I11RA_RAT
ID I11RA_RAT Reviewed; 431 AA.
AC Q99MF4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
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;
DE Short=sIL-11RA;
DE Short=sIL11RA {ECO:0000305};
DE Flags: Precursor;
GN Name=Il11ra1 {ECO:0000312|RGD:621332};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Li R., Hartley L., Robb L.;
RT "Expression of interleukin-11 and interleukin-11 receptor alpha chain in
RT the rat uterus in the peri-implantation period.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
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. Essential for the normal
CC development of craniofacial bones and teeth. Restricts suture fusion
CC and tooth number. {ECO:0000250|UniProtKB:Q14626}.
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]: Membrane
CC {ECO:0000250|UniProtKB:Q14626}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Soluble interleukin-11 receptor subunit alpha]:
CC Secreted {ECO:0000250|UniProtKB:Q14626}.
CC -!- PTM: A short soluble form is also released from the membrane by
CC proteolysis. The sIL11RA is formed either by limited proteolysis of
CC membrane-bound receptors, a process referred to as ectodomain shedding,
CC or directly secreted from the cells after alternative mRNA splicing.
CC mIL11RA is cleaved by the proteases ADAM10, ELANE and PRTN3.
CC {ECO:0000250|UniProtKB:Q14626}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC subfamily. {ECO:0000305}.
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; AF347936; AAK29624.1; -; mRNA.
DR EMBL; BC070921; AAH70921.1; -; mRNA.
DR RefSeq; NP_620816.1; NM_139116.1.
DR RefSeq; XP_006238085.1; XM_006238023.3.
DR AlphaFoldDB; Q99MF4; -.
DR SMR; Q99MF4; -.
DR STRING; 10116.ENSRNOP00000020885; -.
DR GlyGen; Q99MF4; 2 sites.
DR PaxDb; Q99MF4; -.
DR Ensembl; ENSRNOT00000020885; ENSRNOP00000020885; ENSRNOG00000015068.
DR GeneID; 245983; -.
DR KEGG; rno:245983; -.
DR UCSC; RGD:621332; rat.
DR CTD; 16157; -.
DR RGD; 621332; Il11ra1.
DR eggNOG; ENOG502R7G6; Eukaryota.
DR GeneTree; ENSGT00940000160904; -.
DR HOGENOM; CLU_047259_0_1_1; -.
DR InParanoid; Q99MF4; -.
DR OMA; WNFPSSW; -.
DR OrthoDB; 741136at2759; -.
DR PhylomeDB; Q99MF4; -.
DR TreeFam; TF331210; -.
DR PRO; PR:Q99MF4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000015068; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q99MF4; RN.
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; ISO:RGD.
DR GO; GO:0004921; F:interleukin-11 receptor activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; TAS:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0046697; P:decidualization; ISO:RGD.
DR GO; GO:0032502; P:developmental process; ISO:RGD.
DR GO; GO:0007566; P:embryo implantation; IMP:RGD.
DR GO; GO:0060322; P:head development; ISO:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; ISO:RGD.
DR GO; GO:0001779; P:natural killer cell differentiation; ISO:RGD.
DR GO; GO:0001890; P:placenta development; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..431
FT /note="Interleukin-11 receptor subunit alpha"
FT /id="PRO_0000010916"
FT CHAIN 24..?
FT /note="Soluble interleukin-11 receptor subunit alpha"
FT /id="PRO_0000450691"
FT TOPO_DOM 24..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..431
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 310..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 304..308
FT /note="WSXWS motif"
FT COMPBIAS 324..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 431 AA; 46784 MW; E086FD6B1688180B CRC64;
MSSSRSGLTR VLVAVATALV SSSTPCPQAW GPPGVQYGQP GRPVMLCCPG VNAGTPVSWF
RDGDSRLLQG PDSGLGHRLV LAQVDSRDEG TYVCRTLDGV FGGMVTLKLG SPPARPEVSC
QAVDYENFSC TWSPGRVSGL PTRYLTSYRK KTLPGAESQR ESPSTGPWPC PQDPLEASRC
VVHGAEFWSE YRINVTEVNP LGASTCLLDV RLQRILRPDP PQGLRVESVP GYPRRLHASW
TYPASWRRQP HFLLKFRLQY RPAQHPAWST VEPIGLEELI TDAVAGLPHA VRVSARDFLD
AGTWSAWSPE AWGTPSTGPL RDEVPDGSRG HEQKLEAAAQ EDSPAPPSPS LQPDPRPLDH
RDPLEQVAVL ASLGIFSFLG LAVGALALGL WLRLRRSGKD GPQKPGFLAP MIPGDKLPGI
PNLQRTPENF S
