ID   IL2RA_HUMAN             Reviewed;         272 AA.
AC   P01589; Q5W007;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   13-FEB-2019, entry version 200.
DE   RecName: Full=Interleukin-2 receptor subunit alpha;
DE            Short=IL-2 receptor subunit alpha;
DE            Short=IL-2-RA;
DE            Short=IL-2R subunit alpha;
DE            Short=IL2-RA;
DE   AltName: Full=TAC antigen;
DE   AltName: Full=p55;
DE   AltName: CD_antigen=CD25;
DE   Flags: Precursor;
GN   Name=IL2RA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6090949; DOI=10.1038/311631a0;
RA   Nikaido T., Shimizu A., Ishida N., Sabe H., Teshigawara K., Maeda M.,
RA   Uchiyama T., Yodoi J., Honjo T.;
RT   "Molecular cloning of cDNA encoding human interleukin-2 receptor.";
RL   Nature 311:631-635(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6090948; DOI=10.1038/311626a0;
RA   Leonard W.J., Depper J.M., Crabtree G.R., Rudikoff S., Pumphrey J.,
RA   Robb R.J., Kroenke M., Svetlik P.B., Peffer N.J., Waldmann T.A.,
RA   Greene W.C.;
RT   "Molecular cloning and expression of cDNAs for the human interleukin-2
RT   receptor.";
RL   Nature 311:626-631(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2999698; DOI=10.1093/nar/13.21.7579;
RA   Ishida N., Kanamori H., Noma T., Nikaido T., Sabe H., Suzuki N.,
RA   Shimizu A., Honjo T.;
RT   "Molecular cloning and structure of the human interleukin 2 receptor
RT   gene.";
RL   Nucleic Acids Res. 13:7579-7589(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2996141; DOI=10.1126/science.2996141;
RA   Leonard W.J., Depper J.M., Kanehisa M., Kroenke M., Peffer N.J.,
RA   Svetlik P.B., Sullivan M., Greene W.C.;
RT   "Structure of the human interleukin-2 receptor gene.";
RL   Science 230:633-639(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-272.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   PubMed=3030566; DOI=10.1016/0092-8674(87)90754-9;
RA   Cross S.L., Feinberg M.B., Wolf J.B., Holbrook N.J., Wong-Stall F.,
RA   Leonard W.J.;
RT   "Regulation of the human interleukin-2 receptor alpha chain promoter:
RT   activation of a nonfunctional promoter by the transactivator gene of
RT   HTLV-I.";
RL   Cell 49:47-56(1987).
RN   [9]
RP   DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-70; ASN-89; THR-218;
RP   THR-224; THR-229 AND THR-237.
RX   PubMed=3134887; DOI=10.1016/0006-291X(88)90695-X;
RA   Miedel M.C., Hulmes J.D., Weber D.V., Bailon P., Pan Y.C.;
RT   "Structural analysis of recombinant soluble human interleukin-2
RT   receptor. Primary structure, assignment of disulfide bonds and core
RT   IL-2 binding structure.";
RL   Biochem. Biophys. Res. Commun. 154:372-379(1988).
RN   [10]
RP   3D-STRUCTURE MODELING OF 23-83.
RX   PubMed=7529123; DOI=10.1016/S0969-2126(94)00085-9;
RA   Bamborough P., Hedgecock C.J., Richards W.G.;
RT   "The interleukin-2 and interleukin-4 receptors studied by molecular
RT   modelling.";
RL   Structure 2:839-851(1994).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-238 IN COMPLEX WITH IL2;
RP   IL2RB AND IL2RC, AND DISULFIDE BONDS.
RX   PubMed=16293754; DOI=10.1126/science.1117893;
RA   Wang X., Rickert M., Garcia K.C.;
RT   "Structure of the quaternary complex of interleukin-2 with its alpha,
RT   beta, and gammac receptors.";
RL   Science 310:1159-1163(2005).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-233 IN COMPLEX WITH IL2;
RP   IL2RB AND IL2RC, AND DISULFIDE BONDS.
RX   PubMed=16477002; DOI=10.1073/pnas.0511161103;
RA   Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.;
RT   "Crystal structure of the IL-2 signaling complex: paradigm for a
RT   heterotrimeric cytokine receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006).
RN   [13]
RP   INVOLVEMENT IN IDDM10.
RX   PubMed=17676041; DOI=10.1038/ng2102;
RA   Lowe C.E., Cooper J.D., Brusko T., Walker N.M., Smyth D.J., Bailey R.,
RA   Bourget K., Plagnol V., Field S., Atkinson M., Clayton D.G.,
RA   Wicker L.S., Todd J.A.;
RT   "Large-scale genetic fine mapping and genotype-phenotype associations
RT   implicate polymorphism in the IL2RA region in type 1 diabetes.";
RL   Nat. Genet. 39:1074-1082(2007).
RN   [14]
RP   FUNCTION, INVOLVEMENT IN IMD41, VARIANT IMD41 ASN-166, AND
RP   CHARACTERIZATION OF VARIANT IMD41 ASN-166.
RX   PubMed=23416241; DOI=10.1016/j.clim.2013.01.004;
RA   Goudy K., Aydin D., Barzaghi F., Gambineri E., Vignoli M.,
RA   Ciullini Mannurita S., Doglioni C., Ponzoni M., Cicalese M.P.,
RA   Assanelli A., Tommasini A., Brigida I., Dellepiane R.M., Martino S.,
RA   Olek S., Aiuti A., Ciceri F., Roncarolo M.G., Bacchetta R.;
RT   "Human IL2RA null mutation mediates immunodeficiency with
RT   lymphoproliferation and autoimmunity.";
RL   Clin. Immunol. 146:248-261(2013).
RN   [15]
RP   FUNCTION, INVOLVEMENT IN IMD41, AND VARIANT IMD41 SER-41.
RX   PubMed=24116927; DOI=10.1111/cei.12214;
RA   Bezrodnik L., Caldirola M.S., Seminario A.G., Moreira I.,
RA   Gaillard M.I.;
RT   "Follicular bronchiolitis as phenotype associated with CD25
RT   deficiency.";
RL   Clin. Exp. Immunol. 175:227-234(2014).
CC   -!- FUNCTION: Receptor for interleukin-2. The receptor is involved in
CC       the regulation of immune tolerance by controlling regulatory T
CC       cells (TREGs) activity. TREGs suppress the activation and
CC       expansion of autoreactive T-cells. {ECO:0000269|PubMed:23416241,
CC       ECO:0000269|PubMed:24116927}.
CC   -!- SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R
CC       exists in 3 different forms: a high affinity dimer, an
CC       intermediate affinity monomer (beta subunit), and a low affinity
CC       monomer (alpha subunit). The high and intermediate affinity forms
CC       also associate with a gamma subunit. {ECO:0000269|PubMed:16293754,
CC       ECO:0000269|PubMed:16477002}.
CC   -!- INTERACTION:
CC       P60568:IL2; NbExp=3; IntAct=EBI-8614302, EBI-12508717;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- DISEASE: Diabetes mellitus, insulin-dependent, 10 (IDDM10)
CC       [MIM:601942]: A multifactorial disorder of glucose homeostasis
CC       that is characterized by susceptibility to ketoacidosis in the
CC       absence of insulin therapy. Clinical features are polydipsia,
CC       polyphagia and polyuria which result from hyperglycemia-induced
CC       osmotic diuresis and secondary thirst. These derangements result
CC       in long-term complications that affect the eyes, kidneys, nerves,
CC       and blood vessels. {ECO:0000269|PubMed:17676041}. Note=Disease
CC       susceptibility is associated with variations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Immunodeficiency 41 with lymphoproliferation and
CC       autoimmunity (IMD41) [MIM:606367]: A disorder of immune
CC       dysregulation characterized by recurrent viral, fungal, and
CC       bacterial infections, lymphadenopathy, and variable autoimmune
CC       features, such as autoimmune enteropathy and eczematous skin
CC       lesions. {ECO:0000269|PubMed:23416241,
CC       ECO:0000269|PubMed:24116927}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=IL2RAbase; Note=IL2RA mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/IL2RAbase/";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/il2ra/";
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DR   EMBL; X01057; CAA25525.1; -; mRNA.
DR   EMBL; X03131; CAA26906.1; -; Genomic_DNA.
DR   EMBL; X03132; CAA26906.1; JOINED; Genomic_DNA.
DR   EMBL; X03133; CAA26906.1; JOINED; Genomic_DNA.
DR   EMBL; X03134; CAA26906.1; JOINED; Genomic_DNA.
DR   EMBL; X03135; CAA26906.1; JOINED; Genomic_DNA.
DR   EMBL; X03136; CAA26906.1; JOINED; Genomic_DNA.
DR   EMBL; X03137; CAA26906.1; JOINED; Genomic_DNA.
DR   EMBL; X03138; CAA26906.1; JOINED; Genomic_DNA.
DR   EMBL; K03122; AAB59535.1; ALT_SEQ; mRNA.
DR   EMBL; M11066; AAA67527.1; -; Genomic_DNA.
DR   EMBL; M10322; AAA67527.1; JOINED; Genomic_DNA.
DR   EMBL; M11060; AAA67527.1; JOINED; Genomic_DNA.
DR   EMBL; M11061; AAA67527.1; JOINED; Genomic_DNA.
DR   EMBL; M11062; AAA67527.1; JOINED; Genomic_DNA.
DR   EMBL; M11063; AAA67527.1; JOINED; Genomic_DNA.
DR   EMBL; M11064; AAA67527.1; JOINED; Genomic_DNA.
DR   EMBL; M11065; AAA67527.1; JOINED; Genomic_DNA.
DR   EMBL; AY563103; AAS55572.1; -; Genomic_DNA.
DR   EMBL; AL157395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471072; EAW86414.1; -; Genomic_DNA.
DR   EMBL; M15864; AAA59162.1; -; Genomic_DNA.
DR   EMBL; BN000945; CAK26553.1; -; Genomic_DNA.
DR   CCDS; CCDS7076.1; -.
DR   PIR; A44186; UHHU2.
DR   RefSeq; NP_000408.1; NM_000417.2.
DR   RefSeq; NP_001295171.1; NM_001308242.1.
DR   RefSeq; NP_001295172.1; NM_001308243.1.
DR   UniGene; Hs.231367; -.
DR   PDB; 1ILM; Model; -; A=23-83.
DR   PDB; 1ILN; Model; -; A=23-83.
DR   PDB; 1Z92; X-ray; 2.80 A; B=22-238.
DR   PDB; 2B5I; X-ray; 2.30 A; D=22-238.
DR   PDB; 2ERJ; X-ray; 3.00 A; A/E=22-233.
DR   PDB; 3IU3; X-ray; 2.90 A; I/J/K=22-238.
DR   PDB; 3NFP; X-ray; 2.86 A; I/K=22-238.
DR   PDBsum; 1ILM; -.
DR   PDBsum; 1ILN; -.
DR   PDBsum; 1Z92; -.
DR   PDBsum; 2B5I; -.
DR   PDBsum; 2ERJ; -.
DR   PDBsum; 3IU3; -.
DR   PDBsum; 3NFP; -.
DR   ProteinModelPortal; P01589; -.
DR   SMR; P01589; -.
DR   BioGrid; 109774; 4.
DR   CORUM; P01589; -.
DR   DIP; DIP-1080N; -.
DR   IntAct; P01589; 2.
DR   MINT; P01589; -.
DR   STRING; 9606.ENSP00000369293; -.
DR   ChEMBL; CHEMBL1778; -.
DR   DrugBank; DB00041; Aldesleukin.
DR   DrugBank; DB00074; Basiliximab.
DR   DrugBank; DB00111; Daclizumab.
DR   DrugBank; DB00004; Denileukin diftitox.
DR   GuidetoPHARMACOLOGY; 1695; -.
DR   iPTMnet; P01589; -.
DR   PhosphoSitePlus; P01589; -.
DR   BioMuta; IL2RA; -.
DR   DMDM; 124317; -.
DR   PaxDb; P01589; -.
DR   PeptideAtlas; P01589; -.
DR   PRIDE; P01589; -.
DR   ProteomicsDB; 51393; -.
DR   DNASU; 3559; -.
DR   Ensembl; ENST00000379959; ENSP00000369293; ENSG00000134460.
DR   GeneID; 3559; -.
DR   KEGG; hsa:3559; -.
DR   UCSC; uc001iiz.3; human.
DR   CTD; 3559; -.
DR   DisGeNET; 3559; -.
DR   EuPathDB; HostDB:ENSG00000134460.15; -.
DR   GeneCards; IL2RA; -.
DR   HGNC; HGNC:6008; IL2RA.
DR   HPA; CAB002419; -.
DR   HPA; HPA054622; -.
DR   MalaCards; IL2RA; -.
DR   MIM; 147730; gene.
DR   MIM; 601942; phenotype.
DR   MIM; 606367; phenotype.
DR   neXtProt; NX_P01589; -.
DR   OpenTargets; ENSG00000134460; -.
DR   Orphanet; 169100; Immunodeficiency due to CD25 deficiency.
DR   Orphanet; 85410; Oligoarticular juvenile idiopathic arthritis.
DR   Orphanet; 85408; Rheumatoid factor-negative juvenile idiopathic arthritis.
DR   PharmGKB; PA29828; -.
DR   eggNOG; ENOG410J24B; Eukaryota.
DR   eggNOG; ENOG41116U7; LUCA.
DR   GeneTree; ENSGT00390000018872; -.
DR   HOGENOM; HOG000113044; -.
DR   HOVERGEN; HBG052109; -.
DR   InParanoid; P01589; -.
DR   KO; K05068; -.
DR   OMA; HYQCIQG; -.
DR   OrthoDB; 1236351at2759; -.
DR   PhylomeDB; P01589; -.
DR   TreeFam; TF337408; -.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
DR   Reactome; R-HSA-9020558; Interleukin-2 signaling.
DR   Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR   SIGNOR; P01589; -.
DR   ChiTaRS; IL2RA; human.
DR   EvolutionaryTrace; P01589; -.
DR   GeneWiki; IL2RA; -.
DR   GenomeRNAi; 3559; -.
DR   PRO; PR:P01589; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000134460; Expressed in 103 organ(s), highest expression level in lymph node.
DR   ExpressionAtlas; P01589; baseline and differential.
DR   Genevisible; P01589; HS.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005893; C:interleukin-2 receptor complex; TAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0019976; F:interleukin-2 binding; IBA:GO_Central.
DR   GO; GO:0004911; F:interleukin-2 receptor activity; IBA:GO_Central.
DR   GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR   GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR   GO; GO:0008283; P:cell population proliferation; TAS:ProtInc.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
DR   GO; GO:0038110; P:interleukin-2-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0050687; P:negative regulation of defense response to virus; IEA:Ensembl.
DR   GO; GO:0050777; P:negative regulation of immune response; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
DR   GO; GO:0045589; P:regulation of regulatory T cell differentiation; TAS:Reactome.
DR   GO; GO:0046013; P:regulation of T cell homeostatic proliferation; IEA:Ensembl.
DR   GO; GO:0002664; P:regulation of T cell tolerance induction; IMP:UniProtKB.
DR   CDD; cd00033; CCP; 1.
DR   InterPro; IPR015486; IL-2_rcpt_alpha.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR10573; PTHR10573; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   SMART; SM00032; CCP; 2.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   PROSITE; PS50923; SUSHI; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Diabetes mellitus; Disease mutation;
KW   Disulfide bond; Glycoprotein; Immunity; Membrane; Polymorphism;
KW   Receptor; Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21
FT   CHAIN        22    272       Interleukin-2 receptor subunit alpha.
FT                                /FTId=PRO_0000011024.
FT   TOPO_DOM     22    240       Extracellular. {ECO:0000255}.
FT   TRANSMEM    241    259       Helical. {ECO:0000255}.
FT   TOPO_DOM    260    272       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       22     84       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      123    186       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   CARBOHYD     70     70       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:3134887}.
FT   CARBOHYD     89     89       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:3134887}.
FT   CARBOHYD    218    218       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:3134887}.
FT   CARBOHYD    224    224       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:3134887}.
FT   CARBOHYD    229    229       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:3134887}.
FT   CARBOHYD    237    237       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:3134887}.
FT   DISULFID     24    168
FT   DISULFID     49     80
FT   DISULFID     51     82
FT   DISULFID     67    125
FT   DISULFID    152    184
FT   VARIANT      41     41       Y -> S (in IMD41; dbSNP:rs796051888).
FT                                {ECO:0000269|PubMed:24116927}.
FT                                /FTId=VAR_074641.
FT   VARIANT     166    166       S -> N (in IMD41; the receptor does not
FT                                localize to the plasma membrane;
FT                                dbSNP:rs796051887).
FT                                {ECO:0000269|PubMed:23416241}.
FT                                /FTId=VAR_074642.
FT   VARIANT     272    272       I -> T (in dbSNP:rs12722712).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_019280.
FT   STRAND       34     37       {ECO:0000244|PDB:2B5I}.
FT   STRAND       39     41       {ECO:0000244|PDB:2B5I}.
FT   STRAND       46     48       {ECO:0000244|PDB:2B5I}.
FT   STRAND       55     57       {ECO:0000244|PDB:2B5I}.
FT   STRAND       63     67       {ECO:0000244|PDB:2B5I}.
FT   STRAND       74     77       {ECO:0000244|PDB:3NFP}.
FT   STRAND       82     84       {ECO:0000244|PDB:2B5I}.
FT   STRAND      135    137       {ECO:0000244|PDB:3IU3}.
FT   STRAND      143    145       {ECO:0000244|PDB:3NFP}.
FT   STRAND      147    152       {ECO:0000244|PDB:2B5I}.
FT   STRAND      157    162       {ECO:0000244|PDB:2B5I}.
FT   STRAND      164    170       {ECO:0000244|PDB:2B5I}.
FT   STRAND      172    174       {ECO:0000244|PDB:1Z92}.
FT   STRAND      175    177       {ECO:0000244|PDB:2B5I}.
FT   STRAND      182    185       {ECO:0000244|PDB:2B5I}.
SQ   SEQUENCE   272 AA;  30819 MW;  83D907C8C81D2C0E CRC64;
     MDSYLLMWGL LTFIMVPGCQ AELCDDDPPE IPHATFKAMA YKEGTMLNCE CKRGFRRIKS
     GSLYMLCTGN SSHSSWDNQC QCTSSATRNT TKQVTPQPEE QKERKTTEMQ SPMQPVDQAS
     LPGHCREPPP WENEATERIY HFVVGQMVYY QCVQGYRALH RGPAESVCKM THGKTRWTQP
     QLICTGEMET SQFPGEEKPQ ASPEGRPESE TSCLVTTTDF QIQTEMAATM ETSIFTTEYQ
     VAVAGCVFLL ISVLLLSGLT WQRRQRKSRR TI
//