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Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (Membrane glycoprotein 80) (gp80) (CD antigen CD126)

 IL6RA_HUMAN             Reviewed;         468 AA.
P08887; A8KAE8; B2R6V4; Q16202; Q53EQ7; Q5FWG2; Q5VZ23;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
25-OCT-2017, entry version 205.
RecName: Full=Interleukin-6 receptor subunit alpha;
Short=IL-6 receptor subunit alpha;
Short=IL-6R subunit alpha;
Short=IL-6R-alpha;
Short=IL-6RA;
AltName: Full=IL-6R 1;
AltName: Full=Membrane glycoprotein 80;
Short=gp80;
AltName: CD_antigen=CD126;
Flags: Precursor;
Name=IL6R;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3136546; DOI=10.1126/science.3136546;
Yamasaki K., Taga T., Hirata Y., Yawata H., Kawanishi Y., Seed B.,
Taniguchi T., Hirano T., Kishimoto T.;
"Cloning and expression of the human interleukin-6 (BSF-2/IFN beta 2)
receptor.";
Science 241:825-828(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yamasaki K., Taga T., Hirata Y., Yawata H., Kawanishi Y., Seed B.,
Taniguchi T., Hirano T., Kishimoto T.;
"Molecular structure of interleukin 6 receptor.";
Proc. Jpn. Acad., B, Phys. Biol. Sci. 64:209-211(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1872801; DOI=10.1042/bj2770659;
Schooltink H., Stoyan T., Lenz D., Schmitz H., Hirano T.,
Kishimoto T., Heinrich P.C., Rose-John S.;
"Structural and functional studies on the human hepatic interleukin-6
receptor. Molecular cloning and overexpression in HepG2 cells.";
Biochem. J. 277:659-664(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ALA-358.
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 313-365 (ISOFORM 2).
PubMed=8056053; DOI=10.1002/eji.1830240837;
Horiuchi S., Koyanagi Y., Zhou Y., Miyamoto H., Tanaka Y., Waki M.,
Matsumoto A., Yamamoto M., Yamamoto N.;
"Soluble interleukin-6 receptors released from T cell or
granulocyte/macrophage cell lines and human peripheral blood
mononuclear cells are generated through an alternative splicing
mechanism.";
Eur. J. Immunol. 24:1945-1948(1994).
[10]
PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-55; ASN-93 AND ASN-221,
LACK OF GLYCOSYLATION AT ASN-245, AND DISULFIDE BONDS.
PubMed=10066782; DOI=10.1074/jbc.274.11.7207;
Cole A.R., Hall N.E., Treutlein H.R., Eddes J.S., Reid G.E.,
Moritz R.L., Simpson R.J.;
"Disulfide bond structure and N-glycosylation sites of the
extracellular domain of the human interleukin-6 receptor.";
J. Biol. Chem. 274:7207-7215(1999).
[11]
PROTEIN SEQUENCE OF 20-49, AND SUBCELLULAR LOCATION.
PubMed=2529343; DOI=10.1084/jem.170.4.1409;
Novick D., Engelmann H., Wallach D., Rubinstein M.;
"Soluble cytokine receptors are present in normal human urine.";
J. Exp. Med. 170:1409-1414(1989).
[12]
MUTAGENESIS.
PubMed=8467812;
Yawata H., Yasukawa K., Natsuka S., Murakami M., Yamasaki K., Hibi M.,
Taga T., Kishimoto T.;
"Structure-function analysis of human IL-6 receptor: dissociation of
amino acid residues required for IL-6-binding and for IL-6 signal
transduction through gp130.";
EMBO J. 12:1705-1712(1993).
[13]
FUNCTION.
PubMed=11017875;
Martens A.S., Bode J.G., Heinrich P.C., Graeve L.;
"The cytoplasmic domain of the interleukin-6 receptor gp80 mediates
its basolateral sorting in polarized Madin-Darby canine kidney
cells.";
J. Cell Sci. 113:3593-3602(2000).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16270750; DOI=10.1016/j.ejcb.2005.06.001;
Buk D.M., Renner O., Graeve L.;
"Increased association with detergent-resistant membranes/lipid rafts
of apically targeted mutants of the interleukin-6 receptor gp80.";
Eur. J. Cell Biol. 84:819-831(2005).
[15]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-344.
PubMed=12461182; DOI=10.1073/pnas.232432399;
Varghese J.N., Moritz R.L., Lou M.-Z., Van Donkelaar A., Ji H.,
Ivancic N., Branson K.M., Hall N.E., Simpson R.J.;
"Structure of the extracellular domains of the human interleukin-6
receptor alpha-chain.";
Proc. Natl. Acad. Sci. U.S.A. 99:15959-15964(2002).
[16]
X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 115-315.
PubMed=12829785; DOI=10.1126/science.1083901;
Boulanger M.J., Chow D.-C., Brevnova E.E., Garcia K.C.;
"Hexameric structure and assembly of the interleukin-6/IL-6 alpha-
receptor/gp130 complex.";
Science 300:2101-2104(2003).
[17]
POLYMORPHISM, VARIANT ALA-358, AND ASSOCIATION OF VARIANT ALA-358 WITH
IL6 AND SOLUBLE IL6R SERUM LEVELS.
PubMed=17357077; DOI=10.1086/513206;
Health, Aging and Body Composition (Health ABC) Study;
Reich D., Patterson N., Ramesh V., De Jager P.L., McDonald G.J.,
Tandon A., Choy E., Hu D., Tamraz B., Pawlikowska L., Wassel-Fyr C.,
Huntsman S., Waliszewska A., Rossin E., Li R., Garcia M., Reiner A.,
Ferrell R., Cummings S., Kwok P.Y., Harris T., Zmuda J.M., Ziv E.;
"Admixture mapping of an allele affecting interleukin 6 soluble
receptor and interleukin 6 levels.";
Am. J. Hum. Genet. 80:716-726(2007).
-!- FUNCTION: Part of the receptor for interleukin 6. Binds to IL6
with low affinity, but does not transduce a signal. Signal
activation necessitate an association with IL6ST. Activation may
lead to the regulation of the immune response, acute-phase
reactions and hematopoiesis.
-!- FUNCTION: Low concentration of a soluble form of IL6 receptor acts
as an agonist of IL6 activity.
-!- SUBUNIT: Hexamer of two molecules each of IL6, IL6R and IL6ST.
-!- INTERACTION:
P05231:IL6; NbExp=6; IntAct=EBI-299383, EBI-720533;
Q2HRC7:K2 (xeno); NbExp=3; IntAct=EBI-299383, EBI-9007403;
-!- SUBCELLULAR LOCATION: Isoform 1: Basolateral cell membrane;
Single-pass type I membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=P08887-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P08887-2; Sequence=VSP_001682, VSP_001683;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed in peripheral blood
mononuclear cells and weakly found in urine and serum.
-!- DOMAIN: The two fibronectin type-III-like domains, contained in
the N-terminal part, form together a cytokine-binding domain.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- PTM: A short soluble form may also be released from the membrane
by proteolysis.
-!- POLYMORPHISM: Genetic variations in IL6R determine soluble IL6R
serum levels [MIM:614689].
-!- POLYMORPHISM: Genetic variations in IL6R define the IL6 serum
level quantitative trait locus [MIM:614752].
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
subfamily. {ECO:0000305}.
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EMBL; X12830; CAA31312.1; -; mRNA.
EMBL; X58298; CAA41231.1; -; mRNA.
EMBL; AK293013; BAF85702.1; -; mRNA.
EMBL; AK312730; BAG35601.1; -; mRNA.
EMBL; AK223582; BAD97302.1; -; mRNA.
EMBL; AL162591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53200.1; -; Genomic_DNA.
EMBL; BC089410; AAH89410.1; -; mRNA.
EMBL; S72848; AAC60635.1; -; mRNA.
CCDS; CCDS1067.1; -. [P08887-1]
CCDS; CCDS1068.1; -. [P08887-2]
PIR; A41242; A41242.
RefSeq; NP_000556.1; NM_000565.3. [P08887-1]
RefSeq; NP_001193795.1; NM_001206866.1.
RefSeq; NP_852004.1; NM_181359.2. [P08887-2]
UniGene; Hs.135087; -.
PDB; 1N26; X-ray; 2.40 A; A=20-344.
PDB; 1N2Q; Model; -; C/D=20-344.
PDB; 1P9M; X-ray; 3.65 A; C=115-315.
PDB; 2ARW; NMR; -; A=212-336.
PDB; 5FUC; X-ray; 2.70 A; C/D=111-322.
PDBsum; 1N26; -.
PDBsum; 1N2Q; -.
PDBsum; 1P9M; -.
PDBsum; 2ARW; -.
PDBsum; 5FUC; -.
ProteinModelPortal; P08887; -.
SMR; P08887; -.
BioGrid; 109784; 18.
DIP; DIP-162N; -.
ELM; P08887; -.
IntAct; P08887; 6.
MINT; MINT-190110; -.
STRING; 9606.ENSP00000357470; -.
ChEMBL; CHEMBL2364155; -.
DrugBank; DB06273; Tocilizumab.
GuidetoPHARMACOLOGY; 1708; -.
iPTMnet; P08887; -.
PhosphoSitePlus; P08887; -.
BioMuta; IL6R; -.
DMDM; 124343; -.
MaxQB; P08887; -.
PaxDb; P08887; -.
PeptideAtlas; P08887; -.
PRIDE; P08887; -.
DNASU; 3570; -.
Ensembl; ENST00000344086; ENSP00000340589; ENSG00000160712. [P08887-2]
Ensembl; ENST00000368485; ENSP00000357470; ENSG00000160712. [P08887-1]
GeneID; 3570; -.
KEGG; hsa:3570; -.
UCSC; uc001fez.2; human. [P08887-1]
CTD; 3570; -.
DisGeNET; 3570; -.
EuPathDB; HostDB:ENSG00000160712.12; -.
GeneCards; IL6R; -.
HGNC; HGNC:6019; IL6R.
MIM; 147880; gene.
MIM; 614689; phenotype.
MIM; 614752; phenotype.
neXtProt; NX_P08887; -.
OpenTargets; ENSG00000160712; -.
PharmGKB; PA29835; -.
eggNOG; ENOG410II5K; Eukaryota.
eggNOG; ENOG4111XGC; LUCA.
GeneTree; ENSGT00530000063103; -.
HOVERGEN; HBG052118; -.
InParanoid; P08887; -.
KO; K05055; -.
OrthoDB; EOG091G07XD; -.
PhylomeDB; P08887; -.
TreeFam; TF331210; -.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
Reactome; R-HSA-6783589; Interleukin-6 family signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; P08887; -.
SIGNOR; P08887; -.
ChiTaRS; IL6R; human.
EvolutionaryTrace; P08887; -.
GeneWiki; Interleukin-6_receptor; -.
GenomeRNAi; 3570; -.
PMAP-CutDB; P08887; -.
PRO; PR:P08887; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160712; -.
CleanEx; HS_IL6R; -.
ExpressionAtlas; P08887; baseline and differential.
Genevisible; P08887; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005896; C:interleukin-6 receptor complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0070119; F:ciliary neurotrophic factor binding; IPI:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0019981; F:interleukin-6 binding; IPI:BHF-UCL.
GO; GO:0004915; F:interleukin-6 receptor activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0006953; P:acute-phase response; TAS:BHF-UCL.
GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; NAS:BHF-UCL.
GO; GO:0031018; P:endocrine pancreas development; IMP:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; TAS:BHF-UCL.
GO; GO:0002384; P:hepatic immune response; TAS:BHF-UCL.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0002548; P:monocyte chemotaxis; IC:BHF-UCL.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0032717; P:negative regulation of interleukin-8 production; NAS:BHF-UCL.
GO; GO:0002446; P:neutrophil mediated immunity; TAS:BHF-UCL.
GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; TAS:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; TAS:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:BHF-UCL.
GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF00047; ig; 1.
Pfam; PF09240; IL6Ra-bind; 1.
SMART; SM00060; FN3; 1.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 2.
PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000269|PubMed:2529343}.
CHAIN 20 468 Interleukin-6 receptor subunit alpha.
/FTId=PRO_0000010895.
TOPO_DOM 20 365 Extracellular. {ECO:0000255}.
TRANSMEM 366 386 Helical. {ECO:0000255}.
TOPO_DOM 387 468 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 112 Ig-like C2-type.
DOMAIN 113 217 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 218 316 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 303 307 WSXWS motif.
SITE 245 245 Not glycosylated.
{ECO:0000269|PubMed:10066782}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10066782}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10066782}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10066782}.
DISULFID 25 193 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10066782}.
DISULFID 47 96 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10066782}.
DISULFID 121 132 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10066782}.
DISULFID 165 176 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10066782}.
VAR_SEQ 356 365 VQDSSSVPLP -> GSRRRGSCGL (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8056053}.
/FTId=VSP_001682.
VAR_SEQ 366 468 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8056053}.
/FTId=VSP_001683.
VARIANT 358 358 D -> A (significantly associated with
circulating levels of IL6 and soluble
IL6R; dbSNP:rs2228145).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17357077}.
/FTId=VAR_021995.
VARIANT 385 385 V -> I (in dbSNP:rs28730736).
/FTId=VAR_049166.
MUTAGEN 121 121 C->S: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 122 122 F->A: No change of ligand-binding and IL6
signaling. {ECO:0000269|PubMed:8467812}.
MUTAGEN 132 132 C->A: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 134 134 W->L: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 140 140 P->G: No change of ligand-binding and IL6
signaling. {ECO:0000269|PubMed:8467812}.
MUTAGEN 153 153 F->L: No change of ligand-binding and IL6
signaling. {ECO:0000269|PubMed:8467812}.
MUTAGEN 165 165 C->L: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 174 174 F->L: No change of ligand-binding and IL6
signaling. {ECO:0000269|PubMed:8467812}.
MUTAGEN 176 176 C->A: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 184 184 D->T: 30% decrease of ligand-binding and
IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 190 190 V->G: 80% decrease of ligand-binding and
no IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 193 193 C->D: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 211 211 C->A: No change of ligand-binding and IL6
signaling. {ECO:0000269|PubMed:8467812}.
MUTAGEN 217 217 D->V: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 232 232 R->S: 30% decrease of ligand-binding and
IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 233 233 W->Q: 30% decrease of ligand-binding and
increase of IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 254 254 E->A: 50% decrease of ligand-binding and
IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 277 277 C->D: 30% increase of ligand-binding and
100% increase in IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 278 278 V->N: 50% Decrease of ligand-binding and
50% increase in IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 279 279 I->D: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 280 280 H->I: No change of ligand-binding and no
IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 281 281 D->G: 70% decrease of ligand-binding and
no IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 285 285 G->D: 80% decrease of ligand-binding and
no IL6 signaling.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 291 291 Q->K: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
MUTAGEN 293 293 R->G: Complete loss of ligand-binding.
{ECO:0000269|PubMed:8467812}.
CONFLICT 210 210 G -> D (in Ref. 5; BAD97302).
{ECO:0000305}.
STRAND 34 37 {ECO:0000244|PDB:1N26}.
STRAND 43 46 {ECO:0000244|PDB:1N26}.
STRAND 56 63 {ECO:0000244|PDB:1N26}.
STRAND 65 68 {ECO:0000244|PDB:1N26}.
STRAND 72 83 {ECO:0000244|PDB:1N26}.
HELIX 88 90 {ECO:0000244|PDB:1N26}.
STRAND 92 101 {ECO:0000244|PDB:1N26}.
STRAND 105 110 {ECO:0000244|PDB:1N26}.
STRAND 120 125 {ECO:0000244|PDB:1N26}.
STRAND 130 134 {ECO:0000244|PDB:1N26}.
STRAND 145 157 {ECO:0000244|PDB:1N26}.
STRAND 159 168 {ECO:0000244|PDB:1N26}.
TURN 169 172 {ECO:0000244|PDB:1N26}.
STRAND 173 178 {ECO:0000244|PDB:1N26}.
STRAND 187 196 {ECO:0000244|PDB:1N26}.
STRAND 199 202 {ECO:0000244|PDB:1N26}.
STRAND 206 209 {ECO:0000244|PDB:1N26}.
TURN 210 212 {ECO:0000244|PDB:1N26}.
STRAND 220 226 {ECO:0000244|PDB:1N26}.
STRAND 234 239 {ECO:0000244|PDB:1N26}.
STRAND 247 249 {ECO:0000244|PDB:1N26}.
STRAND 251 259 {ECO:0000244|PDB:1N26}.
STRAND 266 269 {ECO:0000244|PDB:1N26}.
HELIX 271 273 {ECO:0000244|PDB:1N26}.
STRAND 275 281 {ECO:0000244|PDB:1N26}.
STRAND 288 296 {ECO:0000244|PDB:1N26}.
TURN 297 299 {ECO:0000244|PDB:1N26}.
STRAND 310 312 {ECO:0000244|PDB:1N26}.
SEQUENCE 468 AA; 51548 MW; 62AA239FA14F1B8B CRC64;
MLAVGCALLA ALLAAPGAAL APRRCPAQEV ARGVLTSLPG DSVTLTCPGV EPEDNATVHW
VLRKPAAGSH PSRWAGMGRR LLLRSVQLHD SGNYSCYRAG RPAGTVHLLV DVPPEEPQLS
CFRKSPLSNV VCEWGPRSTP SLTTKAVLLV RKFQNSPAED FQEPCQYSQE SQKFSCQLAV
PEGDSSFYIV SMCVASSVGS KFSKTQTFQG CGILQPDPPA NITVTAVARN PRWLSVTWQD
PHSWNSSFYR LRFELRYRAE RSKTFTTWMV KDLQHHCVIH DAWSGLRHVV QLRAQEEFGQ
GEWSEWSPEA MGTPWTESRS PPAENEVSTP MQALTTNKDD DNILFRDSAN ATSLPVQDSS
SVPLPTFLVA GGSLAFGTLL CIAIVLRFKK TWKLRALKEG KTSMHPPYSL GQLVPERPRP
TPVLVPLISP PVSPSSLGSD NTSSHNRPDA RDPRSPYDIS NTDYFFPR


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