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Interleukin-11 receptor subunit alpha-1 (IL-11 receptor subunit alpha-1) (IL-11R subunit alpha-1) (IL-11R-alpha-1) (IL-11RA1) (Enhancer trap locus homolog 2) (Etl-2) (Novel cytokine receptor 1) (NR-1) (NR1)

 I11RA_MOUSE             Reviewed;         432 AA.
Q64385; A2AMS4; Q6NSQ0;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 135.
RecName: Full=Interleukin-11 receptor subunit alpha-1;
Short=IL-11 receptor subunit alpha-1;
Short=IL-11R subunit alpha-1;
Short=IL-11R-alpha-1;
Short=IL-11RA1;
AltName: Full=Enhancer trap locus homolog 2;
Short=Etl-2;
AltName: Full=Novel cytokine receptor 1;
Short=NR-1;
Short=NR1;
Flags: Precursor;
Name=Il11ra1; Synonyms=Etl2, Il11ra;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
STRAIN=BALB/cJ;
PubMed=7813775; DOI=10.1006/dbio.1994.1335;
Neuhaus H., Bettenhausen B., Bilinski P., Simon-Chazottes D.,
Guenet J.-L., Gossler A.;
"etl2, a novel putative type-1 cytokine receptor expressed during
mouse embryogenesis at high levels in skin and cells with skeletogenic
potential.";
Dev. Biol. 166:531-542(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=7957045;
Hilton D.J., Hilton A.A., Raicevic A., Rakar S., Harrison-Smith M.,
Gough N.M., Begley C.G., Metcalf D., Nicola N.A., Willson T.A.;
"Cloning of a murine IL-11 receptor alpha-chain; requirement for gp130
for high affinity binding and signal transduction.";
EMBO J. 13:4765-4775(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=8973540; DOI=10.1042/bj3200359;
Bilinski P., Hall M.A., Neuhaus H., Gissel C., Heath J.K., Gossler A.;
"Two differentially expressed interleukin-11 receptor genes in the
mouse genome.";
Biochem. J. 320:359-363(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/Sv; TISSUE=Testis;
PubMed=8662802; DOI=10.1074/jbc.271.23.13754;
Robb L., Hilton D.J., Willson T.A., Begley C.G.;
"Structural analysis of the gene encoding the murine interleukin-11
receptor alpha-chain and a related locus.";
J. Biol. Chem. 271:13754-13761(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor;
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).
[7]
PROTEIN SEQUENCE OF 24-38, AND FUNCTION OF SOLUBLE FORM.
PubMed=9373251;
Curtis D.J., Hilton D.J., Roberts B., Murray L., Nicola N.,
Begley C.G.;
"Recombinant soluble interleukin-11 (IL-11) receptor alpha-chain can
act as an IL-11 antagonist.";
Blood 90:4403-4412(1997).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21741611; DOI=10.1016/j.ajhg.2011.05.024;
Nieminen P., Morgan N.V., Fenwick A.L., Parmanen S., Veistinen L.,
Mikkola M.L., van der Spek P.J., Giraud A., Judd L., Arte S.,
Brueton L.A., Wall S.A., Mathijssen I.M., Maher E.R., Wilkie A.O.,
Kreiborg S., Thesleff I.;
"Inactivation of IL11 signaling causes craniosynostosis, delayed tooth
eruption, and supernumerary teeth.";
Am. J. Hum. Genet. 89:67-81(2011).
-!- FUNCTION: Receptor for interleukin-11. The receptor systems for
IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating
signal transmission. The IL11/IL11RA/IL6ST complex may be involved
in the control of proliferation and/or differentiation of
skeletogenic progenitor or other mesenchymal cells. Essential for
the normal development of craniofacial bones and teeth.
-!- FUNCTION: A soluble form (sIL11RA) can act as an antagonist of
IL11-dependent cell differentiation in cells where both
transmembrane IL11RA and IL6ST are present.
-!- SUBUNIT: On ligand binding, forms a multimer complex with
IL6ST/gp130. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Widely expressed in all adult tissues and in
embryos. Highest levels in kidney, skeletal muscle and embryo.
{ECO:0000269|PubMed:8662802}.
-!- DEVELOPMENTAL STAGE: First detected at low levels at 10.5 dpc in
cranofacial mesenchyme and in parts of the nervous system. At 12.5
dpc, high expression found in heart, diaphragm, bronchi and in the
mesenchyme surrounding precartilage condensations. At later
stages, expressed in dental papilla, dermis, hair follicles and in
the perichondrium and in regions containing chondro and osteo
progenitor cells. {ECO:0000269|PubMed:7813775}.
-!- DISRUPTION PHENOTYPE: Mice have disturbed cranial growth and
suture activity. {ECO:0000269|PubMed:21741611}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X74953; CAA52908.1; -; mRNA.
EMBL; U14412; AAA53248.1; -; mRNA.
EMBL; X94162; CAA63873.1; -; Genomic_DNA.
EMBL; X94163; CAA63873.1; JOINED; Genomic_DNA.
EMBL; AL807796; CAM16061.1; -; Genomic_DNA.
EMBL; BC004619; AAH04619.1; -; mRNA.
EMBL; BC057664; AAH57664.1; -; mRNA.
EMBL; BC069984; AAH69984.1; -; mRNA.
CCDS; CCDS18071.1; -.
PIR; I48343; I48343.
RefSeq; NP_001156873.1; NM_001163401.1.
RefSeq; NP_001165525.1; NM_001172054.1.
RefSeq; NP_034679.1; NM_010549.3.
UniGene; Mm.193451; -.
ProteinModelPortal; Q64385; -.
SMR; Q64385; -.
DIP; DIP-5781N; -.
IntAct; Q64385; 2.
STRING; 10090.ENSMUSP00000095736; -.
PhosphoSitePlus; Q64385; -.
PaxDb; Q64385; -.
PRIDE; Q64385; -.
Ensembl; ENSMUST00000098132; ENSMUSP00000095736; ENSMUSG00000073889.
Ensembl; ENSMUST00000108040; ENSMUSP00000103675; ENSMUSG00000073889.
Ensembl; ENSMUST00000108041; ENSMUSP00000103676; ENSMUSG00000073889.
Ensembl; ENSMUST00000108042; ENSMUSP00000103677; ENSMUSG00000073889.
GeneID; 16157; -.
KEGG; mmu:16157; -.
UCSC; uc008sjr.2; mouse.
CTD; 16157; -.
MGI; MGI:107426; Il11ra1.
eggNOG; ENOG410IJ7D; Eukaryota.
eggNOG; ENOG4111N1H; LUCA.
GeneTree; ENSGT00530000063103; -.
HOGENOM; HOG000231670; -.
HOVERGEN; HBG063427; -.
InParanoid; Q64385; -.
KO; K05056; -.
OMA; WFRDGET; -.
OrthoDB; EOG091G0ER8; -.
PhylomeDB; Q64385; -.
TreeFam; TF331210; -.
Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
PRO; PR:Q64385; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000073889; -.
CleanEx; MM_IL11RA1; -.
Genevisible; Q64385; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019970; F:interleukin-11 binding; IPI:MGI.
GO; GO:0004921; F:interleukin-11 receptor activity; IDA:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0046697; P:decidualization; IMP:MGI.
GO; GO:0032502; P:developmental process; ISS:UniProtKB.
GO; GO:0060322; P:head development; ISS:UniProtKB.
GO; GO:0060135; P:maternal process involved in female pregnancy; IMP:MGI.
GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI.
GO; GO:0001890; P:placenta development; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
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.
SMART; SM00060; FN3; 2.
SMART; SM00409; IG; 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;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000269|PubMed:9373251}.
CHAIN 24 432 Interleukin-11 receptor subunit alpha-1.
/FTId=PRO_0000010914.
TOPO_DOM 24 372 Extracellular. {ECO:0000255}.
TRANSMEM 373 393 Helical. {ECO:0000255}.
TOPO_DOM 394 432 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 110 Ig-like C2-type.
DOMAIN 112 219 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 220 317 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 304 308 WSXWS motif.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 194 194 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 94 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 120 130 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 170 180 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 93 93 V -> I (in Ref. 6; AAH57664/AAH69984).
{ECO:0000305}.
CONFLICT 332 332 G -> R (in Ref. 6; AAH57664/AAH69984).
{ECO:0000305}.
CONFLICT 368 368 V -> I (in Ref. 6; AAH57664/AAH69984).
{ECO:0000305}.
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


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