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Q14627 (I13R2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-13 receptor subunit alpha-2

Short name=IL-13 receptor subunit alpha-2
Short name=IL-13R subunit alpha-2
Short name=IL-13R-alpha-2
Short name=IL-13RA2
Alternative name(s):
Interleukin-13-binding protein
CD_antigen=CD213a2
Gene names
Name:IL13RA2
Synonyms:IL13R
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds as a monomer with high affinity to interleukin-13 (IL13), but not to interleukin-4 (IL4). Ref.8

Subcellular location

Membrane; Single-pass type I membrane protein.

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 3 fibronectin type-III domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 380354Interleukin-13 receptor subunit alpha-2
PRO_0000010942

Regions

Topological domain27 – 343317Extracellular Potential
Transmembrane344 – 36320Helical; Potential
Topological domain364 – 38017Cytoplasmic Potential
Domain34 – 134101Fibronectin type-III 1
Domain139 – 23597Fibronectin type-III 2
Domain240 – 33394Fibronectin type-III 3
Motif322 – 3265WSXWS motif

Amino acid modifications

Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Ref.8
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Disulfide bond65 ↔ 113 Ref.8
Disulfide bond145 ↔ 155 Ref.8
Disulfide bond184 ↔ 197 Ref.8
Disulfide bond269 ↔ 316 Ref.8

Natural variations

Natural variant1111W → R. Ref.5
Corresponds to variant rs17095919 [ dbSNP | Ensembl ].
VAR_021256

Experimental info

Sequence conflict81I → V in BAF84646. Ref.4
Sequence conflict1511Q → R in BAF84646. Ref.4

Secondary structure

................................................. 380
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14627 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3C6ACB1B5562C887

FASTA38044,176
        10         20         30         40         50         60 
MAFVCLAIGC LYTFLISTTF GCTSSSDTEI KVNPPQDFEI VDPGYLGYLY LQWQPPLSLD 

        70         80         90        100        110        120 
HFKECTVEYE LKYRNIGSET WKTIITKNLH YKDGFDLNKG IEAKIHTLLP WQCTNGSEVQ 

       130        140        150        160        170        180 
SSWAETTYWI SPQGIPETKV QDMDCVYYNW QYLLCSWKPG IGVLLDTNYN LFYWYEGLDH 

       190        200        210        220        230        240 
ALQCVDYIKA DGQNIGCRFP YLEASDYKDF YICVNGSSEN KPIRSSYFTF QLQNIVKPLP 

       250        260        270        280        290        300 
PVYLTFTRES SCEIKLKWSI PLGPIPARCF DYEIEIREDD TTLVTATVEN ETYTLKTTNE 

       310        320        330        340        350        360 
TRQLCFVVRS KVNIYCSDDG IWSEWSDKQC WEGEDLSKKT LLRFWLPFGF ILILVIFVTG 

       370        380 
LLLRKPNTYP KMIPEFFCDT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a specific interleukin (IL)-13 binding protein structurally related to the IL-5 receptor alpha chain."
Caput D., Laurent P., Kaghad M., Lelias J.M., Lefort S., Vita N., Ferrara P.
J. Biol. Chem. 271:16921-16926(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Renal cell carcinoma.
[2]"Identification of a third chain for the murine Il-13 receptor."
Donaldson D.D., Whitters M.J., Fitz L., Neben T., Finnerty H., Henderson S.L., O'Hara R.M. Jr., Turner K.J., Wood C.R., Collins M.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[3]"Chromosome mapping and expression of the human interleukin-13 receptor."
Guo J., Apiou F., Mellerin M.P., Lebeau B., Jacques Y., Minvielle S.
Genomics 42:141-145(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[4]"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].
[5]SeattleSNPs variation discovery resource
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-111.
[6]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
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].
Tissue: Lung and Prostate.
[8]"Molecular basis for shared cytokine recognition revealed in the structure of an unusually high affinity complex between IL-13 and IL-13Ralpha2."
Lupardus P.J., Birnbaum M.E., Garcia K.C.
Structure 18:332-342(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH IL13, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-215.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95302 mRNA. Translation: CAA64617.1.
U70981 mRNA. Translation: AAB17170.1.
Y08768 mRNA. Translation: CAA70021.1.
AK291957 mRNA. Translation: BAF84646.1.
AY656702 Genomic DNA. Translation: AAT49099.1.
AL121878 Genomic DNA. Translation: CAD18962.1.
BC020739 mRNA. Translation: AAH20739.1.
BC033705 mRNA. Translation: AAH33705.1.
RefSeqNP_000631.1. NM_000640.2.
UniGeneHs.336046.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LB6X-ray3.05C/D1-380[»]
ProteinModelPortalQ14627.
SMRQ14627. Positions 29-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109812. 1 interaction.
DIPDIP-3340N.
IntActQ14627. 1 interaction.
STRING9606.ENSP00000243213.

Polymorphism databases

DMDM2494720.

Proteomic databases

PaxDbQ14627.
PRIDEQ14627.

Protocols and materials databases

DNASU3598.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243213; ENSP00000243213; ENSG00000123496.
ENST00000371936; ENSP00000361004; ENSG00000123496.
ENST00000599692; ENSP00000469027; ENSG00000268456.
ENST00000601634; ENSP00000471808; ENSG00000268456.
GeneID3598.
KEGGhsa:3598.
UCSCuc004epx.3. human.

Organism-specific databases

CTD3598.
GeneCardsGC0XM114238.
HGNCHGNC:5975. IL13RA2.
HPAHPA055552.
MIM300130. gene.
neXtProtNX_Q14627.
PharmGKBPA29788.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47505.
HOGENOMHOG000004823.
HOVERGENHBG058972.
InParanoidQ14627.
KOK05077.
OMAFYWYEGL.
OrthoDBEOG71P2B1.
PhylomeDBQ14627.
TreeFamTF331549.

Enzyme and pathway databases

SignaLinkQ14627.

Gene expression databases

BgeeQ14627.
CleanExHS_IL13RA2.
GenevestigatorQ14627.

Family and domain databases

Gene3D2.60.40.10. 3 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. 3 hits.
PROSITEPS50853. FN3. 3 hits.
PS01356. HEMATOPO_REC_S_F2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14627.
GeneWikiIL13RA2.
GenomeRNAi3598.
NextBio14061.
PROQ14627.
SOURCESearch...

Entry information

Entry nameI13R2_HUMAN
AccessionPrimary (citable) accession number: Q14627
Secondary accession number(s): A8K7E2, O00667
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 141 of the entry and version 1 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 X

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

Human cell differentiation molecules

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