Interleukin-2 receptor alpha chain precursor

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Reviewed, UniProtKB/Swiss-Prot P01589 (IL2RA_HUMAN)

Last modified July 22, 2008. Version 101. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Interleukin-2 receptor alpha chain
      Short name=IL-2 receptor alpha subunit
      Short name=IL-2-RA
      Short name=IL2-RA
Alternative name(s):
    p55
    TAC antigen
    CD_antigen=CD25

Gene names

Name:

IL2RA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	272 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Receptor for interleukin-2.
Subunit structure	Non-covalent dimer of an alpha and a beta chains. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta chain), and a low affinity monomer (alpha chain). The high and intermediate affinity forms also associate with a gamma chain.
Subcellular location	Membrane; Single-pass type I membrane protein.
Involvement in disease	Genetic variations in IL2RA are associated with susceptibility to insulin-dependent diabetes mellitus type 10 (IDDM10) [MIM:601942].
Sequence similarities	Contains 2 Sushi (CCP/SCR) domains.

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Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Sushi Transmembrane
Molecular function	Receptor
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	apoptosis Traceable author statement. Source: ProtInc cell proliferation Traceable author statement. Source: ProtInc cell surface receptor linked signal transduction Traceable author statement. Source: ProtInc immune response Traceable author statement. Source: ProtInc
Cellular component	plasma membrane Traceable author statement. Source: ProtInc
Molecular function	interleukin-2 receptor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 21

Chain

22 – 272

251

Interleukin-2 receptor alpha chain

Regions

Topological domain

22 – 240

219

Extracellular Potential

Transmembrane

241 – 259

Potential

Topological domain

260 – 272

Cytoplasmic Potential

Domain

22 – 84

Sushi 1

Domain

123 – 186

Sushi 2

Amino acid modifications

Glycosylation

N-linked (GlcNAc...)

Glycosylation

N-linked (GlcNAc...)

Glycosylation

218

O-linked (GalNAc...)

Glycosylation

224

O-linked (GalNAc...)

Glycosylation

229

O-linked (GalNAc...)

Glycosylation

237

O-linked (GalNAc...)

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

272

I → T: dbSNP rs12722712.

Secondary structure

272

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P01589-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 83D907C8C81D2C0E
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FASTA

272

30,819

        10         20         30         40         50         60 
MDSYLLMWGL LTFIMVPGCQ AELCDDDPPE IPHATFKAMA YKEGTMLNCE CKRGFRRIKS 

        70         80         90        100        110        120 
GSLYMLCTGN SSHSSWDNQC QCTSSATRNT TKQVTPQPEE QKERKTTEMQ SPMQPVDQAS 

       130        140        150        160        170        180 
LPGHCREPPP WENEATERIY HFVVGQMVYY QCVQGYRALH RGPAESVCKM THGKTRWTQP 

       190        200        210        220        230        240 
QLICTGEMET SQFPGEEKPQ ASPEGRPESE TSCLVTTTDF QIQTEMAATM ETSIFTTEYQ 

       250        260        270 
VAVAGCVFLL ISVLLLSGLT WQRRQRKSRR TI

« Hide

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References

[1]	"Molecular cloning of cDNA encoding human interleukin-2 receptor." Nikaido T., Shimizu A., Ishida N., Sabe H., Teshigawara K., Maeda M., Uchiyama T., Yodoi J., Honjo T. Nature 311:631-635(1984) [PubMed: 6090949] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning and expression of cDNAs for the human interleukin-2 receptor." Leonard W.J., Depper J.M., Crabtree G.R., Rudikoff S., Pumphrey J., Robb R.J., Kroenke M., Svetlik P.B., Peffer N.J., Waldmann T.A., Greene W.C. Nature 311:626-631(1984) [PubMed: 6090948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Molecular cloning and structure of the human interleukin 2 receptor gene." Ishida N., Kanamori H., Noma T., Nikaido T., Sabe H., Suzuki N., Shimizu A., Honjo T. Nucleic Acids Res. 13:7579-7589(1985) [PubMed: 2999698] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structure of the human interleukin-2 receptor gene." Leonard W.J., Depper J.M., Kanehisa M., Kroenke M., Peffer N.J., Svetlik P.B., Sullivan M., Greene W.C. Science 230:633-639(1985) [PubMed: 2996141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	SeattleSNPs program for genomic applications Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-272.
[6]	"Regulation of the human interleukin-2 receptor alpha chain promoter: activation of a nonfunctional promoter by the transactivator gene of HTLV-I." Cross S.L., Feinberg M.B., Wolf J.B., Holbrook N.J., Wong-Stall F., Leonard W.J. Cell 49:47-56(1987) [PubMed: 3030566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[7]	"Structural analysis of recombinant soluble human interleukin-2 receptor. Primary structure, assignment of disulfide bonds and core IL-2 binding structure." Miedel M.C., Hulmes J.D., Weber D.V., Bailon P., Pan Y.C. Biochem. Biophys. Res. Commun. 154:372-379(1988) [PubMed: 3134887] [Abstract] Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-89; THR-218; THR-224; THR-229 AND THR-237.
[8]	"The interleukin-2 and interleukin-4 receptors studied by molecular modelling." Bamborough P., Hedgecock C.J., Richards W.G. Structure 2:839-851(1994) [PubMed: 7529123] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 23-83.
[9]	"Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors." Wang X., Rickert M., Garcia K.C. Science 310:1159-1163(2005) [PubMed: 16293754] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-238 IN COMPLEX WITH IL2; IL2RB AND IL2RC, DISULFIDE BONDS.
[10]	"Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor." Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A. Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006) [PubMed: 16477002] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-233 IN COMPLEX WITH IL2; IL2RB AND IL2RC, DISULFIDE BONDS.
[11]	"Large-scale genetic fine mapping and genotype-phenotype associations implicate polymorphism in the IL2RA region in type 1 diabetes." Lowe C.E., Cooper J.D., Brusko T., Walker N.M., Smyth D.J., Bailey R., Bourget K., Plagnol V., Field S., Atkinson M., Clayton D.G., Wicker L.S., Todd J.A. Nat. Genet. 39:1074-1082(2007) [PubMed: 17676041] [Abstract] Cited for: INVOLVEMENT IN NIDDM10.
+	Additional computationally mapped references.

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Web resources

IL2RAbase

IL2RA mutation db

SeattleSNPs

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Cross-references

Sequence databases

X01057 mRNA. Translation: CAA25525.1.
X03131

X03138 Genomic DNA. Translation: CAA26906.1.
K03122 mRNA. Translation: AAB59535.1. Sequence problems.
M11066

M11065 Genomic DNA. Translation: AAA67527.1.
AY563103 Genomic DNA. Translation: AAS55572.1.
M15864 Genomic DNA. Translation: AAA59162.1.

PIR

UHHU2. A44186.

RefSeq

NP_000408.1.

UniGene

Hs.231367

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ILM	model	-	A	23-83	[»]
1ILN	model	-	A	23-83	[»]
1Z92	X-ray	2.80	B	22-238	[»]
2B5I	X-ray	2.30	D	22-238	[»]
2ERJ	X-ray	3.00	A/E	22-233	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1080N.

PTM databases

PhosphoSite

P01589.

Genome annotation databases

Ensembl

ENSG00000134460. Homo sapiens. [Contig view]

GeneID

3559.

KEGG

hsa:3559.

Organism-specific databases

H-InvDB

HIX0035309.

HGNC

HGNC:6008. IL2RA.

HPA

CAB002419.

MIM

147730. gene.
601942. phenotype.
606367. phenotype.

PharmGKB

PA29828.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P01589.

HOVERGEN

P01589.

Gene expression databases

ArrayExpress

P01589.

CleanEx

HS_IL2RA.

GermOnline

ENSG00000134460. Homo sapiens.

Family and domain databases

InterPro

IPR016060. Complement_control_module.
IPR015486. IL-2_recpt_a.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Gene3D

G3DSA:2.10.70.10. Complement_control_module. 1 hit.

PANTHER

PTHR10573. IL-2_recpt_a. 1 hit.

Pfam

PF00084. Sushi. 2 hits.
[Graphical view]

SMART

SM00032. CCP. 2 hits.
[Graphical view]

PROSITE

PS50923. SUSHI. 2 hits.
[Graphical view]

BLOCKS

Search...

Other Resources

DrugBank

DB00041. Aldesleukin.
DB00074. Basiliximab.
DB00111. Daclizumab.
DB00004. Denileukin diftitox.

LinkHub

P01589.

SOURCE

Search...

ProtoNet

Search...

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Entry information

Entry name

IL2RA_HUMAN

Accession

Primary (citable) accession number: P01589

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	July 22, 2008
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human cell differentiation molecules

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

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents