IL2RA_HUMAN
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 03-AUG-2022, entry version 218.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 HTLV-
RT I.";
RL Cell 49:47-56(1987).
RN [9]
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-70; ASN-89; THR-218; THR-224;
RP 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 receptor.
RT Primary structure, assignment of disulfide bonds and core IL-2 binding
RT 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; IL2RB
RP 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, beta,
RT 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; IL2RB
RP 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., Wicker L.S.,
RA 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 CHARACTERIZATION
RP 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., Gaillard M.I.;
RT "Follicular bronchiolitis as phenotype associated with CD25 deficiency.";
RL Clin. Exp. Immunol. 175:227-234(2014).
CC -!- FUNCTION: Receptor for interleukin-2. The receptor is involved in the
CC regulation of immune tolerance by controlling regulatory T cells
CC (TREGs) activity. TREGs suppress the activation and expansion of
CC 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 exists
CC in 3 different forms: a high affinity dimer, an intermediate affinity
CC monomer (beta subunit), and a low affinity monomer (alpha subunit). The
CC high and intermediate affinity forms also associate with a gamma
CC subunit. {ECO:0000269|PubMed:16293754, ECO:0000269|PubMed:16477002}.
CC -!- INTERACTION:
CC P01589; P60568: IL2; NbExp=3; IntAct=EBI-8614302, EBI-12508717;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DISEASE: Diabetes mellitus, insulin-dependent, 10 (IDDM10)
CC [MIM:601942]: A multifactorial disorder of glucose homeostasis that is
CC characterized by susceptibility to ketoacidosis in the absence of
CC insulin therapy. Clinical features are polydipsia, polyphagia and
CC polyuria which result from hyperglycemia-induced osmotic diuresis and
CC secondary thirst. These derangements result in long-term complications
CC that affect the eyes, kidneys, nerves, and blood vessels.
CC {ECO:0000269|PubMed:17676041}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- DISEASE: Immunodeficiency 41 with lymphoproliferation and autoimmunity
CC (IMD41) [MIM:606367]: A disorder of immune dysregulation characterized
CC by recurrent viral, fungal, and bacterial infections, lymphadenopathy,
CC and variable autoimmune features, such as autoimmune enteropathy and
CC eczematous skin lesions. {ECO:0000269|PubMed:23416241,
CC ECO:0000269|PubMed:24116927}. Note=The disease is caused by variants
CC 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/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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 PDB; 6VWU; X-ray; 3.40 A; A=22-186.
DR PDB; 6YIO; X-ray; 1.83 A; B=22-213.
DR PDB; 7F9W; EM; 3.20 A; A=26-186.
DR PDBsum; 1Z92; -.
DR PDBsum; 2B5I; -.
DR PDBsum; 2ERJ; -.
DR PDBsum; 3IU3; -.
DR PDBsum; 3NFP; -.
DR PDBsum; 6VWU; -.
DR PDBsum; 6YIO; -.
DR PDBsum; 7F9W; -.
DR AlphaFoldDB; P01589; -.
DR SMR; P01589; -.
DR BioGRID; 109774; 83.
DR CORUM; P01589; -.
DR DIP; DIP-1080N; -.
DR IntAct; P01589; 2.
DR MINT; P01589; -.
DR STRING; 9606.ENSP00000369293; -.
DR BindingDB; P01589; -.
DR ChEMBL; CHEMBL1778; -.
DR DrugBank; DB00041; Aldesleukin.
DR DrugBank; DB00074; Basiliximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00004; Denileukin diftitox.
DR DrugBank; DB15628; Inolimomab.
DR DrugCentral; P01589; -.
DR GuidetoPHARMACOLOGY; 1695; -.
DR GlyGen; P01589; 6 sites.
DR iPTMnet; P01589; -.
DR PhosphoSitePlus; P01589; -.
DR BioMuta; IL2RA; -.
DR DMDM; 124317; -.
DR MassIVE; P01589; -.
DR PaxDb; P01589; -.
DR PeptideAtlas; P01589; -.
DR PRIDE; P01589; -.
DR ProteomicsDB; 51393; -.
DR ABCD; P01589; 13 sequenced antibodies.
DR Antibodypedia; 3715; 3086 antibodies from 52 providers.
DR DNASU; 3559; -.
DR Ensembl; ENST00000379959.8; ENSP00000369293.3; ENSG00000134460.18.
DR GeneID; 3559; -.
DR KEGG; hsa:3559; -.
DR MANE-Select; ENST00000379959.8; ENSP00000369293.3; NM_000417.3; NP_000408.1.
DR UCSC; uc001iiz.3; human.
DR CTD; 3559; -.
DR DisGeNET; 3559; -.
DR GeneCards; IL2RA; -.
DR HGNC; HGNC:6008; IL2RA.
DR HPA; ENSG00000134460; Tissue enhanced (adipose tissue, lymphoid tissue, urinary bladder).
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 polyarticular juvenile idiopathic arthritis.
DR PharmGKB; PA29828; -.
DR VEuPathDB; HostDB:ENSG00000134460; -.
DR eggNOG; ENOG502SUAG; Eukaryota.
DR GeneTree; ENSGT00390000018872; -.
DR InParanoid; P01589; -.
DR OMA; HYQCIQG; -.
DR OrthoDB; 1236351at2759; -.
DR PhylomeDB; P01589; -.
DR TreeFam; TF337408; -.
DR PathwayCommons; P01589; -.
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 SignaLink; P01589; -.
DR SIGNOR; P01589; -.
DR BioGRID-ORCS; 3559; 19 hits in 1067 CRISPR screens.
DR ChiTaRS; IL2RA; human.
DR EvolutionaryTrace; P01589; -.
DR GeneWiki; IL2RA; -.
DR GenomeRNAi; 3559; -.
DR Pharos; P01589; Tclin.
DR PRO; PR:P01589; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P01589; protein.
DR Bgee; ENSG00000134460; Expressed in lymph node and 111 other tissues.
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; TAS:ProtInc.
DR GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
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:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; 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:2000561; P:regulation of CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
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; Diabetes mellitus; Disease variant; Disulfide bond;
KW Glycoprotein; Immunity; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..272
FT /note="Interleukin-2 receptor subunit alpha"
FT /id="PRO_0000011024"
FT TOPO_DOM 22..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..84
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 123..186
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 87..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3134887"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3134887"
FT CARBOHYD 218
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3134887"
FT CARBOHYD 224
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3134887"
FT CARBOHYD 229
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3134887"
FT CARBOHYD 237
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="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
FT /note="Y -> S (in IMD41; dbSNP:rs796051888)"
FT /evidence="ECO:0000269|PubMed:24116927"
FT /id="VAR_074641"
FT VARIANT 166
FT /note="S -> N (in IMD41; the receptor does not localize to
FT the plasma membrane; dbSNP:rs796051887)"
FT /evidence="ECO:0000269|PubMed:23416241"
FT /id="VAR_074642"
FT VARIANT 272
FT /note="I -> T (in dbSNP:rs12722712)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019280"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:6YIO"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6YIO"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6YIO"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6YIO"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6YIO"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3IU3"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3NFP"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:6YIO"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:6YIO"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6YIO"
FT STRAND 182..185
FT /evidence="ECO:0007829|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
