Q14626 (I11RA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin-11 receptor subunit alpha
Short name=IL-11 receptor subunit alpha
Short name=IL-11R subunit alpha
Short name=IL-11R-alpha
Short name=IL-11RA

Gene names

Name:

IL11RA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Restricts suture fusion and tooth number. Ref.9
Subunit structure	On ligand binding, forms a multimer complex with IL6ST/gp130.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in a number of cell lines, including the myelogenous leukemia cell line K-562, the megakaryocytic leukemia cell line M-07e, the erythroleukemia cell line TF-1, and the osteosarcoma cell lines, MG-63 and SaOS-2. Also expressed in normal and malignant prostate epithelial cell lines. Expression levels are increased in prostate carcinoma. Ref.8
Involvement in disease	Craniosynostosis and dental anomalies (CRSDA) [MIM:614188]: A disorder characterized by craniosynostosis, maxillary hypoplasia, and dental anomalies, including malocclusion, delayed and ectopic tooth eruption, and/or supernumerary teeth. Some patients also display minor digit anomalies, such as syndactyly and/or clinodactyly. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9
Sequence similarities	Belongs to the type I cytokine receptor family. Type 3 subfamily. Contains 2 fibronectin type-III domains. Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Craniosynostosis Disease mutation
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokine-mediated signaling pathway Inferred from electronic annotation. Source: GOC embryo implantation Inferred from electronic annotation. Source: Compara head development Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	cytokine receptor activity Inferred from electronic annotation. Source: InterPro transmembrane signaling receptor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform HCR1 (identifier: Q14626-1)

Also known as: Membrane form;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform HCR2 (identifier: Q14626-2)

Also known as: Soluble form; sIL11RA;

The sequence of this isoform differs from the canonical sequence as follows:
     391-422: Missing.

Note: Lacks the entire cytoplasmic domain.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 422	400	Interleukin-11 receptor subunit alpha		PRO_0000010913
Regions
	Topological domain	24 – 370	347	Extracellular Potential
	Transmembrane	371 – 391	21	Helical; Potential
	Topological domain	392 – 422	31	Cytoplasmic Potential
	Domain	27 – 110	84	Ig-like C2-type
	Domain	112 – 214	103	Fibronectin type-III 1
	Domain	218 – 311	94	Fibronectin type-III 2
	Motif	304 – 308	5	WSXWS motif
Amino acid modifications
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Glycosylation	194	1	N-linked (GlcNAc...) Potential
	Disulfide bond	48 ↔ 94		By similarity
	Disulfide bond	120 ↔ 130		By similarity
	Disulfide bond	170 ↔ 180		By similarity
Natural variations
	Alternative sequence	391 – 422	32	Missing in isoform HCR2.		VSP_011879
	Natural variant	65	1	P → T. Ref.4 Corresponds to variant rs11575589 [ dbSNP | Ensembl ].		VAR_019821
	Natural variant	221	1	P → R in CRSDA. Ref.9		VAR_066666
	Natural variant	245	1	S → C in CRSDA. Ref.9		VAR_066667
	Natural variant	296	1	R → W in CRSDA; renders the receptor unable to mediate the IL11 signal. Ref.9		VAR_066668
	Natural variant	308	1	S → STWS in CRSDA.		VAR_066669
	Natural variant	395	1	R → W. Ref.4 Corresponds to variant rs11575580 [ dbSNP | Ensembl ].		VAR_019822

Sequences

	Sequence		Length	Mass (Da)
	Isoform HCR1 (Membrane form) [UniParc]. Last modified November 23, 2004. Version 2. Checksum: 1F8BC05C139FC326	FASTA	422	45,222
	10 20 30 40 50 60 MSSSCSGLSR VLVAVATALV SASSPCPQAW GPPGVQYGQP GRSVKLCCPG VTAGDPVSWF 70 80 90 100 110 120 RDGEPKLLQG PDSGLGHELV LAQADSTDEG TYICQTLDGA LGGTVTLQLG YPPARPVVSC 130 140 150 160 170 180 QAADYENFSC TWSPSQISGL PTRYLTSYRK KTVLGADSQR RSPSTGPWPC PQDPLGAARC 190 200 210 220 230 240 VVHGAEFWSQ YRINVTEVNP LGASTRLLDV SLQSILRPDP PQGLRVESVP GYPRRLRASW 250 260 270 280 290 300 TYPASWPCQP HFLLKFRLQY RPAQHPAWST VEPAGLEEVI TDAVAGLPHA VRVSARDFLD 310 320 330 340 350 360 AGTWSTWSPE AWGTPSTGTI PKEIPAWGQL HTQPEVEPQV DSPAPPRPSL QPHPRLLDHR 370 380 390 400 410 420 DSVEQVAVLA SLGILSFLGL VAGALALGLW LRLRRGGKDG SPKPGFLASV IPVDRRPGAP NL
	Isoform HCR2 (Soluble form) (sIL11RA) [UniParc]. Checksum: 847F8C6F5F52248D	FASTA	390	41,842
	10 20 30 40 50 60 MSSSCSGLSR VLVAVATALV SASSPCPQAW GPPGVQYGQP GRSVKLCCPG VTAGDPVSWF 70 80 90 100 110 120 RDGEPKLLQG PDSGLGHELV LAQADSTDEG TYICQTLDGA LGGTVTLQLG YPPARPVVSC 130 140 150 160 170 180 QAADYENFSC TWSPSQISGL PTRYLTSYRK KTVLGADSQR RSPSTGPWPC PQDPLGAARC 190 200 210 220 230 240 VVHGAEFWSQ YRINVTEVNP LGASTRLLDV SLQSILRPDP PQGLRVESVP GYPRRLRASW 250 260 270 280 290 300 TYPASWPCQP HFLLKFRLQY RPAQHPAWST VEPAGLEEVI TDAVAGLPHA VRVSARDFLD 310 320 330 340 350 360 AGTWSTWSPE AWGTPSTGTI PKEIPAWGQL HTQPEVEPQV DSPAPPRPSL QPHPRLLDHR 370 380 390 DSVEQVAVLA SLGILSFLGL VAGALALGLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of two isoforms of a receptor for the human hematopoietic cytokine interleukin-11." Cherel M., Sorel M., Lebeau B., Dubois S., Moreau J.-F., Bataille R., Minvielle S., Jacques Y. Blood 86:2534-2540(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HCR1 AND HCR2). Tissue: Muscle.
[2]	"Molecular cloning and characterization of the human interleukin-11 receptor alpha-chain gene, IL11RA, located on chromosome 9p13." Van Leuven F., Stas L., Hilliker C., Miyake Y., Bilinski P., Gossler A. Genomics 31:65-70(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM HCR1).
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HCR1).
[4]	SeattleSNPs variation discovery resource Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-65 AND TRP-395.
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HCR1). Tissue: Brain.
[8]	"Increased expression of the interleukin-11 receptor and evidence of STAT3 activation in prostate carcinoma." Campbell C.L., Jiang Z., Savarese D.M., Savarese T.M. Am. J. Pathol. 158:25-32(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Inactivation of IL11 signaling causes craniosynostosis, delayed tooth eruption, and supernumerary teeth." 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. Am. J. Hum. Genet. 89:67-81(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, VARIANTS CRSDA ARG-221; CYS-245; TRP-296 AND THR-TRP-SER-308 INS, CHARACTERIZATION OF VARIANT CRSDA TRP-296.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z38102 mRNA. Translation: CAA86224.1. Z46595 mRNA. Translation: CAA86570.1. U32323 Genomic DNA. Translation: AAB36491.1. U32324 mRNA. Translation: AAB36492.1. BT009864 mRNA. Translation: AAP88866.1. AY532110 Genomic DNA. Translation: AAS00093.1. AL162231 Genomic DNA. Translation: CAH69857.1. CH471071 Genomic DNA. Translation: EAW58423.1. BC003110 mRNA. Translation: AAH03110.1.
IPI	IPI00184319. IPI00375713.
PIR	I37891.
RefSeq	NP_001136256.1. NM_001142784.2.
UniGene	Hs.591088.
3D structure databases
ProteinModelPortal	Q14626.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3776N.
STRING	9606.ENSP00000326500.
PTM databases
PhosphoSite	Q14626.
Polymorphism databases
DMDM	55976300.
Proteomic databases
PaxDb	Q14626.
PRIDE	Q14626.
Protocols and materials databases
DNASU	3590.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000318041; ENSP00000326500; ENSG00000137070. ENST00000378817; ENSP00000368094; ENSG00000137070. ENST00000441545; ENSP00000394391; ENSG00000137070. ENST00000555003; ENSP00000450565; ENSG00000137070.
GeneID	3590.
KEGG	hsa:3590.
UCSC	uc003zvi.3. human.
Organism-specific databases
CTD	3590.
GeneCards	GC09P034650.
HGNC	HGNC:5967. IL11RA.
MIM	600939. gene. 614188. phenotype.
neXtProt	NX_Q14626.
Orphanet	284149. Craniosynostosis and dental anomalies.
PharmGKB	PA29782.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG28915.
HOGENOM	HOG000231670.
HOVERGEN	HBG063427.
InParanoid	Q14626.
KO	K05056.
OMA	TYPASWP.
OrthoDB	EOG4K3KWX.
PhylomeDB	Q14626.
Gene expression databases
ArrayExpress	Q14626.
Bgee	Q14626.
CleanEx	HS_IL11RA.
Genevestigator	Q14626.
GermOnline	ENSG00000137070. Homo sapiens.
Family and domain databases
Gene3D	2.60.40.10. 3 hits.
InterPro	IPR003961. Fibronectin_type3. IPR003530. Hematopoietin_rcpt_L_F3_CS. IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR003599. Ig_sub. [Graphical view]
SMART	SM00060. FN3. 2 hits. SM00409. IG. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits.
PROSITE	PS50853. FN3. 2 hits. PS01354. HEMATOPO_REC_L_F3. 1 hit. PS50835. IG_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL2050.
ChiTaRS	IL11RA. human.
DrugBank	DB00038. Oprelvekin.
GenomeRNAi	3590.
NextBio	14027.
SOURCE	Search...

Entry information

Entry name

I11RA_HUMAN

Accession

Primary (citable) accession number: Q14626
Secondary accession number(s): Q16542, Q5VZ80, Q7KYJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	November 23, 2004
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.