ID   IL7RA_HORSE             Reviewed;         458 AA.
AC   A0MSX9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 65.
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   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kolebacova K.;
RL   Submitted (OCT-2006) 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; EF035169; ABK34942.1; -; mRNA.
DR   RefSeq; NP_001075411.1; NM_001081942.1.
DR   AlphaFoldDB; A0MSX9; -.
DR   SMR; A0MSX9; -.
DR   STRING; 9796.ENSECAP00000008818; -.
DR   PaxDb; A0MSX9; -.
DR   GeneID; 100034169; -.
DR   KEGG; ecb:100034169; -.
DR   CTD; 3575; -.
DR   InParanoid; A0MSX9; -.
DR   OrthoDB; 617812at2759; -.
DR   Proteomes; UP000002281; 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:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
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..458
FT                   /note="Interleukin-7 receptor subunit alpha"
FT                   /id="PRO_0000369416"
FT   TOPO_DOM        21..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..458
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          131..232
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   MOTIF           218..222
FT                   /note="WSXWS motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           271..279
FT                   /note="Box 1 motif"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         281
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
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   458 AA;  51494 MW;  E3178FFAAE089434 CRC64;
     MTILGTTFGM VFYLLQVVSG ESGYAQNGDF EDAELDDYSF SCYSQLEVDG PQHLLSCAFE
     DPDVNSTNLE FEICEGLLEV KCLNFSKLQE TYFIKTKKFL LIGDSTICVK LGGKHITCQK
     LNIVKRVKPE APFDVKVIYR EEANEFVVTF NTSHLQKKYV KDLLHEVVYR LEKNENDWMH
     VNISSTKLTL LQRKLQPNAM YEIKVRSIPN TNYFEGFWSE WSPSSHFRTP ENNSGKMDPV
     LLIISIVSFF SVALMVILAC VLWKKRIKPI VWPSLPDHKK TLEQLCKKPK KNLNVSFNPE
     SFLDCQIHKV DGIQARDEAE AFLQDTFPPQ LDDSEKQRLG GGVQGLNWPS QHAVITPKTF
     GGESPLRCLS GSVTVCDVPV IPSSRPPDCR EGGKNGPHVY QGLLLGAGTT NSTLPHLFPF
     QSGILTLNPA VQGQPLFTSL GSSQEEAYVT MSSFYQNQ