I11RA_PONAB
ID I11RA_PONAB Reviewed; 422 AA.
AC Q5RF19;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Interleukin-11 receptor subunit alpha;
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=IL11RA;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR857342; CAH89638.1; -; mRNA.
DR RefSeq; NP_001128982.1; NM_001135510.1.
DR AlphaFoldDB; Q5RF19; -.
DR SMR; Q5RF19; -.
DR STRING; 9601.ENSPPYP00000021420; -.
DR GeneID; 100190822; -.
DR KEGG; pon:100190822; -.
DR CTD; 3590; -.
DR eggNOG; ENOG502R7G6; Eukaryota.
DR HOGENOM; CLU_047259_0_1_1; -.
DR InParanoid; Q5RF19; -.
DR OMA; WNFPSSW; -.
DR OrthoDB; 741136at2759; -.
DR TreeFam; TF331210; -.
DR Proteomes; UP000001595; Chromosome 9.
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:0004896; F:cytokine receptor activity; IEA:InterPro.
DR GO; GO:0032502; P:developmental process; ISS:UniProtKB.
DR GO; GO:0060322; P:head development; ISS:UniProtKB.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..422
FT /note="Interleukin-11 receptor subunit alpha"
FT /id="PRO_0000229037"
FT CHAIN 23..?
FT /note="Soluble interleukin-11 receptor subunit alpha"
FT /id="PRO_0000450690"
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 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"
SQ SEQUENCE 422 AA; 45298 MW; 72DD5D83399B8649 CRC64;
MSSSCSGLSR VLVAVATALV SASSPCPQAW GPPGVQYGQP GRSVKLCCPG VTAGDPVSWF
RDGEPKLLQG PDSGLGHELV LAQADSTDEG TYICRTLDGA LGGTVTLQLG YPPARPVVSC
QAADYENFSC TWSPSQISGL PTRYLTSYRK KTVLGADSQR RSPSTGPWPC PQDPLGAARC
VVHGAEFWSQ YRINVTEVNP LGASTRLLDV SLQSILRPDP PQGLRVESVP GYPRRLRASW
TYPASWPRQP HFLLKFRLQY RPAQHPAWST VEPAGLEEVI TDAVAGLPHA VRVSARDFLD
AGTWSTWSPE AWGTPSTGTV PKEIPAWGQL HTQPEVEPQV DSPAPPRPSL QPHPRLLDHR
DSVEQVAVLV SLGILSFLGL VAGALALGLW LRLRRGGKDG SPKPGFLASV IPVDRHPGAP
NL
