ID IL3RB_HUMAN Reviewed; 897 AA. AC P32927; Q5JZI1; Q6ICE0; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 27-MAR-2024, entry version 223. DE RecName: Full=Cytokine receptor common subunit beta; DE AltName: Full=CDw131; DE AltName: Full=GM-CSF/IL-3/IL-5 receptor common beta subunit; DE AltName: CD_antigen=CD131; DE Flags: Precursor; GN Name=CSF2RB; Synonyms=IL3RB, IL5RB; 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). RX PubMed=1702217; DOI=10.1073/pnas.87.24.9655; RA Hayashida K., Kitamura T., Gorman D.M., Arai K., Yokota T., Miyajima A.; RT "Molecular cloning of a second subunit of the receptor for human RT granulocyte-macrophage colony-stimulating factor (GM-CSF): reconstitution RT of a high-affinity GM-CSF receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9655-9659(1990). RN [2] RP SEQUENCE REVISION TO 454. RA Kitamura T.; RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP INTERACTION WITH TMEM102. RX PubMed=17828305; DOI=10.1038/sj.onc.1210778; RA Kao C.J., Chiang Y.J., Chen P.H., Lin K.R., Hwang P.I., Yang-Yen H.F., RA Yen J.J.; RT "CBAP interacts with the un-liganded common beta-subunit of the GM-CSF/IL- RT 3/IL-5 receptor and induces apoptosis via mitochondrial dysfunction."; RL Oncogene 27:1397-1403(2008). RN [7] RP INVOLVEMENT IN SMDP5. RX PubMed=21075760; DOI=10.1136/jmg.2010.082586; RA Tanaka T., Motoi N., Tsuchihashi Y., Tazawa R., Kaneko C., Nei T., RA Yamamoto T., Hayashi T., Tagawa T., Nagayasu T., Kuribayashi F., RA Ariyoshi K., Nakata K., Morimoto K.; RT "Adult-onset hereditary pulmonary alveolar proteinosis caused by a single- RT base deletion in CSF2RB."; RL J. Med. Genet. 48:205-209(2011). RN [8] RP FUNCTION, AND INTERACTION WITH IL5 AND IL5RA. RX PubMed=1495999; DOI=10.1073/pnas.89.15.7041; RA Tavernier J., Tuypens T., Plaetinck G., Verhee A., Fiers W., Devos R.; RT "Molecular basis of the membrane-anchored and two soluble isoforms of the RT human interleukin 5 receptor alpha subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 89:7041-7045(1992). RN [9] RP FUNCTION, AND INTERACTION WITH IL5RA AND JAK1. RX PubMed=9516124; RA Ogata N., Kouro T., Yamada A., Koike M., Hanai N., Ishikawa T., Takatsu K.; RT "JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) RT receptor alpha and betac subunit, respectively, and are activated upon IL-5 RT stimulation."; RL Blood 91:2264-2271(1998). RN [10] RP STRUCTURE BY NMR OF 338-438. RX PubMed=10736232; DOI=10.1006/jmbi.2000.3610; RA Mulhern T.D., Lopez A.F., D'Andrea R.J., Gaunt C., Vandeleur L., RA Vadas M.A., Booker G.W., Bagley C.J.; RT "The solution structure of the cytokine-binding domain of the common beta- RT chain of the receptors for granulocyte-macrophage colony-stimulating RT factor, interleukin-3 and interleukin-5."; RL J. Mol. Biol. 297:989-1001(2000). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 338-438. RX PubMed=10753826; RA Rossjohn J., McKinstry W.J., Woodcock J.M., McClure B.J., Hercus T.R., RA Parker M.W., Lopez A.F., Bagley C.J.; RT "Structure of the activation domain of the GM-CSF/IL-3/IL-5 receptor common RT beta-chain bound to an antagonist."; RL Blood 95:2491-2498(2000). RN [12] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-437. RX PubMed=11207369; DOI=10.1016/s0092-8674(01)00213-6; RA Carr P.D., Gustin S.E., Church A.P., Murphy J.M., Ford S.C., Mann D.A., RA Woltring D.M., Walker I., Ollis D.L., Young I.G.; RT "Structure of the complete extracellular domain of the common beta subunit RT of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer RT configuration."; RL Cell 104:291-300(2001). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 25-443, DISULFIDE BONDS, SUBUNIT, RP AND GLYCOSYLATION AT ASN-58 AND ASN-191. RX PubMed=16754968; DOI=10.1107/s1744309106016812; RA Carr P.D., Conlan F., Ford S., Ollis D.L., Young I.G.; RT "An improved resolution structure of the human beta common receptor RT involved in IL-3, IL-5 and GM-CSF signalling which gives better definition RT of the high-affinity binding epitope."; RL Acta Crystallogr. F 62:509-513(2006). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-438 IN COMPLEX WITH CSF2RA AND RP CSF2, SUBUNIT, GLYCOSYLATION AT ASN-58 AND ASN-191, AND DISULFIDE BONDS. RX PubMed=18692472; DOI=10.1016/j.cell.2008.05.053; RA Hansen G., Hercus T.R., McClure B.J., Stomski F.C., Dottore M., Powell J., RA Ramshaw H., Woodcock J.M., Xu Y., Guthridge M., McKinstry W.J., Lopez A.F., RA Parker M.W.; RT "The structure of the GM-CSF receptor complex reveals a distinct mode of RT cytokine receptor activation."; RL Cell 134:496-507(2008). RN [15] RP VARIANT THR-603. RX PubMed=9410898; DOI=10.1172/jci119758; RA Dirksen U., Nishinakamura R., Groneck P., Hattenhorst U., Nogee L., RA Murray R., Burdach S.; RT "Human pulmonary alveolar proteinosis associated with a defect in GM- RT CSF/IL-3/IL-5 receptor common beta chain expression."; RL J. Clin. Invest. 100:2211-2217(1997). CC -!- FUNCTION: Cell surface receptor that plays a role in immune response CC and controls the production and differentiation of hematopoietic CC progenitor cells into lineage-restricted cells. Acts by forming an CC heterodimeric receptor through interaction with different partners such CC as IL3RA, IL5RA or CSF2RA (PubMed:1495999). In turn, participates in CC various signaling pathways including interleukin-3, interleukin-5 and CC granulocyte-macrophage colony-stimulating factor/CSF2 pathways. In CC unstimulated conditions, interacts constitutively with JAK1 and ligand CC binding leads to JAK1 stimulation and subsequent activation of the JAK- CC STAT pathway (PubMed:9516124). {ECO:0000269|PubMed:1495999, CC ECO:0000269|PubMed:9516124}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit CC is common to the IL3, IL5 and GM-CSF receptors (PubMed:1495999). The CC signaling GM-CSF receptor complex is a dodecamer of two head-to-head CC hexamers of two alpha, two beta, and two ligand subunits. Interacts CC with TMEM102; this interaction occurs preferentially in the absence of CC CSF2. Interacts with FCER1G; this interaction is direct. Interacts with CC LYN. Interacts with JAK1 (PubMed:9516124). CC {ECO:0000250|UniProtKB:P26955, ECO:0000269|PubMed:1495999, CC ECO:0000269|PubMed:9516124}. CC -!- INTERACTION: CC P32927; P04141: CSF2; NbExp=2; IntAct=EBI-1809771, EBI-1809826; CC P32927; P08700: IL3; NbExp=2; IntAct=EBI-1809771, EBI-1811718; CC P32927; P05113: IL5; NbExp=2; IntAct=EBI-1809771, EBI-2435811; CC P32927; Q01344: IL5RA; NbExp=3; IntAct=EBI-1809771, EBI-1759442; CC P32927; P05556: ITGB1; NbExp=5; IntAct=EBI-1809771, EBI-703066; CC P32927; O60674: JAK2; NbExp=4; IntAct=EBI-1809771, EBI-518647; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P32927-1; Sequence=Displayed; CC Name=2; CC IsoId=P32927-2; Sequence=VSP_032798; 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: May be phosphorylated by LYN. {ECO:0000250}. CC -!- DISEASE: Pulmonary surfactant metabolism dysfunction 5 (SMDP5) CC [MIM:614370]: A rare lung disorder due to impaired surfactant CC homeostasis. It is characterized by alveolar filling with floccular CC material that stains positive using the periodic acid-Schiff method and CC is derived from surfactant phospholipids and protein components. CC Excessive lipoproteins accumulation in the alveoli results in severe CC respiratory distress. {ECO:0000269|PubMed:21075760}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4 CC subfamily. {ECO:0000305}. 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; M59941; AAA18171.1; -; mRNA. DR EMBL; CR456428; CAG30314.1; -; mRNA. DR EMBL; AL008637; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471095; EAW60125.1; -; Genomic_DNA. DR EMBL; CH471095; EAW60126.1; -; Genomic_DNA. DR CCDS; CCDS13936.1; -. [P32927-1] DR CCDS; CCDS93160.1; -. [P32927-2] DR PIR; A39255; A39255. DR RefSeq; NP_000386.1; NM_000395.2. [P32927-1] DR RefSeq; XP_005261397.1; XM_005261340.3. DR PDB; 1C8P; NMR; -; A=338-438. DR PDB; 1EGJ; X-ray; 2.80 A; A=338-438. DR PDB; 1GH7; X-ray; 3.00 A; A/B=25-437. DR PDB; 2GYS; X-ray; 2.70 A; A/B=25-437. DR PDB; 2NA8; NMR; -; A=432-473. DR PDB; 2NA9; NMR; -; A=432-473. DR PDB; 4NKQ; X-ray; 3.30 A; A=25-438. DR PDB; 5DWU; X-ray; 3.97 A; A=17-240, B=241-443. DR PDBsum; 1C8P; -. DR PDBsum; 1EGJ; -. DR PDBsum; 1GH7; -. DR PDBsum; 2GYS; -. DR PDBsum; 2NA8; -. DR PDBsum; 2NA9; -. DR PDBsum; 4NKQ; -. DR PDBsum; 5DWU; -. DR AlphaFoldDB; P32927; -. DR BMRB; P32927; -. DR SMR; P32927; -. DR BioGRID; 107826; 19. DR ComplexPortal; CPX-512; Granulocyte-macrophage colony-stimulating factor-receptor complex. DR CORUM; P32927; -. DR DIP; DIP-127N; -. DR ELM; P32927; -. DR IntAct; P32927; 17. DR MINT; P32927; -. DR STRING; 9606.ENSP00000384053; -. DR ChEMBL; CHEMBL2364169; -. DR ChEMBL; CHEMBL4804252; -. DR DrugBank; DB05264; NPI 32101. DR DrugBank; DB05943; Resatorvid. DR DrugBank; DB00020; Sargramostim. DR DrugCentral; P32927; -. DR GlyCosmos; P32927; 3 sites, No reported glycans. DR GlyGen; P32927; 3 sites. DR iPTMnet; P32927; -. DR PhosphoSitePlus; P32927; -. DR BioMuta; CSF2RB; -. DR DMDM; 1345923; -. DR jPOST; P32927; -. DR MassIVE; P32927; -. DR PaxDb; 9606-ENSP00000384053; -. DR PeptideAtlas; P32927; -. DR ProteomicsDB; 54888; -. [P32927-1] DR ProteomicsDB; 54889; -. [P32927-2] DR ABCD; P32927; 2 sequenced antibodies. DR Antibodypedia; 4136; 809 antibodies from 40 providers. DR DNASU; 1439; -. DR Ensembl; ENST00000403662.8; ENSP00000384053.3; ENSG00000100368.15. [P32927-1] DR Ensembl; ENST00000406230.5; ENSP00000385271.1; ENSG00000100368.15. [P32927-2] DR GeneID; 1439; -. DR KEGG; hsa:1439; -. DR MANE-Select; ENST00000403662.8; ENSP00000384053.3; NM_000395.3; NP_000386.1. DR UCSC; uc003aqa.5; human. [P32927-1] DR AGR; HGNC:2436; -. DR CTD; 1439; -. DR DisGeNET; 1439; -. DR GeneCards; CSF2RB; -. DR HGNC; HGNC:2436; CSF2RB. DR HPA; ENSG00000100368; Tissue enhanced (bone marrow, lymphoid tissue). DR MalaCards; CSF2RB; -. DR MIM; 138981; gene. DR MIM; 614370; phenotype. DR neXtProt; NX_P32927; -. DR OpenTargets; ENSG00000100368; -. DR Orphanet; 264675; Hereditary pulmonary alveolar proteinosis. DR PharmGKB; PA26939; -. DR VEuPathDB; HostDB:ENSG00000100368; -. DR eggNOG; ENOG502RP2T; Eukaryota. DR GeneTree; ENSGT00510000048963; -. DR HOGENOM; CLU_015884_0_0_1; -. DR InParanoid; P32927; -. DR OMA; LRFCGMY; -. DR OrthoDB; 5353732at2759; -. DR PhylomeDB; P32927; -. DR TreeFam; TF337996; -. DR PathwayCommons; P32927; -. DR Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-5683826; Surfactant metabolism. DR Reactome; R-HSA-5688849; Defective CSF2RB causes SMDP5. DR Reactome; R-HSA-5688890; Defective CSF2RA causes SMDP4. DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling. DR SignaLink; P32927; -. DR SIGNOR; P32927; -. DR BioGRID-ORCS; 1439; 14 hits in 1157 CRISPR screens. DR ChiTaRS; CSF2RB; human. DR EvolutionaryTrace; P32927; -. DR GenomeRNAi; 1439; -. DR Pharos; P32927; Tclin. DR PRO; PR:P32927; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P32927; Protein. DR Bgee; ENSG00000100368; Expressed in blood and 152 other cell types or tissues. DR ExpressionAtlas; P32927; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0030526; C:granulocyte macrophage colony-stimulating factor receptor complex; IDA:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; IDA:UniProt. DR GO; GO:0015026; F:coreceptor activity; IDA:UniProt. DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0036016; P:cellular response to interleukin-3; IEA:GOC. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0038157; P:granulocyte-macrophage colony-stimulating factor signaling pathway; IDA:ComplexPortal. DR GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central. DR GO; GO:0038156; P:interleukin-3-mediated signaling pathway; IDA:UniProt. DR GO; GO:0038043; P:interleukin-5-mediated signaling pathway; IDA:UniProt. DR GO; GO:0070665; P:positive regulation of leukocyte proliferation; IDA:ComplexPortal. DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:ComplexPortal. DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; TAS:ProtInc. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. DR CDD; cd00063; FN3; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. 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 InterPro; IPR011365; IL3_rcpt_beta. DR InterPro; IPR048668; IL3RB_N. DR PANTHER; PTHR23037; CYTOKINE RECEPTOR; 1. DR PANTHER; PTHR23037:SF35; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF21460; IL3Rb_N; 1. DR PIRSF; PIRSF001956; IL3R_beta_c; 1. DR SMART; SM00060; FN3; 2. DR SUPFAM; SSF49265; Fibronectin type III; 4. DR PROSITE; PS50853; FN3; 2. DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1. DR Genevisible; P32927; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT CHAIN 17..897 FT /note="Cytokine receptor common subunit beta" FT /id="PRO_0000010862" FT TOPO_DOM 17..443 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 444..460 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 461..897 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 133..240 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 339..436 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 498..517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 532..630 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 648..812 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 830..849 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 425..429 FT /note="WSXWS motif" FT MOTIF 474..482 FT /note="Box 1 motif" FT COMPBIAS 562..576 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 715..745 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 766 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P26955" FT CARBOHYD 58 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16754968, FT ECO:0000269|PubMed:18692472" FT CARBOHYD 191 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16754968, FT ECO:0000269|PubMed:18692472" FT CARBOHYD 346 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 35..45 FT DISULFID 75..96 FT DISULFID 86..91 FT DISULFID 250..260 FT DISULFID 289..306 FT VAR_SEQ 285 FT /note="G -> GSAVLLR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15461802" FT /id="VSP_032798" FT VARIANT 249 FT /note="E -> Q (in dbSNP:rs16845)" FT /id="VAR_042521" FT VARIANT 603 FT /note="P -> T (in dbSNP:rs1801122)" FT /evidence="ECO:0000269|PubMed:9410898" FT /id="VAR_014801" FT VARIANT 647 FT /note="G -> V (in dbSNP:rs1801115)" FT /id="VAR_014802" FT VARIANT 652 FT /note="V -> M (in dbSNP:rs1801114)" FT /id="VAR_014803" FT VARIANT 696 FT /note="P -> S (in dbSNP:rs16997517)" FT /id="VAR_042522" FT HELIX 28..32 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 39..50 FT /evidence="ECO:0007829|PDB:2GYS" FT HELIX 51..54 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 59..66 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 88..99 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 108..117 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:2GYS" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 137..144 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 147..153 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:4NKQ" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 169..177 FT /evidence="ECO:0007829|PDB:2GYS" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:1GH7" FT STRAND 186..197 FT /evidence="ECO:0007829|PDB:2GYS" FT TURN 199..201 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 207..216 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:1GH7" FT STRAND 233..236 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 246..252 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 254..265 FT /evidence="ECO:0007829|PDB:2GYS" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:2GYS" FT TURN 298..300 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 301..309 FT /evidence="ECO:0007829|PDB:2GYS" FT TURN 313..315 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 318..325 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 330..333 FT /evidence="ECO:0007829|PDB:2GYS" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:1GH7" FT STRAND 344..348 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:1GH7" FT STRAND 355..359 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:1C8P" FT STRAND 370..377 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:2GYS" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:1GH7" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 395..398 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:1GH7" FT STRAND 409..416 FT /evidence="ECO:0007829|PDB:2GYS" FT STRAND 418..420 FT /evidence="ECO:0007829|PDB:1GH7" FT STRAND 432..436 FT /evidence="ECO:0007829|PDB:1EGJ" FT HELIX 442..466 FT /evidence="ECO:0007829|PDB:2NA8" SQ SEQUENCE 897 AA; 97336 MW; 3398E37FDB8F393A CRC64; MVLAQGLLSM ALLALCWERS LAGAEETIPL QTLRCYNDYT SHITCRWADT QDAQRLVNVT LIRRVNEDLL EPVSCDLSDD MPWSACPHPR CVPRRCVIPC QSFVVTDVDY FSFQPDRPLG TRLTVTLTQH VQPPEPRDLQ ISTDQDHFLL TWSVALGSPQ SHWLSPGDLE FEVVYKRLQD SWEDAAILLS NTSQATLGPE HLMPSSTYVA RVRTRLAPGS RLSGRPSKWS PEVCWDSQPG DEAQPQNLEC FFDGAAVLSC SWEVRKEVAS SVSFGLFYKP SPDAGEEECS PVLREGLGSL HTRHHCQIPV PDPATHGQYI VSVQPRRAEK HIKSSVNIQM APPSLNVTKD GDSYSLRWET MKMRYEHIDH TFEIQYRKDT ATWKDSKTET LQNAHSMALP ALEPSTRYWA RVRVRTSRTG YNGIWSEWSE ARSWDTESVL PMWVLALIVI FLTIAVLLAL RFCGIYGYRL RRKWEEKIPN PSKSHLFQNG SAELWPPGSM SAFTSGSPPH QGPWGSRFPE LEGVFPVGFG DSEVSPLTIE DPKHVCDPPS GPDTTPAASD LPTEQPPSPQ PGPPAASHTP EKQASSFDFN GPYLGPPHSR SLPDILGQPE PPQEGGSQKS PPPGSLEYLC LPAGGQVQLV PLAQAMGPGQ AVEVERRPSQ GAAGSPSLES GGGPAPPALG PRVGGQDQKD SPVAIPMSSG DTEDPGVASG YVSSADLVFT PNSGASSVSL VPSLGLPSDQ TPSLCPGLAS GPPGAPGPVK SGFEGYVELP PIEGRSPRSP RNNPVPPEAK SPVLNPGERP ADVSPTSPQP EGLLVLQQVG DYCFLPGLGP GPLSLRSKPS SPGPGPEIKN LDQAFQVKKP PGQAVPQVPV IQLFKALKQQ DYLSLPPWEV NKPGEVC //