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Q6PHB0 (I20RA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-20 receptor subunit alpha

Short name=IL-20 receptor subunit alpha
Short name=IL-20R-alpha
Short name=IL-20RA
Alternative name(s):
IL-20R1
Gene names
Name:Il20ra
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The IL20RA/IL20RB dimer is a receptor for IL19, IL20 and IL24. The IL20RA/IL10RB dimer is a receptor for IL26 By similarity.

Subunit structure

Heterodimer with IL20RB and heterodimer with IL10RB By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Sequence similarities

Belongs to the type II cytokine receptor family.

Contains 2 fibronectin type-III domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 546514Interleukin-20 receptor subunit alpha
PRO_0000011037

Regions

Topological domain33 – 253221Extracellular Potential
Transmembrane254 – 27421Helical; Potential
Topological domain275 – 546272Cytoplasmic Potential
Domain42 – 13897Fibronectin type-III 1
Domain139 – 245107Fibronectin type-III 2

Amino acid modifications

Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Disulfide bond90 ↔ 98 By similarity
Disulfide bond218 ↔ 239 By similarity

Experimental info

Sequence conflict1451V → I in AAH56628. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6PHB0 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: E7EC07DA2D49AF7F

FASTA54661,978
        10         20         30         40         50         60 
MHTPGTPAPG HPDPPPLLLL TLLLLLAASG RAVPCVFCGL PKPTNITFLS INMKNVLHWN 

        70         80         90        100        110        120 
PPESLHGVEV TYTVQYFIYG QKKWLNASKC GSINRTYCDL SVETSDYEHQ FYAKVKAIWE 

       130        140        150        160        170        180 
ARCSEWAETE RFYPFLETQV SPPEVALTTG EKSISIALTA PEKWKRNPQD HTVSMQQIYP 

       190        200        210        220        230        240 
NLKYNVSVYN TKSRRTWSQC VTNSTLVLSW LEPNTLYCVH VESLVPGPPR LPMPSQKQCI 

       250        260        270        280        290        300 
STLEVQTSAW KAKVIFWYVF LTSVIVFLFS AIGYLVYRYI HVGKEKHPAN LVLIYRNEIG 

       310        320        330        340        350        360 
TRVFEPTETI TLNFITFSML DDTKISPKDM NLLDKSSDDI SVNDPEHNEA WEPHWEEVEG 

       370        380        390        400        410        420 
QHLGCSSHLM DAVCGAEQRD GDTSLTQHGW LNSTIPTGET DTEPQYKVLS DFYGEGEIQL 

       430        440        450        460        470        480 
SCEPEEAART EKISEPLVTS ANLDPQLEDL HHLGQEHTVS EDGPEEETSI TVVDWDPQTG 

       490        500        510        520        530        540 
RLCIPSLPIF GRDPENYGHY ERDQLLEGGL LSRLYENQAP DKPEKENENC LTRFMEEWGL 


HVQMES 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Oviduct.
[2]"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].
Strain: 129.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK054215 mRNA. Translation: BAC35695.1.
BC056628 mRNA. Translation: AAH56628.1.
CCDSCCDS23718.1.
RefSeqNP_766374.1. NM_172786.2.
XP_006512789.1. XM_006512726.1.
XP_006512790.1. XM_006512727.1.
UniGeneMm.234667.

3D structure databases

ProteinModelPortalQ6PHB0.
SMRQ6PHB0. Positions 42-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000020185.

PTM databases

PhosphoSiteQ6PHB0.

Proteomic databases

PRIDEQ6PHB0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020185; ENSMUSP00000020185; ENSMUSG00000020007.
GeneID237313.
KEGGmmu:237313.
UCSCuc007eni.1. mouse.

Organism-specific databases

CTD53832.
MGIMGI:3605069. Il20ra.

Phylogenomic databases

eggNOGNOG25594.
GeneTreeENSGT00530000063352.
HOGENOMHOG000112987.
HOVERGENHBG052065.
InParanoidQ6PHB0.
KOK05136.
OMAQFMEEWG.
OrthoDBEOG7C2R12.
PhylomeDBQ6PHB0.
TreeFamTF334107.

Gene expression databases

BgeeQ6PHB0.
CleanExMM_IL20RA.
GenevestigatorQ6PHB0.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015713. IL-20_rcpt_alpha.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
[Graphical view]
PANTHERPTHR20859:SF21. PTHR20859:SF21. 1 hit.
PfamPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio383294.
PROQ6PHB0.
SOURCESearch...

Entry information

Entry nameI20RA_MOUSE
AccessionPrimary (citable) accession number: Q6PHB0
Secondary accession number(s): Q8BW64
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 9, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot