I13R2_CANLF
ID I13R2_CANLF Reviewed; 386 AA.
AC Q95LF0; Q3HTU7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11389954; DOI=10.1016/s0165-2427(01)00271-9;
RA Tang L.;
RT "Molecular cloning of canine IL-13 receptor alpha chain (alpha1 and alpha2)
RT cDNAs and detection of corresponding mRNAs in canine tissues.";
RL Vet. Immunol. Immunopathol. 79:181-195(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16797723; DOI=10.1016/j.vetimm.2006.05.005;
RA Shelton G.D., Hoffman E.P., Ghimbovschi S., Peters I.R., Day M.J.,
RA Mullins M., Moore P.F., Nagaraju K.;
RT "Immunopathogenic pathways in canine inflammatory myopathies resemble human
RT myositis.";
RL Vet. Immunol. Immunopathol. 113:200-214(2006).
CC -!- FUNCTION: Binds as a monomer with high affinity to interleukin-13
CC (IL13). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, placenta, liver, skeletal
CC muscle and thymus. Expression was not seen in whole blood and heart.
CC {ECO:0000269|PubMed:11389954}.
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.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
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DR EMBL; AF314533; AAL14887.1; -; mRNA.
DR EMBL; DQ195087; ABA40744.1; -; mRNA.
DR RefSeq; NP_001003075.1; NM_001003075.1.
DR AlphaFoldDB; Q95LF0; -.
DR SMR; Q95LF0; -.
DR STRING; 9612.ENSCAFP00000026935; -.
DR PaxDb; Q95LF0; -.
DR Ensembl; ENSCAFT00030029038; ENSCAFP00030025314; ENSCAFG00030015759.
DR Ensembl; ENSCAFT00040029968; ENSCAFP00040026037; ENSCAFG00040016209.
DR GeneID; 403622; -.
DR KEGG; cfa:403622; -.
DR CTD; 3598; -.
DR eggNOG; ENOG502RV4W; Eukaryota.
DR HOGENOM; CLU_054773_1_0_1; -.
DR InParanoid; Q95LF0; -.
DR OMA; DCIYYNW; -.
DR OrthoDB; 1151666at2759; -.
DR TreeFam; TF331549; -.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000018230; Expressed in retina and 40 other tissues.
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:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
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; 3.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..386
FT /note="Interleukin-13 receptor subunit alpha-2"
FT /id="PRO_0000010941"
FT TOPO_DOM 22..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..133
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 138..234
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 239..338
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 321..325
FT /note="WSXWS motif"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..112
FT /evidence="ECO:0000250"
FT DISULFID 144..154
FT /evidence="ECO:0000250"
FT DISULFID 183..196
FT /evidence="ECO:0000250"
FT DISULFID 268..315
FT /evidence="ECO:0000250"
SQ SEQUENCE 386 AA; 45110 MW; A16FDF2DD023ED95 CRC64;
MAFIHLDVGF LYTLLVCTAF GSMLSNAEIK VNPPQDFEIV DPGYLGYLSL QWQPPLFPDN
FKECTIEYEL KYRNIDSENW KTIITKNLHY KDGFDLNKGI EAKINTLLPA QCTNGSEVRS
SWAETTYWTS PQGNRETKIQ DMDCVYYNWQ YLVCSWKPGM GVHFDTNYQL FYWYEGLDHS
AECTDYIKVN GKNMGCRFPY LESSDYKDFY ICVNGSSESQ PIRPSYFIFQ LQNIVKPMPP
DYLSLTVKNS EEINLKWNMP KGPIPAKCFI YEIEFTEDGT TWVTTTVENE IQITRTSNES
QKLCFLVRSK VNIYCSDDGI WSEWSDEQCW KGDIWKETLV FFLIPFAFVS IFVLVITCLL
LYKQRALLKT IFHTKKEVFS HQDTFC
