I13R1_MOUSE
ID I13R1_MOUSE Reviewed; 424 AA.
AC O09030; Q7TT27;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Interleukin-13 receptor subunit alpha-1;
DE Short=IL-13 receptor subunit alpha-1;
DE Short=IL-13R subunit alpha-1;
DE Short=IL-13R-alpha-1;
DE Short=IL-13RA1;
DE AltName: Full=Interleukin-13-binding protein;
DE AltName: Full=Novel cytokine receptor 4;
DE Short=NR4;
DE AltName: CD_antigen=CD213a1;
DE Flags: Precursor;
GN Name=Il13ra1; Synonyms=Il13r, Il13ra;
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].
RX PubMed=8552669; DOI=10.1073/pnas.93.1.497;
RA Hilton D.J., Zhang J.-G., Metcalf D., Alexander W.S., Nicola N.A.,
RA Willson T.A.;
RT "Cloning and characterization of a binding subunit of the interleukin 13
RT receptor that is also a component of the interleukin 4 receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:497-501(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Colon;
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 with low affinity to interleukin-13 (IL13). Together
CC with IL4RA can form a functional receptor for IL13. Also serves as an
CC alternate accessory protein to the common cytokine receptor gamma chain
CC for interleukin-4 (IL4) signaling, but cannot replace the function of
CC IL2RG in allowing enhanced interleukin-2 (IL2) binding activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interleukin-13 receptor is a complex of IL4R, IL13RA1, and
CC possibly other components. Interacts with TRAF3IP1 (By similarity).
CC Interacts with IL4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Spleen, liver, thymus, heart, lung, kidney, testis,
CC stomach, brain, skin, and colon; but not skeletal muscle.
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 -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
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DR EMBL; S80963; AAB50695.1; -; mRNA.
DR EMBL; BC052425; AAH52425.2; -; mRNA.
DR EMBL; BC059939; AAH59939.1; -; mRNA.
DR CCDS; CCDS30057.1; -.
DR RefSeq; NP_598751.3; NM_133990.5.
DR AlphaFoldDB; O09030; -.
DR SMR; O09030; -.
DR DIP; DIP-1167N; -.
DR STRING; 10090.ENSMUSP00000033418; -.
DR GlyGen; O09030; 6 sites.
DR iPTMnet; O09030; -.
DR PhosphoSitePlus; O09030; -.
DR MaxQB; O09030; -.
DR PaxDb; O09030; -.
DR PRIDE; O09030; -.
DR ProteomicsDB; 267074; -.
DR Antibodypedia; 385; 562 antibodies from 36 providers.
DR DNASU; 16164; -.
DR Ensembl; ENSMUST00000033418; ENSMUSP00000033418; ENSMUSG00000017057.
DR GeneID; 16164; -.
DR KEGG; mmu:16164; -.
DR UCSC; uc009sxj.1; mouse.
DR CTD; 3597; -.
DR MGI; MGI:105052; Il13ra1.
DR VEuPathDB; HostDB:ENSMUSG00000017057; -.
DR eggNOG; ENOG502RYXH; Eukaryota.
DR GeneTree; ENSGT00940000160896; -.
DR HOGENOM; CLU_039945_1_0_1; -.
DR InParanoid; O09030; -.
DR OMA; YDICEKQ; -.
DR OrthoDB; 1151666at2759; -.
DR PhylomeDB; O09030; -.
DR TreeFam; TF331549; -.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR BioGRID-ORCS; 16164; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Il13ra1; mouse.
DR PRO; PR:O09030; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O09030; protein.
DR Bgee; ENSMUSG00000017057; Expressed in jejunum and 215 other tissues.
DR Genevisible; O09030; MM.
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:0005127; F:ciliary neurotrophic factor receptor binding; 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:0016515; F:interleukin-13 receptor activity; ISO:MGI.
DR GO; GO:0004923; F:leukemia inhibitory factor receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IEA:GOC.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; 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; IPR040566; Il13Ra_Ig.
DR InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF18001; Il13Ra_Ig; 1.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..424
FT /note="Interleukin-13 receptor subunit alpha-1"
FT /id="PRO_0000010940"
FT TOPO_DOM 26..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..121
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 224..336
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 324..328
FT /note="WSXWS motif"
FT MOTIF 371..379
FT /note="Box 1 motif"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..93
FT /evidence="ECO:0000255"
FT DISULFID 132..142
FT /evidence="ECO:0000250"
FT DISULFID 171..183
FT /evidence="ECO:0000250"
SQ SEQUENCE 424 AA; 48402 MW; EB8330A0DC82C9F9 CRC64;
MARPALLGEL LVLLLWTATV GQVAAATEVQ PPVTNLSVSV ENLCTIIWTW SPPEGASPNC
TLRYFSHFDD QQDKKIAPET HRKEELPLDE KICLQVGSQC SANESEKPSP LVKKCISPPE
GDPESAVTEL KCIWHNLSYM KCSWLPGRNT SPDTHYTLYY WYSSLEKSRQ CENIYREGQH
IACSFKLTKV EPSFEHQNVQ IMVKDNAGKI RPSCKIVSLT SYVKPDPPHI KHLLLKNGAL
LVQWKNPQNF RSRCLTYEVE VNNTQTDRHN ILEVEEDKCQ NSESDRNMEG TSCFQLPGVL
ADAVYTVRVR VKTNKLCFDD NKLWSDWSEA QSIGKEQNST FYTTMLLTIP VFVAVAVIIL
LFYLKRLKII IFPPIPDPGK IFKEMFGDQN DDTLHWKKYD IYEKQSKEET DSVVLIENLK
KAAP
