I22R2_MOUSE
ID I22R2_MOUSE Reviewed; 230 AA.
AC Q80XF5; Q3UU14; Q7TNI5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Interleukin-22 receptor subunit alpha-2;
DE Short=IL-22 receptor subunit alpha-2;
DE Short=IL-22R-alpha-2;
DE Short=IL-22RA2;
DE AltName: Full=Cytokine receptor family type 2, soluble 1;
DE Short=CRF2-S1;
DE AltName: Full=Interleukin-22-binding protein;
DE Short=IL-22BP;
DE Short=IL22BP;
DE AltName: Full=ZcytoR16;
DE Flags: Precursor;
GN Name=Il22ra2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=12700595; DOI=10.1038/sj.gene.6363947;
RA Wei C.-C., Ho T.-W., Liang W.-G., Chen G.-Y., Chang M.-S.;
RT "Cloning and characterization of mouse IL-22 binding protein.";
RL Genes Immun. 4:204-211(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=15201862; DOI=10.1038/sj.gene.6364104;
RA Weiss B., Wolk K., Gruenberg B.H., Volk H.D., Sterry W., Asadullah K.,
RA Sabat R.;
RT "Cloning of murine IL-22 receptor alpha 2 and comparison with its human
RT counterpart.";
RL Genes Immun. 5:330-336(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP MUTAGENESIS OF TYR-66 AND ARG-118.
RX PubMed=19285080; DOI=10.1016/j.febslet.2009.03.006;
RA de Moura P.R., Watanabe L., Bleicher L., Colau D., Dumoutier L.,
RA Lemaire M.M., Renauld J.C., Polikarpov I.;
RT "Crystal structure of a soluble decoy receptor IL-22BP bound to
RT interleukin-22.";
RL FEBS Lett. 583:1072-1077(2009).
CC -!- FUNCTION: Receptor for IL22. Binds to IL22, prevents interaction with
CC the functional IL-22R complex and blocks the activity of IL22 (in
CC vitro). May play an important role as an IL22 antagonist in the
CC regulation of inflammatory responses. {ECO:0000269|PubMed:12700595}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12700595}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lymph nodes and at lower levels
CC in lung, spleen, and thymus. Not expressed in kidney, liver and heart.
CC {ECO:0000269|PubMed:15201862}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; AF493604; AAP13730.1; -; mRNA.
DR EMBL; AJ555484; CAD88474.1; -; mRNA.
DR EMBL; AK138913; BAE23815.1; -; mRNA.
DR EMBL; AC153862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23717.1; -.
DR RefSeq; NP_839989.2; NM_178258.5.
DR AlphaFoldDB; Q80XF5; -.
DR SMR; Q80XF5; -.
DR STRING; 10090.ENSMUSP00000042642; -.
DR iPTMnet; Q80XF5; -.
DR PhosphoSitePlus; Q80XF5; -.
DR PaxDb; Q80XF5; -.
DR PRIDE; Q80XF5; -.
DR ProteomicsDB; 269516; -.
DR Antibodypedia; 19779; 370 antibodies from 35 providers.
DR DNASU; 237310; -.
DR Ensembl; ENSMUST00000036564; ENSMUSP00000042642; ENSMUSG00000039760.
DR GeneID; 237310; -.
DR KEGG; mmu:237310; -.
DR UCSC; uc007enh.1; mouse.
DR CTD; 116379; -.
DR MGI; MGI:2665114; Il22ra2.
DR VEuPathDB; HostDB:ENSMUSG00000039760; -.
DR eggNOG; ENOG502S2NT; Eukaryota.
DR GeneTree; ENSGT00940000161124; -.
DR HOGENOM; CLU_081158_1_0_1; -.
DR InParanoid; Q80XF5; -.
DR OMA; SMENYYE; -.
DR OrthoDB; 1078220at2759; -.
DR PhylomeDB; Q80XF5; -.
DR TreeFam; TF332537; -.
DR BioGRID-ORCS; 237310; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q80XF5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q80XF5; protein.
DR Bgee; ENSMUSG00000039760; Expressed in peripheral lymph node and 26 other tissues.
DR Genevisible; Q80XF5; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0042017; F:interleukin-22 binding; ISO:MGI.
DR GO; GO:0042018; F:interleukin-22 receptor activity; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; IDA:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR Pfam; PF09294; Interfer-bind; 1.
DR Pfam; PF01108; Tissue_fac; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Receptor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..230
FT /note="Interleukin-22 receptor subunit alpha-2"
FT /id="PRO_0000011017"
FT DOMAIN 29..128
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 129..230
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT SITE 66
FT /note="Critical for IL22-binding"
FT SITE 118
FT /note="Critical for IL22-binding"
FT DISULFID 205..226
FT /evidence="ECO:0000250"
FT MUTAGEN 66
FT /note="Y->A: Abolishes IL22-binding."
FT /evidence="ECO:0000269|PubMed:19285080"
FT MUTAGEN 118
FT /note="R->A: Abolishes IL22-binding."
FT /evidence="ECO:0000269|PubMed:19285080"
FT CONFLICT 149
FT /note="E -> D (in Ref. 1; AAP13730)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="H -> Q (in Ref. 1; AAP13730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 26613 MW; 9AEBE4EDFBAFC105 CRC64;
MMPKHCLLGL LIILLSSATE IQPARVSLTP QKVRFQSRNF HNILHWQAGS SLPSNNSIYF
VQYKMYGQSQ WEDKVDCWGT TALFCDLTNE TLDPYELYYG RVMTACAGRH SAWTRTPRFT
PWWETKLDPP VVTITRVNAS LRVLLRPPEL PNRNQSGKNA SMETYYGLVY RVFTINNSLE
KEQKAYEGTQ RAVEIEGLIP HSSYCVVAEM YQPMFDRRSP RSKERCVHIP
