IL3RB_HUMAN
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 03-AUG-2022, entry version 214.
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; 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}.
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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 PIR; A39255; A39255.
DR RefSeq; NP_000386.1; NM_000395.2. [P32927-1]
DR RefSeq; XP_005261397.1; XM_005261340.3. [P32927-2]
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; 18.
DR ComplexPortal; CPX-512; Granulocyte-macrophage colony-stimulating factor-receptor complex.
DR CORUM; P32927; -.
DR DIP; DIP-127N; -.
DR ELM; P32927; -.
DR IntAct; P32927; 16.
DR MINT; P32927; -.
DR STRING; 9606.ENSP00000384053; -.
DR ChEMBL; CHEMBL2364169; -.
DR DrugBank; DB05264; NPI 32101.
DR DrugBank; DB05943; Resatorvid.
DR DrugBank; DB00020; Sargramostim.
DR DrugCentral; P32927; -.
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; P32927; -.
DR PeptideAtlas; P32927; -.
DR PRIDE; P32927; -.
DR ProteomicsDB; 54888; -. [P32927-1]
DR ProteomicsDB; 54889; -. [P32927-2]
DR ABCD; P32927; 2 sequenced antibodies.
DR Antibodypedia; 4136; 751 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 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 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 1071 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 150 other tissues.
DR ExpressionAtlas; P32927; baseline and differential.
DR Genevisible; P32927; HS.
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:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; EXP:ComplexPortal.
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; IEA:GOC.
DR GO; GO:0038043; P:interleukin-5-mediated signaling pathway; IEA:GOC.
DR GO; GO:0070665; P:positive regulation of leukocyte proliferation; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; 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; -; 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; IPR015373; Interferon/interleukin_rcp_dom.
DR Pfam; PF09294; Interfer-bind; 1.
DR PIRSF; PIRSF001956; IL3R_beta_c; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
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
