INGR1_MOUSE
ID INGR1_MOUSE Reviewed; 477 AA.
AC P15261; Q91Y85;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Interferon gamma receptor 1 {ECO:0000312|MGI:MGI:107655};
DE Short=IFN-gamma receptor 1;
DE Short=IFN-gamma-R1;
DE AltName: Full=Interferon gamma receptor alpha-chain {ECO:0000250|UniProtKB:P15260};
DE Short=IFN-gamma-R-alpha {ECO:0000250|UniProtKB:P15260};
DE AltName: CD_antigen=CD119;
DE Flags: Precursor;
GN Name=Ifngr1 {ECO:0000312|MGI:MGI:107655}; Synonyms=Ifngr;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2531896; DOI=10.1073/pnas.86.23.9248;
RA Munro S., Maniatis T.;
RT "Expression cloning of the murine interferon gamma receptor cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9248-9252(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2530582; DOI=10.1073/pnas.86.21.8497;
RA Gray P.W., Leong S., Fennie E.H., Farrar M.A., Pingel J.T.,
RA Fernandez-Luna J., Schreiber R.D.;
RT "Cloning and expression of the cDNA for the murine interferon gamma
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8497-8501(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2532365; DOI=10.1073/pnas.86.24.9901;
RA Hemmi S., Peghini P., Metzler M., Merlin G., Dembic Z., Aguet M.;
RT "Cloning of murine interferon gamma receptor cDNA: expression in human
RT cells mediates high-affinity binding but is not sufficient to confer
RT sensitivity to murine interferon gamma.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9901-9905(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2530216; DOI=10.1016/s0021-9258(19)84663-x;
RA Kumar C.S., Muthukumaran G., Frost L.J., Noe M., Ahn Y.H., Mariano T.M.,
RA Pestka S.;
RT "Molecular characterization of the murine interferon gamma receptor cDNA.";
RL J. Biol. Chem. 264:17939-17946(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-35; 133-143; 300-310 AND
RP 428-438, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2137461; DOI=10.1016/s0021-9258(19)39703-0;
RA Cofano F., Moore S.K., Tanaka S., Yuhki N., Landolfo S., Appella E.;
RT "Affinity purification, peptide analysis, and cDNA sequence of the mouse
RT interferon gamma receptor.";
RL J. Biol. Chem. 265:4064-4071(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B10.S/J; TISSUE=Spleen;
RA Ma R.Z., Teuscher C.;
RT "Screening for candidate genes of mouse autoimmnue diseases.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=7890167; DOI=10.1016/0378-1119(94)00869-t;
RA Raval P., Obici S., Russell S.W., Murphy W.J.;
RT "Characterization of the 5' flanking region and gene encoding the mouse
RT interferon-gamma receptor.";
RL Gene 154:219-223(1995).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF TYR-445.
RX PubMed=15284232; DOI=10.1074/jbc.m406413200;
RA Qing Y., Stark G.R.;
RT "Alternative activation of STAT1 and STAT3 in response to interferon-
RT gamma.";
RL J. Biol. Chem. 279:41679-41685(2004).
RN [11]
RP FUNCTION, MUTAGENESIS OF TYR-467, AND INTERACTION WITH SOCS1.
RX PubMed=15522878; DOI=10.1074/jbc.m409863200;
RA Qing Y., Costa-Pereira A.P., Watling D., Stark G.R.;
RT "Role of tyrosine 441 of interferon-gamma receptor subunit 1 in SOCS-1-
RT mediated attenuation of STAT1 activation.";
RL J. Biol. Chem. 280:1849-1853(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; THR-367; SER-370;
RP THR-373; THR-375; SER-379 AND SER-402, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and Testis;
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 [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19889125; DOI=10.1111/j.1600-6143.2009.02858.x;
RA Wei B., Baker S., Wieckiewicz J., Wood K.J.;
RT "IFN-gamma triggered STAT1-PKB/AKT signalling pathway influences the
RT function of alloantigen reactive regulatory T cells.";
RL Am. J. Transplant. 10:69-80(2010).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20926559; DOI=10.1128/jvi.01389-10;
RA Kolokoltsova O.A., Yun N.E., Poussard A.L., Smith J.K., Smith J.N.,
RA Salazar M., Walker A., Tseng C.T., Aronson J.F., Paessler S.;
RT "Mice lacking alpha/beta and gamma interferon receptors are susceptible to
RT junin virus infection.";
RL J. Virol. 84:13063-13067(2010).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27286456; DOI=10.18632/oncotarget.9867;
RA Zhang C., Hou D., Wei H., Zhao M., Yang L., Liu Q., Zhang X., Gong Y.,
RA Shao C.;
RT "Lack of interferon-gamma receptor results in a microenvironment favorable
RT for intestinal tumorigenesis.";
RL Oncotarget 7:42099-42109(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:20926559, PubMed:27286456). Associates with transmembrane
CC accessory factor IFNGR2 to form a functional receptor (PubMed:2530582,
CC PubMed:2532365, PubMed:2137461, PubMed:2531896, PubMed:2530216). Upon
CC ligand binding, the intracellular domain of IFNGR1 opens out to allow
CC association of downstream signaling components JAK1 and JAK2. In turn,
CC activated JAK1 phosphorylates IFNGR1 to form a docking site for STAT1.
CC Subsequent phosphorylation of STAT1 leads to its dimerization,
CC translocation to the nucleus, and stimulation of target gene
CC transcription (PubMed:19889125). STAT3 can also be activated in a
CC similar manner although activation seems weaker (PubMed:15284232).
CC IFNGR1 intracellular domain phosphorylation also provides a docking
CC site for SOCS1 that regulates the JAK-STAT pathway by competing with
CC STAT1 binding to IFNGR1 (PubMed:15522878).
CC {ECO:0000269|PubMed:15284232, ECO:0000269|PubMed:19889125,
CC ECO:0000269|PubMed:20926559, ECO:0000269|PubMed:2137461,
CC ECO:0000269|PubMed:2530216, ECO:0000269|PubMed:2530582,
CC ECO:0000269|PubMed:2531896, ECO:0000269|PubMed:2532365,
CC ECO:0000269|PubMed:27286456}.
CC -!- SUBUNIT: Monomer. Heterodimer with IFNGR2, to form the IFNG receptor
CC complex. Interacts with JAK1. Interacts (when phosphorylated) with
CC STAT1 (By similarity). Interacts with SOCS1 (PubMed:15522878).
CC {ECO:0000250|UniProtKB:P15260, ECO:0000269|PubMed:15522878}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2137461,
CC ECO:0000269|PubMed:2530216, ECO:0000269|PubMed:2530582,
CC ECO:0000269|PubMed:2531896, ECO:0000269|PubMed:2532365}; Single-pass
CC type I membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylated at Ser/Thr residues. Phosphorylation of Tyr-445 is
CC required for IFNG receptor signal transduction. Influenza virus
CC infection leads to phosphorylation in a CSNK1A1-dependent manner.
CC {ECO:0000250|UniProtKB:P15260}.
CC -!- PTM: Ubiquitinated after phosphorylation in a CSNK1A1-dependent manner,
CC leading to the lysosome-dependent degradation. Proteasomally degraded
CC through 'Lys-48'-mediated ubiquitination. Ubiquitination is necessary
CC for efficient IFNGR1 signaling. {ECO:0000250|UniProtKB:P15260}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants show shortened lifespan and
CC enhanced intestinal tumorigenesis. These tumors exhibit increased
CC inflammation (PubMed:27286456). Loss of STAT1 signaling pathway
CC activation is also observed (PubMed:19889125). After viral infection
CC such as junin virus, mice develop disseminated infection and severe
CC disease (PubMed:20926559). {ECO:0000269|PubMed:19889125,
CC ECO:0000269|PubMed:20926559, ECO:0000269|PubMed:27286456}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37895.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M28995; AAA37895.1; ALT_INIT; mRNA.
DR EMBL; M26711; AAA37896.1; -; mRNA.
DR EMBL; M28233; AAA37898.1; -; mRNA.
DR EMBL; M25764; AAA39177.1; -; mRNA.
DR EMBL; J05265; AAA39178.1; -; mRNA.
DR EMBL; AF128216; AAF22557.1; -; mRNA.
DR EMBL; AK151079; BAE30094.1; -; mRNA.
DR EMBL; AK153347; BAE31923.1; -; mRNA.
DR EMBL; AK159359; BAE35017.1; -; mRNA.
DR EMBL; AK169593; BAE41245.1; -; mRNA.
DR EMBL; CH466562; EDL03452.1; -; Genomic_DNA.
DR EMBL; U05960; AAA80980.1; -; Genomic_DNA.
DR CCDS; CCDS35856.1; -.
DR PIR; A34368; A34368.
DR RefSeq; NP_034641.1; NM_010511.3.
DR AlphaFoldDB; P15261; -.
DR SMR; P15261; -.
DR BioGRID; 200542; 8.
DR STRING; 10090.ENSMUSP00000020188; -.
DR GlyGen; P15261; 2 sites.
DR iPTMnet; P15261; -.
DR PhosphoSitePlus; P15261; -.
DR EPD; P15261; -.
DR jPOST; P15261; -.
DR MaxQB; P15261; -.
DR PaxDb; P15261; -.
DR PeptideAtlas; P15261; -.
DR PRIDE; P15261; -.
DR ProteomicsDB; 269407; -.
DR Antibodypedia; 3840; 797 antibodies from 43 providers.
DR DNASU; 15979; -.
DR Ensembl; ENSMUST00000020188; ENSMUSP00000020188; ENSMUSG00000020009.
DR GeneID; 15979; -.
DR KEGG; mmu:15979; -.
DR UCSC; uc007eng.1; mouse.
DR CTD; 3459; -.
DR MGI; MGI:107655; Ifngr1.
DR VEuPathDB; HostDB:ENSMUSG00000020009; -.
DR eggNOG; ENOG502RXGW; Eukaryota.
DR GeneTree; ENSGT00510000048929; -.
DR HOGENOM; CLU_043814_0_0_1; -.
DR InParanoid; P15261; -.
DR OMA; NIMLPKS; -.
DR OrthoDB; 745416at2759; -.
DR PhylomeDB; P15261; -.
DR TreeFam; TF338358; -.
DR Reactome; R-MMU-877300; Interferon gamma signaling.
DR Reactome; R-MMU-877312; Regulation of IFNG signaling.
DR BioGRID-ORCS; 15979; 24 hits in 78 CRISPR screens.
DR ChiTaRS; Ifngr1; mouse.
DR PRO; PR:P15261; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P15261; protein.
DR Bgee; ENSMUSG00000020009; Expressed in skeleton of lower jaw and 257 other tissues.
DR ExpressionAtlas; P15261; baseline and differential.
DR Genevisible; P15261; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0048143; P:astrocyte activation; IGI:ARUK-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0001774; P:microglial cell activation; IGI:ARUK-UCL.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; IGI:ARUK-UCL.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IGI:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:ARUK-UCL.
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 Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2137461"
FT CHAIN 26..477
FT /note="Interferon gamma receptor 1"
FT /evidence="ECO:0000269|PubMed:2137461"
FT /id="PRO_0000011010"
FT TOPO_DOM 26..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 335..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 373
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 445
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15260"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..91
FT /evidence="ECO:0000250"
FT DISULFID 128..174
FT /evidence="ECO:0000250"
FT DISULFID 203..208
FT /evidence="ECO:0000250"
FT DISULFID 222..243
FT /evidence="ECO:0000250"
FT MUTAGEN 445
FT /note="Y->F: Complete loss of STAT1 and STAT3 activation."
FT /evidence="ECO:0000269|PubMed:15284232"
FT MUTAGEN 467
FT /note="Y->F: Complete loss of interaction with SOCS1."
FT /evidence="ECO:0000269|PubMed:15522878"
FT CONFLICT 30
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="E -> G (in Ref. 1; AAA37895, 4; AAA39177 and 5;
FT AAA39178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 52343 MW; 2216663F5B9C5256 CRC64;
MGPQAAAGRM ILLVVLMLSA KVGSGALTST EDPEPPSVPV PTNVLIKSYN LNPVVCWEYQ
NMSQTPIFTV QVKVYSGSWT DSCTNISDHC CNIYEQIMYP DVSAWARVKA KVGQKESDYA
RSKEFLMCLK GKVGPPGLEI RRKKEEQLSV LVFHPEVVVN GESQGTMFGD GSTCYTFDYT
VYVEHNRSGE ILHTKHTVEK EECNETLCEL NISVSTLDSR YCISVDGISS FWQVRTEKSK
DVCIPPFHDD RKDSIWILVV APLTVFTVVI LVFAYWYTKK NSFKRKSIML PKSLLSVVKS
ATLETKPESK YSLVTPHQPA VLESETVICE EPLSTVTAPD SPEAAEQEEL SKETKALEAG
GSTSAMTPDS PPTPTQRRSF SLLSSNQSGP CSLTAYHSRN GSDSGLVGSG SSISDLESLP
NNNSETKMAE HDPPPVRKAP MASGYDKPHM LVDVLVDVGG KESLMGYRLT GEAQELS
