ID   IL7RA_MACFA             Reviewed;         459 AA.
AC   Q38IC7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
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            Short=IL7Ra;
DE   AltName: CD_antigen=CD127;
DE   Flags: Precursor;
GN   Name=IL7R;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen S., Yu L.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for interleukin-7. Also acts as a receptor for
CC       thymic stromal lymphopoietin (TSLP) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The IL7 receptor is a heterodimer of IL7R and IL2RG. The TSLP
CC       receptor is a heterodimer of CRLF2 and IL7R (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell 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   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation. {ECO:0000250}.
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; DQ226543; ABB13531.1; -; mRNA.
DR   RefSeq; NP_001271837.1; NM_001284908.1.
DR   AlphaFoldDB; Q38IC7; -.
DR   SMR; Q38IC7; -.
DR   STRING; 9541.XP_005556772.1; -.
DR   GeneID; 102143679; -.
DR   CTD; 3575; -.
DR   eggNOG; ENOG502S4WE; Eukaryota.
DR   OrthoDB; 617812at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..459
FT                   /note="Interleukin-7 receptor subunit alpha"
FT                   /id="PRO_0000369417"
FT   TOPO_DOM        21..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..459
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          131..231
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   MOTIF           217..221
FT                   /note="WSXWS motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           272..280
FT                   /note="Box 1 motif"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         282
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        74..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..118
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  51665 MW;  5BA043C5D63FF7BD CRC64;
     MTILGTTFGM VFSLLQVVSG ESGYAQNGDL EDAELDDYSF SCYSQLEVNG SQHSLTCAFE
     DPDVNTTNLE FEICGALVEV KCLSFRKLQE IYFIETKKFL LIGKSNICVK VGGKSLTCKK
     IDLTTIVKPE APFDLSVIYR EGANDFVVTF NTSHLQKKYV KVLMHDVAYR QEKDENKWMH
     VNLSSTKLTL LQRNLQPEAM YEIKVRSIPD HYFKGFWSEW SPSYYFRTPE INNSPGEMDP
     ILLTISLLSF FSVALLVILA CVLWKKRIKP IVWPSLPDHK KTLEHLCKKP RKNLNVSFNP
     ESFLDCQIHR VDDIQARDEV EGFLQDTFPQ QLEESKKQRL GGDVQSPSCP SEDVVITPES
     FERDSSLRCL AGNVSACDAP ILSSSRSLDC RESGKNGPHV YQDLLLSLGT TNSTLPPPFS
     LQSGILTLNP VAQGQPILTS LGSNQEEAYV TMSSFYQNQ