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IL21R_MOUSE
ID   IL21R_MOUSE             Reviewed;         529 AA.
AC   Q9JHX3; Q9ESM1;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Interleukin-21 receptor;
DE            Short=IL-21 receptor;
DE            Short=IL-21R;
DE   AltName: Full=Lymphocyte receptor beta;
DE            Short=LR-beta;
DE   AltName: Full=Novel cytokine receptor 8;
DE            Short=NR8;
DE   AltName: Full=Novel interleukin receptor;
DE   AltName: CD_antigen=CD360;
DE   Flags: Precursor;
GN   Name=Il21r; Synonyms=Nilr;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=11081504; DOI=10.1038/35040504;
RA   Parrish-Novak J., Dillon S.R., Nelson A., Hammond A., Sprecher C.,
RA   Gross J.A., Johnston J., Madden K., Xu W., West J., Schrader S.,
RA   Burkhead S., Heipel M., Brandt C., Kuijper J.L., Kramer J., Conklin D.,
RA   Presnell S.R., Berry J., Shiota F., Bort S., Hambly K., Mudri S., Clegg C.,
RA   Moore M., Grant F.J., Lofton-Day C., Gilbert T., Raymond F., Ching A.,
RA   Yao L., Smith D., Webster P., Whitmore T., Maurer M., Kaushansky K.,
RA   Holly R.D., Foster D.;
RT   "Interleukin 21 and its receptor are involved in NK cell expansion and
RT   regulation of lymphocyte function.";
RL   Nature 408:57-63(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen, and Thymus;
RX   PubMed=11016959; DOI=10.1073/pnas.200360997;
RA   Ozaki K., Kikly K., Michalovich D., Young P.R., Leonard W.J.;
RT   "Cloning of a type I cytokine receptor most related to the IL-2 receptor
RT   beta chain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:11439-11444(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Donaldson D.D., Whitters M.J., Fitz L., Unger M., Finnerty H.,
RA   Dagdigian C., Lowe L., Wood C.R., Young D.A., Collins M.;
RT   "Chromosome 16p12 encodes a biologically active IL-2Rb related receptor
RT   with lymphoid restricted expression.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Nomura H., Yaguchi N., Maeda M., Hasegawa M.;
RT   "A novel cytokine receptor NR8 is closely mapped to IL-4R: polymorphism in
RT   Balb/c mouse.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=A/J, B10.S/DvTe, C57BL/6J, NOD/LtJ, and SJL/J; TISSUE=Spleen;
RA   Gao J., Teuscher C.;
RT   "Mus musculus interleukin 21 receptor gene Il21r mRNA.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is a receptor for interleukin-21.
CC   -!- SUBUNIT: Heterodimer with the common gamma subunit. Associates with
CC       JAK1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Selectively expressed in lymphoid tissues. Most
CC       highly expressed in thymus and spleen.
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: C-mannosylated at Trp-214 in the WSXWS motif, the sugar chain
CC       makes extensive hydrogen bonds with Asn-73 sugar, and bridges the two
CC       fibronectin domains transforming the V-shaped receptor into an A-frame.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF254068; AAG29347.1; -; mRNA.
DR   EMBL; AF269134; AAG23420.1; -; mRNA.
DR   EMBL; AF279436; AAF86350.1; -; mRNA.
DR   EMBL; AB049137; BAB13736.1; -; mRNA.
DR   EMBL; AF477982; AAL82632.1; -; mRNA.
DR   EMBL; AF477983; AAL82633.1; -; mRNA.
DR   EMBL; AF477984; AAL82634.1; -; mRNA.
DR   EMBL; AF477985; AAL82635.1; -; mRNA.
DR   EMBL; AF477986; AAL82636.1; -; mRNA.
DR   CCDS; CCDS21823.1; -.
DR   RefSeq; NP_068687.1; NM_021887.2.
DR   AlphaFoldDB; Q9JHX3; -.
DR   SMR; Q9JHX3; -.
DR   STRING; 10090.ENSMUSP00000033000; -.
DR   GlyGen; Q9JHX3; 6 sites.
DR   iPTMnet; Q9JHX3; -.
DR   PhosphoSitePlus; Q9JHX3; -.
DR   PaxDb; Q9JHX3; -.
DR   PRIDE; Q9JHX3; -.
DR   ProteomicsDB; 267040; -.
DR   ABCD; Q9JHX3; 35 sequenced antibodies.
DR   Antibodypedia; 12828; 457 antibodies from 41 providers.
DR   DNASU; 60504; -.
DR   Ensembl; ENSMUST00000033000; ENSMUSP00000033000; ENSMUSG00000030745.
DR   GeneID; 60504; -.
DR   KEGG; mmu:60504; -.
DR   UCSC; uc012ftn.1; mouse.
DR   CTD; 50615; -.
DR   MGI; MGI:1890475; Il21r.
DR   VEuPathDB; HostDB:ENSMUSG00000030745; -.
DR   eggNOG; ENOG502S0QM; Eukaryota.
DR   GeneTree; ENSGT00510000048783; -.
DR   HOGENOM; CLU_039739_0_0_1; -.
DR   InParanoid; Q9JHX3; -.
DR   OMA; RFFQPLY; -.
DR   OrthoDB; 774083at2759; -.
DR   PhylomeDB; Q9JHX3; -.
DR   TreeFam; TF337874; -.
DR   Reactome; R-MMU-9020958; Interleukin-21 signaling.
DR   BioGRID-ORCS; 60504; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Il21r; mouse.
DR   PRO; PR:Q9JHX3; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9JHX3; protein.
DR   Bgee; ENSMUSG00000030745; Expressed in thymus and 45 other tissues.
DR   ExpressionAtlas; Q9JHX3; baseline and differential.
DR   Genevisible; Q9JHX3; 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:0004896; F:cytokine receptor activity; IDA:MGI.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 2.
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   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..529
FT                   /note="Interleukin-21 receptor"
FT                   /id="PRO_0000010882"
FT   TOPO_DOM        20..237
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..529
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          21..118
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          119..228
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          458..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           214..218
FT                   /note="WSXWS motif"
FT   MOTIF           266..274
FT                   /note="Box 1 motif"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        214
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBE5"
FT   DISULFID        20..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..35
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..81
FT                   /evidence="ECO:0000250"
FT   VARIANT         69
FT                   /note="R -> K (in strain: BALB/c and SJL/J)"
FT   VARIANT         200
FT                   /note="V -> M (in strain: BALB/c and SJL/J)"
SQ   SEQUENCE   529 AA;  58355 MW;  8B41816B0D426581 CRC64;
     MPRGPVAALL LLILHGAWSC LDLTCYTDYL WTITCVLETR SPNPSILSLT WQDEYEELQD
     QETFCSLHRS GHNTTHIWYT CHMRLSQFLS DEVFIVNVTD QSGNNSQECG SFVLAESIKP
     APPLNVTVAF SGRYDISWDS AYDEPSNYVL RGKLQYELQY RNLRDPYAVR PVTKLISVDS
     RNVSLLPEEF HKDSSYQLQV RAAPQPGTSF RGTWSEWSDP VIFQTQAGEP EAGWDPHMLL
     LLAVLIIVLV FMGLKIHLPW RLWKKIWAPV PTPESFFQPL YREHSGNFKK WVNTPFTASS
     IELVPQSSTT TSALHLSLYP AKEKKFPGLP GLEEQLECDG MSEPGHWCII PLAAGQAVSA
     YSEERDRPYG LVSIDTVTVG DAEGLCVWPC SCEDDGYPAM NLDAGRESGP NSEDLLLVTD
     PAFLSCGCVS GSGLRLGGSP GSLLDRLRLS FAKEGDWTAD PTWRTGSPGG GSESEAGSPP
     GLDMDTFDSG FAGSDCGSPV ETDEGPPRSY LRQWVVRTPP PVDSGAQSS
 
 
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