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Q01344 (IL5RA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-5 receptor subunit alpha

Short name=IL-5 receptor subunit alpha
Short name=IL-5R subunit alpha
Short name=IL-5R-alpha
Short name=IL-5RA
Alternative name(s):
CDw125
CD_antigen=CD125
Gene names
Name:IL5RA
Synonyms:IL5R
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is the receptor for interleukin-5. The alpha chain binds to IL5.

Subunit structure

Heterodimer of an alpha and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-CSF receptors. Interacts with SDCBP.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed on eosinophils and basophils.

Domain

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.

The box 1 motif is required for JAK interaction and/or activation.

Sequence similarities

Belongs to the type I cytokine receptor family. Type 5 subfamily.

Contains 2 fibronectin type-III domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IL5P051132EBI-1759442,EBI-2435811

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01344-1)

Also known as: Membrane-bound;

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 2 (identifier: Q01344-2)

Also known as: Soluble-S1;

The sequence of this isoform differs from the canonical sequence as follows:
     333-335: NDE → FSR
     336-420: Missing.
Isoform 3 (identifier: Q01344-3)

Also known as: Soluble-S2;

The sequence of this isoform differs from the canonical sequence as follows:
     333-333: N → K
     334-420: Missing.
Isoform 4 (identifier: Q01344-4)

The sequence of this isoform differs from the canonical sequence as follows:
     365-420: CHLWIKLFPPIPAPKSNIKDLFVTTNYEKAGSSETEIEVICYIEKPGVETLEDSVF → KLGPVRRKLKSSVI
Isoform 5 (identifier: Q01344-5)

The sequence of this isoform differs from the canonical sequence as follows:
     123-331: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 420400Interleukin-5 receptor subunit alpha
PRO_0000010893

Regions

Topological domain21 – 342322Extracellular Potential
Transmembrane343 – 36220Helical; Potential
Topological domain363 – 42058Cytoplasmic Potential
Domain32 – 12392Fibronectin type-III 1
Domain241 – 33494Fibronectin type-III 2
Motif322 – 3265WSXWS motif
Motif371 – 3799Box 1 motif

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Disulfide bond134 ↔ 155 Ref.9
Disulfide bond182 ↔ 196 Ref.9
Disulfide bond269 ↔ 316 Ref.9

Natural variations

Alternative sequence123 – 331209Missing in isoform 5.
VSP_047762
Alternative sequence333 – 3353NDE → FSR in isoform 2.
VSP_001678
Alternative sequence3331N → K in isoform 3.
VSP_001680
Alternative sequence334 – 42087Missing in isoform 3.
VSP_001681
Alternative sequence336 – 42085Missing in isoform 2.
VSP_001679
Alternative sequence365 – 42056CHLWI…EDSVF → KLGPVRRKLKSSVI in isoform 4.
VSP_046742
Natural variant1291I → V. Ref.2 Ref.6
Corresponds to variant rs2290610 [ dbSNP | Ensembl ].
VAR_020654
Natural variant2621V → A. Ref.6
Corresponds to variant rs17879690 [ dbSNP | Ensembl ].
VAR_020655

Experimental info

Sequence conflict2121A → S in AAA36110. Ref.1
Sequence conflict2121A → S in AAA59151. Ref.2
Sequence conflict2121A → S in AAA59152. Ref.2

Secondary structure

......................................................... 420
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Membrane-bound) [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 4E0A5F2838B9C4FE

FASTA42047,685
        10         20         30         40         50         60 
MIIVAHVLLI LLGATEILQA DLLPDEKISL LPPVNFTIKV TGLAQVLLQW KPNPDQEQRN 

        70         80         90        100        110        120 
VNLEYQVKIN APKEDDYETR ITESKCVTIL HKGFSASVRT ILQNDHSLLA SSWASAELHA 

       130        140        150        160        170        180 
PPGSPGTSIV NLTCTTNTTE DNYSRLRSYQ VSLHCTWLVG TDAPEDTQYF LYYRYGSWTE 

       190        200        210        220        230        240 
ECQEYSKDTL GRNIACWFPR TFILSKGRDW LAVLVNGSSK HSAIRPFDQL FALHAIDQIN 

       250        260        270        280        290        300 
PPLNVTAEIE GTRLSIQWEK PVSAFPIHCF DYEVKIHNTR NGYLQIEKLM TNAFISIIDD 

       310        320        330        340        350        360 
LSKYDVQVRA AVSSMCREAG LWSEWSQPIY VGNDEHKPLR EWFVIVIMAT ICFILLILSL 

       370        380        390        400        410        420 
ICKICHLWIK LFPPIPAPKS NIKDLFVTTN YEKAGSSETE IEVICYIEKP GVETLEDSVF 

« Hide

Isoform 2 (Soluble-S1) [UniParc].

Checksum: BAED076239845E16
Show »

FASTA33537,984
Isoform 3 (Soluble-S2) [UniParc].

Checksum: 8D9239845E16985B
Show »

FASTA33337,722
Isoform 4 [UniParc].

Checksum: 3044C8640A83F586
Show »

FASTA37842,924
Isoform 5 [UniParc].

Checksum: 475CB1AB3BF8D2B2
Show »

FASTA21123,737

References

« Hide 'large scale' references
[1]"A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF."
Tavernier J., Devos R., Cornelis S., Tuypens T., van der Heyden J., Fiers W., Plaetinck G.
Cell 66:1175-1184(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Molecular cloning and expression of the human interleukin 5 receptor."
Murata Y., Takaki S., Migita M., Kikuchi Y., Tominaga A., Takatsu K.
J. Exp. Med. 175:341-351(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANT VAL-129.
Tissue: Peripheral blood.
[3]"Molecular basis of the membrane-anchored and two soluble isoforms of the human interleukin 5 receptor alpha subunit."
Tavernier J., Tuypens T., Plaetinck G., Verhee A., Fiers W., Devos R.
Proc. Natl. Acad. Sci. U.S.A. 89:7041-7045(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[4]"Isolation of the variants for human interleukin-5 receptor alpha subunit."
Ishihara K., Yamada M., Hirasawa N., Ohuchi K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Trachea.
[6]SeattleSNPs variation discovery resource
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-129 AND ALA-262.
[7]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm."
Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.
Structure 11:845-853(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-420 IN COMPLEX WITH SDCBP.
[9]"Structure analysis of the IL-5 ligand-receptor complex reveals a wrench-like architecture for IL-5Ralpha."
Patino E., Kotzsch A., Saremba S., Nickel J., Schmitz W., Sebald W., Mueller T.D.
Structure 19:1864-1875(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 20-332 IN COMPLEX WITH IL5, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M75914 mRNA. Translation: AAA36110.1.
X61176 mRNA. Translation: CAA43483.1.
X62156 mRNA. Translation: CAA44081.1.
M96651 mRNA. Translation: AAA59151.1.
M96652 mRNA. Translation: AAA59152.1.
AB288090 mRNA. Translation: BAG49562.1.
AK304256 mRNA. Translation: BAG65122.1.
AY642135 Genomic DNA. Translation: AAT45457.1.
AC022002 Genomic DNA. No translation available.
AC024060 Genomic DNA. No translation available.
CCDSCCDS2559.1. [Q01344-1]
CCDS2560.1. [Q01344-2]
CCDS46739.1. [Q01344-3]
CCDS58813.1. [Q01344-4]
PIRA40267.
RefSeqNP_000555.2. NM_000564.4. [Q01344-1]
NP_001230028.1. NM_001243099.1. [Q01344-4]
NP_783851.1. NM_175724.2. [Q01344-3]
NP_783852.1. NM_175725.2. [Q01344-2]
NP_783853.1. NM_175726.3. [Q01344-1]
NP_783854.1. NM_175727.2. [Q01344-3]
NP_783855.1. NM_175728.2. [Q01344-2]
UniGeneHs.68876.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OBXX-ray1.35B413-420[»]
1OBZX-ray1.69P413-420[»]
3QT2X-ray2.55A/B20-335[»]
3VA2X-ray2.70C21-335[»]
ProteinModelPortalQ01344.
SMRQ01344. Positions 27-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109782. 6 interactions.
DIPDIP-3510N.
IntActQ01344. 3 interactions.
STRING9606.ENSP00000256452.

Chemistry

GuidetoPHARMACOLOGY1706.

PTM databases

PhosphoSiteQ01344.

Polymorphism databases

DMDM116242525.

Proteomic databases

PaxDbQ01344.
PRIDEQ01344.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256452; ENSP00000256452; ENSG00000091181. [Q01344-1]
ENST00000311981; ENSP00000309196; ENSG00000091181. [Q01344-2]
ENST00000383846; ENSP00000373358; ENSG00000091181. [Q01344-2]
ENST00000430514; ENSP00000400400; ENSG00000091181. [Q01344-3]
ENST00000438560; ENSP00000390753; ENSG00000091181. [Q01344-4]
ENST00000445864; ENSP00000402598; ENSG00000091181. [Q01344-5]
ENST00000446632; ENSP00000412209; ENSG00000091181. [Q01344-1]
ENST00000456302; ENSP00000392059; ENSG00000091181. [Q01344-3]
GeneID3568.
KEGGhsa:3568.
UCSCuc010hbs.3. human. [Q01344-1]
uc010hbt.2. human. [Q01344-2]
uc010hbu.2. human. [Q01344-3]

Organism-specific databases

CTD3568.
GeneCardsGC03M003111.
HGNCHGNC:6017. IL5RA.
HPAHPA013196.
MIM147851. gene.
neXtProtNX_Q01344.
PharmGKBPA29834.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43089.
HOGENOMHOG000070224.
HOVERGENHBG052117.
InParanoidQ01344.
KOK05067.
OMAAPEDTQY.
OrthoDBEOG71P2B1.
PhylomeDBQ01344.
TreeFamTF331549.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ01344.

Gene expression databases

ArrayExpressQ01344.
BgeeQ01344.
CleanExHS_IL5RA.
GenevestigatorQ01344.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015321. IL-6_rcpt_alpha-bd.
IPR003532. Short_hematopoietin_rcpt_2_CS.
[Graphical view]
PfamPF09240. IL6Ra-bind. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 2 hits.
PS01356. HEMATOPO_REC_S_F2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01344.
GeneWikiInterleukin_5_receptor_alpha_subunit.
GenomeRNAi3568.
NextBio13936.
PROQ01344.
SOURCESearch...

Entry information

Entry nameIL5RA_HUMAN
AccessionPrimary (citable) accession number: Q01344
Secondary accession number(s): B3IU77 expand/collapse secondary AC list , B4E2G0, Q14633, Q15469, Q6ISX9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries