
condition caused by impairment of interferon-gamma mediated
immunity. It is characterized by predisposition to illness caused
by moderately virulent mycobacterial species, such as Bacillus
Calmette-Guerin (BCG) vaccine, environmental non-tuberculous
mycobacteria, and by the more virulent Mycobacterium tuberculosis.
Other microorganisms rarely cause severe clinical disease in
individuals with susceptibility to mycobacterial infections, with
the exception of Salmonella which infects less than 50% of these
individuals. Clinical outcome severity depends on the degree of
impairment of interferon-gamma mediated immunity. Some patients
die of overwhelming mycobacterial disease with lepromatous-like
lesions in early childhood, whereas others develop, later in life,
disseminated but curable infections with tuberculoid granulomas.
{ECO:0000269|PubMed:10811850, ECO:0000269|PubMed:9389728}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Immunodeficiency 27B (IMD27B) [MIM:615978]: A form of
Mendelian susceptibility to mycobacterial disease, a rare
condition caused by impairment of interferon-gamma mediated
immunity. It is characterized by predisposition to illness caused
by moderately virulent mycobacterial species, such as Bacillus
Calmette-Guerin (BCG) vaccine, environmental non-tuberculous
mycobacteria, and by the more virulent Mycobacterium tuberculosis.
Other microorganisms rarely cause severe clinical disease in
individuals with susceptibility to mycobacterial infections, with
the exception of Salmonella which infects less than 50% of these
individuals. Clinical outcome severity depends on the degree of
impairment of interferon-gamma mediated immunity. Some patients
die of overwhelming mycobacterial disease with lepromatous-like
lesions in early childhood, whereas others develop, later in life,
disseminated but curable infections with tuberculoid granulomas.
IMD27B commonly presents with recurrent, moderately severe
infections with environmental mycobacteria or BCG. Salmonellosis
is present in about 5% of patients. {ECO:0000269|PubMed:10192386}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the type II cytokine receptor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=IFNGR1base; Note=IFNGR1 mutation db;
URL="http://structure.bmc.lu.se/idbase/IFNGR1base/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ifngr1/";
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EMBL; J03143; AAA52731.1; -; mRNA.
EMBL; AY594694; AAS89302.1; -; Genomic_DNA.
EMBL; BT006814; AAP35460.1; -; mRNA.
EMBL; AK294252; BAG57548.1; -; mRNA.
EMBL; AL050337; CAB53062.1; -; Genomic_DNA.
EMBL; CH471051; EAW47931.1; -; Genomic_DNA.
EMBL; CH471051; EAW47932.1; -; Genomic_DNA.
EMBL; BC005333; AAH05333.1; -; mRNA.
CCDS; CCDS5185.1; -. [P15260-1]
PIR; A31555; A31555.
RefSeq; NP_000407.1; NM_000416.2. [P15260-1]
UniGene; Hs.520414; -.
PDB; 1FG9; X-ray; 2.90 A; C/D/E=18-262.
PDB; 1FYH; X-ray; 2.04 A; B/E=18-246.
PDB; 1JRH; X-ray; 2.80 A; I=18-125.
PDBsum; 1FG9; -.
PDBsum; 1FYH; -.
PDBsum; 1JRH; -.
ProteinModelPortal; P15260; -.
SMR; P15260; -.
BioGrid; 109681; 31.
DIP; DIP-47N; -.
IntAct; P15260; 7.
MINT; MINT-8013365; -.
STRING; 9606.ENSP00000356713; -.
ChEMBL; CHEMBL2364171; -.
DrugBank; DB00033; Interferon gamma-1b.
iPTMnet; P15260; -.
PhosphoSitePlus; P15260; -.
SwissPalm; P15260; -.
UniCarbKB; P15260; -.
BioMuta; IFNGR1; -.
DMDM; 124474; -.
EPD; P15260; -.
MaxQB; P15260; -.
PaxDb; P15260; -.
PeptideAtlas; P15260; -.
PRIDE; P15260; -.
DNASU; 3459; -.
Ensembl; ENST00000367739; ENSP00000356713; ENSG00000027697. [P15260-1]
GeneID; 3459; -.
KEGG; hsa:3459; -.
UCSC; uc003qho.3; human. [P15260-1]
CTD; 3459; -.
DisGeNET; 3459; -.
EuPathDB; HostDB:ENSG00000027697.12; -.
GeneCards; IFNGR1; -.
HGNC; HGNC:5439; IFNGR1.
HPA; HPA029213; -.
HPA; HPA063871; -.
MalaCards; IFNGR1; -.
MIM; 107470; gene.
MIM; 209950; phenotype.
MIM; 600263; phenotype.
MIM; 615978; phenotype.
neXtProt; NX_P15260; -.
OpenTargets; ENSG00000027697; -.
Orphanet; 319581; Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR1 deficiency.
Orphanet; 319569; Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR1 deficiency.
Orphanet; 99898; Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR1 deficiency.
PharmGKB; PA29675; -.
eggNOG; ENOG410IG11; Eukaryota.
eggNOG; ENOG411218K; LUCA.
GeneTree; ENSGT00510000048929; -.
HOGENOM; HOG000113074; -.
HOVERGEN; HBG052128; -.
InParanoid; P15260; -.
KO; K05132; -.
OMA; NSYHSRN; -.
OrthoDB; EOG091G08ZD; -.
PhylomeDB; P15260; -.
TreeFam; TF338358; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
SignaLink; P15260; -.
SIGNOR; P15260; -.
ChiTaRS; IFNGR1; human.
EvolutionaryTrace; P15260; -.
GeneWiki; Interferon_gamma_receptor_1; -.
GenomeRNAi; 3459; -.
PRO; PR:P15260; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000027697; -.
CleanEx; HS_IFNGR1; -.
ExpressionAtlas; P15260; baseline and differential.
Genevisible; P15260; HS.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0019955; F:cytokine binding; IEA:InterPro.
GO; GO:0004906; F:interferon-gamma receptor activity; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0009615; P:response to virus; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR021126; Interferon_gamma_pox/mammal.
InterPro; IPR008355; Interferon_gamma_rcpt_asu.
PANTHER; PTHR20859:SF5; PTHR20859:SF5; 1.
Pfam; PF07140; IFNGR1; 1.
Pfam; PF01108; Tissue_fac; 1.
PRINTS; PR01777; INTERFERONGR.
SUPFAM; SSF49265; SSF49265; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 17
CHAIN 18 489 Interferon gamma receptor 1.
/FTId=PRO_0000011009.
TOPO_DOM 18 245 Extracellular. {ECO:0000255}.
TRANSMEM 246 266 Helical. {ECO:0000255}.
TOPO_DOM 267 489 Cytoplasmic. {ECO:0000255}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:P15261}.
MOD_RES 372 372 Phosphothreonine.
{ECO:0000250|UniProtKB:P15261}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000250|UniProtKB:P15261}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:P15261}.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 77 85 {ECO:0000269|PubMed:8443182}.
DISULFID 122 167 {ECO:0000269|PubMed:8443182}.
DISULFID 195 200 {ECO:0000269|PubMed:8443182}.
DISULFID 214 235 {ECO:0000269|PubMed:8443182}.
VAR_SEQ 1 28 MALLFLLPLVMQGVSRAEMGTADLGPSS -> MLLKSPENS
LLQFQFKYG (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055589.
VAR_SEQ 184 196 QYKILTQKEDDCD -> KRSCAFSLFSFFI (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055590.
VAR_SEQ 197 489 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055591.
VARIANT 61 61 V -> I (in dbSNP:rs17175322).
{ECO:0000269|Ref.2}.
/FTId=VAR_019281.
VARIANT 77 77 C -> Y (in IMD27A; fails to bind IFN-
gamma; dbSNP:rs104893974).
{ECO:0000269|PubMed:10811850}.
/FTId=VAR_017577.
VARIANT 87 87 I -> T (in IMD27A; impaired response to
IFN-gamma; dbSNP:rs104893973).
{ECO:0000269|PubMed:9389728}.
/FTId=VAR_017578.
VARIANT 99 102 Missing (in IMD27A; fails to bind IFN-
gamma). {ECO:0000269|PubMed:10811850}.
/FTId=VAR_017579.
VARIANT 335 335 H -> P (in dbSNP:rs17175350).
{ECO:0000269|PubMed:12516030,
ECO:0000269|Ref.2}.
/FTId=VAR_019282.
VARIANT 467 467 L -> P (in dbSNP:rs1887415).
{ECO:0000269|PubMed:12516030,
ECO:0000269|Ref.2}.
/FTId=VAR_019283.
STRAND 33 38 {ECO:0000244|PDB:1FYH}.
STRAND 40 42 {ECO:0000244|PDB:1FYH}.
STRAND 45 49 {ECO:0000244|PDB:1FYH}.
STRAND 58 65 {ECO:0000244|PDB:1FYH}.
STRAND 69 71 {ECO:0000244|PDB:1FYH}.
STRAND 74 86 {ECO:0000244|PDB:1FYH}.
HELIX 88 90 {ECO:0000244|PDB:1FYH}.
STRAND 98 106 {ECO:0000244|PDB:1FYH}.
HELIX 121 124 {ECO:0000244|PDB:1FYH}.
STRAND 131 136 {ECO:0000244|PDB:1FYH}.
STRAND 138 146 {ECO:0000244|PDB:1FYH}.
HELIX 149 151 {ECO:0000244|PDB:1FYH}.
STRAND 168 178 {ECO:0000244|PDB:1FYH}.
STRAND 181 191 {ECO:0000244|PDB:1FYH}.
STRAND 197 205 {ECO:0000244|PDB:1FYH}.
STRAND 212 221 {ECO:0000244|PDB:1FYH}.
TURN 222 224 {ECO:0000244|PDB:1FYH}.
STRAND 234 237 {ECO:0000244|PDB:1FYH}.
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


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