I11RA_MOUSE
ID I11RA_MOUSE Reviewed; 432 AA.
AC Q64385; A2AMS4; Q6NSQ0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Interleukin-11 receptor subunit alpha-1 {ECO:0000305};
DE Short=IL-11 receptor subunit alpha-1;
DE Short=IL-11R subunit alpha-1;
DE Short=IL-11R-alpha-1;
DE Short=IL-11RA1;
DE AltName: Full=Enhancer trap locus homolog 2;
DE Short=Etl-2;
DE AltName: Full=Novel cytokine receptor 1;
DE Short=NR-1;
DE Short=NR1;
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=Il11ra1 {ECO:0000312|MGI:MGI:107426}; Synonyms=Etl2, Il11ra;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ;
RX PubMed=7813775; DOI=10.1006/dbio.1994.1335;
RA Neuhaus H., Bettenhausen B., Bilinski P., Simon-Chazottes D., Guenet J.-L.,
RA Gossler A.;
RT "etl2, a novel putative type-1 cytokine receptor expressed during mouse
RT embryogenesis at high levels in skin and cells with skeletogenic
RT potential.";
RL Dev. Biol. 166:531-542(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=7957045; DOI=10.1002/j.1460-2075.1994.tb06802.x;
RA Hilton D.J., Hilton A.A., Raicevic A., Rakar S., Harrison-Smith M.,
RA Gough N.M., Begley C.G., Metcalf D., Nicola N.A., Willson T.A.;
RT "Cloning of a murine IL-11 receptor alpha-chain; requirement for gp130 for
RT high affinity binding and signal transduction.";
RL EMBO J. 13:4765-4775(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8973540; DOI=10.1042/bj3200359;
RA Bilinski P., Hall M.A., Neuhaus H., Gissel C., Heath J.K., Gossler A.;
RT "Two differentially expressed interleukin-11 receptor genes in the mouse
RT genome.";
RL Biochem. J. 320:359-363(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Testis;
RX PubMed=8662802; DOI=10.1074/jbc.271.23.13754;
RA Robb L., Hilton D.J., Willson T.A., Begley C.G.;
RT "Structural analysis of the gene encoding the murine interleukin-11
RT receptor alpha-chain and a related locus.";
RL J. Biol. Chem. 271:13754-13761(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor;
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 [7]
RP PROTEIN SEQUENCE OF 24-38, AND FUNCTION OF SOLUBLE FORM.
RX PubMed=9373251;
RA Curtis D.J., Hilton D.J., Roberts B., Murray L., Nicola N., Begley C.G.;
RT "Recombinant soluble interleukin-11 (IL-11) receptor alpha-chain can act as
RT an IL-11 antagonist.";
RL Blood 90:4403-4412(1997).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN [9]
RP FUNCTION, PROTEOLYTIC CLEAVAGE, AND 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).
CC -!- FUNCTION: Receptor for interleukin-11. The receptor systems for IL6,
CC LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal
CC transmission. The IL11/IL11RA/IL6ST complex may be involved in the
CC control of proliferation and/or differentiation of skeletogenic
CC progenitor or other mesenchymal cells. Essential for the normal
CC development of craniofacial bones and teeth.
CC -!- FUNCTION: [Soluble interleukin-11 receptor subunit alpha]: Soluble form
CC of IL11 receptor (sIL11RA) that acts as an agonist of IL11 activity.
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.
CC {ECO:0000250|UniProtKB:Q14626}.
CC -!- SUBUNIT: On IL11 binding, forms a multimer complex with IL6ST/gp130.
CC {ECO:0000250|UniProtKB:Q14626}.
CC -!- SUBCELLULAR LOCATION: [Interleukin-11 receptor subunit alpha-1]:
CC Membrane {ECO:0000269|PubMed:26876177}; Single-pass type I membrane
CC protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q14626}.
CC -!- SUBCELLULAR LOCATION: [Soluble interleukin-11 receptor subunit alpha]:
CC Secreted {ECO:0000269|PubMed:26876177}.
CC -!- TISSUE SPECIFICITY: Widely expressed in all adult tissues and in
CC embryos. Highest levels in kidney, skeletal muscle and embryo.
CC {ECO:0000269|PubMed:8662802}.
CC -!- DEVELOPMENTAL STAGE: First detected at low levels at 10.5 dpc in
CC cranofacial mesenchyme and in parts of the nervous system. At 12.5 dpc,
CC high expression found in heart, diaphragm, bronchi and in the
CC mesenchyme surrounding precartilage condensations. At later stages,
CC expressed in dental papilla, dermis, hair follicles and in the
CC perichondrium and in regions containing chondro and osteo progenitor
CC cells. {ECO:0000269|PubMed:7813775}.
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 -!- DISRUPTION PHENOTYPE: Mice have disturbed cranial growth and suture
CC activity. {ECO:0000269|PubMed:21741611}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC subfamily. {ECO:0000305}.
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DR EMBL; X74953; CAA52908.1; -; mRNA.
DR EMBL; U14412; AAA53248.1; -; mRNA.
DR EMBL; X94162; CAA63873.1; -; Genomic_DNA.
DR EMBL; X94163; CAA63873.1; JOINED; Genomic_DNA.
DR EMBL; AL807796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004619; AAH04619.1; -; mRNA.
DR EMBL; BC057664; AAH57664.1; -; mRNA.
DR EMBL; BC069984; AAH69984.1; -; mRNA.
DR CCDS; CCDS18071.1; -.
DR PIR; I48343; I48343.
DR RefSeq; NP_001156873.1; NM_001163401.1.
DR RefSeq; NP_001165525.1; NM_001172054.1.
DR RefSeq; NP_034679.1; NM_010549.3.
DR AlphaFoldDB; Q64385; -.
DR SMR; Q64385; -.
DR DIP; DIP-5781N; -.
DR IntAct; Q64385; 2.
DR STRING; 10090.ENSMUSP00000095736; -.
DR GlyGen; Q64385; 2 sites.
DR PhosphoSitePlus; Q64385; -.
DR PaxDb; Q64385; -.
DR PRIDE; Q64385; -.
DR ProteomicsDB; 273334; -.
DR DNASU; 16157; -.
DR Ensembl; ENSMUST00000098132; ENSMUSP00000095736; ENSMUSG00000073889.
DR Ensembl; ENSMUST00000108040; ENSMUSP00000103675; ENSMUSG00000073889.
DR Ensembl; ENSMUST00000108041; ENSMUSP00000103676; ENSMUSG00000073889.
DR Ensembl; ENSMUST00000108042; ENSMUSP00000103677; ENSMUSG00000073889.
DR GeneID; 16157; -.
DR KEGG; mmu:16157; -.
DR UCSC; uc008sjr.2; mouse.
DR CTD; 16157; -.
DR MGI; MGI:107426; Il11ra1.
DR VEuPathDB; HostDB:ENSMUSG00000073889; -.
DR eggNOG; ENOG502R7G6; Eukaryota.
DR GeneTree; ENSGT00940000160904; -.
DR HOGENOM; CLU_047259_0_1_1; -.
DR InParanoid; Q64385; -.
DR OMA; WNFPSSW; -.
DR OrthoDB; 741136at2759; -.
DR PhylomeDB; Q64385; -.
DR TreeFam; TF331210; -.
DR BioGRID-ORCS; 16157; 3 hits in 40 CRISPR screens.
DR ChiTaRS; Il11ra1; mouse.
DR PRO; PR:Q64385; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q64385; protein.
DR Bgee; ENSMUSG00000073889; Expressed in zone of skin and 72 other tissues.
DR Genevisible; Q64385; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPI:MGI.
DR GO; GO:0004921; F:interleukin-11 receptor activity; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0046697; P:decidualization; IMP:MGI.
DR GO; GO:0032502; P:developmental process; ISS:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; ISO:MGI.
DR GO; GO:0060322; P:head development; ISS:UniProtKB.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IMP:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
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 Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:9373251"
FT CHAIN 24..432
FT /note="Interleukin-11 receptor subunit alpha-1"
FT /id="PRO_0000010914"
FT CHAIN 24..?
FT /note="Soluble interleukin-11 receptor subunit alpha"
FT /id="PRO_0000450689"
FT TOPO_DOM 24..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..432
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 151..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..361
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 CONFLICT 93
FT /note="V -> I (in Ref. 6; AAH57664/AAH69984)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="G -> R (in Ref. 6; AAH57664/AAH69984)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="V -> I (in Ref. 6; AAH57664/AAH69984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 46655 MW; 068389943502BBFC CRC64;
MSSSCSGLTR VLVAVATALV SSSSPCPQAW GPPGVQYGQP GRPVMLCCPG VSAGTPVSWF
RDGDSRLLQG PDSGLGHRLV LAQVDSPDEG TYVCQTLDGV SGGMVTLKLG FPPARPEVSC
QAVDYENFSC TWSPGQVSGL PTRYLTSYRK KTLPGAESQR ESPSTGPWPC PQDPLEASRC
VVHGAEFWSE YRINVTEVNP LGASTCLLDV RLQSILRPDP PQGLRVESVP GYPRRLHASW
TYPASWRRQP HFLLKFRLQY RPAQHPAWST VEPIGLEEVI TDAVAGLPHA VRVSARDFLD
AGTWSAWSPE AWGTPSTGPL QDEIPDWSQG HGQQLEAVVA QEDSPAPARP SLQPDPRPLD
HRDPLEQVAV LASLGIFSCL GLAVGALALG LWLRLRRSGK DGPQKPGLLA PMIPVEKLPG
IPNLQRTPEN FS
