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}.
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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 Genevisible; Q9UHF4; HS.
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.
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
//
