位置:首页 > 蛋白库 > I10R1_MOUSE
I10R1_MOUSE
ID   I10R1_MOUSE             Reviewed;         575 AA.
AC   Q61727;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Interleukin-10 receptor subunit alpha;
DE            Short=IL-10 receptor subunit alpha;
DE            Short=IL-10R subunit alpha;
DE            Short=IL-10RA;
DE   AltName: Full=CDw210a;
DE   AltName: Full=Interleukin-10 receptor subunit 1;
DE            Short=IL-10R subunit 1;
DE            Short=IL-10R1;
DE   AltName: CD_antigen=CD210;
DE   Flags: Precursor;
GN   Name=Il10ra; Synonyms=Il10r;
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/6 X AJ F1; TISSUE=Hematopoietic;
RX   PubMed=8248239; DOI=10.1073/pnas.90.23.11267;
RA   Ho A.S.-Y., Liu Y., Khan T.A., Hsu D.-H., Bazan J.F., Moore K.W.;
RT   "A receptor for interleukin 10 is related to interferon receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11267-11271(1993).
RN   [2]
RP   FUNCTION, INTERACTION WITH STAT3, PHOSPHORYLATION AT TYR-443 AND TYR-493,
RP   AND MUTAGENESIS OF TYR-443 AND TYR-493.
RX   PubMed=8910398; DOI=10.1074/jbc.271.44.27954;
RA   Weber-Nordt R.M., Riley J.K., Greenlund A.C., Moore K.W., Darnell J.E.,
RA   Schreiber R.D.;
RT   "Stat3 recruitment by two distinct ligand-induced, tyrosine-phosphorylated
RT   docking sites in the interleukin-10 receptor intracellular domain.";
RL   J. Biol. Chem. 271:27954-27961(1996).
CC   -!- FUNCTION: Cell surface receptor for the cytokine IL10 that participates
CC       in IL10-mediated anti-inflammatory functions, limiting excessive tissue
CC       disruption caused by inflammation. Upon binding to IL10, induces a
CC       conformational change in IL10RB, allowing IL10RB to bind IL10 as well.
CC       In turn, the heterotetrameric assembly complex, composed of two
CC       subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that
CC       are constitutively associated with IL10RA and IL10RB respectively.
CC       These kinases then phosphorylate specific tyrosine residues in the
CC       intracellular domain in IL10RA leading to the recruitment and
CC       subsequent phosphorylation of STAT3 (PubMed:8910398). Once
CC       phosphorylated, STAT3 homodimerizes, translocates to the nucleus and
CC       activates the expression of anti-inflammatory genes. In addition,
CC       IL10RA-mediated activation of STAT3 inhibits starvation-induced
CC       autophagy (By similarity). {ECO:0000250|UniProtKB:Q13651,
CC       ECO:0000269|PubMed:8910398}.
CC   -!- SUBUNIT: Interacts with IL10. Interacts with IL10RB. Interacts (via its
CC       cytoplasmic domain) with JAK1 (via N-terminus). Interacts with BTRC;
CC       this interaction leads to IL10RA ubiquitination and subsequent
CC       degradation (By similarity). Interacts with STAT3 (PubMed:8910398).
CC       {ECO:0000250|UniProtKB:Q13651, ECO:0000269|PubMed:8910398}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13651};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13651}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q13651}.
CC   -!- PTM: Phosphorylated. Phosphorylation of the cytoplasmic tail induced
CC       STAT3 activation. {ECO:0000269|PubMed:8910398}.
CC   -!- PTM: Ubiquitinated by BTRC; ubiquitination leads to endocytosis and
CC       subsequent degradation of IL10RA. {ECO:0000250|UniProtKB:Q13651}.
CC   -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L12120; AAA16156.1; -; mRNA.
DR   CCDS; CCDS23131.1; -.
DR   PIR; A49667; A49667.
DR   RefSeq; NP_032374.1; NM_008348.3.
DR   AlphaFoldDB; Q61727; -.
DR   SMR; Q61727; -.
DR   DIP; DIP-247N; -.
DR   IntAct; Q61727; 1.
DR   STRING; 10090.ENSMUSP00000034594; -.
DR   GlyGen; Q61727; 5 sites.
DR   iPTMnet; Q61727; -.
DR   PhosphoSitePlus; Q61727; -.
DR   PaxDb; Q61727; -.
DR   PRIDE; Q61727; -.
DR   ProteomicsDB; 273067; -.
DR   Antibodypedia; 18560; 858 antibodies from 40 providers.
DR   DNASU; 16154; -.
DR   Ensembl; ENSMUST00000034594; ENSMUSP00000034594; ENSMUSG00000032089.
DR   GeneID; 16154; -.
DR   KEGG; mmu:16154; -.
DR   UCSC; uc009pfn.1; mouse.
DR   CTD; 3587; -.
DR   MGI; MGI:96538; Il10ra.
DR   VEuPathDB; HostDB:ENSMUSG00000032089; -.
DR   eggNOG; ENOG502S2PS; Eukaryota.
DR   GeneTree; ENSGT00510000048847; -.
DR   HOGENOM; CLU_033904_0_0_1; -.
DR   InParanoid; Q61727; -.
DR   OMA; SHFREYE; -.
DR   OrthoDB; 1456451at2759; -.
DR   PhylomeDB; Q61727; -.
DR   TreeFam; TF334107; -.
DR   Reactome; R-MMU-6783783; Interleukin-10 signaling.
DR   BioGRID-ORCS; 16154; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Il10ra; mouse.
DR   PRO; PR:Q61727; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q61727; protein.
DR   Bgee; ENSMUSG00000032089; Expressed in granulocyte and 62 other tissues.
DR   ExpressionAtlas; Q61727; baseline and differential.
DR   Genevisible; Q61727; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0019969; F:interleukin-10 binding; ISO:MGI.
DR   GO; GO:0004920; F:interleukin-10 receptor activity; ISO:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR   GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0070086; P:ubiquitin-dependent endocytosis; ISO:MGI.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF01108; Tissue_fac; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..575
FT                   /note="Interleukin-10 receptor subunit alpha"
FT                   /id="PRO_0000011013"
FT   TOPO_DOM        17..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..575
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         443
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:8910398"
FT   MOD_RES         493
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:8910398"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
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        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        204..225
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         443
FT                   /note="Y->F: Complete loss of STAT3 activation; in
FT                   association with F-493."
FT                   /evidence="ECO:0000269|PubMed:8910398"
FT   MUTAGEN         493
FT                   /note="Y->F: Complete loss of STAT3 activation; in
FT                   association with F-443."
FT                   /evidence="ECO:0000269|PubMed:8910398"
SQ   SEQUENCE   575 AA;  64248 MW;  820B9CD576F686B7 CRC64;
     MLSRLLPFLV TISSLSLEFI AYGTELPSPS YVWFEARFFQ HILHWKPIPN QSESTYYEVA
     LKQYGNSTWN DIHICRKAQA LSCDLTTFTL DLYHRSYGYR ARVRAVDNSQ YSNWTTTETR
     FTVDEVILTV DSVTLKAMDG IIYGTIHPPR PTITPAGDEY EQVFKDLRVY KISIRKFSEL
     KNATKRVKQE TFTLTVPIGV RKFCVKVLPR LESRINKAEW SEEQCLLITT EQYFTVTNLS
     ILVISMLLFC GILVCLVLQW YIRHPGKLPT VLVFKKPHDF FPANPLCPET PDAIHIVDLE
     VFPKVSLELR DSVLHGSTDS GFGSGKPSLQ TEESQFLLPG SHPQIQGTLG KEESPGLQAT
     CGDNTDSGIC LQEPGLHSSM GPAWKQQLGY THQDQDDSDV NLVQNSPGQP KYTQDASALG
     HVCLLEPKAP EEKDQVMVTF QGYQKQTRWK AEAAGPAECL DEEIPLTDAF DPELGVHLQD
     DLAWPPPALA AGYLKQESQG MASAPPGTPS RQWNQLTEEW SLLGVVSCED LSIESWRFAH
     KLDPLDCGAA PGGLLDSLGS NLVTLPLISS LQVEE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024