IL6RB_RAT
ID IL6RB_RAT Reviewed; 918 AA.
AC P40190;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
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;
DE AltName: Full=Oncostatin-M receptor subunit alpha;
DE AltName: CD_antigen=CD130;
DE Flags: Precursor;
GN Name=Il6st {ECO:0000312|RGD:2903};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=1427893; DOI=10.1016/s0888-7543(05)80166-1;
RA Wang Y., Nesbitt J.E., Fuentes N.L., Fuller G.M.;
RT "Molecular cloning and characterization of the rat liver IL-6 signal
RT transducing molecule, gp130.";
RL Genomics 14:666-672(1992).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Signal-transducing molecule. The receptor systems for IL6,
CC LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating
CC signal transmission. Binding of IL6 to IL6R induces IL6ST
CC homodimerization and formation of a high-affinity receptor complex,
CC which activates the intracellular JAK-MAPK and JAK-STAT3 signaling
CC pathways. That causes phosphorylation of IL6ST tyrosine residues which
CC in turn activates STAT3 (By similarity). In parallel, the IL6 signaling
CC pathway induces 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. Also
CC activates the yes-associated protein 1 (YAP) and NOTCH pathways to
CC control inflammation-induced epithelial regeneration, independently of
CC STAT3 (By similarity). Mediates signals which regulate immune response,
CC hematopoiesis, pain control and bone metabolism (By similarity). Has a
CC role in embryonic development (By similarity). Essential for survival
CC of motor and sensory neurons and for differentiation of astrocytes (By
CC similarity). Required for expression of TRPA1 in nociceptive neurons
CC (By similarity). Required for the maintenance of PTH1R expression in
CC the osteoblast lineage and for the stimulation of PTH-induced
CC osteoblast differentiation (By similarity). Required for normal
CC trabecular bone mass and cortical bone composition (By similarity).
CC {ECO:0000250|UniProtKB:P40189, ECO:0000250|UniProtKB:Q00560}.
CC -!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R and
CC IL6ST; associates with the complex IL6:IL6R but does not interact with
CC IL6 (By similarity). Forms heterodimers composed of LIFR and IL6ST
CC (type I OSM receptor) which are activated by LIF and OSM. Also forms
CC heterodimers composed of OSMR and IL6ST (type II receptor) which are
CC activated by OSM but not by LIF. Interacts with HCK (By similarity).
CC Interacts with INPP5D/SHIP1 (By similarity). Interacts with SRC and YES
CC (By similarity). {ECO:0000250|UniProtKB:P40189,
CC ECO:0000250|UniProtKB:Q00560}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P40189};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Found in hepatocytes, astrocytes, fibroblasts and
CC endothelial cells. {ECO:0000269|PubMed:1427893}.
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-781 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 -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; M92340; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A44257; A44257.
DR AlphaFoldDB; P40190; -.
DR SMR; P40190; -.
DR STRING; 10116.ENSRNOP00000018877; -.
DR GlyGen; P40190; 11 sites.
DR iPTMnet; P40190; -.
DR PaxDb; P40190; -.
DR PRIDE; P40190; -.
DR RGD; 2903; Il6st.
DR eggNOG; ENOG502QXEG; Eukaryota.
DR InParanoid; P40190; -.
DR Reactome; R-RNO-1059683; Interleukin-6 signaling.
DR Reactome; R-RNO-110056; MAPK3 (ERK1) activation.
DR Reactome; R-RNO-112411; MAPK1 (ERK2) activation.
DR Reactome; R-RNO-6788467; IL-6-type cytokine receptor ligand interactions.
DR Reactome; R-RNO-9020956; Interleukin-27 signaling.
DR PRO; PR:P40190; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005896; C:interleukin-6 receptor complex; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
DR GO; GO:0005900; C:oncostatin-M receptor complex; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; ISO:RGD.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; ISO:RGD.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:RGD.
DR GO; GO:0038154; P:interleukin-11-mediated signaling pathway; IEA:GOC.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:RGD.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:RGD.
DR GO; GO:0060576; P:intestinal epithelial cell development; ISO:RGD.
DR GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; ISO:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:RGD.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:0046883; P:regulation of hormone secretion; TAS:RGD.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0006642; P:triglyceride mobilization; IMP:RGD.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 6.
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 Pfam; PF00041; fn3; 2.
DR Pfam; PF06328; Lep_receptor_Ig; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 5.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..918
FT /note="Interleukin-6 receptor subunit beta"
FT /id="PRO_0000010901"
FT TOPO_DOM 23..618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..120
FT /note="Ig-like C2-type"
FT DOMAIN 125..215
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 223..323
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 328..418
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 422..516
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 518..612
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 659..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 309..313
FT /note="WSXWS motif"
FT MOTIF 650..658
FT /note="Box 1 motif"
FT COMPBIAS 723..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00560"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
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..181
FT /evidence="ECO:0000250|UniProtKB:P40189"
FT DISULFID 457..465
FT /evidence="ECO:0000250|UniProtKB:P40189"
SQ SEQUENCE 918 AA; 102450 MW; 9E18B6FECFF087F7 CRC64;
MSALRIWLMQ ALLIFLTTES IGQLVEPCGY IYPEFPVVQR GSNFTATCVL KEKCLQVYSV
NATYIVWKTN HVAVPKEQVT VINRTASSVT FTDVVFQNVQ LTCNILSFGQ IEQNVYGITI
LSGYPPDIPT NLSCIVNEGK NMLCQLDPGR ETYLETNYTL KSEWATEKFP DCRTKHGTSS
CMMGYTPIYF VNIEVWVEAE NALGNVSSEP INFDPVDKVK PSPPHNLSVT NSEELSSILK
LAWVNSGLDS ILRLKSDIQY RTKDASTWIQ VPLEDTVSPR TSFTVQDLKP FTEYVFRIRS
IKENGKGYWS DWSEEASGTT YEDRPSKAPS FWYKVNANHP QEYRSARLIW KTLPLSEANG
KILDYEVVLT QSKSVSQTYT VNGTELIVNL TNNRYVASLA ARNVVGKSPA TVLTIPGSHF
KASHPVVDLK AFPKDNLLWV EWTPPSKPVN KYILEWCVLS ENSPCIPDWQ QEDGTVNRTH
LRGSLLESKC YLITVTPVFP GGPGSPESMK AYLKQAAPSK GPTVRTKKVG KNEAVLEWDH
LPVDVQNGFI RNYSISYRTS VGKEMVVRVD SSHTEYTLSS LSSDTLYMVH MAAYTEEGGK
DGPEFTFTTL KFAQGEIEAI VVPVCLAFLL TTLLGVLFCF NKRDLIKKHI WPNVPDPSKS
HIAQWSPHTP PRHNFNSKDQ MYSDANFTDV SVVEIEANNK KPCPDDLKSL DLFKKEKIST
EGHSSGIGGS SCMSSSRPSI SSSEENESAQ STASTVQYST VVHSGYRHQV PSVQVFSRSE
STQPLLDSEE RPEDLQLVDS VDSGDEILPR QQYFKQSCSQ PGASPDVSHF GRSSQVPSGS
EEDFVRLKQQ QVSDHISEPY GSEQRRLFQE GSVADALGTG TDGQIERFES VGMETAMDED
ISKSYLPQTV RQGGYMPQ
