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I15RA_MOUSE
ID   I15RA_MOUSE             Reviewed;         263 AA.
AC   Q60819; A2AP35; A2AP36; A2AP37; Q80Z90; Q80Z91; Q80Z92; Q8R5E4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Interleukin-15 receptor subunit alpha;
DE            Short=IL-15 receptor subunit alpha;
DE            Short=IL-15R-alpha;
DE            Short=IL-15RA;
DE   AltName: CD_antigen=CD215;
DE   Contains:
DE     RecName: Full=Soluble interleukin-15 receptor subunit alpha;
DE              Short=sIL-15 receptor subunit alpha;
DE              Short=sIL-15R-alpha;
DE              Short=sIL-15RA;
DE   Flags: Precursor;
GN   Name=Il15ra;
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] (ISOFORM 1), LIGAND-BINDING, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=7641685; DOI=10.1002/j.1460-2075.1995.tb00035.x;
RA   Giri J.G., Kumaki S., Ahdieh M., Friend D.J., Loomis A., Shanebeck K.,
RA   DuBose R., Cosman D., Park L.S., Anderson D.M.;
RT   "Identification and cloning of a novel IL-15 binding protein that is
RT   structurally related to the alpha chain of the IL-2 receptor.";
RL   EMBO J. 14:3654-3663(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=12885940; DOI=10.1189/jlb.0303097;
RA   Toomey J.A., Gays F., Foster D., Brooks C.G.;
RT   "Cytokine requirements for the growth and development of mouse NK cells in
RT   vitro.";
RL   J. Leukoc. Biol. 74:233-242(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   RETRACTED PAPER.
RX   PubMed=12734349; DOI=10.4049/jimmunol.170.10.5045;
RA   Bulanova E., Budagian V., Orinska Z., Krause H., Paus R., Bulfone-Paus S.;
RT   "Mast cells express novel functional IL-15 receptor alpha isoforms.";
RL   J. Immunol. 170:5045-5055(2003).
RN   [6]
RP   RETRACTION NOTICE OF PUBMED:12734349.
RX   PubMed=21289316; DOI=10.4049/jimmunol.1090143;
RA   Krause H., Paus R., Orinska Z., Bulfone-Paus S.;
RT   "Mast cells express novel functional IL-15 receptor alpha isoforms.";
RL   J. Immunol. 186:2682-2682(2011).
RN   [7]
RP   RETRACTED PAPER.
RX   PubMed=15215246; DOI=10.1074/jbc.m404125200;
RA   Budagian V., Bulanova E., Orinska Z., Ludwig A., Rose-John S., Saftig P.,
RA   Borden E.C., Bulfone-Paus S.;
RT   "Natural soluble interleukin-15Ralpha is generated by cleavage that
RT   involves the tumor necrosis factor-alpha-converting enzyme (TACE/ADAM17).";
RL   J. Biol. Chem. 279:40368-40375(2004).
RN   [8]
RP   RETRACTION NOTICE OF PUBMED:15215246.
RX   PubMed=21516612; DOI=10.1074/jbc.a110.404125;
RA   Budagian V., Bulanova E., Orinska Z., Ludwig A., Rose-John S., Saftig P.,
RA   Borden E.C., Bulfone-Paus S.;
RT   "Natural soluble interleukin-15Ralpha is generated by cleavage that
RT   involves the tumor necrosis factor-alpha-converting enzyme (TACE/ADAM17).";
RL   J. Biol. Chem. 286:9894-9894(2011).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 33-103 IN COMPLEX WITH IL15,
RP   FUNCTION, AND DISULFIDE BONDS.
RX   PubMed=17947230; DOI=10.1074/jbc.m706150200;
RA   Olsen S.K., Ota N., Kishishita S., Kukimoto-Niino M., Murayama K.,
RA   Uchiyama H., Toyama M., Terada T., Shirouzu M., Kanagawa O., Yokoyama S.;
RT   "Crystal Structure of the interleukin-15.interleukin-15 receptor alpha
RT   complex: insights into trans and cis presentation.";
RL   J. Biol. Chem. 282:37191-37204(2007).
CC   -!- FUNCTION: High-affinity receptor for interleukin-15 (PubMed:17947230).
CC       Can signal both in cis and trans where IL15R from one subset of cells
CC       presents IL15 to neighboring IL2RG-expressing cells (PubMed:17947230).
CC       In neutrophils, binds and activates kinase SYK in response to IL15
CC       stimulation (By similarity). In neutrophils, required for IL15-induced
CC       phagocytosis in a SYK-dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:Q13261, ECO:0000269|PubMed:17947230}.
CC   -!- SUBUNIT: The interleukin-15 receptor IL15R is a heterotrimer of IL15RA,
CC       IL2RB and IL2RG. IL15RA also self-associates (By similarity). Interacts
CC       with SYK (By similarity). {ECO:0000250|UniProtKB:Q13261}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q13261}; Single-
CC       pass type I membrane protein {ECO:0000250|UniProtKB:Q13261}. Nucleus
CC       membrane {ECO:0000250|UniProtKB:Q13261}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:Q13261}. Cell surface
CC       {ECO:0000250|UniProtKB:Q13261}.
CC   -!- SUBCELLULAR LOCATION: [Soluble interleukin-15 receptor subunit alpha]:
CC       Secreted, extracellular space {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q60819-1; Sequence=Displayed;
CC       Name=2; Synonyms=1A;
CC         IsoId=Q60819-2; Sequence=VSP_012629, VSP_012630;
CC       Name=3; Synonyms=1B, IL-15R-alphadelta4;
CC         IsoId=Q60819-3; Sequence=VSP_012629, VSP_012630, VSP_012631;
CC       Name=4; Synonyms=1C, IL-15R-alphadelta34;
CC         IsoId=Q60819-4; Sequence=VSP_012628, VSP_012629, VSP_012630,
CC                                  VSP_012631, VSP_012632;
CC       Name=5; Synonyms=2, 2A;
CC         IsoId=Q60819-5; Sequence=VSP_012627, VSP_012628, VSP_012629;
CC       Name=6; Synonyms=IL-15R-alphadelta345;
CC         IsoId=Q60819-6; Sequence=VSP_012628, VSP_012629, VSP_012630,
CC                                  VSP_012631, VSP_012633;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12885940,
CC       ECO:0000269|PubMed:7641685}.
CC   -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000250|UniProtKB:Q13261}.
CC   -!- PTM: A soluble form (sIL-15RA) arises from proteolytic shedding of the
CC       membrane-anchored receptor (By similarity). It also binds IL15 and thus
CC       interferes with IL15 binding to the membrane receptor (By similarity).
CC       {ECO:0000250|UniProtKB:Q13261}.
CC   -!- CAUTION: It was shown that proteolytic cleavage of Il15ra involves
CC       ADAM17/TACE; this publication has later been retracted.
CC       {ECO:0000269|PubMed:15215246, ECO:0000305|PubMed:21516612}.
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DR   EMBL; U22339; AAC52240.1; -; Genomic_DNA.
DR   EMBL; AY219715; AAO62310.1; -; mRNA.
DR   EMBL; AY219716; AAO62311.1; -; mRNA.
DR   EMBL; AY219717; AAO62312.1; -; mRNA.
DR   EMBL; AY221616; AAO74882.1; -; mRNA.
DR   EMBL; AL831794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC022705; AAH22705.1; -; mRNA.
DR   CCDS; CCDS15686.1; -. [Q60819-1]
DR   CCDS; CCDS15687.1; -. [Q60819-5]
DR   CCDS; CCDS70977.1; -. [Q60819-2]
DR   CCDS; CCDS70978.1; -. [Q60819-3]
DR   CCDS; CCDS70979.1; -. [Q60819-4]
DR   PIR; S57346; S57346.
DR   RefSeq; NP_001258426.1; NM_001271497.1. [Q60819-5]
DR   RefSeq; NP_001258428.1; NM_001271499.1. [Q60819-2]
DR   RefSeq; NP_001258429.1; NM_001271500.1. [Q60819-3]
DR   RefSeq; NP_001258430.1; NM_001271501.1. [Q60819-4]
DR   RefSeq; NP_032384.1; NM_008358.2. [Q60819-1]
DR   RefSeq; NP_598597.1; NM_133836.2. [Q60819-5]
DR   RefSeq; XP_006497427.1; XM_006497364.1. [Q60819-5]
DR   RefSeq; XP_017171184.1; XM_017315695.1. [Q60819-6]
DR   PDB; 2PSM; X-ray; 2.19 A; C/F=33-103.
DR   PDBsum; 2PSM; -.
DR   AlphaFoldDB; Q60819; -.
DR   SMR; Q60819; -.
DR   STRING; 10090.ENSMUSP00000077878; -.
DR   GlyGen; Q60819; 1 site.
DR   EPD; Q60819; -.
DR   PaxDb; Q60819; -.
DR   PRIDE; Q60819; -.
DR   ProteomicsDB; 273244; -. [Q60819-1]
DR   ProteomicsDB; 273245; -. [Q60819-2]
DR   ProteomicsDB; 273246; -. [Q60819-3]
DR   ProteomicsDB; 273247; -. [Q60819-4]
DR   ProteomicsDB; 273248; -. [Q60819-5]
DR   ProteomicsDB; 273249; -. [Q60819-6]
DR   Antibodypedia; 24259; 484 antibodies from 35 providers.
DR   DNASU; 16169; -.
DR   Ensembl; ENSMUST00000078834; ENSMUSP00000077878; ENSMUSG00000023206. [Q60819-1]
DR   Ensembl; ENSMUST00000114831; ENSMUSP00000110480; ENSMUSG00000023206. [Q60819-2]
DR   Ensembl; ENSMUST00000114832; ENSMUSP00000110481; ENSMUSG00000023206. [Q60819-6]
DR   Ensembl; ENSMUST00000114833; ENSMUSP00000110482; ENSMUSG00000023206. [Q60819-4]
DR   Ensembl; ENSMUST00000114834; ENSMUSP00000110483; ENSMUSG00000023206. [Q60819-3]
DR   Ensembl; ENSMUST00000128156; ENSMUSP00000126364; ENSMUSG00000023206. [Q60819-5]
DR   Ensembl; ENSMUST00000135341; ENSMUSP00000132731; ENSMUSG00000023206. [Q60819-5]
DR   Ensembl; ENSMUST00000138349; ENSMUSP00000131473; ENSMUSG00000023206. [Q60819-5]
DR   GeneID; 16169; -.
DR   KEGG; mmu:16169; -.
DR   UCSC; uc008iiw.2; mouse. [Q60819-6]
DR   UCSC; uc008iix.2; mouse. [Q60819-1]
DR   UCSC; uc008iiy.2; mouse. [Q60819-2]
DR   UCSC; uc008iiz.2; mouse. [Q60819-3]
DR   UCSC; uc008ija.2; mouse. [Q60819-4]
DR   CTD; 3601; -.
DR   MGI; MGI:104644; Il15ra.
DR   VEuPathDB; HostDB:ENSMUSG00000023206; -.
DR   eggNOG; ENOG502SG86; Eukaryota.
DR   GeneTree; ENSGT00390000000121; -.
DR   HOGENOM; CLU_2014496_0_0_1; -.
DR   InParanoid; Q60819; -.
DR   OMA; QVEMESM; -.
DR   OrthoDB; 1326471at2759; -.
DR   PhylomeDB; Q60819; -.
DR   TreeFam; TF338443; -.
DR   Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR   BioGRID-ORCS; 16169; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Il15ra; mouse.
DR   EvolutionaryTrace; Q60819; -.
DR   PRO; PR:Q60819; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q60819; protein.
DR   Bgee; ENSMUSG00000023206; Expressed in hindlimb stylopod muscle and 154 other tissues.
DR   ExpressionAtlas; Q60819; baseline and differential.
DR   Genevisible; Q60819; MM.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042010; F:interleukin-15 receptor activity; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:MGI.
DR   CDD; cd00033; CCP; 1.
DR   InterPro; IPR042372; IL15RA.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR15060; PTHR15060; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   SMART; SM00032; CCP; 1.
DR   SUPFAM; SSF57535; SSF57535; 1.
DR   PROSITE; PS50923; SUSHI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW   Nucleus; Phosphoprotein; Receptor; Reference proteome; Secreted; Signal;
KW   Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..263
FT                   /note="Interleukin-15 receptor subunit alpha"
FT                   /id="PRO_0000011045"
FT   CHAIN           33..?
FT                   /note="Soluble interleukin-15 receptor subunit alpha"
FT                   /id="PRO_0000333856"
FT   TOPO_DOM        33..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          34..98
FT                   /note="Sushi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          113..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT                   ECO:0000269|PubMed:17947230"
FT   DISULFID        62..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT                   ECO:0000269|PubMed:17947230"
FT   VAR_SEQ         1..97
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:12885940,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012627"
FT   VAR_SEQ         98..128
FT                   /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:12885940,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012628"
FT   VAR_SEQ         129..140
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT                   5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:12885940,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012629"
FT   VAR_SEQ         141..161
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:12885940"
FT                   /id="VSP_012630"
FT   VAR_SEQ         162..194
FT                   /note="Missing (in isoform 3, isoform 4 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:12885940"
FT                   /id="VSP_012631"
FT   VAR_SEQ         195..206
FT                   /note="EISPHSSKMTKV -> M (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_012633"
FT   VAR_SEQ         195
FT                   /note="E -> K (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12885940"
FT                   /id="VSP_012632"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:2PSM"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:2PSM"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:2PSM"
FT   TURN            82..84
FT                   /evidence="ECO:0007829|PDB:2PSM"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:2PSM"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:2PSM"
SQ   SEQUENCE   263 AA;  28061 MW;  BFCC2CE4BA58B504 CRC64;
     MASPQLRGYG VQAIPVLLLL LLLLLLPLRV TPGTTCPPPV SIEHADIRVK NYSVNSRERY
     VCNSGFKRKA GTSTLIECVI NKNTNVAHWT TPSLKCIRDP SLAHYSPVPT VVTPKVTSQP
     ESPSPSAKEP EAFSPKSDTA MTTETAIMPG SRLTPSQTTS AGTTGTGSHK SSRAPSLAAT
     MTLEPTASTS LRITEISPHS SKMTKVAIST SVLLVGAGVV MAFLAWYIKS RQPSQPCRVE
     VETMETVPMT VRASSKEDED TGA
 
 
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