I15RA_HUMAN
ID I15RA_HUMAN Reviewed; 267 AA.
AC Q13261; B4E2C2; Q3B769; Q5JVA1; Q5JVA2; Q5JVA4; Q6B0J2; Q7LDR4; Q7Z609;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, AND VARIANT THR-182.
RC TISSUE=Bone marrow stroma;
RX PubMed=8530383; DOI=10.1074/jbc.270.50.29862;
RA Anderson D.M., Kumaki S., Ahdieh M., Bertles J., Tometsko M., Loomis A.,
RA Giri J., Copeland N.G., Gilbert D.J., Jenkins N.A., Valentine V.,
RA Shapiro D.N., Morris S.W., Park L.S., Cosman D.;
RT "Functional characterization of the human interleukin-15 receptor alpha
RT chain and close linkage of IL15RA and IL2RA genes.";
RL J. Biol. Chem. 270:29862-29869(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-182.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 9), AND VARIANT
RP THR-182.
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-267 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [9]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=10480910; DOI=10.1074/jbc.274.38.26978;
RA Dubois S., Magrangeas F., Lehours P., Raher S., Bernard J., Boisteau O.,
RA Leroy S., Minvielle S., Godard A., Jacques Y.;
RT "Natural splicing of exon 2 of human interleukin-15 receptor alpha-chain
RT mRNA results in a shortened form with a distinct pattern of expression.";
RL J. Biol. Chem. 274:26978-26984(1999).
RN [10]
RP RETRACTED PAPER.
RX PubMed=11714793; DOI=10.4049/jimmunol.167.11.6292;
RA Bulanova E., Budagian V., Pohl T., Krause H., Durkop H., Paus R.,
RA Bulfone-Paus S.;
RT "The IL-15R alpha chain signals through association with Syk in human B
RT cells.";
RL J. Immunol. 167:6292-6302(2001).
RN [11]
RP RETRACTION NOTICE OF PUBMED:11714793.
RX PubMed=21289315; DOI=10.4049/jimmunol.1090142;
RA Pohl T., Krause H., Duerkop H., Paus R., Bulfone-Paus S.;
RT "The IL-15R alpha chain signals through association with Syk in human B
RT cells.";
RL J. Immunol. 186:2681-2681(2011).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=12114302; DOI=10.1111/j.1749-6632.2002.tb04245.x;
RA Kurowska M., Rudnicka W., Maslinska D., Maslinski W.;
RT "Expression of IL-15 and IL-15 receptor isoforms in select structures of
RT human fetal brain.";
RL Ann. N. Y. Acad. Sci. 966:441-445(2002).
RN [13]
RP LIGAND-BINDING.
RX PubMed=15039446; DOI=10.1074/jbc.m312458200;
RA Bernard J., Harb C., Mortier E., Quemener A., Meloen R.H.,
RA Vermot-Desroches C., Wijdeness J., van Dijken P., Grotzinger J.,
RA Slootstra J.W., Plet A., Jacques Y.;
RT "Identification of an interleukin-15alpha receptor-binding site on human
RT interleukin-15.";
RL J. Biol. Chem. 279:24313-24322(2004).
RN [14]
RP SUBCELLULAR LOCATION (SOLUBLE INTERLEUKIN-15 RECEPTOR SUBUNIT ALPHA),
RP PROTEOLYTIC PROCESSING, AND LIGAND-BINDING.
RX PubMed=15265897; DOI=10.4049/jimmunol.173.3.1681;
RA Mortier E., Bernard J., Plet A., Jacques Y.;
RT "Natural, proteolytic release of a soluble form of human IL-15 receptor
RT alpha-chain that behaves as a specific, high affinity IL-15 antagonist.";
RL J. Immunol. 173:1681-1688(2004).
RN [15]
RP FUNCTION, INTERACTION WITH SYK, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15123770; DOI=10.1189/jlb.0605298;
RA Ratthe C., Girard D.;
RT "Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent
RT mechanism: importance of the IL-15Ralpha chain.";
RL J. Leukoc. Biol. 76:162-168(2004).
RN [16]
RP STRUCTURE BY NMR OF 31-96, AND DISULFIDE BONDS.
RX PubMed=16377614; DOI=10.1074/jbc.m513118200;
RA Lorenzen I., Dingley A.J., Jacques Y., Grotzinger J.;
RT "The structure of the interleukin-15 alpha receptor and its implications
RT for ligand binding.";
RL J. Biol. Chem. 281:6642-6647(2006).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-132 IN COMPLEX WITH IL15, AND
RP DISULFIDE BONDS.
RX PubMed=17643103; DOI=10.1038/ni1492;
RA Chirifu M., Hayashi C., Nakamura T., Toma S., Shuto T., Kai H.,
RA Yamagata Y., Davis S.J., Ikemizu S.;
RT "Crystal structure of the IL-15-IL-15Ralpha complex, a cytokine-receptor
RT unit presented in trans.";
RL Nat. Immunol. 8:1001-1007(2007).
CC -!- FUNCTION: High-affinity receptor for interleukin-15 (PubMed:8530383).
CC Can signal both in cis and trans where IL15R from one subset of cells
CC presents IL15 to neighboring IL2RG-expressing cells (By similarity). In
CC neutrophils, binds and activates kinase SYK in response to IL15
CC stimulation (PubMed:15123770). In neutrophils, required for IL15-
CC induced phagocytosis in a SYK-dependent manner (PubMed:15123770).
CC Expression of different isoforms may alter or interfere with signal
CC transduction (PubMed:10480910). {ECO:0000250|UniProtKB:Q60819,
CC ECO:0000269|PubMed:10480910, ECO:0000269|PubMed:15123770,
CC ECO:0000269|PubMed:8530383}.
CC -!- FUNCTION: [Isoform 5]: Does not bind IL15.
CC {ECO:0000269|PubMed:10480910}.
CC -!- FUNCTION: [Isoform 6]: Does not bind IL15.
CC {ECO:0000269|PubMed:10480910}.
CC -!- FUNCTION: [Isoform 7]: Does not bind IL15.
CC {ECO:0000269|PubMed:10480910}.
CC -!- FUNCTION: [Isoform 8]: Does not bind IL15.
CC {ECO:0000269|PubMed:10480910}.
CC -!- SUBUNIT: The interleukin-15 receptor IL15R is a heterotrimer of IL15RA,
CC IL2RB and IL2RG. IL15RA also self-associates (PubMed:17643103).
CC Interacts with SYK (PubMed:15123770). {ECO:0000269|PubMed:15123770,
CC ECO:0000269|PubMed:17643103}.
CC -!- INTERACTION:
CC Q13261; P40933: IL15; NbExp=5; IntAct=EBI-980354, EBI-980274;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10480910}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:10480910}. Nucleus
CC membrane {ECO:0000269|PubMed:10480910}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:10480910}. Cell surface
CC {ECO:0000269|PubMed:15123770}. Note=Mainly found associated with the
CC nuclear membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Endoplasmic reticulum membrane;
CC Single-pass type I membrane protein. Golgi apparatus membrane; Single-
CC pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass
CC type I membrane protein. Membrane; Single-pass type I membrane protein.
CC Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with
CC endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the
CC nuclear membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Endoplasmic reticulum membrane;
CC Single-pass type I membrane protein. Golgi apparatus membrane; Single-
CC pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass
CC type I membrane protein. Membrane; Single-pass type I membrane protein.
CC Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with
CC endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the
CC nuclear membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Endoplasmic reticulum membrane;
CC Single-pass type I membrane protein. Golgi apparatus membrane; Single-
CC pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass
CC type I membrane protein. Membrane; Single-pass type I membrane protein.
CC Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with
CC endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the
CC nuclear membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Endoplasmic reticulum membrane;
CC Single-pass type I membrane protein. Golgi apparatus membrane; Single-
CC pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass
CC type I membrane protein. Membrane; Single-pass type I membrane protein.
CC Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with
CC endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the
CC nuclear membrane.
CC -!- SUBCELLULAR LOCATION: [Soluble interleukin-15 receptor subunit alpha]:
CC Secreted, extracellular space {ECO:0000269|PubMed:15265897}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q13261-1; Sequence=Displayed;
CC Name=2; Synonyms=delta3E1E7Il-15RA;
CC IsoId=Q13261-3; Sequence=VSP_012625;
CC Name=3; Synonyms=E1E7'Il-15RA;
CC IsoId=Q13261-4; Sequence=VSP_012626;
CC Name=4; Synonyms=delta3E1E7'Il-15RA;
CC IsoId=Q13261-5; Sequence=VSP_012625, VSP_012626;
CC Name=5; Synonyms=delta2E1E7Il-15RA;
CC IsoId=Q13261-6; Sequence=VSP_012624;
CC Name=6; Synonyms=delta2E1E7'Il-15RA;
CC IsoId=Q13261-7; Sequence=VSP_012624, VSP_012626;
CC Name=7; Synonyms=delta2deltaE1E73Il-15RA;
CC IsoId=Q13261-8; Sequence=VSP_012623;
CC Name=8; Synonyms=delta2delta3E1E7'Il-15RA;
CC IsoId=Q13261-9; Sequence=VSP_012623, VSP_012626;
CC Name=9;
CC IsoId=Q13261-10; Sequence=VSP_055406;
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils (at protein level)
CC (PubMed:15123770). Expressed in fetal brain with higher expression in
CC the hippocampus and cerebellum than in cortex and thalamus
CC (PubMed:12114302). Higher levels of soluble sIL-15RA form in comparison
CC with membrane-bound forms is present in all brain structures
CC (PubMed:12114302). Isoforms 1, 3, 4, 5, 6, 7, 8 and 9: Widely expressed
CC (PubMed:10480910, PubMed:8530383). {ECO:0000269|PubMed:10480910,
CC ECO:0000269|PubMed:12114302, ECO:0000269|PubMed:15123770,
CC ECO:0000269|PubMed:8530383}.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000269|PubMed:10480910}.
CC -!- PTM: A soluble form (sIL-15RA) arises from proteolytic shedding of the
CC membrane-anchored receptor (PubMed:15265897). It also binds IL-15 and
CC thus interferes with IL-15 binding to the membrane receptor
CC (PubMed:15265897). {ECO:0000269|PubMed:15265897}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88175.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW86419.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il15ra/";
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DR EMBL; U31628; AAC50312.1; -; mRNA.
DR EMBL; CR457064; CAG33345.1; -; mRNA.
DR EMBL; CR542023; CAG46820.1; -; mRNA.
DR EMBL; AY316538; AAP69528.1; -; Genomic_DNA.
DR EMBL; AK304211; BAG65084.1; -; mRNA.
DR EMBL; AL137186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86417.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86418.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86419.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC074726; AAH74726.1; -; mRNA.
DR EMBL; BC107777; AAI07778.1; -; mRNA.
DR EMBL; BC121140; AAI21141.1; -; mRNA.
DR EMBL; BC121141; AAI21142.1; -; mRNA.
DR EMBL; AF035279; AAB88175.1; ALT_INIT; mRNA.
DR CCDS; CCDS58069.1; -. [Q13261-10]
DR CCDS; CCDS7074.1; -. [Q13261-1]
DR CCDS; CCDS7075.2; -. [Q13261-3]
DR RefSeq; NP_001230468.1; NM_001243539.1. [Q13261-10]
DR RefSeq; NP_001243694.1; NM_001256765.1.
DR RefSeq; NP_002180.1; NM_002189.3. [Q13261-1]
DR RefSeq; NP_751950.2; NM_172200.2. [Q13261-3]
DR PDB; 2ERS; NMR; -; A=31-96.
DR PDB; 2Z3Q; X-ray; 1.85 A; B/D=31-132.
DR PDB; 2Z3R; X-ray; 2.00 A; B/D/F/H/J/L/N/P=31-132.
DR PDB; 4GS7; X-ray; 2.35 A; D=30-97.
DR PDBsum; 2ERS; -.
DR PDBsum; 2Z3Q; -.
DR PDBsum; 2Z3R; -.
DR PDBsum; 4GS7; -.
DR AlphaFoldDB; Q13261; -.
DR BMRB; Q13261; -.
DR SMR; Q13261; -.
DR BioGRID; 109814; 9.
DR IntAct; Q13261; 9.
DR ChEMBL; CHEMBL4665592; -.
DR GuidetoPHARMACOLOGY; 1702; -.
DR GlyGen; Q13261; 1 site.
DR iPTMnet; Q13261; -.
DR BioMuta; IL15RA; -.
DR DMDM; 59799763; -.
DR MassIVE; Q13261; -.
DR MaxQB; Q13261; -.
DR PaxDb; Q13261; -.
DR PeptideAtlas; Q13261; -.
DR PRIDE; Q13261; -.
DR ProteomicsDB; 59258; -. [Q13261-1]
DR ProteomicsDB; 59259; -. [Q13261-3]
DR ProteomicsDB; 59260; -. [Q13261-4]
DR ProteomicsDB; 59261; -. [Q13261-5]
DR ProteomicsDB; 59262; -. [Q13261-6]
DR ProteomicsDB; 59264; -. [Q13261-8]
DR Antibodypedia; 24259; 484 antibodies from 35 providers.
DR DNASU; 3601; -.
DR Ensembl; ENST00000379971.5; ENSP00000369306.1; ENSG00000134470.21. [Q13261-9]
DR Ensembl; ENST00000379977.8; ENSP00000369312.3; ENSG00000134470.21. [Q13261-1]
DR Ensembl; ENST00000397250.6; ENSP00000380422.2; ENSG00000134470.21. [Q13261-8]
DR Ensembl; ENST00000397255.7; ENSP00000380426.3; ENSG00000134470.21. [Q13261-4]
DR Ensembl; ENST00000525219.6; ENSP00000431529.2; ENSG00000134470.21. [Q13261-10]
DR Ensembl; ENST00000528354.5; ENSP00000435454.1; ENSG00000134470.21. [Q13261-3]
DR Ensembl; ENST00000530685.5; ENSP00000435995.1; ENSG00000134470.21. [Q13261-5]
DR GeneID; 3601; -.
DR KEGG; hsa:3601; -.
DR MANE-Select; ENST00000379977.8; ENSP00000369312.3; NM_002189.4; NP_002180.1.
DR UCSC; uc001iiv.4; human. [Q13261-1]
DR CTD; 3601; -.
DR DisGeNET; 3601; -.
DR GeneCards; IL15RA; -.
DR HGNC; HGNC:5978; IL15RA.
DR HPA; ENSG00000134470; Low tissue specificity.
DR MIM; 601070; gene.
DR neXtProt; NX_Q13261; -.
DR OpenTargets; ENSG00000134470; -.
DR PharmGKB; PA29791; -.
DR VEuPathDB; HostDB:ENSG00000134470; -.
DR GeneTree; ENSGT00390000000121; -.
DR HOGENOM; CLU_063804_1_0_1; -.
DR InParanoid; Q13261; -.
DR OMA; QVEMESM; -.
DR OrthoDB; 1326471at2759; -.
DR PhylomeDB; Q13261; -.
DR TreeFam; TF338443; -.
DR PathwayCommons; Q13261; -.
DR Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR SignaLink; Q13261; -.
DR SIGNOR; Q13261; -.
DR BioGRID-ORCS; 3601; 13 hits in 1089 CRISPR screens.
DR EvolutionaryTrace; Q13261; -.
DR GeneWiki; Interleukin_15_receptor,_alpha_subunit; -.
DR GenomeRNAi; 3601; -.
DR Pharos; Q13261; Tbio.
DR PRO; PR:Q13261; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q13261; protein.
DR Bgee; ENSG00000134470; Expressed in right lung and 133 other tissues.
DR ExpressionAtlas; Q13261; baseline and differential.
DR Genevisible; Q13261; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; 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:0004896; F:cytokine receptor activity; TAS:UniProtKB.
DR GO; GO:0042010; F:interleukin-15 receptor activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
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 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; Cytoplasmic vesicle; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Secreted; Signal; Sushi;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..267
FT /note="Interleukin-15 receptor subunit alpha"
FT /id="PRO_0000011044"
FT CHAIN 31..?
FT /note="Soluble interleukin-15 receptor subunit alpha"
FT /id="PRO_0000333855"
FT TOPO_DOM 31..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..95
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 102..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..75
FT DISULFID 59..93
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055406"
FT VAR_SEQ 30..127
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_012623"
FT VAR_SEQ 31..95
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_012624"
FT VAR_SEQ 95..128
FT /note="RDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKE -> K (in isoform
FT 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8530383"
FT /id="VSP_012625"
FT VAR_SEQ 232..267
FT /note="QTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL -> ASVCSCHPRSAG
FT HTCSVGSVC (in isoform 3, isoform 4, isoform 6 and isoform
FT 8)"
FT /evidence="ECO:0000303|PubMed:8530383"
FT /id="VSP_012626"
FT VARIANT 182
FT /note="N -> T (in dbSNP:rs2228059)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8530383, ECO:0000269|Ref.3"
FT /id="VAR_020967"
FT CONFLICT 200
FT /note="G -> D (in Ref. 8; AAH74726)"
FT /evidence="ECO:0000305"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:2Z3Q"
SQ SEQUENCE 267 AA; 28233 MW; A9CFC885189E96BE CRC64;
MAPRRARGCR TLGLPALLLL LLLRPPATRG ITCPPPMSVE HADIWVKSYS LYSRERYICN
SGFKRKAGTS SLTECVLNKA TNVAHWTTPS LKCIRDPALV HQRPAPPSTV TTAGVTPQPE
SLSPSGKEPA ASSPSSNNTA ATTAAIVPGS QLMPSKSPST GTTEISSHES SHGTPSQTTA
KNWELTASAS HQPPGVYPQG HSDTTVAIST STVLLCGLSA VSLLACYLKS RQTPPLASVE
MEAMEALPVT WGTSSRDEDL ENCSHHL
