ID INLR1_HUMAN Reviewed; 520 AA. AC Q8IU57; Q5VTX5; Q5VTX7; Q5VTX8; Q6ZML8; Q8IV66; Q8IZI7; Q8IZI8; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 171. DE RecName: Full=Interferon lambda receptor 1; DE Short=IFN-lambda receptor 1; DE Short=IFN-lambda-R1; DE AltName: Full=Cytokine receptor class-II member 12; DE AltName: Full=Cytokine receptor family 2 member 12; DE Short=CRF2-12; DE AltName: Full=Interleukin-28 receptor subunit alpha; DE Short=IL-28 receptor subunit alpha; DE Short=IL-28R-alpha; DE Short=IL-28RA; DE AltName: Full=Likely interleukin or cytokine receptor 2; DE Short=LICR2; DE Flags: Precursor; GN Name=IFNLR1; Synonyms=IL28RA, LICR2; 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] (ISOFORMS 1 AND 4), AND FUNCTION. RX PubMed=12521379; DOI=10.1042/bj20021935; RA Dumoutier L., Lejeune D., Hor S., Fickenscher H., Renauld J.-C.; RT "Cloning of a new type II cytokine receptor activating signal transducer RT and activator of transcription (STAT)1, STAT2 and STAT3."; RL Biochem. J. 370:391-396(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE RP SPECIFICITY, AND SUBUNIT. RX PubMed=12469119; DOI=10.1038/ni873; RA Sheppard P., Kindsvogel W., Xu W., Henderson K., Schlutsmeyer S., RA Whitmore T.E., Kuestner R., Garrigues U., Birks C., Roraback J., RA Ostrander C., Dong D., Shin J., Presnell S., Fox B., Haldeman B., RA Cooper E., Taft D., Gilbert T., Grant F.J., Tackett M., Krivan W., RA McKnight G., Clegg C., Foster D., Klucher K.M.; RT "IL-28, IL-29 and their class II cytokine receptor IL-28R."; RL Nat. Immunol. 4:63-68(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP SUBUNIT. RX PubMed=12483210; DOI=10.1038/ni875; RA Kotenko S.V., Gallagher G., Baurin V.V., Lewis-Antes A., Shen M., RA Shah N.K., Langer J.A., Sheikh F., Dickensheets H., Donnelly R.P.; RT "IFN-lambdas mediate antiviral protection through a distinct class II RT cytokine receptor complex."; RL Nat. Immunol. 4:69-77(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Spleen; 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 [5] 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 [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [8] RP MUTAGENESIS OF LYS-319 AND LYS-320, AND UBIQUITINATION. RX PubMed=36379255; DOI=10.1016/j.jbc.2022.102698; RA Tsai M., Osman W., Adair J., ElMergawy R., Chafin L., Johns F., Farkas D., RA Elhance A., Londino J., Mallampalli R.K.; RT "The E3 ligase subunit FBXO45 binds the interferon-lambda receptor and RT promotes its degradation during influenza virus infection."; RL J. Biol. Chem. 298:102698-102698(2022). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 19-226 IN COMPLEX WITH IFNL1, RP GLYCOSYLATION AT ASN-29; ASN-36 AND ASN-142, AND DISULFIDE BONDS. RX PubMed=20934432; DOI=10.1016/j.jmb.2010.09.068; RA Miknis Z.J., Magracheva E., Li W., Zdanov A., Kotenko S.V., Wlodawer A.; RT "Crystal structure of human interferon-lambda1 in complex with its high- RT affinity receptor interferon-lambdaR1."; RL J. Mol. Biol. 404:650-664(2010). CC -!- FUNCTION: The IFNLR1/IL10RB dimer is a receptor for the cytokine CC ligands IFNL2 and IFNL3 and mediates their antiviral activity. The CC ligand/receptor complex stimulate the activation of the JAK/STAT CC signaling pathway leading to the expression of IFN-stimulated genes CC (ISG), which contribute to the antiviral state. Determines the cell CC type specificity of the lambda interferon action. Shows a more CC restricted pattern of expression in the epithelial tissues thereby CC limiting responses to lambda interferons primarily to epithelial cells CC of the respiratory, gastrointestinal, and reproductive tracts. Seems CC not to be essential for early virus-activated host defense in vaginal CC infection, but plays an important role in Toll-like receptor (TLR)- CC induced antiviral defense. Plays a significant role in the antiviral CC immune defense in the intestinal epithelium. CC {ECO:0000269|PubMed:12469119, ECO:0000269|PubMed:12483210, CC ECO:0000269|PubMed:12521379}. CC -!- SUBUNIT: Heterodimer with IL10RB. {ECO:0000269|PubMed:12469119, CC ECO:0000269|PubMed:12483210, ECO:0000269|PubMed:20934432}. CC -!- INTERACTION: CC Q8IU57; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-373215, EBI-12109402; CC Q8IU57; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-373215, EBI-12244618; CC Q8IU57; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-373215, EBI-12019274; CC Q8IU57; P09466: PAEP; NbExp=3; IntAct=EBI-373215, EBI-465167; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=IL-28R-alpha-v1; CC IsoId=Q8IU57-1; Sequence=Displayed; CC Name=2; Synonyms=IL-28R-alpha-v2; CC IsoId=Q8IU57-2; Sequence=VSP_011890; CC Name=3; Synonyms=IL-28R-alpha-v3; CC IsoId=Q8IU57-3; Sequence=VSP_011888, VSP_011889, VSP_011892; CC Name=4; Synonyms=Secreted; CC IsoId=Q8IU57-4; Sequence=VSP_011891, VSP_011892; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12469119, CC ECO:0000269|PubMed:12483210}. CC -!- PTM: Ubiquitinated by FBXO45-containing E3 ligase leading to CC proteasomal degradation. {ECO:0000269|PubMed:36379255}. CC -!- SIMILARITY: Belongs to the type II cytokine receptor family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD18707.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AJ534330; CAD58829.1; -; mRNA. DR EMBL; AJ534331; CAD58830.1; -; mRNA. DR EMBL; AY129151; AAN28266.1; -; mRNA. DR EMBL; AY129152; AAN28267.1; -; mRNA. DR EMBL; AY129153; AAN28268.1; -; mRNA. DR EMBL; AF439325; AAN63632.1; -; mRNA. DR EMBL; AK160364; BAD18707.1; ALT_INIT; mRNA. DR EMBL; AL590683; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471134; EAW95114.1; -; Genomic_DNA. DR EMBL; CH471134; EAW95115.1; -; Genomic_DNA. DR EMBL; CH471134; EAW95117.1; -; Genomic_DNA. DR EMBL; CH471134; EAW95118.1; -; Genomic_DNA. DR EMBL; BC140872; AAI40873.1; -; mRNA. DR CCDS; CCDS248.1; -. [Q8IU57-1] DR CCDS; CCDS249.1; -. [Q8IU57-2] DR CCDS; CCDS250.1; -. [Q8IU57-4] DR RefSeq; NP_734464.1; NM_170743.3. [Q8IU57-1] DR RefSeq; NP_775087.1; NM_173064.2. [Q8IU57-2] DR RefSeq; NP_775088.1; NM_173065.2. [Q8IU57-4] DR PDB; 3OG4; X-ray; 2.16 A; B=19-226. DR PDB; 3OG6; X-ray; 2.10 A; B=19-226. DR PDB; 5IXD; X-ray; 2.85 A; B=250-299. DR PDB; 5IXI; X-ray; 2.57 A; B=250-259. DR PDB; 5L04; X-ray; 2.10 A; B=260-307. DR PDB; 5T5W; X-ray; 2.85 A; B=21-226. DR PDBsum; 3OG4; -. DR PDBsum; 3OG6; -. DR PDBsum; 5IXD; -. DR PDBsum; 5IXI; -. DR PDBsum; 5L04; -. DR PDBsum; 5T5W; -. DR AlphaFoldDB; Q8IU57; -. DR SMR; Q8IU57; -. DR BioGRID; 127873; 49. DR ComplexPortal; CPX-6011; Interferon lambda receptor-ligand complex, IFNL1 variant. DR ComplexPortal; CPX-6012; Interferon lambda receptor-ligand complex, IFNL2 variant. DR ComplexPortal; CPX-6013; Interferon lambda receptor-ligand complex, IFNL3 variant. DR ComplexPortal; CPX-6014; Interferon lambda receptor-ligand complex, IFNL4 variant. DR DIP; DIP-31197N; -. DR IntAct; Q8IU57; 7. DR STRING; 9606.ENSP00000327824; -. DR ChEMBL; CHEMBL3831284; -. DR GlyCosmos; Q8IU57; 4 sites, No reported glycans. DR GlyGen; Q8IU57; 4 sites. DR iPTMnet; Q8IU57; -. DR PhosphoSitePlus; Q8IU57; -. DR BioMuta; IFNLR1; -. DR DMDM; 55976528; -. DR MassIVE; Q8IU57; -. DR PaxDb; 9606-ENSP00000327824; -. DR PeptideAtlas; Q8IU57; -. DR ABCD; Q8IU57; 4 sequenced antibodies. DR Antibodypedia; 2700; 326 antibodies from 30 providers. DR DNASU; 163702; -. DR Ensembl; ENST00000327535.6; ENSP00000327824.1; ENSG00000185436.12. [Q8IU57-1] DR Ensembl; ENST00000327575.6; ENSP00000328994.2; ENSG00000185436.12. [Q8IU57-4] DR Ensembl; ENST00000374418.3; ENSP00000363539.3; ENSG00000185436.12. [Q8IU57-3] DR Ensembl; ENST00000374421.7; ENSP00000363542.3; ENSG00000185436.12. [Q8IU57-2] DR GeneID; 163702; -. DR KEGG; hsa:163702; -. DR MANE-Select; ENST00000327535.6; ENSP00000327824.1; NM_170743.4; NP_734464.1. DR UCSC; uc001bir.4; human. [Q8IU57-1] DR AGR; HGNC:18584; -. DR CTD; 163702; -. DR DisGeNET; 163702; -. DR GeneCards; IFNLR1; -. DR HGNC; HGNC:18584; IFNLR1. DR HPA; ENSG00000185436; Low tissue specificity. DR MIM; 607404; gene. DR neXtProt; NX_Q8IU57; -. DR OpenTargets; ENSG00000185436; -. DR PharmGKB; PA134984880; -. DR VEuPathDB; HostDB:ENSG00000185436; -. DR eggNOG; ENOG502S4B0; Eukaryota. DR GeneTree; ENSGT00510000048978; -. DR HOGENOM; CLU_043104_1_0_1; -. DR InParanoid; Q8IU57; -. DR OMA; FLCPQKE; -. DR OrthoDB; 5323728at2759; -. DR PhylomeDB; Q8IU57; -. DR TreeFam; TF336003; -. DR PathwayCommons; Q8IU57; -. DR Reactome; R-HSA-449836; Other interleukin signaling. DR Reactome; R-HSA-8854691; Interleukin-20 family signaling. DR SignaLink; Q8IU57; -. DR SIGNOR; Q8IU57; -. DR BioGRID-ORCS; 163702; 79 hits in 1162 CRISPR screens. DR ChiTaRS; IFNLR1; human. DR GeneWiki; Interleukin_28_receptor,_alpha_subunit; -. DR GenomeRNAi; 163702; -. DR Pharos; Q8IU57; Tbio. DR PRO; PR:Q8IU57; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8IU57; Protein. DR Bgee; ENSG00000185436; Expressed in ileal mucosa and 142 other cell types or tissues. DR ExpressionAtlas; Q8IU57; baseline and differential. DR GO; GO:0032002; C:interleukin-28 receptor complex; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central. DR GO; GO:0098586; P:cellular response to virus; NAS:ComplexPortal. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB. DR GO; GO:0002385; P:mucosal immune response; ISS:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB. DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:ARUK-UCL. DR GO; GO:0050691; P:regulation of defense response to virus by host; IDA:UniProtKB. DR GO; GO:0034342; P:response to type III interferon; ISS:UniProtKB. DR GO; GO:0038196; P:type III interferon-mediated signaling pathway; NAS:ComplexPortal. DR CDD; cd21910; JAK1bd_box_IFNLR1; 1. DR DisProt; DP02446; -. 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 PANTHER; PTHR20859:SF55; INTERFERON LAMBDA RECEPTOR 1; 1. DR PANTHER; PTHR20859; INTERFERON/INTERLEUKIN RECEPTOR; 1. DR Pfam; PF01108; Tissue_fac; 1. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR PROSITE; PS50853; FN3; 1. DR Genevisible; Q8IU57; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; Disulfide bond; KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..520 FT /note="Interferon lambda receptor 1" FT /id="PRO_0000011019" FT TOPO_DOM 21..228 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 229..249 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 250..520 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 26..126 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 302..439 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 477..520 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 324..338 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 379..400 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 505..520 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 29 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20934432" FT CARBOHYD 36 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20934432" FT CARBOHYD 142 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20934432" FT CARBOHYD 169 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 74..82 FT /evidence="ECO:0000269|PubMed:20934432" FT DISULFID 86..150 FT /evidence="ECO:0000269|PubMed:20934432" FT DISULFID 195..217 FT /evidence="ECO:0000269|PubMed:20934432" FT VAR_SEQ 171..211 FT /note="TLFPVTPHGQPVQITLQPAASEHHCLSARTIYTFSVPKYSK -> VGSSFPA FT PRLGPLLHPFLLRFFSPSQPAPAPLLQEVFPVHS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12469119" FT /id="VSP_011888" FT VAR_SEQ 212..244 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12469119" FT /id="VSP_011889" FT VAR_SEQ 224..244 FT /note="EANWAFLVLPSLLILLLVIAA -> GLFWTHTPCGNLSAQQTRVRE (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:12521379" FT /id="VSP_011891" FT VAR_SEQ 245..520 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:12469119, FT ECO:0000303|PubMed:12521379" FT /id="VSP_011892" FT VAR_SEQ 268..296 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12469119" FT /id="VSP_011890" FT MUTAGEN 319 FT /note="K->R: More resistant to viral-induced degradation; FT when associated with R-320." FT /evidence="ECO:0000269|PubMed:36379255" FT MUTAGEN 320 FT /note="K->R: More resistant to viral-induced degradation; FT when associated with R-319." FT /evidence="ECO:0000269|PubMed:36379255" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 38..44 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:3OG6" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:3OG4" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:3OG6" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:5T5W" FT STRAND 79..83 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 98..104 FT /evidence="ECO:0007829|PDB:3OG6" FT HELIX 119..122 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 138..144 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 156..164 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:3OG4" FT STRAND 180..185 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 192..209 FT /evidence="ECO:0007829|PDB:3OG6" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:3OG6" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:5IXI" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:5L04" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:5L04" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:5L04" SQ SEQUENCE 520 AA; 57653 MW; CEDAEE57F85D69AC CRC64; MAGPERWGPL LLCLLQAAPG RPRLAPPQNV TLLSQNFSVY LTWLPGLGNP QDVTYFVAYQ SSPTRRRWRE VEECAGTKEL LCSMMCLKKQ DLYNKFKGRV RTVSPSSKSP WVESEYLDYL FEVEPAPPVL VLTQTEEILS ANATYQLPPC MPPLDLKYEV AFWKEGAGNK TLFPVTPHGQ PVQITLQPAA SEHHCLSART IYTFSVPKYS KFSKPTCFLL EVPEANWAFL VLPSLLILLL VIAAGGVIWK TLMGNPWFQR AKMPRALDFS GHTHPVATFQ PSRPESVNDL FLCPQKELTR GVRPTPRVRA PATQQTRWKK DLAEDEEEED EEDTEDGVSF QPYIEPPSFL GQEHQAPGHS EAGGVDSGRP RAPLVPSEGS SAWDSSDRSW ASTVDSSWDR AGSSGYLAEK GPGQGPGGDG HQESLPPPEF SKDSGFLEEL PEDNLSSWAT WGTLPPEPNL VPGGPPVSLQ TLTFCWESSP EEEEEARESE IEDSDAGSWG AESTQRTEDR GRTLGHYMAR //