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Protein

Interleukin-22 receptor subunit alpha-2

Gene

Il22ra2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for IL22. Binds to IL22, prevents interaction with the functional IL-22R complex and blocks the activity of IL22 (in vitro). May play an important role as an IL22 antagonist in the regulation of inflammatory responses.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei66 – 661Critical for IL22-binding
Sitei118 – 1181Critical for IL22-binding

GO - Molecular functioni

GO - Biological processi

  • cytokine-mediated signaling pathway Source: MGI
  • negative regulation of inflammatory response Source: MGI
  • regulation of tyrosine phosphorylation of Stat3 protein Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiR-MMU-8854691. Interleukin-19, 20, 22, 24.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-22 receptor subunit alpha-2
Short name:
IL-22 receptor subunit alpha-2
Short name:
IL-22R-alpha-2
Short name:
IL-22RA2
Alternative name(s):
Cytokine receptor family type 2, soluble 1
Short name:
CRF2-S1
Interleukin-22-binding protein
Short name:
IL-22BP
Short name:
IL22BP
ZcytoR16
Gene namesi
Name:Il22ra2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2665114. Il22ra2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661Y → A: Abolishes IL22-binding. 1 Publication
Mutagenesisi118 – 1181R → A: Abolishes IL22-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 230210Interleukin-22 receptor subunit alpha-2PRO_0000011017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi205 ↔ 226By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ80XF5.
PRIDEiQ80XF5.

PTM databases

iPTMnetiQ80XF5.

Expressioni

Tissue specificityi

Highly expressed in lymph nodes and at lower levels in lung, spleen, and thymus. Not expressed in kidney, liver and heart.1 Publication

Gene expression databases

CleanExiMM_IL22RA2.
GenevisibleiQ80XF5. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000042642.

Structurei

3D structure databases

ProteinModelPortaliQ80XF5.
SMRiQ80XF5. Positions 27-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 128100Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini129 – 230102Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the type II cytokine receptor family.Curated
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IVX1. Eukaryota.
ENOG410YNE2. LUCA.
GeneTreeiENSGT00530000063352.
HOGENOMiHOG000082681.
HOVERGENiHBG052067.
InParanoidiQ80XF5.
KOiK05139.
OMAiPYYGRVR.
OrthoDBiEOG7C2R12.
TreeFamiTF332537.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80XF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMPKHCLLGL LIILLSSATE IQPARVSLTP QKVRFQSRNF HNILHWQAGS
60 70 80 90 100
SLPSNNSIYF VQYKMYGQSQ WEDKVDCWGT TALFCDLTNE TLDPYELYYG
110 120 130 140 150
RVMTACAGRH SAWTRTPRFT PWWETKLDPP VVTITRVNAS LRVLLRPPEL
160 170 180 190 200
PNRNQSGKNA SMETYYGLVY RVFTINNSLE KEQKAYEGTQ RAVEIEGLIP
210 220 230
HSSYCVVAEM YQPMFDRRSP RSKERCVHIP
Length:230
Mass (Da):26,613
Last modified:October 3, 2012 - v2
Checksum:i9AEBE4EDFBAFC105
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491E → D in AAP13730 (PubMed:12700595).Curated
Sequence conflicti228 – 2281H → Q in AAP13730 (PubMed:12700595).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF493604 mRNA. Translation: AAP13730.1.
AJ555484 mRNA. Translation: CAD88474.1.
AK138913 mRNA. Translation: BAE23815.1.
AC153862 Genomic DNA. No translation available.
CCDSiCCDS23717.1.
RefSeqiNP_839989.2. NM_178258.5.
UniGeneiMm.331979.

Genome annotation databases

EnsembliENSMUST00000036564; ENSMUSP00000042642; ENSMUSG00000039760.
GeneIDi237310.
KEGGimmu:237310.
UCSCiuc007enh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF493604 mRNA. Translation: AAP13730.1.
AJ555484 mRNA. Translation: CAD88474.1.
AK138913 mRNA. Translation: BAE23815.1.
AC153862 Genomic DNA. No translation available.
CCDSiCCDS23717.1.
RefSeqiNP_839989.2. NM_178258.5.
UniGeneiMm.331979.

3D structure databases

ProteinModelPortaliQ80XF5.
SMRiQ80XF5. Positions 27-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000042642.

PTM databases

iPTMnetiQ80XF5.

Proteomic databases

PaxDbiQ80XF5.
PRIDEiQ80XF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036564; ENSMUSP00000042642; ENSMUSG00000039760.
GeneIDi237310.
KEGGimmu:237310.
UCSCiuc007enh.1. mouse.

Organism-specific databases

CTDi116379.
MGIiMGI:2665114. Il22ra2.

Phylogenomic databases

eggNOGiENOG410IVX1. Eukaryota.
ENOG410YNE2. LUCA.
GeneTreeiENSGT00530000063352.
HOGENOMiHOG000082681.
HOVERGENiHBG052067.
InParanoidiQ80XF5.
KOiK05139.
OMAiPYYGRVR.
OrthoDBiEOG7C2R12.
TreeFamiTF332537.

Enzyme and pathway databases

ReactomeiR-MMU-8854691. Interleukin-19, 20, 22, 24.

Miscellaneous databases

PROiQ80XF5.
SOURCEiSearch...

Gene expression databases

CleanExiMM_IL22RA2.
GenevisibleiQ80XF5. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of mouse IL-22 binding protein."
    Wei C.-C., Ho T.-W., Liang W.-G., Chen G.-Y., Chang M.-S.
    Genes Immun. 4:204-211(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: BALB/cJ.
  2. "Cloning of murine IL-22 receptor alpha 2 and comparison with its human counterpart."
    Weiss B., Wolk K., Gruenberg B.H., Volk H.D., Sterry W., Asadullah K., Sabat R.
    Genes Immun. 5:330-336(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Spleen.
  3. "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.
    , 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: Aorta and Vein.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22."
    de Moura P.R., Watanabe L., Bleicher L., Colau D., Dumoutier L., Lemaire M.M., Renauld J.C., Polikarpov I.
    FEBS Lett. 583:1072-1077(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-66 AND ARG-118.

Entry informationi

Entry nameiI22R2_MOUSE
AccessioniPrimary (citable) accession number: Q80XF5
Secondary accession number(s): Q3UU14, Q7TNI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.