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Interleukin-13 receptor subunit alpha-2 (IL-13 receptor subunit alpha-2) (IL-13R subunit alpha-2) (IL-13R-alpha-2) (IL-13RA2) (Interleukin-13-binding protein) (CD antigen CD213a2)

 I13R2_HUMAN             Reviewed;         380 AA.
Q14627; A8K7E2; O00667;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 177.
RecName: Full=Interleukin-13 receptor subunit alpha-2;
Short=IL-13 receptor subunit alpha-2;
Short=IL-13R subunit alpha-2;
Short=IL-13R-alpha-2;
Short=IL-13RA2;
AltName: Full=Interleukin-13-binding protein;
AltName: CD_antigen=CD213a2;
Flags: Precursor;
Name=IL13RA2; Synonyms=IL13R;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Renal cell carcinoma;
PubMed=8663118; DOI=10.1074/jbc.271.28.16921;
Caput D., Laurent P., Kaghad M., Lelias J.M., Lefort S., Vita N.,
Ferrara P.;
"Cloning and characterization of a specific interleukin (IL)-13
binding protein structurally related to the IL-5 receptor alpha
chain.";
J. Biol. Chem. 271:16921-16926(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
Donaldson D.D., Whitters M.J., Fitz L., Neben T., Finnerty H.,
Henderson S.L., O'Hara R.M. Jr., Turner K.J., Wood C.R., Collins M.;
"Identification of a third chain for the murine Il-13 receptor.";
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9177784; DOI=10.1006/geno.1997.4628;
Guo J., Apiou F., Mellerin M.P., Lebeau B., Jacques Y., Minvielle S.;
"Chromosome mapping and expression of the human interleukin-13
receptor.";
Genomics 42:141-145(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-111.
SeattleSNPs variation discovery resource;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH IL13, FUNCTION,
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-215.
PubMed=20223216; DOI=10.1016/j.str.2010.01.003;
Lupardus P.J., Birnbaum M.E., Garcia K.C.;
"Molecular basis for shared cytokine recognition revealed in the
structure of an unusually high affinity complex between IL-13 and IL-
13Ralpha2.";
Structure 18:332-342(2010).
-!- FUNCTION: Binds as a monomer with high affinity to interleukin-13
(IL13), but not to interleukin-4 (IL4).
{ECO:0000269|PubMed:20223216}.
-!- INTERACTION:
P36222:CHI3L1; NbExp=2; IntAct=EBI-4320063, EBI-6917454;
P35225:IL13; NbExp=8; IntAct=EBI-4320063, EBI-1647828;
P17931:LGALS3; NbExp=2; IntAct=EBI-4320063, EBI-1170392;
Q86XT9:TMEM219; NbExp=9; IntAct=EBI-4320063, EBI-20264080;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il13ra2/";
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EMBL; X95302; CAA64617.1; -; mRNA.
EMBL; U70981; AAB17170.1; -; mRNA.
EMBL; Y08768; CAA70021.1; -; mRNA.
EMBL; AK291957; BAF84646.1; -; mRNA.
EMBL; AY656702; AAT49099.1; -; Genomic_DNA.
EMBL; AL121878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020739; AAH20739.1; -; mRNA.
EMBL; BC033705; AAH33705.1; -; mRNA.
CCDS; CCDS14565.1; -.
RefSeq; NP_000631.1; NM_000640.2.
UniGene; Hs.336046; -.
PDB; 3LB6; X-ray; 3.05 A; C/D=1-380.
PDBsum; 3LB6; -.
ProteinModelPortal; Q14627; -.
SMR; Q14627; -.
BioGrid; 109812; 121.
DIP; DIP-3340N; -.
IntAct; Q14627; 18.
MINT; Q14627; -.
STRING; 9606.ENSP00000243213; -.
ChEMBL; CHEMBL3713941; -.
DrugBank; DB05078; AER001.
iPTMnet; Q14627; -.
BioMuta; IL13RA2; -.
DMDM; 2494720; -.
MaxQB; Q14627; -.
PaxDb; Q14627; -.
PeptideAtlas; Q14627; -.
PRIDE; Q14627; -.
ProteomicsDB; 60078; -.
DNASU; 3598; -.
Ensembl; ENST00000243213; ENSP00000243213; ENSG00000123496.
Ensembl; ENST00000371936; ENSP00000361004; ENSG00000123496.
GeneID; 3598; -.
KEGG; hsa:3598; -.
UCSC; uc004epx.4; human.
CTD; 3598; -.
DisGeNET; 3598; -.
EuPathDB; HostDB:ENSG00000123496.7; -.
GeneCards; IL13RA2; -.
HGNC; HGNC:5975; IL13RA2.
MIM; 300130; gene.
neXtProt; NX_Q14627; -.
OpenTargets; ENSG00000123496; -.
PharmGKB; PA29788; -.
eggNOG; ENOG410IUDW; Eukaryota.
eggNOG; ENOG4111JMU; LUCA.
GeneTree; ENSGT00530000063295; -.
HOGENOM; HOG000004823; -.
HOVERGEN; HBG058972; -.
InParanoid; Q14627; -.
KO; K05077; -.
OMA; LFYWYEG; -.
OrthoDB; EOG091G0FOF; -.
PhylomeDB; Q14627; -.
TreeFam; TF331549; -.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
SignaLink; Q14627; -.
EvolutionaryTrace; Q14627; -.
GeneWiki; IL13RA2; -.
GenomeRNAi; 3598; -.
PRO; PR:Q14627; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000123496; Expressed in 115 organ(s), highest expression level in sperm.
CleanEx; HS_IL13RA2; -.
Genevisible; Q14627; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004896; F:cytokine receptor activity; TAS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
GO; GO:0002638; P:negative regulation of immunoglobulin production; IEA:Ensembl.
GO; GO:0043305; P:negative regulation of mast cell degranulation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF09240; IL6Ra-bind; 1.
SUPFAM; SSF49265; SSF49265; 3.
PROSITE; PS50853; FN3; 3.
PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Membrane; Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 380 Interleukin-13 receptor subunit alpha-2.
/FTId=PRO_0000010942.
TOPO_DOM 27 343 Extracellular. {ECO:0000255}.
TRANSMEM 344 363 Helical. {ECO:0000255}.
TOPO_DOM 364 380 Cytoplasmic. {ECO:0000255}.
DOMAIN 34 134 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 139 235 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 240 333 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 322 326 WSXWS motif.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20223216}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 65 113 {ECO:0000269|PubMed:20223216}.
DISULFID 145 155 {ECO:0000269|PubMed:20223216}.
DISULFID 184 197 {ECO:0000269|PubMed:20223216}.
DISULFID 269 316 {ECO:0000269|PubMed:20223216}.
VARIANT 111 111 W -> R (in dbSNP:rs17095919).
{ECO:0000269|Ref.5}.
/FTId=VAR_021256.
CONFLICT 8 8 I -> V (in Ref. 4; BAF84646).
{ECO:0000305}.
CONFLICT 151 151 Q -> R (in Ref. 4; BAF84646).
{ECO:0000305}.
STRAND 36 41 {ECO:0000244|PDB:3LB6}.
STRAND 44 54 {ECO:0000244|PDB:3LB6}.
STRAND 68 75 {ECO:0000244|PDB:3LB6}.
STRAND 82 94 {ECO:0000244|PDB:3LB6}.
STRAND 101 108 {ECO:0000244|PDB:3LB6}.
HELIX 111 114 {ECO:0000244|PDB:3LB6}.
STRAND 115 117 {ECO:0000244|PDB:3LB6}.
STRAND 126 128 {ECO:0000244|PDB:3LB6}.
STRAND 141 148 {ECO:0000244|PDB:3LB6}.
TURN 149 151 {ECO:0000244|PDB:3LB6}.
STRAND 152 158 {ECO:0000244|PDB:3LB6}.
STRAND 168 174 {ECO:0000244|PDB:3LB6}.
STRAND 185 189 {ECO:0000244|PDB:3LB6}.
STRAND 194 198 {ECO:0000244|PDB:3LB6}.
STRAND 206 208 {ECO:0000244|PDB:3LB6}.
STRAND 210 217 {ECO:0000244|PDB:3LB6}.
STRAND 226 230 {ECO:0000244|PDB:3LB6}.
HELIX 232 234 {ECO:0000244|PDB:3LB6}.
STRAND 235 237 {ECO:0000244|PDB:3LB6}.
STRAND 242 246 {ECO:0000244|PDB:3LB6}.
STRAND 256 259 {ECO:0000244|PDB:3LB6}.
STRAND 262 264 {ECO:0000244|PDB:3LB6}.
STRAND 270 274 {ECO:0000244|PDB:3LB6}.
STRAND 287 291 {ECO:0000244|PDB:3LB6}.
STRAND 308 312 {ECO:0000244|PDB:3LB6}.
TURN 314 316 {ECO:0000244|PDB:3LB6}.
SEQUENCE 380 AA; 44176 MW; 3C6ACB1B5562C887 CRC64;
MAFVCLAIGC LYTFLISTTF GCTSSSDTEI KVNPPQDFEI VDPGYLGYLY LQWQPPLSLD
HFKECTVEYE LKYRNIGSET WKTIITKNLH YKDGFDLNKG IEAKIHTLLP WQCTNGSEVQ
SSWAETTYWI SPQGIPETKV QDMDCVYYNW QYLLCSWKPG IGVLLDTNYN LFYWYEGLDH
ALQCVDYIKA DGQNIGCRFP YLEASDYKDF YICVNGSSEN KPIRSSYFTF QLQNIVKPLP
PVYLTFTRES SCEIKLKWSI PLGPIPARCF DYEIEIREDD TTLVTATVEN ETYTLKTTNE
TRQLCFVVRS KVNIYCSDDG IWSEWSDKQC WEGEDLSKKT LLRFWLPFGF ILILVIFVTG
LLLRKPNTYP KMIPEFFCDT


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U1815m CLIA kit IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Mouse,Mus musculus 96T
U2031m CLIA kit IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Mouse,Mus musculus 96T


 

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