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   13-SEP-2023, entry version 167.
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/";
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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; 2.
DR   DIP; DIP-3776N; -.
DR   IntAct; Q14626; 2.
DR   STRING; 9606.ENSP00000450565; -.
DR   ChEMBL; CHEMBL2050; -.
DR   DrugBank; DB00038; Oprelvekin.
DR   DrugCentral; Q14626; -.
DR   GlyCosmos; Q14626; 2 sites, No reported glycans.
DR   GlyGen; Q14626; 2 sites.
DR   iPTMnet; Q14626; -.
DR   PhosphoSitePlus; Q14626; -.
DR   BioMuta; IL11RA; -.
DR   DMDM; 55976300; -.
DR   PaxDb; Q14626; -.
DR   PeptideAtlas; Q14626; -.
DR   ProteomicsDB; 60076; -. [Q14626-1]
DR   ProteomicsDB; 60077; -. [Q14626-2]
DR   Antibodypedia; 25597; 389 antibodies from 33 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   AGR; HGNC:5967; -.
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; YENISCT; -.
DR   OrthoDB; 5358722at2759; -.
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; 9 hits in 1164 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:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0019970; F:interleukin-11 binding; IBA:GO_Central.
DR   GO; GO:0004921; F:interleukin-11 receptor activity; IDA:UniProt.
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:0038154; P:interleukin-11-mediated signaling pathway; IDA:UniProt.
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; Immunoglobulins; 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; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
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
//