INGR2_HUMAN
ID INGR2_HUMAN Reviewed; 337 AA.
AC P38484; Q9BTL5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Interferon gamma receptor 2 {ECO:0000312|HGNC:HGNC:5440};
DE Short=IFN-gamma receptor 2;
DE Short=IFN-gamma-R2;
DE AltName: Full=Interferon gamma receptor accessory factor 1 {ECO:0000303|PubMed:8124716};
DE Short=AF-1 {ECO:0000303|PubMed:8124716};
DE AltName: Full=Interferon gamma receptor beta-chain {ECO:0000303|PubMed:7615558};
DE Short=IFN-gamma-R-beta {ECO:0000303|PubMed:7615558};
DE AltName: Full=Interferon gamma transducer 1 {ECO:0000312|HGNC:HGNC:5440};
DE Flags: Precursor;
GN Name=IFNGR2 {ECO:0000312|HGNC:HGNC:5440};
GN Synonyms=IFNGT1 {ECO:0000312|HGNC:HGNC:5440};
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], FUNCTION, AND VARIANT ARG-64.
RC TISSUE=Lung fibroblast;
RX PubMed=8124716; DOI=10.1016/0092-8674(94)90354-9;
RA Soh J., Donnelly R.J., Kotenko S., Mariano T.M., Cook J.R., Wang N.,
RA Emanuel S.L., Schwartz B., Miki T., Pestka S.;
RT "Identification and sequence of an accessory factor required for activation
RT of the human interferon gamma receptor.";
RL Cell 76:793-802(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-58; LYS-147 AND
RP GLU-182.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-64.
RC TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=8910544; DOI=10.1074/jbc.271.46.28947;
RA Rhee S., Ebensperger C., Dembic Z., Pestka S.;
RT "The structure of the gene for the second chain of the human interferon
RT gamma receptor.";
RL J. Biol. Chem. 271:28947-28952(1996).
RN [5]
RP FUNCTION, AND INTERACTION WITH INGR1 AND JAK2.
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 [6]
RP FUNCTION, AND INTERACTION WITH JAK2.
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 [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10605012; DOI=10.4049/jimmunol.164.1.201;
RA Rigamonti L., Ariotti S., Losana G., Gradini R., Russo M.A., Jouanguy E.,
RA Casanova J.L., Forni G., Novelli F.;
RT "Surface expression of the IFN-gamma R2 chain is regulated by intracellular
RT trafficking in human T lymphocytes.";
RL J. Immunol. 164:201-207(2000).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, MOTIF, AND MUTAGENESIS OF 274-ARG-GLY-275;
RP LEU-276; ILE-277; 276-LEU-ILE-277 AND 278-LYS-TYR-279.
RX PubMed=15356148; DOI=10.4049/jimmunol.173.6.3991;
RA Rosenzweig S.D., Schwartz O.M., Brown M.R., Leto T.L., Holland S.M.;
RT "Characterization of a dipeptide motif regulating IFN-gamma receptor 2
RT plasma membrane accumulation and IFN-gamma responsiveness.";
RL J. Immunol. 173:3991-3999(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 28-247, SUBCELLULAR LOCATION,
RP GLYCOSYLATION AT ASN-56; ASN-110; ASN-137; ASN-231; ASN-85 AND ASN-219,
RP MUTAGENESIS OF ASN-110; ASN-137 AND ASN-231, AND DISULFIDE BOND.
RX PubMed=27599734; DOI=10.1107/s2059798316012237;
RA Mikulecky P., Zahradnik J., Kolenko P., Cerny J., Charnavets T.,
RA Kolarova L., Necasova I., Pham P.N., Schneider B.;
RT "Crystal structure of human interferon-gamma receptor 2 reveals the
RT structural basis for receptor specificity.";
RL Acta Crystallogr. D 75:1017-1024(2016).
RN [10]
RP VARIANT IMD28 CYS-114.
RX PubMed=10608793; DOI=10.1086/315197;
RA Doeffinger R., Jouanguy E., Dupuis S., Fondaneche M.C., Stephan J.L.,
RA Emile J.F., Lamhamedi-Cherradi S., Altare F., Pallier A.,
RA Barcenas-Morales G., Meinl E., Krause C., Pestka S., Schreiber R.D.,
RA Novelli F., Casanova J.L.;
RT "Partial interferon-gamma receptor signaling chain deficiency in a patient
RT with bacille Calmette-Guerin and Mycobacterium abscessus infection.";
RL J. Infect. Dis. 181:379-384(2000).
RN [11]
RP VARIANTS IMD28 ASN-168 AND 222-ASN--SER-230 DEL, MUTAGENESIS OF THR-168,
RP CHARACTERIZATION OF VARIANTS IMD28 ASN-168 AND 222-ASN--SER-230 DEL, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15924140; DOI=10.1038/ng1581;
RA Vogt G., Chapgier A., Yang K., Chuzhanova N., Feinberg J., Fieschi C.,
RA Boisson-Dupuis S., Alcais A., Filipe-Santos O., Bustamante J.,
RA de Beaucoudrey L., Al-Mohsen I., Al-Hajjar S., Al-Ghonaium A., Adimi P.,
RA Mirsaeidi M., Khalilzadeh S., Rosenzweig S., de la Calle-Martin O.,
RA Bauer T.R., Puck J.M., Ochs H.D., Furthner D., Engelhorn C.,
RA Belohradsky B., Mansouri D., Holland S.M., Schreiber R.D., Abel L.,
RA Cooper D.N., Soudais C., Casanova J.-L.;
RT "Gains of glycosylation comprise an unexpectedly large group of pathogenic
RT mutations.";
RL Nat. Genet. 37:692-700(2005).
RN [12]
RP VARIANT IMD28 ARG-227, AND CHARACTERIZATION OF VARIANT IMD28 ARG-227.
RX PubMed=22902943; DOI=10.1016/j.jinf.2012.08.008;
RA Kilic S.S., van Wengen A., de Paus R.A., Celebi S., Meziane B.,
RA Hafizoglu D., van Dissel J.T., van de Vosse E.;
RT "Severe disseminated mycobacterial infection in a boy with a novel mutation
RT leading to IFN-gammaR2 deficiency.";
RL J. Infect. 65:568-572(2012).
RN [13]
RP VARIANTS IMD28 PHE-124 AND ARG-141, CHARACTERIZATION OF VARIANTS IMD28
RP CYS-114; PHE-124; ARG-141; ASN-168 AND ARG-227, AND SUBCELLULAR LOCATION.
RX PubMed=23963039; DOI=10.1182/blood-2013-01-480814;
RA Moncada-Velez M., Martinez-Barricarte R., Bogunovic D., Kong X.F.,
RA Blancas-Galicia L., Tirpan C., Aksu G., Vincent Q.B., Boisson B., Itan Y.,
RA Ramirez-Alejo N., Okada S., Kreins A.Y., Bryant V.L., Franco J.L.,
RA Migaud M., Espinosa-Padilla S., Yamazaki-Nakashimada M.,
RA Espinosa-Rosales F., Kutukculer N., Abel L., Bustamante J., Vogt G.,
RA Casanova J.L., Boisson-Dupuis S.;
RT "Partial IFN-gammaR2 deficiency is due to protein misfolding and can be
RT rescued by inhibitors of glycosylation.";
RL Blood 122:2390-2401(2013).
CC -!- FUNCTION: Associates with IFNGR1 to form a receptor for the cytokine
CC interferon gamma (IFNG) (PubMed:8124716,
CC PubMed:7673114,PubMed:7615558). Ligand binding stimulates activation of
CC the JAK/STAT signaling pathway (PubMed:8124716, PubMed:7673114,
CC PubMed:15356148). Required for signal transduction in contrast to other
CC receptor subunit responsible for ligand binding (PubMed:7673114).
CC {ECO:0000269|PubMed:15356148, ECO:0000269|PubMed:7615558,
CC ECO:0000269|PubMed:7673114, ECO:0000269|PubMed:8124716}.
CC -!- SUBUNIT: Heterodimer with IFNGR1, to form the IFNG receptor complex
CC (PubMed:7615558). Interacts (via intracellular domain) with JAK2
CC (PubMed:7615558, PubMed:7673114). {ECO:0000269|PubMed:7615558,
CC ECO:0000269|PubMed:7673114}.
CC -!- INTERACTION:
CC P38484; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-3905457, EBI-10827839;
CC P38484; Q12983: BNIP3; NbExp=3; IntAct=EBI-3905457, EBI-749464;
CC P38484; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-3905457, EBI-12244618;
CC P38484; Q6UX41-6: BTNL8; NbExp=3; IntAct=EBI-3905457, EBI-17442596;
CC P38484; Q8IX05: CD302; NbExp=3; IntAct=EBI-3905457, EBI-14259393;
CC P38484; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-3905457, EBI-12256978;
CC P38484; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-3905457, EBI-11989440;
CC P38484; Q07325: CXCL9; NbExp=3; IntAct=EBI-3905457, EBI-3911467;
CC P38484; P54852: EMP3; NbExp=3; IntAct=EBI-3905457, EBI-3907816;
CC P38484; O75355-2: ENTPD3; NbExp=3; IntAct=EBI-3905457, EBI-12279764;
CC P38484; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-3905457, EBI-10976398;
CC P38484; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-3905457, EBI-6166686;
CC P38484; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-3905457, EBI-8503746;
CC P38484; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3905457, EBI-10266796;
CC P38484; Q01453: PMP22; NbExp=3; IntAct=EBI-3905457, EBI-2845982;
CC P38484; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-3905457, EBI-10244780;
CC P38484; O75396: SEC22B; NbExp=3; IntAct=EBI-3905457, EBI-1058865;
CC P38484; O95562: SFT2D2; NbExp=3; IntAct=EBI-3905457, EBI-4402330;
CC P38484; P11686: SFTPC; NbExp=3; IntAct=EBI-3905457, EBI-10197617;
CC P38484; Q9NWF4: SLC52A1; NbExp=3; IntAct=EBI-3905457, EBI-12904614;
CC P38484; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-3905457, EBI-741850;
CC P38484; P0DN84: STRIT1; NbExp=3; IntAct=EBI-3905457, EBI-12200293;
CC P38484; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-3905457, EBI-10171534;
CC P38484; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-3905457, EBI-2844246;
CC P38484; Q8N511: TMEM199; NbExp=3; IntAct=EBI-3905457, EBI-10265825;
CC P38484; A2RU14: TMEM218; NbExp=3; IntAct=EBI-3905457, EBI-10173151;
CC P38484; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-3905457, EBI-11956809;
CC P38484; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-3905457, EBI-2852148;
CC P38484; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-3905457, EBI-12111910;
CC P38484; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-3905457, EBI-16746122;
CC P38484; O60636: TSPAN2; NbExp=3; IntAct=EBI-3905457, EBI-3914288;
CC P38484; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-3905457, EBI-11988865;
CC P38484; Q53HI1: UNC50; NbExp=3; IntAct=EBI-3905457, EBI-7601760;
CC P38484; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-3905457, EBI-10254561;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15356148,
CC ECO:0000269|PubMed:15924140, ECO:0000269|PubMed:27599734}; Single-pass
CC type I membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:10605012}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:23963039};
CC Single-pass type I membrane protein {ECO:0000255}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:23963039}; Single-pass type I
CC membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:10605012}. Note=Has low cell surface expression and
CC high cytoplasmic expression in T cells. The bias towards cytoplasmic
CC expression may be due to ligand-independent receptor internalization
CC and recycling. {ECO:0000269|PubMed:10605012,
CC ECO:0000269|PubMed:15356148}.
CC -!- TISSUE SPECIFICITY: Expressed in T-cells (at protein level).
CC {ECO:0000269|PubMed:10605012}.
CC -!- DISEASE: Immunodeficiency 28 (IMD28) [MIM:614889]: A form of Mendelian
CC susceptibility to mycobacterial disease, a rare condition caused by
CC impairment of interferon-gamma mediated immunity. It is characterized
CC by predisposition to illness caused by moderately virulent
CC mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine,
CC environmental non-tuberculous mycobacteria, and by the more virulent
CC Mycobacterium tuberculosis. Other microorganisms rarely cause severe
CC clinical disease in individuals with susceptibility to mycobacterial
CC infections, with the exception of Salmonella which infects less than
CC 50% of these individuals. Clinical outcome severity depends on the
CC degree of impairment of interferon-gamma mediated immunity. Some
CC patients die of overwhelming mycobacterial disease with lepromatous-
CC like lesions in early childhood, whereas others develop, later in life,
CC disseminated but curable infections with tuberculoid granulomas. IMD28
CC is an autosomal recessive disease that manifests early in life, with
CC severe, often fatal, infection. {ECO:0000269|PubMed:10608793,
CC ECO:0000269|PubMed:15924140, ECO:0000269|PubMed:22902943,
CC ECO:0000269|PubMed:23963039}. 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=IFNGR2base; Note=IFNGR2 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/IFNGR2base/";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ifngr2/";
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DR EMBL; U05875; AAA16955.1; -; mRNA.
DR EMBL; U05877; AAA16956.1; -; mRNA.
DR EMBL; AY644470; AAT45458.1; -; Genomic_DNA.
DR EMBL; BC003624; AAH03624.1; -; mRNA.
DR EMBL; U68755; AAC52066.1; -; Genomic_DNA.
DR CCDS; CCDS33544.1; -.
DR PIR; I38500; I38500.
DR RefSeq; NP_005525.2; NM_005534.3.
DR PDB; 5EH1; X-ray; 1.80 A; A=28-247.
DR PDB; 6E3K; X-ray; 3.25 A; E/I=28-247.
DR PDB; 6E3L; X-ray; 3.80 A; E/I=28-247.
DR PDBsum; 5EH1; -.
DR PDBsum; 6E3K; -.
DR PDBsum; 6E3L; -.
DR AlphaFoldDB; P38484; -.
DR SMR; P38484; -.
DR BioGRID; 109682; 60.
DR ComplexPortal; CPX-6015; Interferon gamma receptor-ligand complex.
DR IntAct; P38484; 37.
DR STRING; 9606.ENSP00000290219; -.
DR ChEMBL; CHEMBL2364171; -.
DR DrugBank; DB00033; Interferon gamma-1b.
DR GlyGen; P38484; 6 sites.
DR iPTMnet; P38484; -.
DR PhosphoSitePlus; P38484; -.
DR BioMuta; IFNGR2; -.
DR DMDM; 145559548; -.
DR MassIVE; P38484; -.
DR PaxDb; P38484; -.
DR PeptideAtlas; P38484; -.
DR PRIDE; P38484; -.
DR Antibodypedia; 703; 453 antibodies from 33 providers.
DR DNASU; 3460; -.
DR Ensembl; ENST00000290219.11; ENSP00000290219.5; ENSG00000159128.15.
DR Ensembl; ENST00000576463.5; ENSP00000458487.2; ENSG00000262795.5.
DR GeneID; 3460; -.
DR KEGG; hsa:3460; -.
DR MANE-Select; ENST00000290219.11; ENSP00000290219.5; NM_005534.4; NP_005525.2.
DR UCSC; uc002yrp.4; human.
DR CTD; 3460; -.
DR DisGeNET; 3460; -.
DR GeneCards; IFNGR2; -.
DR HGNC; HGNC:5440; IFNGR2.
DR HPA; ENSG00000159128; Low tissue specificity.
DR MalaCards; IFNGR2; -.
DR MIM; 147569; gene.
DR MIM; 614889; phenotype.
DR neXtProt; NX_P38484; -.
DR OpenTargets; ENSG00000159128; -.
DR Orphanet; 319589; Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency.
DR Orphanet; 319574; Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency.
DR Orphanet; 319547; Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR2 deficiency.
DR PharmGKB; PA29676; -.
DR VEuPathDB; HostDB:ENSG00000159128; -.
DR eggNOG; ENOG502S6E7; Eukaryota.
DR GeneTree; ENSGT00940000160503; -.
DR InParanoid; P38484; -.
DR OMA; WVETDPF; -.
DR OrthoDB; 965164at2759; -.
DR PhylomeDB; P38484; -.
DR TreeFam; TF337223; -.
DR PathwayCommons; P38484; -.
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; P38484; -.
DR SIGNOR; P38484; -.
DR BioGRID-ORCS; 3460; 28 hits in 1088 CRISPR screens.
DR ChiTaRS; IFNGR2; human.
DR GenomeRNAi; 3460; -.
DR Pharos; P38484; Tbio.
DR PRO; PR:P38484; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P38484; protein.
DR Bgee; ENSG00000159128; Expressed in monocyte and 96 other tissues.
DR ExpressionAtlas; P38484; baseline and differential.
DR Genevisible; P38484; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:UniProtKB.
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:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
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:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR Pfam; PF09294; Interfer-bind; 1.
DR Pfam; PF01108; Tissue_fac; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Disease variant; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..337
FT /note="Interferon gamma receptor 2"
FT /id="PRO_0000011011"
FT TOPO_DOM 28..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..129
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 142..240
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 276..277
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000269|PubMed:15356148"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27599734"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27599734"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27599734"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27599734"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27599734"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27599734"
FT DISULFID 86..94
FT /evidence="ECO:0000269|PubMed:27599734"
FT DISULFID 209..234
FT /evidence="ECO:0000269|PubMed:27599734"
FT VARIANT 58
FT /note="T -> R (in dbSNP:rs4986958)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_020003"
FT VARIANT 64
FT /note="Q -> R (in dbSNP:rs9808753)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8124716"
FT /id="VAR_002718"
FT VARIANT 114
FT /note="R -> C (in IMD28; encodes misfolded protein with
FT abnormal glycosylation; affects receptor trafficking to the
FT cell surface; reduces response to IFNG;
FT dbSNP:rs1243506079)"
FT /evidence="ECO:0000269|PubMed:10608793,
FT ECO:0000269|PubMed:23963039"
FT /id="VAR_075305"
FT VARIANT 124
FT /note="S -> F (in IMD28; encodes misfolded protein with
FT abnormal glycosylation; affects receptor trafficking to the
FT cell surface; reduces response to IFNG)"
FT /evidence="ECO:0000269|PubMed:23963039"
FT /id="VAR_075306"
FT VARIANT 141
FT /note="G -> R (in IMD28; encodes misfolded protein with
FT abnormal glycosylation; affects receptor trafficking to the
FT cell surface; reduces response to IFNG;
FT dbSNP:rs1196094724)"
FT /evidence="ECO:0000269|PubMed:23963039"
FT /id="VAR_075307"
FT VARIANT 147
FT /note="E -> K (in dbSNP:rs17878639)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021383"
FT VARIANT 168
FT /note="T -> N (in IMD28; does not affect receptor
FT trafficking to the cell surface; loss of function due to
FT gain of N-glycosylation; dbSNP:rs74315444)"
FT /evidence="ECO:0000269|PubMed:15924140,
FT ECO:0000269|PubMed:23963039"
FT /id="VAR_023281"
FT VARIANT 182
FT /note="K -> E (in dbSNP:rs17878711)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021384"
FT VARIANT 222..230
FT /note="Missing (in IMD28; affects receptor trafficking to
FT the cell surface)"
FT /evidence="ECO:0000269|PubMed:15924140"
FT /id="VAR_023282"
FT VARIANT 227
FT /note="G -> R (in IMD28; encodes misfolded protein with
FT abnormal glycosylation; affects receptor trafficking to the
FT cell surface; reduces response to IFNG)"
FT /evidence="ECO:0000269|PubMed:22902943,
FT ECO:0000269|PubMed:23963039"
FT /id="VAR_075308"
FT MUTAGEN 110
FT /note="N->Q: Complete inhibition of transport to the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:27599734"
FT MUTAGEN 137
FT /note="N->Q: Complete inhibition of transport to the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:27599734"
FT MUTAGEN 168
FT /note="T->A,Q: Does not affect function."
FT /evidence="ECO:0000269|PubMed:15924140"
FT MUTAGEN 231
FT /note="N->Q: Complete inhibition of transport to the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:27599734"
FT MUTAGEN 274..275
FT /note="Missing: Leads to overaccumulation on the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:15356148"
FT MUTAGEN 276..277
FT /note="LI->AA: Leads to overaccumulation on the cell
FT membrane. Enhances function."
FT /evidence="ECO:0000269|PubMed:15356148"
FT MUTAGEN 276..277
FT /note="Missing: Leads to overaccumulation on the cell
FT membrane. Enhances function."
FT /evidence="ECO:0000269|PubMed:15356148"
FT MUTAGEN 276
FT /note="L->A: Leads to small increase in accumulation on the
FT cell membrane."
FT /evidence="ECO:0000269|PubMed:15356148"
FT MUTAGEN 277
FT /note="I->A: Does not affect accumulation on the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:15356148"
FT MUTAGEN 278..279
FT /note="Missing: Does not affect accumulation on the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:15356148"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5EH1"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6E3K"
FT STRAND 109..119
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5EH1"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:5EH1"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 187..199
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 207..218
FT /evidence="ECO:0007829|PDB:5EH1"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6E3K"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5EH1"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:5EH1"
SQ SEQUENCE 337 AA; 37806 MW; 18C68BAF7D91B8AA CRC64;
MRPTLLWSLL LLLGVFAAAA AAPPDPLSQL PAPQHPKIRL YNAEQVLSWE PVALSNSTRP
VVYQVQFKYT DSKWFTADIM SIGVNCTQIT ATECDFTAAS PSAGFPMDFN VTLRLRAELG
ALHSAWVTMP WFQHYRNVTV GPPENIEVTP GEGSLIIRFS SPFDIADTST AFFCYYVHYW
EKGGIQQVKG PFRSNSISLD NLKPSRVYCL QVQAQLLWNK SNIFRVGHLS NISCYETMAD
ASTELQQVIL ISVGTFSLLS VLAGACFFLV LKYRGLIKYW FHTPPSIPLQ IEEYLKDPTQ
PILEALDKDS SPKDDVWDSV SIISFPEKEQ EDVLQTL
