INLR1_HUMAN
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 03-AUG-2022, entry version 163.
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 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 -!- 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};
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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; 36.
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 GlyGen; Q8IU57; 4 sites.
DR iPTMnet; Q8IU57; -.
DR PhosphoSitePlus; Q8IU57; -.
DR BioMuta; IFNLR1; -.
DR DMDM; 55976528; -.
DR MassIVE; Q8IU57; -.
DR PaxDb; Q8IU57; -.
DR PeptideAtlas; Q8IU57; -.
DR PRIDE; Q8IU57; -.
DR ABCD; Q8IU57; 4 sequenced antibodies.
DR Antibodypedia; 2700; 276 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 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; 577004at2759; -.
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; 75 hits in 1077 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 140 other tissues.
DR ExpressionAtlas; Q8IU57; baseline and differential.
DR Genevisible; Q8IU57; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032002; C:interleukin-28 receptor complex; IDA: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; IC: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 signaling pathway; IC:ComplexPortal.
DR DisProt; DP02446; -.
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; 2.
DR PROSITE; PS50853; FN3; 1.
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.
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 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
