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Database: UniProt
Entry: A5HJM1
LinkDB: A5HJM1
Original site: A5HJM1 
ID   IL7RA_CALJA             Reviewed;         459 AA.
AC   A5HJM1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 76.
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   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Matsuzawa A., Kohu K., Suemizu H., Sasaki E., Yagita H., Suzuki D.,
RA   Kametani Y., Habu S., Satake M.;
RL   Submitted (APR-2007) 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; EF534213; ABQ09497.1; -; mRNA.
DR   RefSeq; XP_002745108.1; XM_002745062.3.
DR   AlphaFoldDB; A5HJM1; -.
DR   SMR; A5HJM1; -.
DR   STRING; 9483.ENSCJAP00000034071; -.
DR   GlyCosmos; A5HJM1; 3 sites, No reported glycans.
DR   Ensembl; ENSCJAT00000035995.5; ENSCJAP00000034071.2; ENSCJAG00000018379.5.
DR   GeneID; 100397720; -.
DR   KEGG; cjc:100397720; -.
DR   CTD; 3575; -.
DR   eggNOG; ENOG502S4WE; Eukaryota.
DR   GeneTree; ENSGT00510000048500; -.
DR   HOGENOM; CLU_045398_0_0_1; -.
DR   InParanoid; A5HJM1; -.
DR   OMA; QIHRVDD; -.
DR   OrthoDB; 4143009at2759; -.
DR   TreeFam; TF336573; -.
DR   Proteomes; UP000008225; Chromosome 2.
DR   Bgee; ENSCJAG00000018379; Expressed in liver and 3 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0004896; F:cytokine receptor activity; IEA:Ensembl.
DR   GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR   GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR   GO; GO:0070233; P:negative regulation of T cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; IEA:Ensembl.
DR   GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR   GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.1870; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR23037; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR23037:SF27; INTERLEUKIN-7 RECEPTOR SUBUNIT ALPHA; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF18447; FN3_7; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 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_0000369415"
FT   TOPO_DOM        21..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..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   REGION          327..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   COMPBIAS        330..357
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        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;  51456 MW;  37541A485D1D6583 CRC64;
     MTILGTTFGV FFSLLQVVSG ESGYAQNGDL EDAELDDYSF SCYSQLEVNG SQHSLTCAFE
     DPDVNTTNLE FEICGALVEV RCLNFRKLQE IYLIETKKFL LIGNSNICVK AGEKSLTCKN
     VNVATIVKPE APFDLSVIYR EGANDFLVTF NTSHLQKKYV KVLMHDVAYR HEKDENNWMH
     VNLSSTKLTL LQRKLQPKAT YEIKVRSIPG DYFKGFWSEW SPSYYFRTPE INNHSGETNP
     TLLTISILSV LSVVLLVILA CVLWKKRIKP IIWPSLPDHK KTLEHLCKKP SKNLIVSFNP
     ESFLDCQIHR VDDIQARDEV EGFLQDTVPP QLEESETQRP GGDVQSPSWP SENVVTTPET
     FGRDSPLRCL AGNVSAHDAP ILSSSRSLDC RESATNGPHV NQDLLLSLGT TNSTLPPSFP
     PQSRILTLNP VAQGQPILTF LGSNKEEAYV TMSSFCQKR
//
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