ILRL1_MOUSE
ID ILRL1_MOUSE Reviewed; 567 AA.
AC P14719; Q05208;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Interleukin-1 receptor-like 1;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Interleukin-33 receptor alpha chain {ECO:0000303|PubMed:18003919};
DE AltName: Full=Lymphocyte antigen 84;
DE AltName: Full=Protein ST2;
DE AltName: Full=Protein T1;
DE Flags: Precursor;
GN Name=Il1rl1; Synonyms=Ly84, St2, Ste2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC STRAIN=BALB/cJ;
RX PubMed=2532153; DOI=10.1016/0014-5793(89)81679-5;
RA Tominaga S.;
RT "A putative protein of a growth specific cDNA from BALB/c-3T3 cells is
RT highly similar to the extracellular portion of mouse interleukin 1
RT receptor.";
RL FEBS Lett. 258:301-304(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B).
RC STRAIN=C3H/He; TISSUE=Spleen;
RX PubMed=1832015; DOI=10.1016/0167-4781(91)90029-l;
RA Tominaga S., Jenkins N.A., Gilbert D.J., Copeland N.G., Tetsuka T.;
RT "Molecular cloning of the murine ST2 gene. Characterization and chromosomal
RT mapping.";
RL Biochim. Biophys. Acta 1090:1-8(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX PubMed=2527364; DOI=10.1073/pnas.86.15.5708;
RA Klemenz R., Hoffmann S., Werenskiold A.K.;
RT "Serum- and oncoprotein-mediated induction of a gene with sequence
RT similarity to the gene encoding carcinoembryonic antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5708-5712(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=7916701; DOI=10.1016/0014-5793(93)81333-u;
RA Yanagisawa K., Takagi T., Tsukamoto T., Tetsuka T., Tominaga S.;
RT "Presence of a novel primary response gene ST2L, encoding a product highly
RT similar to the interleukin 1 receptor type 1.";
RL FEBS Lett. 318:83-87(1993).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=8131748; DOI=10.1002/j.1460-2075.1994.tb06367.x;
RA Bergers G., Reikersdorfer A., Braselmann S., Graninger P., Busslinger M.;
RT "Alternative promoter usage of the Fos-responsive gene Fit-1 generates mRNA
RT isoforms coding for either secreted or membrane-bound proteins related to
RT the IL-1 receptor.";
RL EMBO J. 13:1176-1188(1994).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17675517; DOI=10.4049/jimmunol.179.4.2551;
RA Chackerian A.A., Oldham E.R., Murphy E.E., Schmitz J., Pflanz S.,
RA Kastelein R.A.;
RT "IL-1 receptor accessory protein and ST2 comprise the IL-33 receptor
RT complex.";
RL J. Immunol. 179:2551-2555(2007).
RN [7]
RP INTERACTION WITH IL1RAP.
RX PubMed=18003919; DOI=10.1073/pnas.0705939104;
RA Ali S., Huber M., Kollewe C., Bischoff S.C., Falk W., Martin M.U.;
RT "IL-1 receptor accessory protein is essential for IL-33-induced activation
RT of T lymphocytes and mast cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18660-18665(2007).
RN [8]
RP FUNCTION (ISOFORM B), AND INTERACTION WITH IL1RAP.
RX PubMed=18450470; DOI=10.1016/j.cyto.2008.03.008;
RA Palmer G., Lipsky B.P., Smithgall M.D., Meininger D., Siu S.,
RA Talabot-Ayer D., Gabay C., Smith D.E.;
RT "The IL-1 receptor accessory protein (AcP) is required for IL-33 signaling
RT and soluble AcP enhances the ability of soluble ST2 to inhibit IL-33.";
RL Cytokine 42:358-364(2008).
RN [9]
RP INTERACTION WITH KIT, AND SUBUNIT.
RX PubMed=20200353; DOI=10.1182/blood-2009-10-247411;
RA Drube S., Heink S., Walter S., Loehn T., Grusser M., Gerbaulet A.,
RA Berod L., Schons J., Dudeck A., Freitag J., Grotha S., Reich D.,
RA Rudeschko O., Norgauer J., Hartmann K., Roers A., Kamradt T.;
RT "The receptor tyrosine kinase c-Kit controls IL-33 receptor signaling in
RT mast cells.";
RL Blood 115:3899-3906(2010).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=21349253; DOI=10.1016/j.brainres.2011.02.045;
RA Yasuoka S., Kawanokuchi J., Parajuli B., Jin S., Doi Y., Noda M.,
RA Sonobe Y., Takeuchi H., Mizuno T., Suzumura A.;
RT "Production and functions of IL-33 in the central nervous system.";
RL Brain Res. 1385:8-17(2011).
RN [11]
RP FUNCTION.
RX PubMed=29045903; DOI=10.1016/j.immuni.2017.09.015;
RA Osbourn M., Soares D.C., Vacca F., Cohen E.S., Scott I.C., Gregory W.F.,
RA Smyth D.J., Toivakka M., Kemter A.M., le Bihan T., Wear M., Hoving D.,
RA Filbey K.J., Hewitson J.P., Henderson H., Gonzalez-Ciscar A., Errington C.,
RA Vermeren S., Astier A.L., Wallace W.A., Schwarze J., Ivens A.C.,
RA Maizels R.M., McSorley H.J.;
RT "HpARI Protein Secreted by a Helminth Parasite Suppresses Interleukin-33.";
RL Immunity 47:739-751(2017).
RN [12] {ECO:0007744|PDB:5VI4}
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 26-326, DISULFIDE BOND, AND
RP INTERACTION WITH IL1RAP.
RX PubMed=28930661; DOI=10.1016/j.immuni.2017.08.004;
RA Gunther S., Deredge D., Bowers A.L., Luchini A., Bonsor D.A.,
RA Beadenkopf R., Liotta L., Wintrode P.L., Sundberg E.J.;
RT "IL-1 Family Cytokines Use Distinct Molecular Mechanisms to Signal through
RT Their Shared Co-receptor.";
RL Immunity 47:510-523.e4(2017).
CC -!- FUNCTION: Receptor for interleukin-33 (IL-33); signaling requires
CC association of the coreceptor IL1RAP (PubMed:18450470, PubMed:17675517,
CC PubMed:29045903). Its stimulation recruits MYD88, IRAK1, IRAK4, and
CC TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2,
CC MAPK14, and MAPK8 (By similarity). Possibly involved in helper T-cell
CC function. {ECO:0000250|UniProtKB:Q01638, ECO:0000269|PubMed:17675517,
CC ECO:0000269|PubMed:18450470, ECO:0000269|PubMed:29045903}.
CC -!- FUNCTION: [Isoform B]: Inhibits IL-33 signaling.
CC {ECO:0000269|PubMed:18450470}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBUNIT: Interacts with MYD88, IRAK1, IRAK4, and TRAF6 (By similarity).
CC Bound to its ligand IL33, interacts with IL1RAP to form the minimal
CC interleukin-33 signaling complex with a 1:1:1 stoichiometry. Interacts
CC with KIT (bound to KITLG/SCF). A mast cell-specific KITLG/SCF-induced
CC interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and
CC MYD88. Interacts with TMED1. {ECO:0000250|UniProtKB:Q01638,
CC ECO:0000269|PubMed:17675517, ECO:0000269|PubMed:18003919,
CC ECO:0000269|PubMed:18450470, ECO:0000269|PubMed:20200353,
CC ECO:0000269|PubMed:28930661}.
CC -!- INTERACTION:
CC P14719; Q61730: Il1rap; NbExp=3; IntAct=EBI-525078, EBI-525035;
CC P14719; Q6PCT2: FBXL19; Xeno; NbExp=3; IntAct=EBI-525078, EBI-6664563;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=Membrane-bound, ST2L;
CC IsoId=P14719-1; Sequence=Displayed;
CC Name=B; Synonyms=Soluble, ST2;
CC IsoId=P14719-2; Sequence=VSP_002668, VSP_002669;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in hematopoietic tissues,
CC and in macrophage, erythroid, epithelial and fibroblast cell lines.
CC Isoform A is expressed in brain astrocytes and microglia. Isoform B is
CC expressed in brain endothelial cells. {ECO:0000269|PubMed:21349253,
CC ECO:0000269|PubMed:8131748}.
CC -!- DEVELOPMENTAL STAGE: Expressed first in the fetal liver and then in
CC lung and hematopoietic tissues.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; Y07519; CAA68812.1; -; mRNA.
DR EMBL; X60184; CAA42742.1; -; Genomic_DNA.
DR EMBL; M24843; AAA40160.1; -; mRNA.
DR EMBL; D13695; BAA02854.1; -; mRNA.
DR CCDS; CCDS35548.1; -. [P14719-1]
DR CCDS; CCDS56626.1; -. [P14719-2]
DR PIR; S29498; S29498.
DR RefSeq; NP_001020773.1; NM_001025602.3. [P14719-1]
DR RefSeq; NP_001281100.1; NM_001294171.1. [P14719-2]
DR RefSeq; NP_034873.2; NM_010743.3. [P14719-2]
DR RefSeq; XP_006495804.1; XM_006495741.1. [P14719-1]
DR RefSeq; XP_006495807.1; XM_006495744.2. [P14719-1]
DR RefSeq; XP_017174571.1; XM_017319082.1. [P14719-1]
DR PDB; 5VI4; X-ray; 2.79 A; B/E=26-326.
DR PDBsum; 5VI4; -.
DR AlphaFoldDB; P14719; -.
DR SMR; P14719; -.
DR BioGRID; 201248; 2.
DR CORUM; P14719; -.
DR DIP; DIP-34958N; -.
DR IntAct; P14719; 4.
DR STRING; 10090.ENSMUSP00000095379; -.
DR GlyGen; P14719; 9 sites.
DR iPTMnet; P14719; -.
DR PhosphoSitePlus; P14719; -.
DR EPD; P14719; -.
DR MaxQB; P14719; -.
DR PaxDb; P14719; -.
DR PRIDE; P14719; -.
DR ProteomicsDB; 269402; -. [P14719-1]
DR ProteomicsDB; 269403; -. [P14719-2]
DR ABCD; P14719; 2 sequenced antibodies.
DR Antibodypedia; 2362; 572 antibodies from 39 providers.
DR DNASU; 17082; -.
DR Ensembl; ENSMUST00000053043; ENSMUSP00000054914; ENSMUSG00000026069. [P14719-1]
DR Ensembl; ENSMUST00000097772; ENSMUSP00000095379; ENSMUSG00000026069. [P14719-1]
DR Ensembl; ENSMUST00000173514; ENSMUSP00000133784; ENSMUSG00000026069. [P14719-2]
DR Ensembl; ENSMUST00000174335; ENSMUSP00000134351; ENSMUSG00000026069. [P14719-2]
DR GeneID; 17082; -.
DR KEGG; mmu:17082; -.
DR UCSC; uc007aub.3; mouse. [P14719-1]
DR CTD; 9173; -.
DR MGI; MGI:98427; Il1rl1.
DR VEuPathDB; HostDB:ENSMUSG00000026069; -.
DR eggNOG; ENOG502RU6H; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR HOGENOM; CLU_025552_3_2_1; -.
DR InParanoid; P14719; -.
DR OMA; MQGTIKW; -.
DR OrthoDB; 1109920at2759; -.
DR PhylomeDB; P14719; -.
DR TreeFam; TF325519; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-9014843; Interleukin-33 signaling.
DR BioGRID-ORCS; 17082; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Il1rl1; mouse.
DR PRO; PR:P14719; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P14719; protein.
DR Bgee; ENSMUSG00000026069; Expressed in endothelial cell of lymphatic vessel and 50 other tissues.
DR ExpressionAtlas; P14719; baseline and differential.
DR Genevisible; P14719; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
DR GO; GO:0002113; F:interleukin-33 binding; IPI:UniProtKB.
DR GO; GO:0002114; F:interleukin-33 receptor activity; IBA:GO_Central.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IGI:BHF-UCL.
DR GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IGI:BHF-UCL.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:BHF-UCL.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IGI:BHF-UCL.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IMP:BHF-UCL.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR004074; IL-1_rcpt_I/II-typ.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..567
FT /note="Interleukin-1 receptor-like 1"
FT /id="PRO_0000015443"
FT TOPO_DOM 27..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..109
FT /note="Ig-like C2-type 1"
FT DOMAIN 120..203
FT /note="Ig-like C2-type 2"
FT DOMAIN 217..324
FT /note="Ig-like C2-type 3"
FT DOMAIN 380..540
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 204..216
FT /note="Flexible linker"
FT /evidence="ECO:0000250"
FT ACT_SITE 466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:28930661"
FT DISULFID 117..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:28930661"
FT DISULFID 139..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:28930661"
FT DISULFID 240..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:28930661"
FT DISULFID 243..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:28930661"
FT VAR_SEQ 329..337
FT /note="IDHRSIYYI -> SKECPSHIA (in isoform B)"
FT /evidence="ECO:0000303|PubMed:2527364,
FT ECO:0000303|PubMed:2532153"
FT /id="VSP_002668"
FT VAR_SEQ 338..567
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:2527364,
FT ECO:0000303|PubMed:2532153"
FT /id="VSP_002669"
FT VARIANT 192
FT /note="A -> V (in strain: C3H/He)"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 183..193
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 196..209
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 252..262
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:5VI4"
SQ SEQUENCE 567 AA; 64801 MW; 9228CE227D95B0BC CRC64;
MIDRQRMGLW ALAILTLPMY LTVTEGSKSS WGLENEALIV RCPQRGRSTY PVEWYYSDTN
ESIPTQKRNR IFVSRDRLKF LPARVEDSGI YACVIRSPNL NKTGYLNVTI HKKPPSCNIP
DYLMYSTVRG SDKNFKITCP TIDLYNWTAP VQWFKNCKAL QEPRFRAHRS YLFIDNVTHD
DEGDYTCQFT HAENGTNYIV TATRSFTVEE KGFSMFPVIT NPPYNHTMEV EIGKPASIAC
SACFGKGSHF LADVLWQINK TVVGNFGEAR IQEEEGRNES SSNDMDCLTS VLRITGVTEK
DLSLEYDCLA LNLHGMIRHT IRLRRKQPID HRSIYYIVAG CSLLLMFINV LVIVLKVFWI
EVALFWRDIV TPYKTRNDGK LYDAYIIYPR VFRGSAAGTH SVEYFVHHTL PDVLENKCGY
KLCIYGRDLL PGQDAATVVE SSIQNSRRQV FVLAPHMMHS KEFAYEQEIA LHSALIQNNS
KVILIEMEPL GEASRLQVGD LQDSLQHLVK IQGTIKWRED HVADKQSLSS KFWKHVRYQM
PVPERASKTA SVAAPLSGKA CLDLKHF
