ID I20RA_HUMAN Reviewed; 553 AA.
AC Q9UHF4; Q14CW2; Q6UWA9; Q96SH8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 01-MAY-2013, entry version 107.
DE RecName: Full=Interleukin-20 receptor subunit alpha;
DE Short=IL-20 receptor subunit alpha;
DE Short=IL-20R-alpha;
DE Short=IL-20RA;
DE AltName: Full=Cytokine receptor class-II member 8;
DE AltName: Full=Cytokine receptor family 2 member 8;
DE Short=CRF2-8;
DE AltName: Full=IL-20R1;
DE AltName: Full=ZcytoR7;
DE Flags: Precursor;
GN Name=IL20RA; ORFNames=UNQ681/PRO1315;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ILE-259 AND
RP PHE-382.
RA Lok S., Kho C.-J., Jelmberg A., Adams R., Whitmore T., Farrah T.,
RA O'Hara P.;
RT "Homo sapiens cytokine receptor homolog.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP ILE-259.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-259.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ILE-259.
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 30-44.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP SUBUNIT, LIGAND-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=11163236; DOI=10.1016/S0092-8674(01)00187-8;
RA Blumberg H., Conklin D., Xu W.F., Grossmann A., Brender T.,
RA Carollo S., Eagan M., Foster D., Haldeman B.A., Hammond A., Haugen H.,
RA Jelinek L., Kelly J.D., Madden K., Maurer M.F., Parrish-Novak J.,
RA Prunkard D., Sexson S., Sprecher C., Waggie K., West J.,
RA Whitmore T.E., Yao L., Kuechle M.K., Dale B.A., Chandrasekher Y.A.;
RT "Interleukin 20: discovery, receptor identification, and role in
RT epidermal function.";
RL Cell 104:9-19(2001).
RN [8]
RP LIGAND-BINDING.
RX PubMed=11564763;
RA Dumoutier L., Leemans C., Lejeune D., Kotenko S.V., Renauld J.-C.;
RT "STAT activation by IL-19, IL-20 and mda-7 through IL-20 receptor
RT complexes of two types.";
RL J. Immunol. 167:3545-3549(2001).
RN [9]
RP SUBUNIT, AND LIGAND-BINDING.
RX PubMed=12351624; DOI=10.1074/jbc.M205114200;
RA Parrish-Novak J., Xu W., Brender T., Yao L., Jones C., West J.,
RA Brandt C., Jelinek L., Madden K., McKernan P.A., Foster D.C.,
RA Jaspers S., Chandrasekher Y.A.;
RT "Interleukins 19, 20, and 24 signal through two distinct receptor
RT complexes. Differences in receptor-ligand interactions mediate unique
RT biological functions.";
RL J. Biol. Chem. 277:47517-47523(2002).
RN [10]
RP SUBUNIT, AND LIGAND-BINDING.
RX PubMed=14580208; DOI=10.1021/bi0354583;
RA Pletnev S., Magracheva E., Kozlov S., Tobin G., Kotenko S.V.,
RA Wlodawer A., Zdanov A.;
RT "Characterization of the recombinant extracellular domains of human
RT interleukin-20 receptors and their complexes with interleukin-19 and
RT interleukin-20.";
RL Biochemistry 42:12617-12624(2003).
RN [11]
RP SUBUNIT, LIGAND-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=14764663;
RA Sheikh F., Baurin V.V., Lewis-Antes A., Shah N.K., Smirnov S.V.,
RA Anantha S., Dickensheets H., Dumoutier L., Renauld J.-C., Zdanov A.,
RA Donnelly R.P., Kotenko S.V.;
RT "IL-26 signals through a novel receptor complex composed of IL-20
RT receptor 1 and IL-10 receptor 2.";
RL J. Immunol. 172:2006-2010(2004).
CC -!- FUNCTION: The IL20RA/IL20RB dimer is a receptor for IL19, IL20 and
CC IL24. The IL20RA/IL10RB dimer is a receptor for IL26.
CC -!- SUBUNIT: Heterodimer with IL20RB and heterodimer with IL10RB.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHF4-2; Sequence=VSP_011497, VSP_011498;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in skin
CC and testis and high levels in brain. Highly expressed in psoriatic
CC skin.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC -!- SIMILARITY: Contains 2 fibronectin type-III domains.
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DR EMBL; AF184971; AAF01320.1; -; mRNA.
DR EMBL; AY358883; AAQ89242.1; -; mRNA.
DR EMBL; AL135902; CAC38375.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47936.1; -; Genomic_DNA.
DR EMBL; BC113574; AAI13575.1; -; mRNA.
DR EMBL; BC113602; AAI13603.1; -; mRNA.
DR IPI; IPI00004366; -.
DR IPI; IPI00454990; -.
DR RefSeq; NP_055247.2; NM_014432.2.
DR UniGene; Hs.445868; -.
DR PDB; 4DOH; X-ray; 2.80 A; E/R=29-245.
DR PDBsum; 4DOH; -.
DR ProteinModelPortal; Q9UHF4; -.
DR IntAct; Q9UHF4; 1.
DR STRING; 9606.ENSP00000314976; -.
DR PhosphoSite; Q9UHF4; -.
DR DMDM; 145559483; -.
DR PaxDb; Q9UHF4; -.
DR PRIDE; Q9UHF4; -.
DR DNASU; 53832; -.
DR Ensembl; ENST00000316649; ENSP00000314976; ENSG00000016402.
DR Ensembl; ENST00000367748; ENSP00000356722; ENSG00000016402.
DR GeneID; 53832; -.
DR KEGG; hsa:53832; -.
DR UCSC; uc003qhi.3; human.
DR UCSC; uc003qhk.3; human.
DR CTD; 53832; -.
DR GeneCards; GC06M137321; -.
DR H-InvDB; HIX0006246; -.
DR HGNC; HGNC:6003; IL20RA.
DR HPA; CAB024990; -.
DR HPA; HPA042281; -.
DR MIM; 605620; gene.
DR neXtProt; NX_Q9UHF4; -.
DR PharmGKB; PA29818; -.
DR eggNOG; NOG25594; -.
DR HOGENOM; HOG000112987; -.
DR HOVERGEN; HBG052065; -.
DR InParanoid; Q9UHF4; -.
DR KO; K05136; -.
DR OMA; FMEEWGL; -.
DR OrthoDB; EOG4WH8KR; -.
DR GenomeRNAi; 53832; -.
DR NextBio; 56162; -.
DR ArrayExpress; Q9UHF4; -.
DR Bgee; Q9UHF4; -.
DR CleanEx; HS_IL20RA; -.
DR Genevestigator; Q9UHF4; -.
DR GermOnline; ENSG00000016402; Homo sapiens.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon_alpha/beta_rcpt_bsu.
DR InterPro; IPR015713; Interleukin-20_rcpt_asu.
DR PANTHER; PTHR20859:SF21; PTHR20859:SF21; 1.
DR Pfam; PF09294; Interfer-bind; 1.
DR SUPFAM; SSF49265; FN_III-like; 2.
DR PROSITE; PS50853; FN3; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 29
FT CHAIN 30 553 Interleukin-20 receptor subunit alpha.
FT /FTId=PRO_0000011036.
FT TOPO_DOM 30 250 Extracellular (Potential).
FT TRANSMEM 251 271 Helical; (Potential).
FT TOPO_DOM 272 553 Cytoplasmic (Potential).
FT DOMAIN 37 136 Fibronectin type-III 1.
FT DOMAIN 138 237 Fibronectin type-III 2.
FT COMPBIAS 353 356 Poly-Glu.
FT CARBOHYD 42 42 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 83 83 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 91 91 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 182 182 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 191 191 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 200 200 N-linked (GlcNAc...) (Potential).
FT DISULFID 87 95 By similarity.
FT DISULFID 215 236 By similarity.
FT VAR_SEQ 1 111 Missing (in isoform 2).
FT /FTId=VSP_011497.
FT VAR_SEQ 112 135 VKAIWGTKCSKWAESGRFYPFLET -> MSYNGLHQRVFKE
FT LKLLTLCSISS (in isoform 2).
FT /FTId=VSP_011498.
FT VARIANT 259 259 V -> I (in dbSNP:rs1555498).
FT /FTId=VAR_031613.
FT VARIANT 382 382 L -> F (in dbSNP:rs1342642).
FT /FTId=VAR_031614.
FT STRAND 41 48
FT STRAND 51 57
FT STRAND 68 75
FT HELIX 85 87
FT STRAND 88 96
FT TURN 98 101
FT STRAND 108 118
FT HELIX 131 134
FT STRAND 141 145
FT STRAND 151 156
FT HELIX 172 175
FT STRAND 180 187
FT TURN 188 191
FT STRAND 192 198
FT STRAND 200 205
FT STRAND 213 221
FT STRAND 223 225
FT STRAND 233 238
SQ SEQUENCE 553 AA; 62485 MW; D5C2621FDC848328 CRC64;
MRAPGRPALR PLPLPPLLLL LLAAPWGRAV PCVSGGLPKP ANITFLSINM KNVLQWTPPE
GLQGVKVTYT VQYFIYGQKK WLNKSECRNI NRTYCDLSAE TSDYEHQYYA KVKAIWGTKC
SKWAESGRFY PFLETQIGPP EVALTTDEKS ISVVLTAPEK WKRNPEDLPV SMQQIYSNLK
YNVSVLNTKS NRTWSQCVTN HTLVLTWLEP NTLYCVHVES FVPGPPRRAQ PSEKQCARTL
KDQSSEFKAK IIFWYVLPVS ITVFLFSVMG YSIYRYIHVG KEKHPANLIL IYGNEFDKRF
FVPAEKIVIN FITLNISDDS KISHQDMSLL GKSSDVSSLN DPQPSGNLRP PQEEEEVKHL
GYASHLMEIF CDSEENTEGT SLTQQESLSR TIPPDKTVIE YEYDVRTTDI CAGPEEQELS
LQEEVSTQGT LLESQAALAV LGPQTLQYSY TPQLQDLDPL AQEHTDSEEG PEEEPSTTLV
DWDPQTGRLC IPSLSSFDQD SEGCEPSEGD GLGEEGLLSR LYEEPAPDRP PGENETYLMQ
FMEEWGLYVQ MEN
//
