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Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)

 IL6RB_RAT               Reviewed;         918 AA.
P40190;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
05-DEC-2018, entry version 140.
RecName: Full=Interleukin-6 receptor subunit beta;
Short=IL-6 receptor subunit beta;
Short=IL-6R subunit beta;
Short=IL-6R-beta;
Short=IL-6RB;
AltName: Full=Interleukin-6 signal transducer;
AltName: Full=Membrane glycoprotein 130;
Short=gp130;
AltName: Full=Oncostatin-M receptor subunit alpha;
AltName: CD_antigen=CD130;
Flags: Precursor;
Name=Il6st;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=1427893; DOI=10.1016/S0888-7543(05)80166-1;
Wang Y., Nesbitt J.E., Fuentes N.L., Fuller G.M.;
"Molecular cloning and characterization of the rat liver IL-6 signal
transducing molecule, gp130.";
Genomics 14:666-672(1992).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Signal-transducing molecule. The receptor systems for
IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for
initiating signal transmission. Binding of IL6 to IL6R induces
IL6ST homodimerization and formation of a high-affinity receptor
complex, which activates Janus kinases. That causes
phosphorylation of IL6ST tyrosine residues which in turn activates
STAT3. Mediates signals which regulate immune response,
hematopoiesis, pain control and bone metabolism. Has a role in
embryonic development. Does not bind IL6. Essential for survival
of motor and sensory neurons and for differentiation of
astrocytes. Required for expression of TRPA1 in nociceptive
neurons. Required for the maintenance of PTH1R expression in the
osteoblast lineage and for the stimulation of PTH-induced
osteoblast differentiation. Required for normal trabecular bone
mass and cortical bone composition. {ECO:0000250|UniProtKB:P40189,
ECO:0000250|UniProtKB:Q00560}.
-!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R
and IL6ST. Forms heterodimers composed of LIFR and IL6ST (type I
OSM receptor) which are activated by LIF and OSM. Also forms
heterodimers composed of OSMR and IL6ST (type II receptor) which
are activated by OSM but not by LIF. Interacts with HCK. Interacts
with INPP5D/SHIP1. {ECO:0000250|UniProtKB:P40189,
ECO:0000250|UniProtKB:Q00560}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P40189}; Single-pass type I membrane
protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Found in hepatocytes, astrocytes, fibroblasts
and endothelial cells. {ECO:0000269|PubMed:1427893}.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: Phosphorylation of Ser-781 down-regulates cell surface
expression. {ECO:0000250|UniProtKB:P40189}.
-!- PTM: Heavily N-glycosylated. Glycosylation is required for protein
stability and localization in plasma membrane but not for ligand
binding. {ECO:0000250|UniProtKB:P40189}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M92340; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A44257; A44257.
UniGene; Rn.12138; -.
ProteinModelPortal; P40190; -.
STRING; 10116.ENSRNOP00000018877; -.
iPTMnet; P40190; -.
PaxDb; P40190; -.
PRIDE; P40190; -.
RGD; 2903; Il6st.
eggNOG; ENOG410IF1N; Eukaryota.
eggNOG; ENOG410YNQ4; LUCA.
HOGENOM; HOG000015771; -.
HOVERGEN; HBG052119; -.
InParanoid; P40190; -.
PRO; PR:P40190; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; IBA:GO_Central.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0005896; C:interleukin-6 receptor complex; IBA:GO_Central.
GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
GO; GO:0005900; C:oncostatin-M receptor complex; IBA:GO_Central.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; IBA:GO_Central.
GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:RGD.
GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; IEA:GOC.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IEA:GOC.
GO; GO:0008284; P:positive regulation of cell proliferation; IBA:GO_Central.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IBA:GO_Central.
GO; GO:0046883; P:regulation of hormone secretion; TAS:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0006642; P:triglyceride mobilization; IMP:RGD.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010457; IgC2-like_lig-bd.
Pfam; PF00041; fn3; 2.
Pfam; PF06328; Lep_receptor_Ig; 1.
SMART; SM00060; FN3; 4.
SUPFAM; SSF49265; SSF49265; 5.
PROSITE; PS50853; FN3; 4.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 918 Interleukin-6 receptor subunit beta.
/FTId=PRO_0000010901.
TOPO_DOM 23 618 Extracellular. {ECO:0000255}.
TRANSMEM 619 640 Helical. {ECO:0000255}.
TOPO_DOM 641 918 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 120 Ig-like C2-type.
DOMAIN 125 215 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 223 323 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 328 418 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 422 516 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 518 612 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 309 313 WSXWS motif.
MOTIF 650 658 Box 1 motif.
COMPBIAS 724 754 Ser-rich.
MOD_RES 660 660 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
MOD_RES 666 666 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
MOD_RES 788 788 Phosphoserine.
{ECO:0000250|UniProtKB:Q00560}.
MOD_RES 828 828 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 552 552 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 54 {ECO:0000250|UniProtKB:P40189}.
DISULFID 48 103 {ECO:0000250|UniProtKB:P40189}.
DISULFID 134 144 {ECO:0000250|UniProtKB:P40189}.
DISULFID 172 181 {ECO:0000250|UniProtKB:P40189}.
DISULFID 457 465 {ECO:0000250|UniProtKB:P40189}.
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


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