ID I20RA_HUMAN Reviewed; 553 AA. AC Q9UHF4; B4DLR5; F5H675; Q14CW2; Q6UWA9; Q96SH8; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 24-JAN-2024, entry version 177. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ILE-259 AND 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 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., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ILE-259. RC TISSUE=Fibroblast; 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 [4] 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., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., 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., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] 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., 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] 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 verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [8] 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., Carollo S., RA Eagan M., Foster D., Haldeman B.A., Hammond A., Haugen H., Jelinek L., RA Kelly J.D., Madden K., Maurer M.F., Parrish-Novak J., Prunkard D., RA Sexson S., Sprecher C., Waggie K., West J., Whitmore T.E., Yao L., RA Kuechle M.K., Dale B.A., Chandrasekher Y.A.; RT "Interleukin 20: discovery, receptor identification, and role in epidermal RT function."; RL Cell 104:9-19(2001). RN [9] RP LIGAND-BINDING. RX PubMed=11564763; DOI=10.4049/jimmunol.167.7.3545; 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 complexes RT of two types."; RL J. Immunol. 167:3545-3549(2001). RN [10] 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., Brandt C., RA Jelinek L., Madden K., McKernan P.A., Foster D.C., Jaspers S., RA 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 [11] RP SUBUNIT, AND LIGAND-BINDING. RX PubMed=14580208; DOI=10.1021/bi0354583; RA Pletnev S., Magracheva E., Kozlov S., Tobin G., Kotenko S.V., Wlodawer A., RA 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 [12] RP SUBUNIT, LIGAND-BINDING, AND TISSUE SPECIFICITY. RX PubMed=14764663; DOI=10.4049/jimmunol.172.4.2006; 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 receptor RT 1 and IL-10 receptor 2."; RL J. Immunol. 172:2006-2010(2004). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 29-245 IN COMPLEX WITH IL20RB AND RP IL20, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=22802649; DOI=10.1073/pnas.1117551109; RA Logsdon N.J., Deshpande A., Harris B.D., Rajashankar K.R., Walter M.R.; RT "Structural basis for receptor sharing and activation by interleukin-20 RT receptor-2 (IL-20R2) binding cytokines."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12704-12709(2012). 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 {ECO:0000269|PubMed:11163236, ECO:0000269|PubMed:12351624, CC ECO:0000269|PubMed:14580208, ECO:0000269|PubMed:14764663, CC ECO:0000269|PubMed:22802649}. CC -!- INTERACTION: CC Q9UHF4; PRO_0000015381 [Q9NYY1]: IL20; NbExp=4; IntAct=EBI-2933034, EBI-14022785; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UHF4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UHF4-2; Sequence=VSP_011497, VSP_011498; CC Name=3; CC IsoId=Q9UHF4-3; Sequence=VSP_054741; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in skin and CC testis and high levels in brain. Highly expressed in psoriatic skin. CC {ECO:0000269|PubMed:11163236, ECO:0000269|PubMed:14764663}. 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; AF184971; AAF01320.1; -; mRNA. DR EMBL; AY358883; AAQ89242.1; -; mRNA. DR EMBL; AK297121; BAG59627.1; -; mRNA. DR EMBL; AL135902; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47936.1; -; Genomic_DNA. DR EMBL; BC113574; AAI13575.1; -; mRNA. DR EMBL; BC113602; AAI13603.1; -; mRNA. DR CCDS; CCDS5181.1; -. [Q9UHF4-1] DR CCDS; CCDS64535.1; -. [Q9UHF4-2] DR CCDS; CCDS64536.1; -. [Q9UHF4-3] DR RefSeq; NP_001265651.1; NM_001278722.1. [Q9UHF4-3] DR RefSeq; NP_001265652.1; NM_001278723.1. [Q9UHF4-2] DR RefSeq; NP_001265653.1; NM_001278724.1. DR RefSeq; NP_055247.3; NM_014432.3. [Q9UHF4-1] DR RefSeq; XP_011534206.1; XM_011535904.2. DR PDB; 4DOH; X-ray; 2.80 A; E/R=29-245. DR PDBsum; 4DOH; -. DR AlphaFoldDB; Q9UHF4; -. DR SMR; Q9UHF4; -. DR BioGRID; 119804; 33. DR IntAct; Q9UHF4; 34. DR STRING; 9606.ENSP00000314976; -. DR GlyCosmos; Q9UHF4; 6 sites, No reported glycans. DR GlyGen; Q9UHF4; 6 sites. DR BioMuta; IL20RA; -. DR DMDM; 145559483; -. DR PaxDb; 9606-ENSP00000314976; -. DR PeptideAtlas; Q9UHF4; -. DR Antibodypedia; 33022; 448 antibodies from 30 providers. DR DNASU; 53832; -. DR Ensembl; ENST00000316649.10; ENSP00000314976.5; ENSG00000016402.14. [Q9UHF4-1] DR Ensembl; ENST00000367748.4; ENSP00000356722.1; ENSG00000016402.14. [Q9UHF4-2] DR Ensembl; ENST00000541547.5; ENSP00000437843.1; ENSG00000016402.14. [Q9UHF4-3] DR GeneID; 53832; -. DR KEGG; hsa:53832; -. DR MANE-Select; ENST00000316649.10; ENSP00000314976.5; NM_014432.4; NP_055247.4. DR UCSC; uc003qhj.5; human. [Q9UHF4-1] DR AGR; HGNC:6003; -. DR CTD; 53832; -. DR DisGeNET; 53832; -. DR GeneCards; IL20RA; -. DR HGNC; HGNC:6003; IL20RA. DR HPA; ENSG00000016402; Tissue enhanced (skin). DR MIM; 605620; gene. DR neXtProt; NX_Q9UHF4; -. DR OpenTargets; ENSG00000016402; -. DR PharmGKB; PA29818; -. DR VEuPathDB; HostDB:ENSG00000016402; -. DR eggNOG; ENOG502RPFC; Eukaryota. DR GeneTree; ENSGT00940000157314; -. DR HOGENOM; CLU_527430_0_0_1; -. DR InParanoid; Q9UHF4; -. DR OMA; MINFITL; -. DR OrthoDB; 5307423at2759; -. DR PhylomeDB; Q9UHF4; -. DR TreeFam; TF334107; -. DR PathwayCommons; Q9UHF4; -. DR Reactome; R-HSA-8854691; Interleukin-20 family signaling. DR SignaLink; Q9UHF4; -. DR SIGNOR; Q9UHF4; -. DR BioGRID-ORCS; 53832; 8 hits in 1146 CRISPR screens. DR ChiTaRS; IL20RA; human. DR GeneWiki; Interleukin_20_receptor,_alpha_subunit; -. DR GenomeRNAi; 53832; -. DR Pharos; Q9UHF4; Tbio. DR PRO; PR:Q9UHF4; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9UHF4; Protein. DR Bgee; ENSG00000016402; Expressed in olfactory segment of nasal mucosa and 133 other cell types or tissues. DR ExpressionAtlas; Q9UHF4; baseline and differential. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central. DR GO; GO:0042015; F:interleukin-20 binding; IBA:GO_Central. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0045124; P:regulation of bone resorption; IEA:Ensembl. DR CDD; cd00063; FN3; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR015373; Interferon/interleukin_rcp_dom. DR PANTHER; PTHR20859; INTERFERON/INTERLEUKIN RECEPTOR; 1. DR PANTHER; PTHR20859:SF86; INTERLEUKIN-20 RECEPTOR SUBUNIT ALPHA; 1. DR Pfam; PF09294; Interfer-bind; 1. DR Pfam; PF01108; Tissue_fac; 1. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR PROSITE; PS50853; FN3; 2. DR Genevisible; Q9UHF4; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 30..553 FT /note="Interleukin-20 receptor subunit alpha" FT /id="PRO_0000011036" FT TOPO_DOM 30..250 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 251..271 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 272..553 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 37..135 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 136..242 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 333..353 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 462..515 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 333..347 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 479..502 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 42 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 83 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 91 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 191 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 200 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 87..95 FT /evidence="ECO:0000269|PubMed:22802649" FT DISULFID 215..236 FT /evidence="ECO:0000269|PubMed:22802649" FT VAR_SEQ 1..111 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_011497" FT VAR_SEQ 1..49 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054741" FT VAR_SEQ 112..135 FT /note="VKAIWGTKCSKWAESGRFYPFLET -> MSYNGLHQRVFKELKLLTLCSISS FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_011498" FT VARIANT 259 FT /note="V -> I (in dbSNP:rs1555498)" FT /evidence="ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.1, ECO:0000269|Ref.5" FT /id="VAR_031613" FT VARIANT 382 FT /note="L -> F (in dbSNP:rs1342642)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_031614" FT CONFLICT 96 FT /note="D -> V (in Ref. 3; BAG59627)" FT /evidence="ECO:0000305" FT STRAND 41..48 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 68..75 FT /evidence="ECO:0007829|PDB:4DOH" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 88..96 FT /evidence="ECO:0007829|PDB:4DOH" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 108..118 FT /evidence="ECO:0007829|PDB:4DOH" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 141..145 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:4DOH" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 180..187 FT /evidence="ECO:0007829|PDB:4DOH" FT TURN 188..191 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 192..198 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 200..205 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 213..221 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:4DOH" FT STRAND 233..238 FT /evidence="ECO:0007829|PDB:4DOH" 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 //