IL1R2_HUMAN
ID IL1R2_HUMAN Reviewed; 398 AA.
AC P27930; D3DVJ5; Q6LCE6; Q9UE68;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Interleukin-1 receptor type 2;
DE Short=IL-1R-2;
DE Short=IL-1RT-2;
DE Short=IL-1RT2;
DE AltName: Full=CD121 antigen-like family member B;
DE AltName: Full=CDw121b;
DE AltName: Full=IL-1 type II receptor;
DE AltName: Full=Interleukin-1 receptor beta;
DE Short=IL-1R-beta;
DE AltName: Full=Interleukin-1 receptor type II;
DE AltName: CD_antigen=CD121b;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 2, membrane form;
DE Short=mIL-1R2;
DE Short=mIL-1RII;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 2, soluble form;
DE Short=sIL-1R2;
DE Short=sIL-1RII;
DE Flags: Precursor;
GN Name=IL1R2; Synonyms=IL1RB;
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 LONG).
RC TISSUE=B-cell;
RX PubMed=1833184; DOI=10.1002/j.1460-2075.1991.tb07831.x;
RA McMahan C.J., Slack J.L., Mosley B., Cosman D., Lupton S.D., Brunton L.L.,
RA Grubin C.E., Wignall J.M., Jenkins N.A., Brannan C.I., Copeland N.G.,
RA Huebner K., Croce C.M., Cannizzarro L.A., Benjamin D., Dower S.K.,
RA Spriggs M.K., Sims J.E.;
RT "A novel IL-1 receptor, cloned from B cells by mammalian expression, is
RT expressed in many cell types.";
RL EMBO J. 10:2821-2832(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), IL1B-BINDING, AND SUBCELLULAR
RP LOCATION (ISOFORM SHORT).
RX PubMed=8702856; DOI=10.1074/jbc.271.34.20965;
RA Liu C., Hart R.P., Liu X.J., Clevenger W., Maki R.A., Souza E.B.;
RT "Cloning and characterization of an alternatively processed human type II
RT interleukin-1 receptor mRNA.";
RL J. Biol. Chem. 271:20965-20972(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA Chou H.-H., Takashiba T., Takigawa M., Maeda H., Asahara Y., Nishimura F.,
RA Arai H., Murayama Y.;
RT "Complete nucleotide sequence and expression of the human interleukin-1
RT receptor type II in human gingival fibroblasts.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-181 AND LYS-292.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Ovary;
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 FUNCTION, PROTEOLYTIC PROCESSING, AND LIGAND-BINDING.
RX PubMed=7989776;
RA Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J.,
RA Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.;
RT "Elevated levels of shed type II IL-1 receptor in sepsis. Potential role
RT for type II receptor in regulation of IL-1 responses.";
RL J. Immunol. 153:5802-5809(1994).
RN [9]
RP LIGAND-BINDING.
RX PubMed=7878046; DOI=10.1073/pnas.92.5.1714;
RA Symons J.A., Young P.R., Duff G.W.;
RT "Soluble type II interleukin 1 (IL-1) receptor binds and blocks processing
RT of IL-1 beta precursor and loses affinity for IL-1 receptor antagonist.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1714-1718(1995).
RN [10]
RP PROTEOLYTIC PROCESSING.
RX PubMed=9395521; DOI=10.1074/jbc.272.50.31764;
RA Orlando S., Sironi M., Bianchi G., Drummond A.H., Boraschi D., Yabes D.,
RA Mantovani A.;
RT "Role of metalloproteases in the release of the IL-1 type II decoy
RT receptor.";
RL J. Biol. Chem. 272:31764-31769(1997).
RN [11]
RP FUNCTION, AND INTERACTION WITH IL1RAP.
RX PubMed=9862719;
RA Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D.,
RA Martin M.U.;
RT "The type II IL-1 receptor interacts with the IL-1 receptor accessory
RT protein: a novel mechanism of regulation of IL-1 responsiveness.";
RL J. Immunol. 161:6871-6877(1998).
RN [12]
RP FUNCTION AS DECOY RECEPTOR.
RX PubMed=10975853; DOI=10.4049/jimmunol.165.6.3350;
RA Neumann D., Kollewe C., Martin M.U., Boraschi D.;
RT "The membrane form of the type II IL-1 receptor accounts for inhibitory
RT function.";
RL J. Immunol. 165:3350-3357(2000).
RN [13]
RP FUNCTION AS DECOY RECEPTOR.
RX PubMed=12530978; DOI=10.1016/s1074-7613(02)00514-9;
RA Smith D.E., Hanna R., Friend D., Moore H., Chen H., Farese A.M.,
RA MacVittie T.J., Virca G.D., Sims J.E.;
RT "The soluble form of IL-1 receptor accessory protein enhances the ability
RT of soluble type II IL-1 receptor to inhibit IL-1 action.";
RL Immunity 18:87-96(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 14-343 IN COMPLEX WITH IL1RAP AND
RP IL1B, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-112 AND ASN-219.
RX PubMed=20802483; DOI=10.1038/ni.1925;
RA Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.;
RT "Structural insights into the assembly and activation of IL-1beta with its
RT receptors.";
RL Nat. Immunol. 11:905-911(2010).
CC -!- FUNCTION: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B
CC activities. Serves as a decoy receptor by competitive binding to IL1B
CC and preventing its binding to IL1R1. Also modulates cellular response
CC through non-signaling association with IL1RAP after binding to IL1B.
CC IL1R2 (membrane and secreted forms) preferentially binds IL1B and
CC poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with
CC high affinity; this complex formation may be the dominant mechanism for
CC neutralization of IL1B by secreted/soluble receptors.
CC {ECO:0000269|PubMed:10975853, ECO:0000269|PubMed:12530978,
CC ECO:0000269|PubMed:7989776, ECO:0000269|PubMed:9862719}.
CC -!- SUBUNIT: Associates with IL1RAP to form a non-signaling interleukin-1
CC receptor complex. {ECO:0000269|PubMed:20802483}.
CC -!- INTERACTION:
CC P27930; P01583: IL1A; NbExp=4; IntAct=EBI-2831568, EBI-1749782;
CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Secreted
CC {ECO:0000269|PubMed:8702856}.
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P27930-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P27930-2; Sequence=VSP_042222;
CC -!- PTM: A soluble form (sIL1R2) can also be produced by proteolytic
CC cleavage at the cell surface (shedding) involving a metalloproteinase;
CC hovever, several sIL1R2 forms ranging from 45 and 60 kDa are reported.
CC {ECO:0000269|PubMed:7989776, ECO:0000269|PubMed:9395521}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il1r2/";
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DR EMBL; X59770; CAA42441.1; -; mRNA.
DR EMBL; U64094; AAB05878.1; -; mRNA.
DR EMBL; U74649; AAD00242.1; -; mRNA.
DR EMBL; AY124010; AAM64221.1; -; Genomic_DNA.
DR EMBL; AC007165; AAK52072.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01800.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01801.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01802.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01803.1; -; Genomic_DNA.
DR EMBL; BC039031; AAH39031.1; -; mRNA.
DR CCDS; CCDS2054.1; -. [P27930-1]
DR CCDS; CCDS58719.1; -. [P27930-2]
DR PIR; S17428; S17428.
DR RefSeq; NP_001248348.1; NM_001261419.1. [P27930-2]
DR RefSeq; NP_004624.1; NM_004633.3. [P27930-1]
DR RefSeq; XP_006712797.1; XM_006712734.3. [P27930-1]
DR RefSeq; XP_011510106.1; XM_011511804.2. [P27930-1]
DR PDB; 3O4O; X-ray; 3.30 A; C=14-343.
DR PDBsum; 3O4O; -.
DR AlphaFoldDB; P27930; -.
DR SASBDB; P27930; -.
DR SMR; P27930; -.
DR BioGRID; 113605; 69.
DR DIP; DIP-61267N; -.
DR IntAct; P27930; 41.
DR MINT; P27930; -.
DR STRING; 9606.ENSP00000330959; -.
DR GlyConnect; 1949; 8 N-Linked glycans (2 sites).
DR GlyGen; P27930; 5 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; P27930; -.
DR PhosphoSitePlus; P27930; -.
DR BioMuta; IL1R2; -.
DR DMDM; 124310; -.
DR EPD; P27930; -.
DR jPOST; P27930; -.
DR MassIVE; P27930; -.
DR PaxDb; P27930; -.
DR PeptideAtlas; P27930; -.
DR PRIDE; P27930; -.
DR ProteomicsDB; 54427; -. [P27930-1]
DR ProteomicsDB; 54428; -. [P27930-2]
DR Antibodypedia; 17756; 669 antibodies from 41 providers.
DR DNASU; 7850; -.
DR Ensembl; ENST00000332549.8; ENSP00000330959.3; ENSG00000115590.14. [P27930-1]
DR Ensembl; ENST00000393414.6; ENSP00000377066.2; ENSG00000115590.14. [P27930-1]
DR Ensembl; ENST00000441002.1; ENSP00000414611.1; ENSG00000115590.14. [P27930-2]
DR GeneID; 7850; -.
DR KEGG; hsa:7850; -.
DR MANE-Select; ENST00000332549.8; ENSP00000330959.3; NM_004633.4; NP_004624.1.
DR UCSC; uc002tbm.4; human. [P27930-1]
DR CTD; 7850; -.
DR DisGeNET; 7850; -.
DR GeneCards; IL1R2; -.
DR HGNC; HGNC:5994; IL1R2.
DR HPA; ENSG00000115590; Tissue enhanced (lymphoid).
DR MIM; 147811; gene.
DR neXtProt; NX_P27930; -.
DR OpenTargets; ENSG00000115590; -.
DR PharmGKB; PA29810; -.
DR VEuPathDB; HostDB:ENSG00000115590; -.
DR eggNOG; ENOG502QVTS; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR HOGENOM; CLU_051287_0_0_1; -.
DR InParanoid; P27930; -.
DR OMA; CDEMSIE; -.
DR OrthoDB; 985064at2759; -.
DR PhylomeDB; P27930; -.
DR TreeFam; TF325519; -.
DR PathwayCommons; P27930; -.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR SignaLink; P27930; -.
DR SIGNOR; P27930; -.
DR BioGRID-ORCS; 7850; 31 hits in 1065 CRISPR screens.
DR ChiTaRS; IL1R2; human.
DR EvolutionaryTrace; P27930; -.
DR GeneWiki; Interleukin_1_receptor,_type_II; -.
DR GenomeRNAi; 7850; -.
DR Pharos; P27930; Tbio.
DR PRO; PR:P27930; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P27930; protein.
DR Bgee; ENSG00000115590; Expressed in corpus epididymis and 160 other tissues.
DR ExpressionAtlas; P27930; baseline and differential.
DR Genevisible; P27930; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019966; F:interleukin-1 binding; IBA:GO_Central.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IBA:GO_Central.
DR GO; GO:0004910; F:interleukin-1, type II, blocking receptor activity; IEA:InterPro.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0032690; P:negative regulation of interleukin-1 alpha production; IEA:Ensembl.
DR GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0010955; P:negative regulation of protein processing; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 3.
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; IPR004077; IL-1_rcpt_II-typ.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF18452; Ig_6; 1.
DR PRINTS; PR01539; INTRLEUKN1R2.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT CHAIN 14..398
FT /note="Interleukin-1 receptor type 2, membrane form"
FT /id="PRO_0000015439"
FT CHAIN 14..?
FT /note="Interleukin-1 receptor type 2, soluble form"
FT /id="PRO_0000415348"
FT TOPO_DOM 14..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..124
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 237..349
FT /note="Ig-like C2-type 3"
FT REGION 329..343
FT /note="Contains proteolytic cleavage site"
FT /evidence="ECO:0000305"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20802483"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20802483"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20802483"
FT DISULFID 50..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20802483"
FT DISULFID 152..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20802483"
FT DISULFID 258..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20802483"
FT VAR_SEQ 297..398
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8702856"
FT /id="VSP_042222"
FT VARIANT 181
FT /note="E -> K (in dbSNP:rs28385682)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019132"
FT VARIANT 292
FT /note="E -> K (in dbSNP:rs3218976)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019133"
FT CONFLICT 123
FT /note="L -> F (in Ref. 2; AAD00242)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="K -> R (in Ref. 2; AAD00242)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="L -> Q (in Ref. 2; AAD00242)"
FT /evidence="ECO:0000305"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 115..126
FT /evidence="ECO:0007829|PDB:3O4O"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3O4O"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3O4O"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:3O4O"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 219..229
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:3O4O"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3O4O"
SQ SEQUENCE 398 AA; 45421 MW; 2C2A03ADA6F3AC5B CRC64;
MLRLYVLVMG VSAFTLQPAA HTGAARSCRF RGRHYKREFR LEGEPVALRC PQVPYWLWAS
VSPRINLTWH KNDSARTVPG EEETRMWAQD GALWLLPALQ EDSGTYVCTT RNASYCDKMS
IELRVFENTD AFLPFISYPQ ILTLSTSGVL VCPDLSEFTR DKTDVKIQWY KDSLLLDKDN
EKFLSVRGTT HLLVHDVALE DAGYYRCVLT FAHEGQQYNI TRSIELRIKK KKEETIPVII
SPLKTISASL GSRLTIPCKV FLGTGTPLTT MLWWTANDTH IESAYPGGRV TEGPRQEYSE
NNENYIEVPL IFDPVTREDL HMDFKCVVHN TLSFQTLRTT VKEASSTFSW GIVLAPLSLA
FLVLGGIWMH RRCKHRTGKA DGLTVLWPHH QDFQSYPK
