I11RA_HUMAN
ID I11RA_HUMAN Reviewed; 422 AA.
AC Q14626; Q16542; Q5VZ80; Q7KYJ7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Interleukin-11 receptor subunit alpha {ECO:0000305};
DE Short=IL-11 receptor subunit alpha;
DE Short=IL-11R subunit alpha;
DE Short=IL-11R-alpha;
DE Short=IL-11RA;
DE Contains:
DE RecName: Full=Soluble interleukin-11 receptor subunit alpha {ECO:0000305};
DE Short=sIL-11R {ECO:0000303|PubMed:26876177};
DE Short=sIL-11RA;
DE Short=sIL11RA {ECO:0000305};
DE Flags: Precursor;
GN Name=IL11RA {ECO:0000312|HGNC:HGNC:5967};
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] (ISOFORMS HCR1 AND HCR2), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Muscle;
RX PubMed=7670098;
RA Cherel M., Sorel M., Lebeau B., Dubois S., Moreau J.-F., Bataille R.,
RA Minvielle S., Jacques Y.;
RT "Molecular cloning of two isoforms of a receptor for the human
RT hematopoietic cytokine interleukin-11.";
RL Blood 86:2534-2540(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM HCR1).
RX PubMed=8808281; DOI=10.1006/geno.1996.0010;
RA Van Leuven F., Stas L., Hilliker C., Miyake Y., Bilinski P., Gossler A.;
RT "Molecular cloning and characterization of the human interleukin-11
RT receptor alpha-chain gene, IL11RA, located on chromosome 9p13.";
RL Genomics 31:65-70(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HCR1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-65 AND TRP-395.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HCR1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11141475; DOI=10.1016/s0002-9440(10)63940-5;
RA Campbell C.L., Jiang Z., Savarese D.M., Savarese T.M.;
RT "Increased expression of the interleukin-11 receptor and evidence of STAT3
RT activation in prostate carcinoma.";
RL Am. J. Pathol. 158:25-32(2001).
RN [9]
RP FUNCTION (ISOFORM HCR2), PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF ARG-355, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26876177; DOI=10.1016/j.celrep.2016.01.053;
RA Lokau J., Nitz R., Agthe M., Monhasery N., Aparicio-Siegmund S.,
RA Schumacher N., Wolf J., Moeller-Hackbarth K., Waetzig G.H., Groetzinger J.,
RA Mueller-Newen G., Rose-John S., Scheller J., Garbers C.;
RT "Proteolytic Cleavage Governs Interleukin-11 Trans-signaling.";
RL Cell Rep. 14:1761-1773(2016).
RN [10]
RP FUNCTION (ISOFORM HCR2).
RX PubMed=30279168; DOI=10.1126/scisignal.aar7388;
RA Lamertz L., Rummel F., Polz R., Baran P., Hansen S., Waetzig G.H.,
RA Moll J.M., Floss D.M., Scheller J.;
RT "Soluble gp130 prevents interleukin-6 and interleukin-11 cluster signaling
RT but not intracellular autocrine responses.";
RL Sci. Signal. 11:0-0(2018).
RN [11]
RP VARIANTS CRSDA ARG-221; CYS-245; TRP-296 AND THR-TRP-SER-308 INS,
RP CHARACTERIZATION OF VARIANT CRSDA TRP-296, AND FUNCTION.
RX PubMed=21741611; DOI=10.1016/j.ajhg.2011.05.024;
RA Nieminen P., Morgan N.V., Fenwick A.L., Parmanen S., Veistinen L.,
RA Mikkola M.L., van der Spek P.J., Giraud A., Judd L., Arte S., Brueton L.A.,
RA Wall S.A., Mathijssen I.M., Maher E.R., Wilkie A.O., Kreiborg S.,
RA Thesleff I.;
RT "Inactivation of IL11 signaling causes craniosynostosis, delayed tooth
RT eruption, and supernumerary teeth.";
RL Am. J. Hum. Genet. 89:67-81(2011).
CC -!- FUNCTION: Receptor for interleukin-11 (IL11). The receptor systems for
CC IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating
CC signal transmission. The IL11/IL11RA/IL6ST complex may be involved in
CC the control of proliferation and/or differentiation of skeletogenic
CC progenitor or other mesenchymal cells (Probable). Essential for the
CC normal development of craniofacial bones and teeth. Restricts suture
CC fusion and tooth number. {ECO:0000269|PubMed:21741611, ECO:0000305}.
CC -!- FUNCTION: [Soluble interleukin-11 receptor subunit alpha]: Soluble form
CC of IL11 receptor (sIL11RA) that acts as an agonist of IL11 activity
CC (PubMed:30279168, PubMed:26876177). The IL11:sIL11RA complex binds to
CC IL6ST/gp130 on cell surfaces and induces signaling also on cells that
CC do not express membrane-bound IL11RA in a process called IL11 trans-
CC signaling (PubMed:30279168, PubMed:26876177).
CC {ECO:0000269|PubMed:26876177, ECO:0000269|PubMed:30279168}.
CC -!- FUNCTION: [Isoform HCR2]: Soluble form of IL11 receptor (sIL11RA) that
CC acts as an agonist of IL11 activity (PubMed:30279168, PubMed:26876177).
CC The IL11:sIL11RA complex binds to IL6ST/gp130 on cell surfaces and
CC induces signaling also on cells that do not express membrane-bound
CC IL11RA in a process called IL11 trans-signaling (PubMed:30279168,
CC PubMed:26876177). {ECO:0000269|PubMed:26876177,
CC ECO:0000269|PubMed:30279168}.
CC -!- SUBUNIT: On IL11 binding, forms a multimer complex with IL6ST/gp130.
CC {ECO:0000305|PubMed:26876177, ECO:0000305|PubMed:30279168}.
CC -!- INTERACTION:
CC Q14626; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-13638581, EBI-2804156;
CC -!- SUBCELLULAR LOCATION: [Interleukin-11 receptor subunit alpha]: Membrane
CC {ECO:0000269|PubMed:26876177}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Soluble interleukin-11 receptor subunit alpha]:
CC Secreted {ECO:0000269|PubMed:26876177}.
CC -!- SUBCELLULAR LOCATION: [Isoform HCR2]: Secreted
CC {ECO:0000269|PubMed:26876177}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=HCR1 {ECO:0000303|PubMed:7670098}; Synonyms=Membrane form, mIL11RA
CC {ECO:0000303|PubMed:26876177};
CC IsoId=Q14626-1; Sequence=Displayed;
CC Name=HCR2 {ECO:0000303|PubMed:7670098}; Synonyms=Soluble form, sIL11RA
CC {ECO:0000303|PubMed:26876177};
CC IsoId=Q14626-2; Sequence=VSP_011879;
CC -!- TISSUE SPECIFICITY: Expressed in a number of cell lines, including the
CC myelogenous leukemia cell line K-562, the megakaryocytic leukemia cell
CC line M-07e, the erythroleukemia cell line TF-1, and the osteosarcoma
CC cell lines, MG-63 and SaOS-2 (PubMed:7670098). Also expressed in normal
CC and malignant prostate epithelial cell lines. Expression levels are
CC increased in prostate carcinoma. {ECO:0000269|PubMed:11141475,
CC ECO:0000269|PubMed:7670098}.
CC -!- PTM: A short soluble form is also released from the membrane by
CC proteolysis (PubMed:26876177). The sIL11RA is formed either by limited
CC proteolysis of membrane-bound receptors, a process referred to as
CC ectodomain shedding, or directly secreted from the cells after
CC alternative mRNA splicing (PubMed:26876177). mIL11RA is cleaved by the
CC proteases ADAM10, ELANE and PRTN3 (PubMed:26876177).
CC {ECO:0000269|PubMed:26876177}.
CC -!- DISEASE: Craniosynostosis and dental anomalies (CRSDA) [MIM:614188]: A
CC disorder characterized by craniosynostosis, maxillary hypoplasia, and
CC dental anomalies, including malocclusion, delayed and ectopic tooth
CC eruption, and/or supernumerary teeth. Some patients also display minor
CC digit anomalies, such as syndactyly and/or clinodactyly.
CC {ECO:0000269|PubMed:21741611}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform HCR2]: Lacks the entire cytoplasmic domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il11ra/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z38102; CAA86224.1; -; mRNA.
DR EMBL; Z46595; CAA86570.1; -; mRNA.
DR EMBL; U32323; AAB36491.1; -; Genomic_DNA.
DR EMBL; U32324; AAB36492.1; -; mRNA.
DR EMBL; BT009864; AAP88866.1; -; mRNA.
DR EMBL; AY532110; AAS00093.1; -; Genomic_DNA.
DR EMBL; AL162231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58423.1; -; Genomic_DNA.
DR EMBL; BC003110; AAH03110.1; -; mRNA.
DR CCDS; CCDS6567.1; -. [Q14626-1]
DR PIR; I37891; I37891.
DR RefSeq; NP_001136256.1; NM_001142784.2. [Q14626-1]
DR PDB; 6O4P; X-ray; 3.43 A; A/B=23-363.
DR PDBsum; 6O4P; -.
DR AlphaFoldDB; Q14626; -.
DR SASBDB; Q14626; -.
DR SMR; Q14626; -.
DR BioGRID; 109804; 1.
DR DIP; DIP-3776N; -.
DR IntAct; Q14626; 2.
DR STRING; 9606.ENSP00000450565; -.
DR ChEMBL; CHEMBL2050; -.
DR DrugBank; DB00038; Oprelvekin.
DR DrugCentral; Q14626; -.
DR GlyGen; Q14626; 2 sites.
DR iPTMnet; Q14626; -.
DR PhosphoSitePlus; Q14626; -.
DR BioMuta; IL11RA; -.
DR DMDM; 55976300; -.
DR PaxDb; Q14626; -.
DR PeptideAtlas; Q14626; -.
DR PRIDE; Q14626; -.
DR ProteomicsDB; 60076; -. [Q14626-1]
DR ProteomicsDB; 60077; -. [Q14626-2]
DR Antibodypedia; 25597; 344 antibodies from 32 providers.
DR DNASU; 3590; -.
DR Ensembl; ENST00000318041.13; ENSP00000326500.8; ENSG00000137070.19. [Q14626-1]
DR Ensembl; ENST00000441545.7; ENSP00000394391.3; ENSG00000137070.19. [Q14626-1]
DR Ensembl; ENST00000555981.6; ENSP00000450640.2; ENSG00000137070.19. [Q14626-1]
DR Ensembl; ENST00000602473.5; ENSP00000473647.1; ENSG00000137070.19. [Q14626-2]
DR Ensembl; ENST00000690286.1; ENSP00000509204.1; ENSG00000137070.19. [Q14626-1]
DR GeneID; 3590; -.
DR KEGG; hsa:3590; -.
DR MANE-Select; ENST00000441545.7; ENSP00000394391.3; NM_001142784.3; NP_001136256.1.
DR UCSC; uc031tdp.2; human. [Q14626-1]
DR CTD; 3590; -.
DR DisGeNET; 3590; -.
DR GeneCards; IL11RA; -.
DR HGNC; HGNC:5967; IL11RA.
DR HPA; ENSG00000137070; Low tissue specificity.
DR MalaCards; IL11RA; -.
DR MIM; 600939; gene.
DR MIM; 614188; phenotype.
DR neXtProt; NX_Q14626; -.
DR OpenTargets; ENSG00000137070; -.
DR Orphanet; 284149; Craniosynostosis-dental anomalies.
DR PharmGKB; PA29782; -.
DR VEuPathDB; HostDB:ENSG00000137070; -.
DR eggNOG; ENOG502R7G6; Eukaryota.
DR GeneTree; ENSGT00940000160904; -.
DR HOGENOM; CLU_047259_0_1_1; -.
DR InParanoid; Q14626; -.
DR OMA; WNFPSSW; -.
DR PhylomeDB; Q14626; -.
DR TreeFam; TF331210; -.
DR PathwayCommons; Q14626; -.
DR Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
DR SignaLink; Q14626; -.
DR SIGNOR; Q14626; -.
DR BioGRID-ORCS; 3590; 8 hits in 1080 CRISPR screens.
DR GeneWiki; Interleukin_11_receptor_alpha_subunit; -.
DR GenomeRNAi; 3590; -.
DR Pharos; Q14626; Tclin.
DR PRO; PR:Q14626; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q14626; protein.
DR Bgee; ENSG00000137070; Expressed in apex of heart and 157 other tissues.
DR ExpressionAtlas; Q14626; baseline and differential.
DR Genevisible; Q14626; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019970; F:interleukin-11 binding; IBA:GO_Central.
DR GO; GO:0004921; F:interleukin-11 receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0032502; P:developmental process; IMP:UniProtKB.
DR GO; GO:0060322; P:head development; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Craniosynostosis; Disease variant;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..422
FT /note="Interleukin-11 receptor subunit alpha"
FT /id="PRO_0000010913"
FT CHAIN 23..?
FT /note="Soluble interleukin-11 receptor subunit alpha"
FT /id="PRO_0000450688"
FT TOPO_DOM 24..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..110
FT /note="Ig-like C2-type"
FT DOMAIN 112..219
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 220..317
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 335..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 304..308
FT /note="WSXWS motif"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 120..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 170..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 391..422
FT /note="Missing (in isoform HCR2)"
FT /evidence="ECO:0000303|PubMed:7670098"
FT /id="VSP_011879"
FT VARIANT 65
FT /note="P -> T (in dbSNP:rs11575589)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019821"
FT VARIANT 221
FT /note="P -> R (in CRSDA; dbSNP:rs387906785)"
FT /evidence="ECO:0000269|PubMed:21741611"
FT /id="VAR_066666"
FT VARIANT 245
FT /note="S -> C (in CRSDA; dbSNP:rs387906786)"
FT /evidence="ECO:0000269|PubMed:21741611"
FT /id="VAR_066667"
FT VARIANT 296
FT /note="R -> W (in CRSDA; renders the receptor unable to
FT mediate the IL11 signal; dbSNP:rs387906784)"
FT /evidence="ECO:0000269|PubMed:21741611"
FT /id="VAR_066668"
FT VARIANT 308
FT /note="S -> STWS (in CRSDA)"
FT /id="VAR_066669"
FT VARIANT 395
FT /note="R -> W (in dbSNP:rs11575580)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019822"
FT MUTAGEN 355
FT /note="R->E: Decreases proteolyisis by ADAM10."
FT /evidence="ECO:0000269|PubMed:26876177"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:6O4P"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 187..199
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:6O4P"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:6O4P"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6O4P"
SQ SEQUENCE 422 AA; 45222 MW; 1F8BC05C139FC326 CRC64;
MSSSCSGLSR VLVAVATALV SASSPCPQAW GPPGVQYGQP GRSVKLCCPG VTAGDPVSWF
RDGEPKLLQG PDSGLGHELV LAQADSTDEG TYICQTLDGA LGGTVTLQLG YPPARPVVSC
QAADYENFSC TWSPSQISGL PTRYLTSYRK KTVLGADSQR RSPSTGPWPC PQDPLGAARC
VVHGAEFWSQ YRINVTEVNP LGASTRLLDV SLQSILRPDP PQGLRVESVP GYPRRLRASW
TYPASWPCQP HFLLKFRLQY RPAQHPAWST VEPAGLEEVI TDAVAGLPHA VRVSARDFLD
AGTWSTWSPE AWGTPSTGTI PKEIPAWGQL HTQPEVEPQV DSPAPPRPSL QPHPRLLDHR
DSVEQVAVLA SLGILSFLGL VAGALALGLW LRLRRGGKDG SPKPGFLASV IPVDRRPGAP
NL
