P78552 (I13R1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin-13 receptor subunit alpha-1
Short name=IL-13 receptor subunit alpha-1
Short name=IL-13R subunit alpha-1
Short name=IL-13R-alpha-1
Short name=IL-13RA1

Alternative name(s):
Cancer/testis antigen 19
Short name=CT19
CD_antigen=CD213a1

Gene names

Name:	IL13RA1
Synonyms:	IL13R, IL13RA

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	427 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 with low affinity to interleukin-13 (IL13). Together with IL4RA can form a functional receptor for IL13. Also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity.
Subunit structure	Interleukin-13 receptor is a complex of IL4R, IL13RA1, and possibly other components. Interacts with TRAF3IP1. Ref.9 Ref.10
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Ubiquitous. Highest levels in heart, liver, skeletal muscle and ovary; lowest levels in brain, lung and kidney. Also found in B-cells, T-cells and endothelial cells.
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.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokine-mediated signaling pathway Inferred from electronic annotation. Source: GOC
Cellular_component	interleukin-13 receptor complex Traceable author statement Ref.1. Source: ProtInc
Molecular_function	cytokine receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IL13	P35225	4	EBI-1391535,EBI-1647828
IL4	P05112	3	EBI-1391535,EBI-367025
TRAF3IP1	Q8TDR0	3	EBI-1391535,EBI-928811

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 427

406

Interleukin-13 receptor subunit alpha-1

PRO_0000010939

Regions

Topological domain

22 – 343

322

Extracellular Potential

Transmembrane

344 – 367

24

Helical; Potential

Topological domain

368 – 427

60

Cytoplasmic Potential

Motif

327 – 331

5

WSXWS motif

Motif

374 – 382

9

Box 1 motif

Amino acid modifications

Glycosylation

37

1

N-linked (GlcNAc...) Potential

Glycosylation

61

1

N-linked (GlcNAc...) Potential

Glycosylation

105

1

N-linked (GlcNAc...) Potential

Glycosylation

138

1

N-linked (GlcNAc...) Potential

Glycosylation

157

1

N-linked (GlcNAc...) Potential

Glycosylation

235

1

N-linked (GlcNAc...) Potential

Glycosylation

265

1

N-linked (GlcNAc...) Potential

Glycosylation

293

1

N-linked (GlcNAc...) Potential

Glycosylation

329

1

N-linked (GlcNAc...) Potential

Glycosylation

341

1

N-linked (GlcNAc...) Potential

Disulfide bond

62 ↔ 102

Ref.10

Disulfide bond

95 ↔ 117

Ref.10

Disulfide bond

134 ↔ 144

Ref.10

Disulfide bond

173 ↔ 185

Ref.10

Disulfide bond

257 ↔ 320

Ref.10

Disulfide bond

282 ↔ 296

Ref.10

Experimental info

Sequence conflict

130

1

T → I in AAB37127. Ref.3

Sequence conflict

358

1

G → D in AAB37127. Ref.3

Secondary structure

1

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427

Helix Strand Turn

Details...

Beta strand

36 – 43

8

Turn

44 – 46

3

Beta strand

47 – 53

7

Beta strand

66 – 68

3

Helix

71 – 73

3

Beta strand

77 – 87

11

Beta strand

94 – 100

7

Beta strand

114 – 118

5

Turn

125 – 127

3

Beta strand

130 – 137

8

Turn

138 – 140

3

Beta strand

141 – 147

7

Beta strand

158 – 166

9

Beta strand

176 – 179

4

Beta strand

182 – 188

7

Beta strand

202 – 208

7

Beta strand

216 – 220

5

Beta strand

222 – 227

6

Beta strand

232 – 239

8

Beta strand

242 – 248

7

Helix

255 – 257

3

Beta strand

258 – 265

8

Turn

267 – 270

4

Beta strand

272 – 278

7

Beta strand

292 – 299

8

Beta strand

308 – 316

9

Turn

318 – 320

3

Beta strand

334 – 337

4

Sequences

	Sequence		Length	Mass (Da)
	P78552 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 5983B3E8F554107B	FASTA	427	48,760
	10 20 30 40 50 60 MEWPARLCGL WALLLCAGGG GGGGGAAPTE TQPPVTNLSV SVENLCTVIW TWNPPEGASS 70 80 90 100 110 120 NCSLWYFSHF GDKQDKKIAP ETRRSIEVPL NERICLQVGS QCSTNESEKP SILVEKCISP 130 140 150 160 170 180 PEGDPESAVT ELQCIWHNLS YMKCSWLPGR NTSPDTNYTL YYWHRSLEKI HQCENIFREG 190 200 210 220 230 240 QYFGCSFDLT KVKDSSFEQH SVQIMVKDNA GKIKPSFNIV PLTSRVKPDP PHIKNLSFHN 250 260 270 280 290 300 DDLYVQWENP QNFISRCLFY EVEVNNSQTE THNVFYVQEA KCENPEFERN VENTSCFMVP 310 320 330 340 350 360 GVLPDTLNTV RIRVKTNKLC YEDDKLWSNW SQEMSIGKKR NSTLYITMLL IVPVIVAGAI 370 380 390 400 410 420 IVLLLYLKRL KIIIFPPIPD PGKIFKEMFG DQNDDTLHWK KYDIYEKQTK EETDSVVLIE NLKKASQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the human IL-13R alpha1 chain and reconstitution with the IL4R alpha of a functional IL-4/IL-13 receptor complex." Miloux B., Laurent P., Bonnin O., Lupker J., Caput D., Vita N., Ferrara P. FEBS Lett. 401:163-166(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Carcinoma.
[2]	Gauchat J.-F., Schlagenhauf E., Feng N.P., Moser R., Yamage M., Jeannin P., Alouani S., Elson G., Notarangelo L.D., Wells T., Eugster H.P., Bonnefoy J.-Y. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: B-cell.
[3]	"cDNA cloning and characterization of the human interleukin 13 receptor alpha chain." Aman M.J., Tayebi N., Obiri N.I., Puri R.K., Modi W.S., Leonard W.J. J. Biol. Chem. 271:29265-29270(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: T-cell.
[4]	Wada M., Hisano T., Kuwano M. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. , 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]. Tissue: Hippocampus.
[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]	Mural R.J., Istrail S., Sutton 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].
[8]	"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: Pancreas.
[9]	"MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network." Ling L., Goeddel D.V. J. Biol. Chem. 275:23852-23860(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRAF3IP1.
[10]	"Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system." LaPorte S.L., Juo Z.S., Vaclavikova J., Colf L.A., Qi X., Heller N.M., Keegan A.D., Garcia K.C. Cell 132:259-272(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 29-342 IN COMPLEXES WITH IL4; IL4RA AND IL13, DISULFIDE BONDS, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y10659 mRNA. Translation: CAA71669.1.
Y09328 mRNA. Translation: CAA70508.1.
U62858 mRNA. Translation: AAB37127.1.
U81379 mRNA. Translation: AAD00510.3.
AK313467 mRNA. Translation: BAG36253.1.
AL391280 Genomic DNA. Translation: CAI41410.1.
CH471161 Genomic DNA. Translation: EAW89893.1.
BC009960 mRNA. Translation: AAH09960.1.

IPI

IPI00020354.

RefSeq

NP_001551.1. NM_001560.2.

UniGene

Hs.496646.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BPN	X-ray	3.02	C	29-342	[»]
3BPO	X-ray	3.00	C	29-342	[»]
4HWB	X-ray	2.61	A	223-336	[»]

ProteinModelPortal

P78552.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3225N.

IntAct

P78552. 6 interactions.

STRING

9606.ENSP00000360730.

PTM databases

PhosphoSite

P78552.

Polymorphism databases

DMDM

2494718.

Proteomic databases

PaxDb

P78552.

PRIDE

P78552.

Protocols and materials databases

DNASU

3597.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371666; ENSP00000360730; ENSG00000131724.

GeneID

3597.

KEGG

hsa:3597.

UCSC

uc004eqs.3. human.

Organism-specific databases

CTD

3597.

GeneCards

GC0XP117861.

HGNC

HGNC:5974. IL13RA1.

HPA

HPA001008.
HPA001587.

MIM

300119. gene.

neXtProt

NX_P78552.

PharmGKB

PA200.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG44457.

HOGENOM

HOG000230941.

HOVERGEN

HBG052060.

InParanoid

P78552.

KO

K05076.

OMA

EDDKLWS.

OrthoDB

EOG4PZJ6P.

PhylomeDB

P78552.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.

Gene expression databases

ArrayExpress

P78552.

Bgee

P78552.

CleanEx

HS_IL13RA1.

Genevestigator

P78552.

GermOnline

ENSG00000131724. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 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. 2 hits.

PROSITE

PS01356. HEMATOPO_REC_S_F2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

IL13RA1. human.

EvolutionaryTrace

P78552.

GenomeRNAi

3597.

NextBio

14057.

SOURCE

Search...

Entry information

Entry name

I13R1_HUMAN

Accession

Primary (citable) accession number: P78552
Secondary accession number(s): O95646, Q5JSL4, Q99656

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 126 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.