I13R2_MOUSE
ID I13R2_MOUSE Reviewed; 383 AA.
AC O88786; A3F812; Q3V2V5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Interleukin-13 receptor subunit alpha-2;
DE Short=IL-13 receptor subunit alpha-2;
DE Short=IL-13R subunit alpha-2;
DE Short=IL-13R-alpha-2;
DE Short=IL-13RA2;
DE AltName: CD_antigen=CD213a2;
DE Flags: Precursor;
GN Name=Il13ra2;
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] (ISOFORM 1), AND FUNCTION.
RC STRAIN=C3H/HeJ; TISSUE=Thymus;
RX PubMed=9725226;
RA Donaldson D.D., Whitters M.J., Fitz L., Neben T.Y., Finnerty H.,
RA Henderson S.L., O'Hara R.M. Jr., Beier D.R., Turner K.J., Wood C.R.,
RA Collins M.;
RT "The murine IL-13 receptor alpha 2: molecular cloning, characterization,
RT and comparison with murine IL-13 receptor alpha 1.";
RL J. Immunol. 161:2317-2324(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=17114462; DOI=10.4049/jimmunol.177.11.7905;
RA Tabata Y., Chen W., Warrier M.R., Gibson A.M., Daines M.O., Hershey G.K.;
RT "Allergy-driven alternative splicing of IL-13 receptor alpha2 yields
RT distinct membrane and soluble forms.";
RL J. Immunol. 177:7905-7912(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Spleen;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds as a monomer with high affinity to interleukin-13
CC (IL13). {ECO:0000269|PubMed:9725226}.
CC -!- INTERACTION:
CC O88786; Q61362: Chi3l1; NbExp=12; IntAct=EBI-20260800, EBI-8392424;
CC O88786; P20109: Il13; NbExp=4; IntAct=EBI-20260800, EBI-20559598;
CC O88786; P16110: Lgals3; NbExp=2; IntAct=EBI-20260800, EBI-3508325;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88786-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88786-2; Sequence=VSP_037588, VSP_037589;
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
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DR EMBL; U65747; AAC33240.1; -; mRNA.
DR EMBL; EF219410; ABN11267.1; -; mRNA.
DR EMBL; AK089687; BAE43400.1; -; mRNA.
DR EMBL; AL662932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466610; EDL14709.1; -; Genomic_DNA.
DR EMBL; BC003723; AAH03723.1; -; mRNA.
DR CCDS; CCDS30460.1; -. [O88786-1]
DR RefSeq; NP_001292988.1; NM_001306059.1. [O88786-2]
DR RefSeq; NP_032382.1; NM_008356.4. [O88786-1]
DR RefSeq; XP_006528770.1; XM_006528707.3. [O88786-1]
DR RefSeq; XP_006528771.1; XM_006528708.3. [O88786-1]
DR RefSeq; XP_017173884.1; XM_017318395.1. [O88786-2]
DR AlphaFoldDB; O88786; -.
DR SMR; O88786; -.
DR BioGRID; 200615; 5.
DR IntAct; O88786; 6.
DR STRING; 10090.ENSMUSP00000033646; -.
DR GlyGen; O88786; 4 sites.
DR MaxQB; O88786; -.
DR PaxDb; O88786; -.
DR PRIDE; O88786; -.
DR ProteomicsDB; 273299; -. [O88786-1]
DR ProteomicsDB; 273300; -. [O88786-2]
DR Antibodypedia; 29593; 568 antibodies from 39 providers.
DR DNASU; 16165; -.
DR Ensembl; ENSMUST00000033646; ENSMUSP00000033646; ENSMUSG00000031289. [O88786-1]
DR Ensembl; ENSMUST00000112827; ENSMUSP00000108446; ENSMUSG00000031289. [O88786-1]
DR GeneID; 16165; -.
DR KEGG; mmu:16165; -.
DR UCSC; uc009unf.1; mouse. [O88786-1]
DR UCSC; uc012hqe.1; mouse. [O88786-2]
DR CTD; 3598; -.
DR MGI; MGI:1277954; Il13ra2.
DR VEuPathDB; HostDB:ENSMUSG00000031289; -.
DR eggNOG; ENOG502RV4W; Eukaryota.
DR GeneTree; ENSGT00940000159971; -.
DR HOGENOM; CLU_054773_1_0_1; -.
DR InParanoid; O88786; -.
DR OMA; DCIYYNW; -.
DR OrthoDB; 1151666at2759; -.
DR PhylomeDB; O88786; -.
DR TreeFam; TF331549; -.
DR BioGRID-ORCS; 16165; 1 hit in 71 CRISPR screens.
DR PRO; PR:O88786; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O88786; protein.
DR Bgee; ENSMUSG00000031289; Expressed in cumulus cell and 42 other tissues.
DR Genevisible; O88786; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IMP:MGI.
DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..383
FT /note="Interleukin-13 receptor subunit alpha-2"
FT /id="PRO_0000378452"
FT TOPO_DOM 22..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..128
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 131..219
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 234..332
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 316..320
FT /note="WSXWS motif"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..107
FT /evidence="ECO:0000250"
FT DISULFID 139..149
FT /evidence="ECO:0000250"
FT DISULFID 178..191
FT /evidence="ECO:0000250"
FT DISULFID 263..310
FT /evidence="ECO:0000250"
FT VAR_SEQ 327..339
FT /note="GYTGPDSKIIFIV -> EPPCGSEQRSVCL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17114462"
FT /id="VSP_037588"
FT VAR_SEQ 340..383
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17114462"
FT /id="VSP_037589"
FT CONFLICT 330
FT /note="G -> W (in Ref. 3; BAE43400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 44483 MW; C25212325C47E35B CRC64;
MAFVHIRCLC FILLCTITGY SLEIKVNPPQ DFEILDPGLL GYLYLQWKPP VVIEKFKGCT
LEYELKYRNV DSDSWKTIIT RNLIYKDGFD LNKGIEGKIR THLSEHCTNG SEVQSPWIEA
SYGISDEGSL ETKIQDMKCI YYNWQYLVCS WKPGKTVYSD TNYTMFFWYE GLDHALQCAD
YLQHDEKNVG CKLSNLDSSD YKDFFICVNG SSKLEPIRSS YTVFQLQNIV KPLPPEFLHI
SVENSIDIRM KWSTPGGPIP PRCYTYEIVI REDDISWESA TDKNDMKLKR RANESEDLCF
FVRCKVNIYC ADDGIWSEWS EEECWEGYTG PDSKIIFIVP VCLFFIFLLL LLCLIVEKEE
PEPTLSLHVD LNKEVCAYED TLC
