ID   IL6RB_MOUSE             Reviewed;         917 AA.
AC   Q00560; G5E8D2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   04-NOV-2026, entry version 216.
DE   RecName: Full=Interleukin-6 receptor subunit beta {ECO:0000305};
DE            Short=IL-6 receptor subunit beta;
DE            Short=IL-6R subunit beta;
DE            Short=IL-6R-beta;
DE            Short=IL-6RB;
DE   AltName: Full=Interleukin-6 signal transducer;
DE   AltName: Full=Membrane glycoprotein 130;
DE            Short=gp130 {ECO:0000303|PubMed:1602143};
DE   AltName: Full=Oncostatin-M receptor subunit alpha;
DE   AltName: CD_antigen=CD130;
DE   Flags: Precursor;
GN   Name=Il6st {ECO:0000312|MGI:MGI:96560};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=ICR; TISSUE=Macrophage;
RX   PubMed=1602143; DOI=10.4049/jimmunol.148.12.4066;
RA   Saito M., Yoshida K., Hibi M., Taga T., Kishimoto T.;
RT   "Molecular cloning of a murine IL-6 receptor-associated signal transducer,
RT   gp130, and its regulated expression in vivo.";
RL   J. Immunol. 148:4066-4071(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8552649; DOI=10.1073/pnas.93.1.407;
RA   Yoshida K., Taga T., Saito M., Suematsu S., Kumanogoh A., Tanaka T.,
RA   Fujiwara H., Hirata M., Yamagami T., Nakahata T., Hirabayashi T.,
RA   Yoneda Y., Tanaka K., Wang W.Z., Mori C., Shiota K., Yoshida N.,
RA   Kishimoto T.;
RT   "Targeted disruption of gp130, a common signal transducer for the
RT   interleukin 6 family of cytokines, leads to myocardial and hematological
RT   disorders.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:407-411(1996).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9348227; DOI=10.1210/endo.138.11.5534;
RA   Kawasaki K., Gao Y.H., Yokose S., Kaji Y., Nakamura T., Suda T.,
RA   Yoshida K., Taga T., Kishimoto T., Kataoka H., Yuasa T., Norimatsu H.,
RA   Yamaguchi A.;
RT   "Osteoclasts are present in gp130-deficient mice.";
RL   Endocrinology 138:4959-4965(1997).
RN   [6]
RP   FUNCTION.
RC   TISSUE=Thymus;
RX   PubMed=9202125; DOI=10.1038/43206;
RA   Starr R., Willson T.A., Viney E.M., Murray L.J.L., Rayner J.R.,
RA   Jenkins B.J., Gonda T.J., Alexander W.S., Metcalf D., Nicola N.A.,
RA   Hilton D.J.;
RT   "A family of cytokine-inducible inhibitors of signaling.";
RL   Nature 387:917-921(1997).
RN   [7]
RP   SUBUNIT.
RX   PubMed=9920829; DOI=10.1182/blood.v93.3.804;
RA   Tanaka M., Hara T., Copeland N.G., Gilbert D.J., Jenkins N.A., Miyajima A.;
RT   "Reconstitution of the functional mouse oncostatin M (OSM) receptor:
RT   molecular cloning of the OSM receptor beta subunit.";
RL   Blood 93:804-815(1999).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10377352; DOI=10.1523/jneurosci.19-13-05429.1999;
RA   Nakashima K., Wiese S., Yanagisawa M., Arakawa H., Kimura N., Hisatsune T.,
RA   Yoshida K., Kishimoto T., Sendtner M., Taga T.;
RT   "Developmental requirement of gp130 signaling in neuronal survival and
RT   astrocyte differentiation.";
RL   J. Neurosci. 19:5429-5434(1999).
RN   [9]
RP   FUNCTION.
RX   PubMed=10661409; DOI=10.1016/s1074-7613(00)80162-4;
RA   Ohtani T., Ishihara K., Atsumi T., Nishida K., Kaneko Y., Miyata T.,
RA   Itoh S., Narimatsu M., Maeda H., Fukada T., Itoh M., Okano H., Hibi M.,
RA   Hirano T.;
RT   "Dissection of signaling cascades through gp130 in vivo: reciprocal roles
RT   for STAT3- and SHP2-mediated signals in immune responses.";
RL   Immunity 12:95-105(2000).
RN   [10]
RP   INTERACTION WITH INPP5D.
RX   PubMed=17105399; DOI=10.1089/scd.2006.15.641;
RA   Desponts C., Ninos J.M., Kerr W.G.;
RT   "s-SHIP associates with receptor complexes essential for pluripotent stem
RT   cell growth and survival.";
RL   Stem Cells Dev. 15:641-646(2006).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [14]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24339143; DOI=10.1002/jbmr.2159;
RA   Johnson R.W., Brennan H.J., Vrahnas C., Poulton I.J., McGregor N.E.,
RA   Standal T., Walker E.C., Koh T.T., Nguyen H., Walsh N.C., Forwood M.R.,
RA   Martin T.J., Sims N.A.;
RT   "The primary function of gp130 signaling in osteoblasts is to maintain bone
RT   formation and strength, rather than promote osteoclast formation.";
RL   J. Bone Miner. Res. 29:1492-1505(2014).
RN   [15]
RP   FUNCTION.
RX   PubMed=25228504; DOI=10.1530/joe-14-0424;
RA   Standal T., Johnson R.W., McGregor N.E., Poulton I.J., Ho P.W.,
RA   Martin T.J., Sims N.A.;
RT   "gp130 in late osteoblasts and osteocytes is required for PTH-induced
RT   osteoblast differentiation.";
RL   J. Endocrinol. 223:181-190(2014).
RN   [16]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25057188; DOI=10.1523/jneurosci.5161-13.2014;
RA   Malsch P., Andratsch M., Vogl C., Link A.S., Alzheimer C., Brierley S.M.,
RA   Hughes P.A., Kress M.;
RT   "Deletion of interleukin-6 signal transducer gp130 in small sensory neurons
RT   attenuates mechanonociception and down-regulates TRPA1 expression.";
RL   J. Neurosci. 34:9845-9856(2014).
RN   [17]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26255596; DOI=10.1016/j.bone.2015.08.005;
RA   Johnson R.W., McGregor N.E., Brennan H.J., Crimeen-Irwin B., Poulton I.J.,
RA   Martin T.J., Sims N.A.;
RT   "Glycoprotein130 (Gp130)/interleukin-6 (IL-6) signalling in osteoclasts
RT   promotes bone formation in periosteal and trabecular bone.";
RL   Bone 81:343-351(2015).
RN   [18]
RP   FUNCTION.
RX   PubMed=25731159; DOI=10.1038/nature14228;
RA   Taniguchi K., Wu L.W., Grivennikov S.I., de Jong P.R., Lian I., Yu F.X.,
RA   Wang K., Ho S.B., Boland B.S., Chang J.T., Sandborn W.J., Hardiman G.,
RA   Raz E., Maehara Y., Yoshimura A., Zucman-Rossi J., Guan K.L., Karin M.;
RT   "A gp130-Src-YAP module links inflammation to epithelial regeneration.";
RL   Nature 519:57-62(2015).
RN   [19]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY OBESITY.
RX   PubMed=28402851; DOI=10.1016/j.celrep.2017.03.043;
RA   Timper K., Denson J.L., Steculorum S.M., Heilinger C., Engstroem-Ruud L.,
RA   Wunderlich C.M., Rose-John S., Wunderlich F.T., Bruening J.C.;
RT   "IL-6 Improves Energy and Glucose Homeostasis in Obesity via Enhanced
RT   Central IL-6 trans-Signaling.";
RL   Cell Rep. 19:267-280(2017).
RN   [20]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=27893700; DOI=10.1038/ni.3632;
RA   Heink S., Yogev N., Garbers C., Herwerth M., Aly L., Gasperi C.,
RA   Husterer V., Croxford A.L., Moeller-Hackbarth K., Bartsch H.S., Sotlar K.,
RA   Krebs S., Regen T., Blum H., Hemmer B., Misgeld T., Wunderlich T.F.,
RA   Hidalgo J., Oukka M., Rose-John S., Schmidt-Supprian M., Waisman A.,
RA   Korn T.;
RT   "Trans-presentation of IL-6 by dendritic cells is required for the priming
RT   of pathogenic TH17 cells.";
RL   Nat. Immunol. 18:74-85(2017).
CC   -!- FUNCTION: Functions as a shared signal-transducing subunit not only for
CC       IL6 but also for other cytokine receptor complexes, including IL6, LIF,
CC       OSM, CNTF, IL11, CTF1, BSF3, MT-RNR2/humanin, CLCF1 and the
CC       heterodimeric complex CRLF1-CLCF1 (PubMed:1602143). Engages site 2 of
CC       CNTF, CLCF1, LIF, and IL-6, and site 3 of IL27 and IL6. Initiates
CC       signal transmission through three mechanisms (By similarity). Binding
CC       of cytokines, such as IL6 or IL11 to the alpha-chains of their specific
CC       cell surface receptor triggers homodimerization of IL6ST/gp130
CC       (PubMed:10661409, PubMed:1602143). In contrast, binding of other IL-6
CC       family cytokines can result in the formation of a IL6ST/gp130
CC       heterodimer with another signal-transducing receptor, such as LIFR or
CC       OSMR (By similarity). Moreover, binding of CNTF or CLCF1 or the
CC       heterodimeric complex CRLF1-CLCF1 or MT-RNR2/humanin to the non-
CC       signaling receptor CNTFR induces heterodimerization of the IL6ST/gp130
CC       with LIFR or IL27RA/WSX1 (in the case of MT-RNR2/humanin) (By
CC       similarity). Mechanistically, homodimerization or heterodimerization of
CC       IL6ST/gp130 activate JAK tyrosine kinases bound to their intracellular
CC       domains (PubMed:10661409, PubMed:1602143). These kinases subsequently
CC       phosphorylate the homodimer or heterodimer form of IL6ST/gp130
CC       (PubMed:10661409, PubMed:1602143). The tyrosine phosphorylated
CC       signaling receptors serve in turn as docking sites for recruitment and
CC       activation of signal transducer and activators of transcription (STATs)
CC       (PubMed:10661409, PubMed:1602143). The IL6 signaling pathway induces,
CC       in parallel, the expression of two cytokine receptor signaling
CC       inhibitors, SOCS1 and SOCS3, which inhibit JAK and terminate the
CC       activity of the IL6 signaling pathway as a negative feedback loop
CC       (PubMed:9202125). Also activates the yes-associated protein 1 (YAP) and
CC       NOTCH pathways to control inflammation-induced epithelial regeneration,
CC       independently of STAT3 (PubMed:25731159). Mediates signals which
CC       regulate immune response, hematopoiesis, pain control and bone
CC       metabolism (PubMed:10661409, PubMed:25057188, PubMed:26255596,
CC       PubMed:8552649). Has a role in embryonic development (PubMed:10661409).
CC       Essential for survival of motor and sensory neurons and for
CC       differentiation of astrocytes (PubMed:10377352). Required for
CC       expression of TRPA1 in nociceptive neurons (PubMed:25057188). Required
CC       for the maintenance of PTH1R expression in the osteoblast lineage and
CC       for the stimulation of PTH-induced osteoblast differentiation
CC       (PubMed:25228504). Required for normal trabecular bone mass and
CC       cortical bone composition (By similarity) (PubMed:24339143,
CC       PubMed:26255596, PubMed:9348227). {ECO:0000250|UniProtKB:P40189,
CC       ECO:0000269|PubMed:10377352, ECO:0000269|PubMed:10661409,
CC       ECO:0000269|PubMed:1602143, ECO:0000269|PubMed:24339143,
CC       ECO:0000269|PubMed:25057188, ECO:0000269|PubMed:25228504,
CC       ECO:0000269|PubMed:25731159, ECO:0000269|PubMed:26255596,
CC       ECO:0000269|PubMed:8552649, ECO:0000269|PubMed:9202125,
CC       ECO:0000269|PubMed:9348227}.
CC   -!- SUBUNIT: Homodimer in the IL6 complex receptor. Component of a hexamer
CC       of two molecules each of IL6, IL6R and IL6ST; associates with the
CC       complex IL6:IL6R but does not interact with IL6 (By similarity). Forms
CC       heterodimers composed of LIFR and IL6ST (type I OSM receptor) which are
CC       activated by LIF and OSM (By similarity). Also forms heterodimers
CC       composed of OSMR and IL6ST (type II receptor) which are activated by
CC       OSM but not by LIF (PubMed:9920829). Component of the humanin (HN)
CC       receptor complex composed of IL6ST/GP130, IL27RA/WSX1 and CNTFR; MT-
CC       RNR2, the neuroprotective peptide HN, binds to CNTFR and IL27RA.
CC       Interacts with HCK (By similarity). Interacts with INPP5D/SHIP1
CC       (PubMed:17105399). Interacts with SRC and YES. Interacts with ARMH4;
CC       this interaction prevents IL6ST protein homodimerization and bridges
CC       ARMH4 with IL6R and STAT3 and therefore inhibits phosphorylation of
CC       STAT3 at 'Tyr-705' (By similarity). Interacts with JAK1 or JAK2;
CC       constitutively associates with Jak kinases, which then become activated
CC       upon ligand-induced dimerization of the IL6ST. Component of the ciliary
CC       neurotrophic factor receptor (CNTFR) complex composed of CNTFR, LIFR
CC       and IL6ST. Component of the interleukin-27 signaling complex composed
CC       of IL27, EBI3, IL6ST/GP130 and IL27RA/WSX1; a heterodimeric cytokine,
CC       composed of IL27/p28 and a soluble receptor EBI3, that signals via
CC       IL27RA/WSX1 and IL6ST/GP130 (By similarity).
CC       {ECO:0000250|UniProtKB:P40189, ECO:0000269|PubMed:17105399,
CC       ECO:0000269|PubMed:9920829}.
CC   -!- INTERACTION:
CC       Q00560; O35718: Socs3; NbExp=6; IntAct=EBI-3862992, EBI-2659360;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P40189};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expression not restricted to IL6-responsive cells.
CC       Found in tissues such as brain, heart, thymus, spleen, kidney, lung and
CC       liver. Found in all the cell lines tested except BaF-B03. Expressed
CC       paraventricular nucleus of the hypothalamus (PubMed:28402851).
CC       {ECO:0000269|PubMed:1602143, ECO:0000269|PubMed:28402851}.
CC   -!- DEVELOPMENTAL STAGE: In embryonic stem cells it is found from day 6 of
CC       gestation. It reaches a peak on day 8 and gradually declines during the
CC       rest of embryogenesis. {ECO:0000269|PubMed:1602143}.
CC   -!- INDUCTION: In paraventricular nucleus of the hypothalamus, expression
CC       is enhanced by obesity. {ECO:0000269|PubMed:28402851}.
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: Phosphorylation of Ser-780 down-regulates cell surface expression.
CC       {ECO:0000250|UniProtKB:P40189}.
CC   -!- PTM: Heavily N-glycosylated. Glycosylation is required for protein
CC       stability and localization in plasma membrane but not for ligand
CC       binding. {ECO:0000250|UniProtKB:P40189}.
CC   -!- DISRUPTION PHENOTYPE: Progressively lethal between 12.5 dpc and birth
CC       (PubMed:8552649). Embryos show hypoplastic ventricular myocardium
CC       without septal and trabecular defect, reduced numbers of pluripotential
CC       and committed hematopoietic progenitors in liver and reduced
CC       differentiated lineages in thymus (PubMed:8552649). Impaired
CC       differentiation of astrocytes and decreased number of dorsal root
CC       ganglion and motor neurons at 18.5 dpc (PubMed:10377352). Decreased
CC       volume of mineralized trabecular bones, while number of osteoclasts is
CC       increased (PubMed:26255596, PubMed:9348227). Conditional knockout from
CC       the entire osteoblast lineage or specifically in osteocytes causes no
CC       significant skeletal or morphological defects but mice show 30% lower
CC       trabecular bone formation rate and larger cortical diameter compared to
CC       wild type (PubMed:24339143, PubMed:26255596). Conditional knockout in
CC       primary nociceptive afferents causes reduced sensitivity to mechanical
CC       stimulation due to reduced sensitivity of nociceptive neurons and
CC       reduces TRPA1 mRNA expression in dorsal root ganglion neurons
CC       (PubMed:25057188). {ECO:0000269|PubMed:10377352,
CC       ECO:0000269|PubMed:24339143, ECO:0000269|PubMed:25057188,
CC       ECO:0000269|PubMed:26255596, ECO:0000269|PubMed:8552649,
CC       ECO:0000269|PubMed:9348227}.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X62646; CAA44515.1; -; mRNA.
DR   EMBL; M83336; AAA37723.1; -; mRNA.
DR   EMBL; AC159196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466568; EDL18412.1; -; Genomic_DNA.
DR   CCDS; CCDS26773.1; -.
DR   PIR; I49699; I49699.
DR   RefSeq; NP_034690.3; NM_010560.3.
DR   RefSeq; XP_036013751.1; XM_036157858.1.
DR   PDB; 2BBU; NMR; -; B=750-764.
DR   PDB; 2HMH; X-ray; 2.00 A; B=753-763.
DR   PDB; 4GL9; X-ray; 3.90 A; I/J/K/L=750-764.
DR   PDB; 6C5X; X-ray; 3.10 A; G=754-763.
DR   PDB; 7Z0L; EM; 4.00 A; A=28-319.
DR   PDB; 8QY4; EM; 3.06 A; C/F=1-917.
DR   PDB; 8QY5; EM; 3.10 A; A/D=1-917.
DR   PDB; 8QY6; EM; 3.16 A; A/D=1-917.
DR   PDB; 8V2B; EM; 3.67 A; B=23-617.
DR   PDB; 8V2C; EM; 3.46 A; B=23-617.
DR   AlphaFoldDB; Q00560; -.
DR   EMDB; EMD-14427; -.
DR   EMDB; EMD-18741; -.
DR   EMDB; EMD-18742; -.
DR   EMDB; EMD-18743; -.
DR   EMDB; EMD-42904; -.
DR   EMDB; EMD-42905; -.
DR   SMR; Q00560; -.
DR   BioGRID; 200643; 14.
DR   CORUM; Q00560; -.
DR   DIP; DIP-5782N; -.
DR   FunCoup; Q00560; 652.
DR   IntAct; Q00560; 7.
DR   STRING; 10090.ENSMUSP00000138836; -.
DR   GlyConnect; Q00560; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q00560; 11 sites, 10 glycans.
DR   GlyGen; Q00560; 23 sites, 10 N-linked glycans (10 sites), 1 O-linked glycan (12 sites).
DR   iPTMnet; Q00560; -.
DR   PhosphoSitePlus; Q00560; -.
DR   SwissPalm; Q00560; -.
DR   jPOST; Q00560; -.
DR   PaxDb; 10090-ENSMUSP00000138836; -.
DR   ProteomicsDB; 269398; -.
DR   Pumba; Q00560; -.
DR   Antibodypedia; 2448; 902 antibodies from 43 providers.
DR   DNASU; 16195; -.
DR   Ensembl; ENSMPUT00000007596; ENSMPUP00000007476; ENSMPUG00000007532.
DR   Ensembl; ENSMUST00000070731.11; ENSMUSP00000064205.5; ENSMUSG00000021756.13.
DR   Ensembl; ENSMUST00000183663.8; ENSMUSP00000138836.2; ENSMUSG00000021756.13.
DR   Ensembl; ENSMUST00000184311.8; ENSMUSP00000139227.2; ENSMUSG00000021756.13.
DR   GeneID; 16195; -.
DR   KEGG; mmu:16195; -.
DR   UCSC; uc007rwg.2; mouse.
DR   AGR; MGI:96560; -.
DR   CTD; 3572; -.
DR   MGI; MGI:96560; Il6st.
DR   VEuPathDB; HostDB:ENSMUSG00000021756; -.
DR   eggNOG; ENOG502QXEG; Eukaryota.
DR   GeneTree; ENSGT00940000159608; -.
DR   InParanoid; Q00560; -.
DR   OMA; AAHPITN; -.
DR   OrthoDB; 9934532at2759; -.
DR   PhylomeDB; Q00560; -.
DR   Reactome; R-MMU-1059683; Interleukin-6 signaling.
DR   Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
DR   Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
DR   Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR   Reactome; R-MMU-8984722; Interleukin-35 Signalling.
DR   Reactome; R-MMU-9020956; Interleukin-27 signaling.
DR   Reactome; R-MMU-9958825; Activation of STAT3 by cadherin engagement.
DR   BioGRID-ORCS; 16195; 2 hits in 80 CRISPR screens.
DR   EvolutionaryTrace; Q00560; -.
DR   PRO; PR:Q00560; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q00560; protein.
DR   Bgee; ENSMUSG00000021756; Expressed in decidua and 261 other cell types or tissues.
DR   ExpressionAtlas; Q00560; baseline and differential.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; ISO:GO_Central.
DR   GO; GO:7770013; C:humanin receptor complex; ISO:GO_Central.
DR   GO; GO:0005896; C:interleukin-6 receptor complex; ISO:GO_Central.
DR   GO; GO:0045121; C:membrane raft; ISO:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043235; C:signaling receptor complex; ISO:GO_Central.
DR   GO; GO:0005900; C:type I oncostatin-M receptor complex; IDA:UniProtKB.
DR   GO; GO:0140370; C:type II oncostatin-M receptor complex; ISO:GO_Central.
DR   GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; ISO:GO_Central.
DR   GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; ISO:GO_Central.
DR   GO; GO:0015026; F:coreceptor activity; ISO:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; ISO:GO_Central.
DR   GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR   GO; GO:0004896; F:cytokine receptor activity; ISS:UniProtKB.
DR   GO; GO:0019838; F:growth factor binding; ISO:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0045509; F:interleukin-27 receptor activity; ISO:GO_Central.
DR   GO; GO:0019981; F:interleukin-6 binding; IEA:Ensembl.
DR   GO; GO:0004915; F:interleukin-6 receptor activity; ISO:GO_Central.
DR   GO; GO:0005138; F:interleukin-6 receptor binding; IEA:Ensembl.
DR   GO; GO:0004923; F:leukemia inhibitory factor receptor activity; IEA:Ensembl.
DR   GO; GO:0004924; F:oncostatin-M receptor activity; IDA:UniProtKB.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:GO_Central.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:GO_Central.
DR   GO; GO:0035425; P:autocrine signaling; ISO:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; ISO:GO_Central.
DR   GO; GO:0008283; P:cell population proliferation; ISO:GO_Central.
DR   GO; GO:0007259; P:cell surface receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR   GO; GO:0097696; P:cell surface receptor signaling pathway via STAT; ISO:GO_Central.
DR   GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; ISO:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
DR   GO; GO:0038154; P:interleukin-11-mediated signaling pathway; ISO:GO_Central.
DR   GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:GO_Central.
DR   GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0060576; P:intestinal epithelial cell development; IDA:UniProtKB.
DR   GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; ISO:GO_Central.
DR   GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:GO_Central.
DR   GO; GO:0070104; P:negative regulation of interleukin-6-mediated signaling pathway; ISO:GO_Central.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:GO_Central.
DR   GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0002821; P:positive regulation of adaptive immune response; ISO:GO_Central.
DR   GO; GO:0048711; P:positive regulation of astrocyte differentiation; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:GO_Central.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:GO_Central.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:GO_Central.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; IDA:MGI.
DR   GO; GO:0034097; P:response to cytokine; ISO:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IDA:MGI.
DR   GO; GO:0006642; P:triglyceride mobilization; ISO:GO_Central.
DR   CDD; cd00063; FN3; 3.
DR   FunFam; 2.60.40.10:FF:000281; Cytokine receptor like factor 1; 1.
DR   FunFam; 2.60.40.10:FF:000414; Interleukin-6 receptor subunit beta; 1.
DR   FunFam; 2.60.40.10:FF:000524; Interleukin-6 receptor subunit beta; 1.
DR   FunFam; 2.60.40.10:FF:000542; Interleukin-6 receptor subunit beta; 1.
DR   FunFam; 2.60.40.10:FF:000855; Interleukin-6 receptor subunit beta; 1.
DR   FunFam; 2.60.40.10:FF:000563; interleukin-6 receptor subunit beta; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   IDEAL; IID50222; -.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR010457; IgC2-like_lig-bd.
DR   InterPro; IPR050379; Type-I_Cytokine_Rcpt.
DR   PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR23036:SF83; INTERLEUKIN-6 RECEPTOR SUBUNIT BETA; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF06328; Lep_receptor_Ig; 1.
DR   Pfam; PF25552; LIFR_D4; 1.
DR   SMART; SM00060; FN3; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 4.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..917
FT                   /note="Interleukin-6 receptor subunit beta"
FT                   /id="PRO_0000010900"
FT   TOPO_DOM        23..617
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        618..639
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        640..917
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..120
FT                   /note="Ig-like C2-type"
FT   DOMAIN          128..221
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          222..322
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          327..417
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          422..515
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          517..611
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          658..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           308..312
FT                   /note="WSXWS motif"
FT   MOTIF           649..657
FT                   /note="Box 1 motif"
FT   COMPBIAS        729..753
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         659
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   MOD_RES         780
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   MOD_RES         787
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         827
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   MOD_RES         837
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..54
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   DISULFID        48..103
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   DISULFID        134..144
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   DISULFID        172..180
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   DISULFID        456..464
FT                   /evidence="ECO:0000250|UniProtKB:P40189"
FT   CONFLICT        756
FT                   /note="Q -> E (in Ref. 1; CAA44515/AAA37723)"
FT                   /evidence="ECO:0000305"
FT   STRAND          28..35
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          44..50
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           52..58
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:8QY5"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          97..107
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          111..123
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           125..129
FT                   /evidence="ECO:0007829|PDB:8QY5"
FT   STRAND          130..137
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          143..147
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          159..164
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          165..168
FT                   /evidence="ECO:0007829|PDB:8QY5"
FT   STRAND          175..181
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          188..190
FT                   /evidence="ECO:0007829|PDB:8V2C"
FT   STRAND          192..200
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           220..223
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          224..230
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          238..243
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           246..249
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          253..263
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           272..275
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          280..284
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          292..301
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           308..314
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          315..318
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          329..334
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          341..350
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   HELIX           354..357
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          361..369
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          375..392
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          394..404
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          410..414
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          426..433
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          436..442
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          449..457
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          460..462
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          466..472
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          476..479
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          489..498
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          501..513
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          522..528
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          533..538
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   TURN            542..544
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          551..561
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          564..569
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          574..577
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          586..594
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          597..600
FT                   /evidence="ECO:0007829|PDB:8QY4"
FT   STRAND          604..606
FT                   /evidence="ECO:0007829|PDB:8QY4"
SQ   SEQUENCE   917 AA;  102451 MW;  EDA69AB865E5A6E8 CRC64;
     MSAPRIWLAQ ALLFFLTTES IGQLLEPCGY IYPEFPVVQR GSNFTAICVL KEACLQHYYV
     NASYIVWKTN HAAVPREQVT VINRTTSSVT FTDVVLPSVQ LTCNILSFGQ IEQNVYGVTM
     LSGFPPDKPT NLTCIVNEGK NMLCQWDPGR ETYLETNYTL KSEWATEKFP DCQSKHGTSC
     MVSYMPTYYV NIEVWVEAEN ALGKVSSESI NFDPVDKVKP TPPYNLSVTN SEELSSILKL
     SWVSSGLGGL LDLKSDIQYR TKDASTWIQV PLEDTMSPRT SFTVQDLKPF TEYVFRIRSI
     KDSGKGYWSD WSEEASGTTY EDRPSRPPSF WYKTNPSHGQ EYRSVRLIWK ALPLSEANGK
     ILDYEVILTQ SKSVSQTYTV TGTELTVNLT NDRYVASLAA RNKVGKSAAA VLTIPSPHVT
     AAYSVVNLKA FPKDNLLWVE WTPPPKPVSK YILEWCVLSE NAPCVEDWQQ EDATVNRTHL
     RGRLLESKCY QITVTPVFAT GPGGSESLKA YLKQAAPARG PTVRTKKVGK NEAVLAWDQI
     PVDDQNGFIR NYSISYRTSV GKEMVVHVDS SHTEYTLSSL SSDTLYMVRM AAYTDEGGKD
     GPEFTFTTPK FAQGEIEAIV VPVCLAFLLT TLLGVLFCFN KRDLIKKHIW PNVPDPSKSH
     IAQWSPHTPP RHNFNSKDQM YSDGNFTDVS VVEIEANNKK PCPDDLKSVD LFKKEKVSTE
     GHSSGIGGSS CMSSSRPSIS SNEENESAQS TASTVQYSTV VHSGYRHQVP SVQVFSRSES
     TQPLLDSEER PEDLQLVDSV DGGDEILPRQ PYFKQNCSQP EACPEISHFE RSNQVLSGNE
     EDFVRLKQQQ VSDHISQPYG SEQRRLFQEG STADALGTGA DGQMERFESV GMETTIDEEI
     PKSYLPQTVR QGGYMPQ
//