IL7RA_MOUSE
ID IL7RA_MOUSE Reviewed; 459 AA.
AC P16872; Q9R0C1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Interleukin-7 receptor subunit alpha;
DE Short=IL-7 receptor subunit alpha;
DE Short=IL-7R subunit alpha;
DE Short=IL-7R-alpha;
DE Short=IL-7RA;
DE AltName: CD_antigen=CD127;
DE Flags: Precursor;
GN Name=Il7r;
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=2317865; DOI=10.1016/0092-8674(90)90342-c;
RA Goodwin R.G., Friend D., Ziegler S.F., Jerzy R., Falk B.A., Gimpel S.,
RA Cosman D., Dower S.K., March C.J., Namen A.E., Park L.S.;
RT "Cloning of the human and murine interleukin-7 receptors: demonstration of
RT a soluble form and homology to a new receptor superfamily.";
RL Cell 60:941-951(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=10556186;
RA Lo M., Bloom M.L., Imada K., Berg M., Bollenbacher J.M., Bloom E.T.,
RA Kelsall B.L., Leonard W.J.;
RT "Restoration of lymphoid populations in a murine model of X-linked severe
RT combined immunodeficiency by a gene-therapy approach.";
RL Blood 94:3027-3036(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 231-239 AND 264-272.
RX PubMed=2038316; DOI=10.1128/mcb.11.6.3052-3059.1991;
RA Pleiman C.M., Gimpel S.D., Park L.S., Harada H., Taniguchi T.,
RA Ziegler S.F.;
RT "Organization of the murine and human interleukin-7 receptor genes: two
RT mRNAs generated by differential splicing and presence of a type I-
RT interferon-inducible promoter.";
RL Mol. Cell. Biol. 11:3052-3059(1991).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-239 IN COMPLEX WITH CRLF2 AND
RP TSLP, AND DISULFIDE BONDS.
RX PubMed=24632570; DOI=10.1038/nsmb.2794;
RA Verstraete K., van Schie L., Vyncke L., Bloch Y., Tavernier J., Pauwels E.,
RA Peelman F., Savvides S.N.;
RT "Structural basis of the proinflammatory signaling complex mediated by
RT TSLP.";
RL Nat. Struct. Mol. Biol. 21:375-382(2014).
CC -!- FUNCTION: Receptor for interleukin-7. Also acts as a receptor for
CC thymic stromal lymphopoietin (TSLP).
CC -!- SUBUNIT: The IL7 receptor is a heterodimer of IL7R and IL2RG. The TSLP
CC receptor is a heterodimer of CRLF2 and IL7R.
CC {ECO:0000269|PubMed:24632570}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Spleen, thymus and fetal liver.
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 -!- PTM: N-glycosylated IL-7Ralpha binds IL7 300-fold more tightly than the
CC unglycosylated form. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
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DR EMBL; M29697; AAA39304.1; -; mRNA.
DR EMBL; AF078906; AAF06717.1; -; mRNA.
DR EMBL; AK042264; BAC31208.1; -; mRNA.
DR EMBL; CH466581; EDL03312.1; -; Genomic_DNA.
DR CCDS; CCDS27376.1; -.
DR PIR; D34791; D34791.
DR RefSeq; NP_032398.3; NM_008372.4.
DR PDB; 4NN5; X-ray; 1.90 A; B=21-239.
DR PDB; 4NN6; X-ray; 2.54 A; B=21-239.
DR PDB; 4NN7; X-ray; 3.78 A; B=21-239.
DR PDB; 5J12; X-ray; 3.55 A; B=21-239.
DR PDBsum; 4NN5; -.
DR PDBsum; 4NN6; -.
DR PDBsum; 4NN7; -.
DR PDBsum; 5J12; -.
DR AlphaFoldDB; P16872; -.
DR SMR; P16872; -.
DR DIP; DIP-59472N; -.
DR IntAct; P16872; 3.
DR STRING; 10090.ENSMUSP00000003981; -.
DR GlyGen; P16872; 3 sites.
DR iPTMnet; P16872; -.
DR PhosphoSitePlus; P16872; -.
DR EPD; P16872; -.
DR PaxDb; P16872; -.
DR PRIDE; P16872; -.
DR ProteomicsDB; 266970; -.
DR Antibodypedia; 4129; 1310 antibodies from 47 providers.
DR DNASU; 16197; -.
DR Ensembl; ENSMUST00000003981; ENSMUSP00000003981; ENSMUSG00000003882.
DR GeneID; 16197; -.
DR KEGG; mmu:16197; -.
DR UCSC; uc007vfo.2; mouse.
DR CTD; 3575; -.
DR MGI; MGI:96562; Il7r.
DR VEuPathDB; HostDB:ENSMUSG00000003882; -.
DR eggNOG; ENOG502S4WE; Eukaryota.
DR GeneTree; ENSGT00510000048500; -.
DR HOGENOM; CLU_045398_0_0_1; -.
DR InParanoid; P16872; -.
DR OMA; QIHRVDD; -.
DR OrthoDB; 617812at2759; -.
DR PhylomeDB; P16872; -.
DR TreeFam; TF336573; -.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 16197; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Il7r; mouse.
DR PRO; PR:P16872; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P16872; protein.
DR Bgee; ENSMUSG00000003882; Expressed in peripheral lymph node and 78 other tissues.
DR ExpressionAtlas; P16872; baseline and differential.
DR Genevisible; P16872; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; ISO:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IGI:MGI.
DR GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
DR GO; GO:0048535; P:lymph node development; IMP:MGI.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; IMP:MGI.
DR GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; ISO:MGI.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0008361; P:regulation of cell size; IDA:MGI.
DR GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IMP:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR040997; FN3_7.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF18447; FN3_7; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT CHAIN 21..459
FT /note="Interleukin-7 receptor subunit alpha"
FT /id="PRO_0000010910"
FT TOPO_DOM 21..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 131..232
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 337..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 218..222
FT /note="WSXWS motif"
FT MOTIF 272..280
FT /note="Box 1 motif"
FT COMPBIAS 343..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..57
FT /evidence="ECO:0000269|PubMed:24632570"
FT DISULFID 74..82
FT /evidence="ECO:0000269|PubMed:24632570"
FT DISULFID 108..118
FT /evidence="ECO:0000269|PubMed:24632570"
FT CONFLICT 299..302
FT /note="NPES -> IPEI (in Ref. 1; AAA39304)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="S -> I (in Ref. 1; AAA39304)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="V -> F (in Ref. 1; AAA39304)"
FT /evidence="ECO:0000305"
FT STRAND 40..51
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:4NN5"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:4NN5"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4NN5"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 179..191
FT /evidence="ECO:0007829|PDB:4NN5"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:4NN5"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4NN5"
SQ SEQUENCE 459 AA; 51605 MW; 52ADF78C8C01D2EE CRC64;
MMALGRAFAI VFCLIQAVSG ESGNAQDGDL EDADADDHSF WCHSQLEVDG SQHLLTCAFN
DSDINTANLE FQICGALLRV KCLTLNKLQD IYFIKTSEFL LIGSSNICVK LGQKNLTCKN
MAINTIVKAE APSDLKVVYR KEANDFLVTF NAPHLKKKYL KKVKHDVAYR PARGESNWTH
VSLFHTRTTI PQRKLRPKAM YEIKVRSIPH NDYFKGFWSE WSPSSTFETP EPKNQGGWDP
VLPSVTILSL FSVFLLVILA HVLWKKRIKP VVWPSLPDHK KTLEQLCKKP KTSLNVSFNP
ESFLDCQIHE VKGVEARDEV ESFLPNDLPA QPEELETQGH RAAVHSANRS PETSVSPPET
VRRESPLRCL ARNLSTCNAP PLLSSRSPDY RDGDRNRPPV YQDLLPNSGN TNVPVPVPQP
LPFQSGILIP VSQRQPISTS SVLNQEEAYV TMSSFYQNK
