Q14627 (I13R2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	380 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	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.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	extracellular space Traceable author statement PubMed 9083087. Source: ProtInc integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytokine receptor activity Traceable author statement PubMed 9725226. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 380

354

Interleukin-13 receptor subunit alpha-2

PRO_0000010942

Regions

Topological domain

27 – 343

317

Extracellular Potential

Transmembrane

344 – 363

20

Helical; Potential

Topological domain

364 – 380

17

Cytoplasmic Potential

Domain

31 – 124

94

Fibronectin type-III 1

Domain

137 – 225

89

Fibronectin type-III 2

Domain

238 – 336

99

Fibronectin type-III 3

Motif

322 – 326

5

WSXWS motif

Amino acid modifications

Glycosylation

115

1

N-linked (GlcNAc...) Potential

Glycosylation

215

1

N-linked (GlcNAc...) Ref.8

Glycosylation

290

1

N-linked (GlcNAc...) Potential

Glycosylation

299

1

N-linked (GlcNAc...) Potential

Disulfide bond

65 ↔ 113

Ref.8

Disulfide bond

145 ↔ 155

Ref.8

Disulfide bond

184 ↔ 197

Ref.8

Disulfide bond

269 ↔ 316

Ref.8

Natural variations

Natural variant

111

1

W → R. Ref.5
Corresponds to variant rs17095919 [ dbSNP | Ensembl ].

VAR_021256

Experimental info

Sequence conflict

8

1

I → V in BAF84646. Ref.4

Sequence conflict

151

1

Q → R in BAF84646. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

380

Helix Strand Turn

Details...

Beta strand

36 – 41

6

Beta strand

44 – 54

11

Beta strand

68 – 75

8

Beta strand

82 – 94

13

Beta strand

101 – 108

8

Helix

111 – 114

4

Beta strand

115 – 117

3

Beta strand

124 – 128

5

Beta strand

141 – 148

8

Turn

149 – 151

3

Beta strand

152 – 158

7

Beta strand

168 – 174

7

Beta strand

185 – 189

5

Beta strand

193 – 198

6

Beta strand

206 – 208

3

Beta strand

210 – 218

9

Beta strand

226 – 230

5

Helix

232 – 234

3

Beta strand

242 – 245

4

Beta strand

256 – 259

4

Beta strand

262 – 264

3

Beta strand

270 – 275

6

Beta strand

287 – 291

5

Beta strand

308 – 312

5

Turn

314 – 316

3

Sequences

	Sequence		Length	Mass (Da)
	Q14627 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3C6ACB1B5562C887	FASTA	380	44,176
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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

SeattleSNPs

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.

IPI

IPI00032199.

RefSeq

NP_000631.1. NM_000640.2.

UniGene

Hs.336046.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LB6	X-ray	3.05	C/D	1-380	[»]

ProteinModelPortal

Q14627.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3340N.

IntAct

Q14627. 1 interaction.

STRING

9606.ENSP00000243213.

Polymorphism databases

DMDM

2494720.

Proteomic databases

PaxDb

Q14627.

PRIDE

Q14627.

Protocols and materials databases

DNASU

3598.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000243213; ENSP00000243213; ENSG00000123496.
ENST00000371936; ENSP00000361004; ENSG00000123496.
ENST00000599692; ENSP00000469027; ENSG00000268456.
ENST00000601634; ENSP00000471808; ENSG00000268456.

GeneID

3598.

KEGG

hsa:3598.

UCSC

uc004epx.3. human.

Organism-specific databases

CTD

3598.

GeneCards

GC0XM114238.

HGNC

HGNC:5975. IL13RA2.

MIM

300130. gene.

neXtProt

NX_Q14627.

PharmGKB

PA29788.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG47505.

HOGENOM

HOG000004823.

HOVERGEN

HBG058972.

InParanoid

Q14627.

KO

K05077.

OMA

FYWYEGL.

OrthoDB

EOG469QVQ.

PhylomeDB

Q14627.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.

Gene expression databases

Bgee

Q14627.

CleanEx

HS_IL13RA2.

Genevestigator

Q14627.

GermOnline

ENSG00000123496. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015321. IL6_recept-bd.
IPR003532. Short_hematopoietin_rcpt_2_CS.
[Graphical view]

Pfam

PF09240. IL6Ra-bind. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 3 hits.

PROSITE

PS50853. FN3. False negative.
PS01356. HEMATOPO_REC_S_F2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q14627.

GenomeRNAi

3598.

NextBio

14061.

SOURCE

Search...

Entry information

Entry name

I13R2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 130 of the entry and version 1 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.