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Interleukin-15 receptor subunit alpha (IL-15 receptor subunit alpha) (IL-15R-alpha) (IL-15RA) (CD antigen CD215) [Cleaved into: Soluble interleukin-15 receptor subunit alpha (sIL-15 receptor subunit alpha) (sIL-15R-alpha) (sIL-15RA)]

 I15RA_HUMAN             Reviewed;         267 AA.
Q13261; B4E2C2; Q3B769; Q5JVA1; Q5JVA2; Q5JVA4; Q6B0J2; Q7LDR4;
Q7Z609;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 153.
RecName: Full=Interleukin-15 receptor subunit alpha;
Short=IL-15 receptor subunit alpha;
Short=IL-15R-alpha;
Short=IL-15RA;
AltName: CD_antigen=CD215;
Contains:
RecName: Full=Soluble interleukin-15 receptor subunit alpha;
Short=sIL-15 receptor subunit alpha;
Short=sIL-15R-alpha;
Short=sIL-15RA;
Flags: Precursor;
Name=IL15RA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE
SPECIFICITY, AND VARIANT THR-182.
TISSUE=Bone marrow stroma;
PubMed=8530383; DOI=10.1074/jbc.270.50.29862;
Anderson D.M., Kumaki S., Ahdieh M., Bertles J., Tometsko M.,
Loomis A., Giri J., Copeland N.G., Gilbert D.J., Jenkins N.A.,
Valentine V., Shapiro D.N., Morris S.W., Park L.S., Cosman D.;
"Functional characterization of the human interleukin-15 receptor
alpha chain and close linkage of IL15RA and IL2RA genes.";
J. Biol. Chem. 270:29862-29869(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-182.
SeattleSNPs variation discovery resource;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 9), AND VARIANT
THR-182.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-267 (ISOFORM 1).
TISSUE=Brain;
PubMed=9110174;
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[9]
ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=10480910; DOI=10.1074/jbc.274.38.26978;
Dubois S., Magrangeas F., Lehours P., Raher S., Bernard J.,
Boisteau O., Leroy S., Minvielle S., Godard A., Jacques Y.;
"Natural splicing of exon 2 of human interleukin-15 receptor alpha-
chain mRNA results in a shortened form with a distinct pattern of
expression.";
J. Biol. Chem. 274:26978-26984(1999).
[10]
FUNCTION, INTERACTION WITH SYK, PHOSPHORYLATION BY SYK, AND
MUTAGENESIS OF TYR-227.
PubMed=11714793; DOI=10.4049/jimmunol.167.11.6292;
Bulanova E., Budagian V., Pohl T., Krause H., Durkop H., Paus R.,
Bulfone-Paus S.;
"The IL-15R alpha chain signals through association with Syk in human
B cells.";
J. Immunol. 167:6292-6302(2001).
[11]
TISSUE SPECIFICITY.
PubMed=12114302; DOI=10.1111/j.1749-6632.2002.tb04245.x;
Kurowska M., Rudnicka W., Maslinska D., Maslinski W.;
"Expression of IL-15 and IL-15 receptor isoforms in select structures
of human fetal brain.";
Ann. N. Y. Acad. Sci. 966:441-445(2002).
[12]
LIGAND-BINDING.
PubMed=15039446; DOI=10.1074/jbc.M312458200;
Bernard J., Harb C., Mortier E., Quemener A., Meloen R.H.,
Vermot-Desroches C., Wijdeness J., van Dijken P., Grotzinger J.,
Slootstra J.W., Plet A., Jacques Y.;
"Identification of an interleukin-15alpha receptor-binding site on
human interleukin-15.";
J. Biol. Chem. 279:24313-24322(2004).
[13]
PROTEOLYTIC PROCESSING, AND LIGAND-BINDING.
PubMed=15265897; DOI=10.4049/jimmunol.173.3.1681;
Mortier E., Bernard J., Plet A., Jacques Y.;
"Natural, proteolytic release of a soluble form of human IL-15
receptor alpha-chain that behaves as a specific, high affinity IL-15
antagonist.";
J. Immunol. 173:1681-1688(2004).
[14]
STRUCTURE BY NMR OF 31-96, AND DISULFIDE BONDS.
PubMed=16377614; DOI=10.1074/jbc.M513118200;
Lorenzen I., Dingley A.J., Jacques Y., Grotzinger J.;
"The structure of the interleukin-15 alpha receptor and its
implications for ligand binding.";
J. Biol. Chem. 281:6642-6647(2006).
[15]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-132 IN COMPLEX WITH IL15,
AND DISULFIDE BONDS.
PubMed=17643103; DOI=10.1038/ni1492;
Chirifu M., Hayashi C., Nakamura T., Toma S., Shuto T., Kai H.,
Yamagata Y., Davis S.J., Ikemizu S.;
"Crystal structure of the IL-15-IL-15Ralpha complex, a cytokine-
receptor unit presented in trans.";
Nat. Immunol. 8:1001-1007(2007).
-!- FUNCTION: High-affinity receptor for interleukin-15. Can signal
both in cis and trans where IL15R from one subset of cells
presents IL15 to neighboring IL2RG-expressing cells. Expression of
different isoforms may alter or interfere with signal
transduction. Isoform 5, isoform 6, isoform 7 and isoform 8 do not
bind IL15. Signal transduction involves SYK.
{ECO:0000269|PubMed:11714793, ECO:0000269|PubMed:8530383}.
-!- SUBUNIT: The interleukin-15 receptor IL15R is a heterotrimer of
IL15RA, IL2RB and IL2RG. IL15RA also self-associates (By
similarity). Interacts with SYK. {ECO:0000250,
ECO:0000269|PubMed:11714793, ECO:0000269|PubMed:17643103}.
-!- INTERACTION:
P40933:IL15; NbExp=5; IntAct=EBI-980354, EBI-980274;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10480910};
Single-pass type I membrane protein {ECO:0000269|PubMed:10480910}.
Nucleus membrane {ECO:0000269|PubMed:10480910}; Single-pass type I
membrane protein {ECO:0000269|PubMed:10480910}. Note=Mainly found
associated with the nuclear membrane.
-!- SUBCELLULAR LOCATION: Isoform 5: Endoplasmic reticulum membrane;
Single-pass type I membrane protein. Golgi apparatus membrane;
Single-pass type I membrane protein. Cytoplasmic vesicle membrane;
Single-pass type I membrane protein. Membrane; Single-pass type I
membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform
8 are associated with endoplasmic reticulum, Golgi and cytoplasmic
vesicles, but not with the nuclear membrane.
-!- SUBCELLULAR LOCATION: Isoform 6: Endoplasmic reticulum membrane;
Single-pass type I membrane protein. Golgi apparatus membrane;
Single-pass type I membrane protein. Cytoplasmic vesicle membrane;
Single-pass type I membrane protein. Membrane; Single-pass type I
membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform
8 are associated with endoplasmic reticulum, Golgi and cytoplasmic
vesicles, but not with the nuclear membrane.
-!- SUBCELLULAR LOCATION: Isoform 7: Endoplasmic reticulum membrane;
Single-pass type I membrane protein. Golgi apparatus membrane;
Single-pass type I membrane protein. Cytoplasmic vesicle membrane;
Single-pass type I membrane protein. Membrane; Single-pass type I
membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform
8 are associated with endoplasmic reticulum, Golgi and cytoplasmic
vesicles, but not with the nuclear membrane.
-!- SUBCELLULAR LOCATION: Isoform 8: Endoplasmic reticulum membrane;
Single-pass type I membrane protein. Golgi apparatus membrane;
Single-pass type I membrane protein. Cytoplasmic vesicle membrane;
Single-pass type I membrane protein. Membrane; Single-pass type I
membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform
8 are associated with endoplasmic reticulum, Golgi and cytoplasmic
vesicles, but not with the nuclear membrane.
-!- SUBCELLULAR LOCATION: Soluble interleukin-15 receptor subunit
alpha: Secreted, extracellular space.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1;
IsoId=Q13261-1; Sequence=Displayed;
Name=2; Synonyms=delta3E1E7Il-15RA;
IsoId=Q13261-3; Sequence=VSP_012625;
Name=3; Synonyms=E1E7'Il-15RA;
IsoId=Q13261-4; Sequence=VSP_012626;
Name=4; Synonyms=delta3E1E7'Il-15RA;
IsoId=Q13261-5; Sequence=VSP_012625, VSP_012626;
Name=5; Synonyms=delta2E1E7Il-15RA;
IsoId=Q13261-6; Sequence=VSP_012624;
Name=6; Synonyms=delta2E1E7'Il-15RA;
IsoId=Q13261-7; Sequence=VSP_012624, VSP_012626;
Name=7; Synonyms=delta2deltaE1E73Il-15RA;
IsoId=Q13261-8; Sequence=VSP_012623;
Name=8; Synonyms=delta2delta3E1E7'Il-15RA;
IsoId=Q13261-9; Sequence=VSP_012623, VSP_012626;
Name=9;
IsoId=Q13261-10; Sequence=VSP_055406;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1, isoform 3, isoform 4, isoform 5,
isoform 6, isoform 7, isoform 8 and isoform 9 are widely
expressed. Expressed in fetal brain with higher expression in the
hippocampus and cerebellum than in cortex and thalamus. Higher
levels of soluble sIL-15RA form in comparison with membrane-bound
forms is present in all brain structures.
{ECO:0000269|PubMed:10480910, ECO:0000269|PubMed:12114302,
ECO:0000269|PubMed:8530383}.
-!- PTM: A soluble form (sIL-15RA) arises from proteolytic shedding of
the membrane-anchored receptor. The cleavage involves ADAM17/TACE
(By similarity). It also binds IL-15 and thus interferes with IL-
15 binding to the membrane receptor. {ECO:0000250,
ECO:0000269|PubMed:15265897}.
-!- PTM: Phosphorylated by activated SYK.
{ECO:0000269|PubMed:11714793}.
-!- PTM: N-glycosylated and O-glycosylated.
{ECO:0000269|PubMed:10480910}.
-!- SEQUENCE CAUTION:
Sequence=AAB88175.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAI41080.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW86419.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il15ra/";
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EMBL; U31628; AAC50312.1; -; mRNA.
EMBL; CR457064; CAG33345.1; -; mRNA.
EMBL; CR542023; CAG46820.1; -; mRNA.
EMBL; AY316538; AAP69528.1; -; Genomic_DNA.
EMBL; AK304211; BAG65084.1; -; mRNA.
EMBL; AL137186; CAI41080.1; ALT_SEQ; Genomic_DNA.
EMBL; AL137186; CAI41082.1; -; Genomic_DNA.
EMBL; AL137186; CAI41083.1; -; Genomic_DNA.
EMBL; CH471072; EAW86417.1; -; Genomic_DNA.
EMBL; CH471072; EAW86418.1; -; Genomic_DNA.
EMBL; CH471072; EAW86419.1; ALT_SEQ; Genomic_DNA.
EMBL; BC074726; AAH74726.1; -; mRNA.
EMBL; BC107777; AAI07778.1; -; mRNA.
EMBL; BC121140; AAI21141.1; -; mRNA.
EMBL; BC121141; AAI21142.1; -; mRNA.
EMBL; AF035279; AAB88175.1; ALT_INIT; mRNA.
CCDS; CCDS58069.1; -. [Q13261-10]
CCDS; CCDS7074.1; -. [Q13261-1]
CCDS; CCDS7075.2; -. [Q13261-3]
RefSeq; NP_001230468.1; NM_001243539.1. [Q13261-10]
RefSeq; NP_001243694.1; NM_001256765.1.
RefSeq; NP_002180.1; NM_002189.3. [Q13261-1]
RefSeq; NP_751950.2; NM_172200.2. [Q13261-3]
UniGene; Hs.445124; -.
PDB; 2ERS; NMR; -; A=31-96.
PDB; 2Z3Q; X-ray; 1.85 A; B/D=31-132.
PDB; 2Z3R; X-ray; 2.00 A; B/D/F/H/J/L/N/P=31-132.
PDB; 4GS7; X-ray; 2.35 A; D=30-97.
PDBsum; 2ERS; -.
PDBsum; 2Z3Q; -.
PDBsum; 2Z3R; -.
PDBsum; 4GS7; -.
ProteinModelPortal; Q13261; -.
SMR; Q13261; -.
BioGrid; 109814; 8.
IntAct; Q13261; 9.
STRING; 9606.ENSP00000369312; -.
iPTMnet; Q13261; -.
BioMuta; IL15RA; -.
DMDM; 59799763; -.
MaxQB; Q13261; -.
PaxDb; Q13261; -.
PeptideAtlas; Q13261; -.
PRIDE; Q13261; -.
Ensembl; ENST00000379971; ENSP00000369306; ENSG00000134470. [Q13261-9]
Ensembl; ENST00000379977; ENSP00000369312; ENSG00000134470. [Q13261-1]
Ensembl; ENST00000397250; ENSP00000380422; ENSG00000134470. [Q13261-8]
Ensembl; ENST00000397255; ENSP00000380426; ENSG00000134470. [Q13261-4]
Ensembl; ENST00000525219; ENSP00000431529; ENSG00000134470. [Q13261-10]
Ensembl; ENST00000528354; ENSP00000435454; ENSG00000134470. [Q13261-3]
Ensembl; ENST00000530685; ENSP00000435995; ENSG00000134470. [Q13261-5]
GeneID; 3601; -.
KEGG; hsa:3601; -.
UCSC; uc001iiv.4; human. [Q13261-1]
CTD; 3601; -.
DisGeNET; 3601; -.
GeneCards; IL15RA; -.
H-InvDB; HIX0035314; -.
HGNC; HGNC:5978; IL15RA.
HPA; CAB026215; -.
MIM; 601070; gene.
neXtProt; NX_Q13261; -.
OpenTargets; ENSG00000134470; -.
PharmGKB; PA29791; -.
eggNOG; ENOG410IWP4; Eukaryota.
eggNOG; ENOG410Z8MM; LUCA.
GeneTree; ENSGT00390000000121; -.
HOGENOM; HOG000036788; -.
HOVERGEN; HBG052061; -.
InParanoid; Q13261; -.
KO; K05074; -.
PhylomeDB; Q13261; -.
TreeFam; TF338443; -.
Reactome; R-HSA-449836; Other interleukin signaling.
SignaLink; Q13261; -.
SIGNOR; Q13261; -.
EvolutionaryTrace; Q13261; -.
GeneWiki; Interleukin_15_receptor,_alpha_subunit; -.
GenomeRNAi; 3601; -.
PMAP-CutDB; Q13261; -.
PRO; PR:Q13261; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000134470; -.
CleanEx; HS_IL15RA; -.
ExpressionAtlas; Q13261; baseline and differential.
Genevisible; Q13261; HS.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004896; F:cytokine receptor activity; TAS:UniProtKB.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00033; CCP; 1.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
SMART; SM00032; CCP; 1.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS50923; SUSHI; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Golgi apparatus; Membrane; Nucleus; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Secreted; Signal; Sushi;
Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 267 Interleukin-15 receptor subunit alpha.
/FTId=PRO_0000011044.
CHAIN 31 ? Soluble interleukin-15 receptor subunit
alpha.
/FTId=PRO_0000333855.
TOPO_DOM 31 205 Extracellular. {ECO:0000255}.
TRANSMEM 206 228 Helical. {ECO:0000255}.
TOPO_DOM 229 267 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 95 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 75
DISULFID 59 93
VAR_SEQ 1 36 Missing (in isoform 9).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055406.
VAR_SEQ 30 127 Missing (in isoform 7 and isoform 8).
{ECO:0000305}.
/FTId=VSP_012623.
VAR_SEQ 31 95 Missing (in isoform 5 and isoform 6).
{ECO:0000305}.
/FTId=VSP_012624.
VAR_SEQ 95 128 RDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKE -> K
(in isoform 2 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8530383}.
/FTId=VSP_012625.
VAR_SEQ 232 267 QTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL -> A
SVCSCHPRSAGHTCSVGSVC (in isoform 3,
isoform 4, isoform 6 and isoform 8).
{ECO:0000303|PubMed:8530383}.
/FTId=VSP_012626.
VARIANT 182 182 N -> T (in dbSNP:rs2228059).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8530383,
ECO:0000269|Ref.3}.
/FTId=VAR_020967.
MUTAGEN 227 227 Y->F: Abrogates association with SYK and
phosphorylation upon IL-15 stimulation.
{ECO:0000269|PubMed:11714793}.
CONFLICT 200 200 G -> D (in Ref. 8; AAH74726).
{ECO:0000305}.
STRAND 42 44 {ECO:0000244|PDB:2Z3Q}.
STRAND 54 59 {ECO:0000244|PDB:2Z3Q}.
STRAND 63 65 {ECO:0000244|PDB:2Z3Q}.
STRAND 72 77 {ECO:0000244|PDB:2Z3Q}.
TURN 79 81 {ECO:0000244|PDB:2Z3Q}.
STRAND 84 86 {ECO:0000244|PDB:2Z3Q}.
STRAND 93 95 {ECO:0000244|PDB:2Z3Q}.
HELIX 97 102 {ECO:0000244|PDB:2Z3Q}.
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


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