IL7RA_HUMAN
ID IL7RA_HUMAN Reviewed; 459 AA.
AC P16871; B2RCS6; B4DVT1; Q05CU8; Q6NSP4; Q6NWM0; Q6NWM1; Q6NWM2; Q6NWM3;
AC Q6SV45; Q9UPC1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Interleukin-7 receptor subunit alpha;
DE Short=IL-7 receptor subunit alpha;
DE Short=IL-7R subunit alpha;
DE Short=IL-7R-alpha;
DE Short=IL-7RA;
DE AltName: Full=CDw127;
DE AltName: CD_antigen=CD127;
DE Flags: Precursor;
GN Name=IL7R;
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), ALTERNATIVE SPLICING, AND VARIANTS
RP THR-66; ILE-138 AND VAL-356.
RC TISSUE=B-cell;
RX PubMed=2317865; DOI=10.1016/0092-8674(90)90342-c;
RA Goodwin R.G., Friend D., Ziegler S.F., Jerzy R., Falk B.A., Gimpel S.,
RA Cosman D., Dower S.K., March C.J., Namen A.E., Park L.S.;
RT "Cloning of the human and murine interleukin-7 receptors: demonstration of
RT a soluble form and homology to a new receptor superfamily.";
RL Cell 60:941-951(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=2038316; DOI=10.1128/mcb.11.6.3052-3059.1991;
RA Pleiman C.M., Gimpel S.D., Park L.S., Harada H., Taniguchi T.,
RA Ziegler S.F.;
RT "Organization of the murine and human interleukin-7 receptor genes: two
RT mRNAs generated by differential splicing and presence of a type I-
RT interferon-inducible promoter.";
RL Mol. Cell. Biol. 11:3052-3059(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), INVOLVEMENT IN T(-)B(+)NK(+)
RP SCID, AND VARIANTS THR-66; ILE-138 AND ILE-244.
RX PubMed=9843216; DOI=10.1038/3877;
RA Puel A., Ziegler S.F., Buckley R.H., Leonard W.J.;
RT "Defective IL7R expression in T(-)B(+)NK(+) severe combined
RT immunodeficiency.";
RL Nat. Genet. 20:394-397(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANTS
RP THR-66; ILE-138 AND VAL-356.
RC TISSUE=Spleen;
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 [GENOMIC DNA] (ISOFORM 1), AND VARIANTS THR-66;
RP ASP-113; ILE-138 AND ILE-244.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-66;
RP ILE-138 AND VAL-356.
RC TISSUE=Testis;
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 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-239 IN COMPLEX WITH IL7,
RP SUBUNIT, GLYCOSYLATION AT ASN-49; ASN-65 AND ASN-151, AND DISULFIDE BONDS.
RX PubMed=19141282; DOI=10.1016/j.str.2008.10.019;
RA McElroy C.A., Dohm J.A., Walsh S.T.;
RT "Structural and biophysical studies of the human IL-7/IL-7Ralpha complex.";
RL Structure 17:54-65(2009).
RN [9]
RP INVOLVEMENT IN T(-)B(+)NK(+) SCID, AND VARIANT T(-)B(+)NK(+) SCID SER-132.
RX PubMed=11023514;
RA Roifman C.M., Zhang J., Chitayat D., Sharfe N.;
RT "A partial deficiency of interleukin-7R alpha is sufficient to abrogate T-
RT cell development and cause severe combined immunodeficiency.";
RL Blood 96:2803-2807(2000).
RN [10]
RP VARIANT ILE-244, AND ASSOCIATION WITH MS3.
RX PubMed=17660817; DOI=10.1038/ng2103;
RA Gregory S.G., Schmidt S., Seth P., Oksenberg J.R., Hart J., Prokop A.,
RA Caillier S.J., Ban M., Goris A., Barcellos L.F., Lincoln R., McCauley J.L.,
RA Sawcer S.J., Compston D.A., Dubois B., Hauser S.L., Garcia-Blanco M.A.,
RA Pericak-Vance M.A., Haines J.L.;
RT "Interleukin 7 receptor alpha chain (IL7R) shows allelic and functional
RT association with multiple sclerosis.";
RL Nat. Genet. 39:1083-1091(2007).
CC -!- FUNCTION: Receptor for interleukin-7. Also acts as a receptor for
CC thymic stromal lymphopoietin (TSLP).
CC -!- SUBUNIT: The IL7 receptor is a heterodimer of IL7R and IL2RG. The TSLP
CC receptor is a heterodimer of CRLF2 and IL7R.
CC {ECO:0000269|PubMed:19141282}.
CC -!- INTERACTION:
CC P16871; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-80490, EBI-11522760;
CC P16871; O95236-2: APOL3; NbExp=3; IntAct=EBI-80490, EBI-11976321;
CC P16871; P27449: ATP6V0C; NbExp=3; IntAct=EBI-80490, EBI-721179;
CC P16871; Q8IX05: CD302; NbExp=3; IntAct=EBI-80490, EBI-14259393;
CC P16871; Q92520: FAM3C; NbExp=3; IntAct=EBI-80490, EBI-2876774;
CC P16871; P13232: IL7; NbExp=10; IntAct=EBI-80490, EBI-80516;
CC P16871; Q13021: MALL; NbExp=3; IntAct=EBI-80490, EBI-750078;
CC P16871; P11836: MS4A1; NbExp=3; IntAct=EBI-80490, EBI-2808234;
CC P16871; P31431: SDC4; NbExp=3; IntAct=EBI-80490, EBI-3913237;
CC P16871; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-80490, EBI-10171534;
CC P16871; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-80490, EBI-2852148;
CC P16871; O95183: VAMP5; NbExp=3; IntAct=EBI-80490, EBI-10191195;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=H20;
CC IsoId=P16871-1; Sequence=Displayed;
CC Name=3; Synonyms=H1;
CC IsoId=P16871-2; Sequence=VSP_001714;
CC Name=4; Synonyms=H6, Secreted;
CC IsoId=P16871-3; Sequence=VSP_001713;
CC Name=2; Synonyms=Secreted;
CC IsoId=P16871-4; Sequence=VSP_012618, VSP_012619;
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- PTM: N-glycosylated IL-7Ralpha binds IL7 300-fold more tightly than the
CC unglycosylated form. {ECO:0000269|PubMed:19141282}.
CC -!- DISEASE: Severe combined immunodeficiency autosomal recessive T-cell-
CC negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID)
CC [MIM:608971]: A form of severe combined immunodeficiency (SCID), a
CC genetically and clinically heterogeneous group of rare congenital
CC disorders characterized by impairment of both humoral and cell-mediated
CC immunity, leukopenia, and low or absent antibody levels. Patients
CC present in infancy recurrent, persistent infections by opportunistic
CC organisms. The common characteristic of all types of SCID is absence of
CC T-cell-mediated cellular immunity due to a defect in T-cell
CC development. {ECO:0000269|PubMed:11023514, ECO:0000269|PubMed:9843216}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Multiple sclerosis 3 (MS3) [MIM:612595]: A multifactorial,
CC inflammatory, demyelinating disease of the central nervous system.
CC Sclerotic lesions are characterized by perivascular infiltration of
CC monocytes and lymphocytes and appear as indurated areas in pathologic
CC specimens (sclerosis in plaques). The pathological mechanism is
CC regarded as an autoimmune attack of the myelin sheath, mediated by both
CC cellular and humoral immunity. Clinical manifestations include visual
CC loss, extra-ocular movement disorders, paresthesias, loss of sensation,
CC weakness, dysarthria, spasticity, ataxia and bladder dysfunction.
CC Genetic and environmental factors influence susceptibility to the
CC disease. {ECO:0000269|PubMed:17660817}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC A polymorphism at position 244 strongly influences susceptibility to
CC multiple sclerosis. Overtransmission of the major 'C' allele coding for
CC Thr-244 is detected in offspring affected with multiple sclerosis. In
CC vitro analysis of transcripts from minigenes containing either 'C'
CC allele (Thr-244) or 'T' allele (Ile-244) shows that the 'C' allele
CC results in an approximately two-fold increase in the skipping of exon
CC 6, leading to increased production of a soluble form of IL7R. Thus, the
CC multiple sclerosis associated 'C' risk allele of IL7R would probably
CC decrease membrane-bound expression of IL7R. As this risk allele is
CC common in the general population, some additional triggers are probably
CC required for the development and progression of MS.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20717.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=IL7Rbase; Note=IL7R mutation db;
CC URL="http://structure.bmc.lu.se/idbase/IL7Rbase/";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il7r/";
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DR EMBL; M29696; AAA59157.1; -; mRNA.
DR EMBL; AF043129; AAC83204.1; -; Genomic_DNA.
DR EMBL; AF043123; AAC83204.1; JOINED; Genomic_DNA.
DR EMBL; AF043124; AAC83204.1; JOINED; Genomic_DNA.
DR EMBL; AF043125; AAC83204.1; JOINED; Genomic_DNA.
DR EMBL; AF043126; AAC83204.1; JOINED; Genomic_DNA.
DR EMBL; AF043127; AAC83204.1; JOINED; Genomic_DNA.
DR EMBL; AF043128; AAC83204.1; JOINED; Genomic_DNA.
DR EMBL; AK301220; BAG62793.1; -; mRNA.
DR EMBL; AK315251; BAG37673.1; -; mRNA.
DR EMBL; AY449709; AAR08908.1; -; Genomic_DNA.
DR EMBL; AC112204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020717; AAH20717.1; ALT_SEQ; mRNA.
DR EMBL; BC067537; AAH67537.1; -; mRNA.
DR EMBL; BC067538; AAH67538.1; -; mRNA.
DR EMBL; BC067539; AAH67539.1; -; mRNA.
DR EMBL; BC067540; AAH67540.1; -; mRNA.
DR EMBL; BC069999; AAH69999.1; -; mRNA.
DR CCDS; CCDS3911.1; -. [P16871-1]
DR PIR; A34791; A34791.
DR PIR; B34791; B34791.
DR PIR; C34791; C34791.
DR RefSeq; NP_002176.2; NM_002185.3. [P16871-1]
DR PDB; 3DI2; X-ray; 2.70 A; B/D=21-239.
DR PDB; 3DI3; X-ray; 2.90 A; B=21-239.
DR PDB; 3UP1; X-ray; 2.15 A; A/B=21-239.
DR PDB; 5J11; X-ray; 2.56 A; B=21-236.
DR PDB; 6P50; X-ray; 2.90 A; C=21-239.
DR PDB; 6P67; X-ray; 2.90 A; G/I/J/K=21-239.
DR PDBsum; 3DI2; -.
DR PDBsum; 3DI3; -.
DR PDBsum; 3UP1; -.
DR PDBsum; 5J11; -.
DR PDBsum; 6P50; -.
DR PDBsum; 6P67; -.
DR AlphaFoldDB; P16871; -.
DR SASBDB; P16871; -.
DR SMR; P16871; -.
DR BioGRID; 109789; 130.
DR DIP; DIP-3045N; -.
DR ELM; P16871; -.
DR IntAct; P16871; 18.
DR MINT; P16871; -.
DR STRING; 9606.ENSP00000306157; -.
DR GuidetoPHARMACOLOGY; 1698; -.
DR GlyGen; P16871; 6 sites.
DR iPTMnet; P16871; -.
DR PhosphoSitePlus; P16871; -.
DR BioMuta; IL7R; -.
DR DMDM; 215274000; -.
DR MassIVE; P16871; -.
DR MaxQB; P16871; -.
DR PaxDb; P16871; -.
DR PeptideAtlas; P16871; -.
DR PRIDE; P16871; -.
DR ProteomicsDB; 53396; -. [P16871-1]
DR ProteomicsDB; 53397; -. [P16871-2]
DR ProteomicsDB; 53398; -. [P16871-3]
DR ProteomicsDB; 53399; -. [P16871-4]
DR ABCD; P16871; 4 sequenced antibodies.
DR Antibodypedia; 4129; 1310 antibodies from 47 providers.
DR DNASU; 3575; -.
DR Ensembl; ENST00000303115.8; ENSP00000306157.3; ENSG00000168685.15. [P16871-1]
DR Ensembl; ENST00000506850.5; ENSP00000421207.1; ENSG00000168685.15. [P16871-3]
DR GeneID; 3575; -.
DR KEGG; hsa:3575; -.
DR MANE-Select; ENST00000303115.8; ENSP00000306157.3; NM_002185.5; NP_002176.2.
DR UCSC; uc003jjs.5; human. [P16871-1]
DR CTD; 3575; -.
DR DisGeNET; 3575; -.
DR GeneCards; IL7R; -.
DR HGNC; HGNC:6024; IL7R.
DR HPA; ENSG00000168685; Tissue enhanced (lymphoid).
DR MalaCards; IL7R; -.
DR MIM; 146661; gene.
DR MIM; 608971; phenotype.
DR MIM; 612595; phenotype.
DR neXtProt; NX_P16871; -.
DR OpenTargets; ENSG00000168685; -.
DR Orphanet; 39041; Omenn syndrome.
DR Orphanet; 169154; T-B+ severe combined immunodeficiency due to IL-7Ralpha deficiency.
DR PharmGKB; PA29840; -.
DR VEuPathDB; HostDB:ENSG00000168685; -.
DR eggNOG; ENOG502S4WE; Eukaryota.
DR GeneTree; ENSGT00510000048500; -.
DR HOGENOM; CLU_045398_0_0_1; -.
DR InParanoid; P16871; -.
DR OMA; QIHRVDD; -.
DR OrthoDB; 617812at2759; -.
DR PhylomeDB; P16871; -.
DR TreeFam; TF336573; -.
DR PathwayCommons; P16871; -.
DR Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P16871; -.
DR SIGNOR; P16871; -.
DR BioGRID-ORCS; 3575; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; IL7R; human.
DR EvolutionaryTrace; P16871; -.
DR GeneWiki; Interleukin-7_receptor-%CE%B1; -.
DR GenomeRNAi; 3575; -.
DR Pharos; P16871; Tbio.
DR PRO; PR:P16871; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P16871; protein.
DR Bgee; ENSG00000168685; Expressed in right lung and 146 other tissues.
DR ExpressionAtlas; P16871; baseline and differential.
DR Genevisible; P16871; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003823; F:antigen binding; TAS:ProtInc.
DR GO; GO:0004896; F:cytokine receptor activity; IDA:UniProtKB.
DR GO; GO:0004917; F:interleukin-7 receptor activity; TAS:ProtInc.
DR GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; IDA:UniProtKB.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:0000018; P:regulation of DNA recombination; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR040997; FN3_7.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF18447; FN3_7; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; SCID; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT CHAIN 21..459
FT /note="Interleukin-7 receptor subunit alpha"
FT /id="PRO_0000010909"
FT TOPO_DOM 21..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 131..231
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 217..221
FT /note="WSXWS motif"
FT MOTIF 272..280
FT /note="Box 1 motif"
FT MOD_RES 282
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19141282"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19141282"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19141282"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..57
FT /evidence="ECO:0000269|PubMed:19141282"
FT DISULFID 74..82
FT /evidence="ECO:0000269|PubMed:19141282"
FT DISULFID 108..118
FT /evidence="ECO:0000269|PubMed:19141282"
FT VAR_SEQ 237..459
FT /note="EMDPILLTISILSFFSVALLVILACVLWKKRIKPIVWPSLPDHKKTLEHLCK
FT KPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSP
FT NCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLL
FT SLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ -> LS
FT LSYGPVSPIIRRLWNIFVRNQEK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_001713"
FT VAR_SEQ 237..252
FT /note="EMDPILLTISILSFFS -> LSLSYGPVSPIIRQEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2038316"
FT /id="VSP_012618"
FT VAR_SEQ 253..459
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2038316"
FT /id="VSP_012619"
FT VAR_SEQ 293..459
FT /note="NLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDV
FT QSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQD
FT LLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ ->
FT VSVFGA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001714"
FT VARIANT 66
FT /note="I -> T (in dbSNP:rs1494558)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2317865,
FT ECO:0000269|PubMed:9843216, ECO:0000269|Ref.5"
FT /id="VAR_021286"
FT VARIANT 113
FT /note="E -> D (in dbSNP:rs11567735)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021287"
FT VARIANT 132
FT /note="P -> S (in T(-)B(+)NK(+) SCID; dbSNP:rs104893894)"
FT /evidence="ECO:0000269|PubMed:11023514"
FT /id="VAR_034870"
FT VARIANT 138
FT /note="V -> I (in dbSNP:rs1494555)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2317865,
FT ECO:0000269|PubMed:9843216, ECO:0000269|Ref.5"
FT /id="VAR_021288"
FT VARIANT 244
FT /note="T -> I (in dbSNP:rs6897932)"
FT /evidence="ECO:0000269|PubMed:17660817,
FT ECO:0000269|PubMed:9843216, ECO:0000269|Ref.5"
FT /id="VAR_021289"
FT VARIANT 356
FT /note="I -> V (in dbSNP:rs3194051)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2038316,
FT ECO:0000269|PubMed:2317865"
FT /id="VAR_021290"
FT VARIANT 414
FT /note="T -> M (in dbSNP:rs2229232)"
FT /id="VAR_047742"
FT CONFLICT 39
FT /note="S -> T (in Ref. 7; AAH67539)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="Q -> R (in Ref. 7; AAH67538)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="S -> P (in Ref. 7; AAH67537)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="R -> G (in Ref. 7; AAH67539)"
FT /evidence="ECO:0000305"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:3UP1"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:3UP1"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3UP1"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 179..191
FT /evidence="ECO:0007829|PDB:3UP1"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:3UP1"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3DI3"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3UP1"
SQ SEQUENCE 459 AA; 51579 MW; EF50BF2615EEF50C CRC64;
MTILGTTFGM VFSLLQVVSG ESGYAQNGDL EDAELDDYSF SCYSQLEVNG SQHSLTCAFE
DPDVNITNLE FEICGALVEV KCLNFRKLQE IYFIETKKFL LIGKSNICVK VGEKSLTCKK
IDLTTIVKPE APFDLSVVYR EGANDFVVTF NTSHLQKKYV KVLMHDVAYR QEKDENKWTH
VNLSSTKLTL LQRKLQPAAM YEIKVRSIPD HYFKGFWSEW SPSYYFRTPE INNSSGEMDP
ILLTISILSF FSVALLVILA CVLWKKRIKP IVWPSLPDHK KTLEHLCKKP RKNLNVSFNP
ESFLDCQIHR VDDIQARDEV EGFLQDTFPQ QLEESEKQRL GGDVQSPNCP SEDVVITPES
FGRDSSLTCL AGNVSACDAP ILSSSRSLDC RESGKNGPHV YQDLLLSLGT TNSTLPPPFS
LQSGILTLNP VAQGQPILTS LGSNQEEAYV TMSSFYQNQ
