ID   I13R2_RAT               Reviewed;         385 AA.
AC   Q8VHK6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 108.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=12241113; DOI=10.1023/a:1019690120307;
RA   Wu A.H., Low W.C.;
RT   "Molecular cloning of the rat IL-13 alpha 2 receptor cDNA and its
RT   expression in rat tissues.";
RL   J. Neurooncol. 59:99-105(2002).
CC   -!- FUNCTION: Binds as a monomer with high affinity to interleukin-13
CC       (IL13). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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; AF448818; AAL57513.1; -; mRNA.
DR   AlphaFoldDB; Q8VHK6; -.
DR   SMR; Q8VHK6; -.
DR   STRING; 10116.ENSRNOP00000041564; -.
DR   GlyGen; Q8VHK6; 4 sites.
DR   PaxDb; Q8VHK6; -.
DR   PRIDE; Q8VHK6; -.
DR   RGD; 620838; Il13ra2.
DR   eggNOG; ENOG502RV4W; Eukaryota.
DR   InParanoid; Q8VHK6; -.
DR   PhylomeDB; Q8VHK6; -.
DR   PRO; PR:Q8VHK6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; ISO:RGD.
DR   GO; GO:0002638; P:negative regulation of immunoglobulin production; ISO:RGD.
DR   GO; GO:0043305; P:negative regulation of mast cell degranulation; ISO:RGD.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..385
FT                   /note="Interleukin-13 receptor subunit alpha-2"
FT                   /id="PRO_0000378453"
FT   TOPO_DOM        24..336
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..130
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          133..221
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          236..334
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   MOTIF           318..322
FT                   /note="WSXWS motif"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        141..151
FT                   /evidence="ECO:0000250"
FT   DISULFID        180..193
FT                   /evidence="ECO:0000250"
FT   DISULFID        265..312
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  44622 MW;  EE06FF0E434737E2 CRC64;
     MALMAVNTRC LCLFLLCTIT GHSLEIKVNP PQDFEILDPG LLGYLYLQWK PPVVMDNFKE
     CKLEYELKYR NVDSDSWKTI ITRNLIYKDG FDLNKGIEGK IRTHLSEHCT NGSEVQSPWT
     EASYGIADEG SLGTKIQDMK CIYYNWQYLV CSWKPGKTVH SDTNYTMFFW YEGLDHALQC
     ADYLQDNEKN VGCKLSNLDS SDYKDFFIRV NGSSKLEPIR SSYMVFQLQN IVKPLPPEFL
     HISVENSIDI RMKWSTPGGP IPPSCYTYEI VVREDDISWE SATDKNDMKL KRRANESEDL
     CFFVRCKINI YCADDGIWSE WSEEECWEGY TGPDSKIVFI VPVCLFFIFL LLLLCLIVEK
     EDPEPTLSLH VDLNKEMYAY EETLC