I22R1_HUMAN
ID I22R1_HUMAN Reviewed; 574 AA.
AC Q8N6P7; A8K839; B2R9Y9; Q9HB22;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Interleukin-22 receptor subunit alpha-1;
DE Short=IL-22 receptor subunit alpha-1;
DE Short=IL-22R-alpha-1;
DE Short=IL-22RA1;
DE AltName: Full=Cytokine receptor class-II member 9;
DE AltName: Full=Cytokine receptor family 2 member 9;
DE Short=CRF2-9;
DE AltName: Full=ZcytoR11;
DE Flags: Precursor;
GN Name=IL22RA1; Synonyms=IL22R;
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], AND VARIANT GLY-518.
RX PubMed=10875937; DOI=10.1074/jbc.m005304200;
RA Xie M.-H., Aggarwal S., Ho W.-H., Foster J., Zhang Z., Stinson J.,
RA Wood W.I., Goddard A.D., Gurney A.L.;
RT "Interleukin (IL)-22, a novel human cytokine that signals through the
RT interferon receptor-related proteins CRF2-4 and IL-22R.";
RL J. Biol. Chem. 275:31335-31339(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-518.
RC TISSUE=Esophagus, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal cortex;
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 [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11035029; DOI=10.1074/jbc.m007837200;
RA Kotenko S.V., Izotova L.S., Mirochnitchenko O.V., Esterova E.,
RA Dickensheets H., Donnelly R.P., Pestka S.;
RT "Identification of the functional interleukin-22 (IL-22) receptor complex:
RT the IL-10R2 chain (IL-10Rbeta) is a common chain of both the IL-10 and IL-
RT 22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor
RT complexes.";
RL J. Biol. Chem. 276:2725-2732(2001).
RN [7]
RP FUNCTION.
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=12407026; DOI=10.1093/intimm/dxf096;
RA Lecart S., Morel F., Noraz N., Pene J., Garcia M., Boniface K.,
RA Lecron J.-C., Yssel H.;
RT "IL-22, in contrast to IL-10, does not induce Ig production, due to absence
RT of a functional IL-22 receptor on activated human B cells.";
RL Int. Immunol. 14:1351-1356(2002).
RN [9]
RP FUNCTION.
RX PubMed=11706020; DOI=10.1074/jbc.m106043200;
RA Wang M., Tan Z., Zhang R., Kotenko S.V., Liang P.;
RT "Interleukin 24 (MDA-7/MOB-5) signals through two heterodimeric receptors,
RT IL-22R1/IL-20R2 and IL-20R1/IL-20R2.";
RL J. Biol. Chem. 277:7341-7347(2002).
RN [10]
RP FUNCTION.
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 FUNCTION.
RX PubMed=12941841;
RA Ramesh R., Mhashilkar A.M., Tanaka F., Saito Y., Branch C.D., Sieger K.,
RA Mumm J.B., Stewart A.L., Boquoi A., Dumoutier L., Grimm E.A.,
RA Renauld J.-C., Kotenko S., Chada S.;
RT "Melanoma differentiation-associated gene 7/interleukin (IL)-24 is a novel
RT ligand that regulates angiogenesis via the IL-22 receptor.";
RL Cancer Res. 63:5105-5113(2003).
RN [12]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15308104; DOI=10.1016/j.immuni.2004.07.007;
RA Wolk K., Kunz S., Witte E., Friedrich M., Asadullah K., Sabat R.;
RT "IL-22 increases the innate immunity of tissues.";
RL Immunity 21:241-254(2004).
RN [13]
RP SUBUNIT.
RX PubMed=15120653; DOI=10.1016/j.intimp.2004.01.010;
RA Li J., Tomkinson K.N., Tan X.-Y., Wu P., Yan G., Spaulding V., Deng B.,
RA Annis-Freeman B., Heveron K., Zollner R., De Zutter G., Wright J.F.,
RA Crawford T.K., Liu W., Jacobs K.A., Wolfman N.M., Ling V., Pittman D.D.,
RA Veldman G.M., Fouser L.A.;
RT "Temporal associations between interleukin 22 and the extracellular domains
RT of IL-22R and IL-10R2.";
RL Int. Immunopharmacol. 4:693-708(2004).
RN [14]
RP FUNCTION.
RX PubMed=17204547; DOI=10.1152/ajpgi.00239.2006;
RA Brand S., Dambacher J., Beigel F., Zitzmann K., Heeg M.H.J., Weiss T.S.,
RA Pruefer T., Olszak T., Steib C.J., Storr M., Goeke B., Diepolder H.,
RA Bilzer M., Thasler W.E., Auernhammer C.J.;
RT "IL-22-mediated liver cell regeneration is abrogated by SOCS-1/3
RT overexpression in vitro.";
RL Am. J. Physiol. 292:G1019-G1028(2007).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=17900301; DOI=10.1111/j.1365-2249.2007.03511.x;
RA Boniface K., Guignouard E., Pedretti N., Garcia M., Delwail A.,
RA Bernard F.-X., Nau F., Guillet G., Dagregorio G., Yssel H., Lecron J.-C.,
RA Morel F.;
RT "A role for T cell-derived interleukin 22 in psoriatic skin inflammation.";
RL Clin. Exp. Immunol. 150:407-415(2007).
RN [16]
RP ASSOCIATION WITH CHRONIC RHINOSINUSITIS.
RX PubMed=17906500; DOI=10.1097/mlg.0b013e31811edd4f;
RA Ramanathan M. Jr., Spannhake E.W., Lane A.P.;
RT "Chronic rhinosinusitis with nasal polyps is associated with decreased
RT expression of mucosal interleukin 22 receptor.";
RL Laryngoscope 117:1839-1843(2007).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=17828272; DOI=10.1038/nm1651;
RA Kebir H., Kreymborg K., Ifergan I., Dodelet-Devillers A., Cayrol R.,
RA Bernard M., Giuliani F., Arbour N., Becher B., Prat A.;
RT "Human TH17 lymphocytes promote blood-brain barrier disruption and central
RT nervous system inflammation.";
RL Nat. Med. 13:1173-1175(2007).
RN [18]
RP TISSUE SPECIFICITY.
RX PubMed=18061474; DOI=10.1016/j.cyto.2007.10.004;
RA Kragstrup T.W., Otkjaer K., Holm C., Jorgensen A., Hokland M., Iversen L.,
RA Deleuran B.;
RT "The expression of IL-20 and IL-24 and their shared receptors are increased
RT in rheumatoid arthritis and spondyloarthropathy.";
RL Cytokine 41:16-23(2008).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-228 IN COMPLEX WITH IL22,
RP MUTAGENESIS OF LYS-58 AND TYR-60, AND DISULFIDE BONDS.
RX PubMed=18675809; DOI=10.1016/j.febslet.2008.07.046;
RA Bleicher L., de Moura P.R., Watanabe L., Colau D., Dumoutier L.,
RA Renauld J.-C., Polikarpov I.;
RT "Crystal structure of the IL-22/IL-22R1 complex and its implications for
RT the IL-22 signaling mechanism.";
RL FEBS Lett. 582:2985-2992(2008).
CC -!- FUNCTION: Component of the receptor for IL20, IL22 and IL24. Component
CC of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling
CC via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and
CC Akt kinases pathways. Component of one of the receptor for IL20 and
CC IL24 formed by IL22RA1 and IL20RB also signaling through STATs
CC activation. Mediates IL24 antiangiogenic activity as well as IL24
CC inhibitory effect on endothelial cell tube formation and
CC differentiation. {ECO:0000269|PubMed:11035029,
CC ECO:0000269|PubMed:11564763, ECO:0000269|PubMed:11706020,
CC ECO:0000269|PubMed:12351624, ECO:0000269|PubMed:12941841,
CC ECO:0000269|PubMed:17204547}.
CC -!- SUBUNIT: Heterodimer with IL10RB and with IL20RB. IL22 binding to
CC heterodimer is greater than binding to IL22RA1 alone.
CC {ECO:0000269|PubMed:11035029, ECO:0000269|PubMed:15120653,
CC ECO:0000269|PubMed:18675809}.
CC -!- INTERACTION:
CC Q8N6P7; Q08334: IL10RB; NbExp=5; IntAct=EBI-3940749, EBI-11175900;
CC Q8N6P7; Q9GZX6: IL22; NbExp=9; IntAct=EBI-3940749, EBI-8040250;
CC Q8N6P7; PRO_0000015383 [Q9GZX6]: IL22; NbExp=5; IntAct=EBI-3940749, EBI-11315863;
CC Q8N6P7; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-3940749, EBI-1055254;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in colon, liver, lung, pancreas and
CC kidney. No expression in immune cells such as monocytes, T-cells, and
CC NK-cells. Expressed in keratinocytes of normal skin as well as in
CC psoriatic skin lesion. Detected in normal blood brain barrier
CC endothelial cells as well as in multiple sclerosis lesions; Strongly
CC expressed on central nervous system vessels within infiltrated multiple
CC sclerosis lesions. Overexpressed in synovial fluid cells from
CC rheumatoid arthritis and spondyloarthropathy patients.
CC {ECO:0000269|PubMed:12407026, ECO:0000269|PubMed:15308104,
CC ECO:0000269|PubMed:17828272, ECO:0000269|PubMed:17900301,
CC ECO:0000269|PubMed:18061474}.
CC -!- INDUCTION: By IFNG/IFN-gamma in keratinocytes.
CC {ECO:0000269|PubMed:15308104}.
CC -!- MISCELLANEOUS: Failure of medical and surgical therapy in Chronic
CC rhinosinusitis with nasal polyps is associated with decreased
CC expression of IL22RA1.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL22RA1ID44568ch1p36.html";
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DR EMBL; AF286095; AAG22073.1; -; mRNA.
DR EMBL; AK292204; BAF84893.1; -; mRNA.
DR EMBL; AK313971; BAG36686.1; -; mRNA.
DR EMBL; AL590683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW95111.1; -; Genomic_DNA.
DR EMBL; BC029273; AAH29273.1; -; mRNA.
DR CCDS; CCDS247.1; -.
DR RefSeq; NP_067081.2; NM_021258.3.
DR PDB; 3DGC; X-ray; 2.50 A; R/S=17-226.
DR PDB; 3DLQ; X-ray; 1.90 A; R=18-228.
DR PDB; 6DF3; X-ray; 2.15 A; L=24-228.
DR PDBsum; 3DGC; -.
DR PDBsum; 3DLQ; -.
DR PDBsum; 6DF3; -.
DR AlphaFoldDB; Q8N6P7; -.
DR SMR; Q8N6P7; -.
DR BioGRID; 121855; 28.
DR DIP; DIP-42031N; -.
DR IntAct; Q8N6P7; 8.
DR MINT; Q8N6P7; -.
DR STRING; 9606.ENSP00000270800; -.
DR GlyGen; Q8N6P7; 2 sites.
DR iPTMnet; Q8N6P7; -.
DR PhosphoSitePlus; Q8N6P7; -.
DR BioMuta; IL22RA1; -.
DR DMDM; 74751067; -.
DR jPOST; Q8N6P7; -.
DR MassIVE; Q8N6P7; -.
DR PaxDb; Q8N6P7; -.
DR PeptideAtlas; Q8N6P7; -.
DR PRIDE; Q8N6P7; -.
DR ProteomicsDB; 72209; -.
DR Antibodypedia; 15695; 452 antibodies from 35 providers.
DR DNASU; 58985; -.
DR Ensembl; ENST00000270800.2; ENSP00000270800.1; ENSG00000142677.4.
DR GeneID; 58985; -.
DR KEGG; hsa:58985; -.
DR MANE-Select; ENST00000270800.2; ENSP00000270800.1; NM_021258.4; NP_067081.2.
DR UCSC; uc001biq.3; human.
DR CTD; 58985; -.
DR DisGeNET; 58985; -.
DR GeneCards; IL22RA1; -.
DR HGNC; HGNC:13700; IL22RA1.
DR HPA; ENSG00000142677; Tissue enriched (pancreas).
DR MIM; 605457; gene.
DR neXtProt; NX_Q8N6P7; -.
DR OpenTargets; ENSG00000142677; -.
DR PharmGKB; PA29823; -.
DR VEuPathDB; HostDB:ENSG00000142677; -.
DR eggNOG; ENOG502S4IS; Eukaryota.
DR GeneTree; ENSGT00940000161366; -.
DR HOGENOM; CLU_033634_0_0_1; -.
DR InParanoid; Q8N6P7; -.
DR OMA; CQQITRK; -.
DR OrthoDB; 1078220at2759; -.
DR PhylomeDB; Q8N6P7; -.
DR TreeFam; TF334107; -.
DR PathwayCommons; Q8N6P7; -.
DR Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR SignaLink; Q8N6P7; -.
DR SIGNOR; Q8N6P7; -.
DR BioGRID-ORCS; 58985; 6 hits in 1064 CRISPR screens.
DR ChiTaRS; IL22RA1; human.
DR EvolutionaryTrace; Q8N6P7; -.
DR GenomeRNAi; 58985; -.
DR Pharos; Q8N6P7; Tbio.
DR PRO; PR:Q8N6P7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N6P7; protein.
DR Bgee; ENSG00000142677; Expressed in body of pancreas and 112 other tissues.
DR Genevisible; Q8N6P7; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0004904; F:interferon receptor activity; TAS:UniProtKB.
DR GO; GO:0042015; F:interleukin-20 binding; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF01108; Tissue_fac; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..574
FT /note="Interleukin-22 receptor subunit alpha-1"
FT /id="PRO_0000324320"
FT TOPO_DOM 16..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..124
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 141..221
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 388..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..79
FT /evidence="ECO:0000269|PubMed:18675809"
FT DISULFID 128..217
FT /evidence="ECO:0000269|PubMed:18675809"
FT VARIANT 130
FT /note="S -> P (in dbSNP:rs34900099)"
FT /id="VAR_039699"
FT VARIANT 205
FT /note="V -> I (in dbSNP:rs16829204)"
FT /id="VAR_039700"
FT VARIANT 209
FT /note="A -> S (in dbSNP:rs34379702)"
FT /id="VAR_039701"
FT VARIANT 222
FT /note="L -> P (in dbSNP:rs34782294)"
FT /id="VAR_039702"
FT VARIANT 407
FT /note="M -> V (in dbSNP:rs35401673)"
FT /id="VAR_039703"
FT VARIANT 518
FT /note="R -> G (in dbSNP:rs3795299)"
FT /evidence="ECO:0000269|PubMed:10875937,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_039704"
FT MUTAGEN 58
FT /note="K->A: Strongly reduced response to IL22."
FT /evidence="ECO:0000269|PubMed:18675809"
FT MUTAGEN 60
FT /note="Y->A,R: Loss of response to IL22."
FT /evidence="ECO:0000269|PubMed:18675809"
FT CONFLICT 117
FT /note="Q -> R (in Ref. 2; BAF84893)"
FT /evidence="ECO:0000305"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:6DF3"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6DF3"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6DF3"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:3DLQ"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6DF3"
FT STRAND 177..190
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3DLQ"
SQ SEQUENCE 574 AA; 63077 MW; D46CC71D496F3420 CRC64;
MRTLLTILTV GSLAAHAPED PSDLLQHVKF QSSNFENILT WDSGPEGTPD TVYSIEYKTY
GERDWVAKKG CQRITRKSCN LTVETGNLTE LYYARVTAVS AGGRSATKMT DRFSSLQHTT
LKPPDVTCIS KVRSIQMIVH PTPTPIRAGD GHRLTLEDIF HDLFYHLELQ VNRTYQMHLG
GKQREYEFFG LTPDTEFLGT IMICVPTWAK ESAPYMCRVK TLPDRTWTYS FSGAFLFSMG
FLVAVLCYLS YRYVTKPPAP PNSLNVQRVL TFQPLRFIQE HVLIPVFDLS GPSSLAQPVQ
YSQIRVSGPR EPAGAPQRHS LSEITYLGQP DISILQPSNV PPPQILSPLS YAPNAAPEVG
PPSYAPQVTP EAQFPFYAPQ AISKVQPSSY APQATPDSWP PSYGVCMEGS GKDSPTGTLS
SPKHLRPKGQ LQKEPPAGSC MLGGLSLQEV TSLAMEESQE AKSLHQPLGI CTDRTSDPNV
LHSGEEGTPQ YLKGQLPLLS SVQIEGHPMS LPLQPPSRPC SPSDQGPSPW GLLESLVCPK
DEAKSPAPET SDLEQPTELD SLFRGLALTV QWES
