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Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]

 IL1R1_HUMAN             Reviewed;         569 AA.
P14778; Q587I7;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
05-DEC-2018, entry version 212.
RecName: Full=Interleukin-1 receptor type 1;
Short=IL-1R-1;
Short=IL-1RT-1;
Short=IL-1RT1;
AltName: Full=CD121 antigen-like family member A;
AltName: Full=Interleukin-1 receptor alpha;
Short=IL-1R-alpha;
AltName: Full=Interleukin-1 receptor type I;
AltName: Full=p80;
AltName: CD_antigen=CD121a;
Contains:
RecName: Full=Interleukin-1 receptor type 1, membrane form;
Short=mIL-1R1;
Short=mIL-1RI;
Contains:
RecName: Full=Interleukin-1 receptor type 1, soluble form;
Short=sIL-1R1;
Short=sIL-1RI;
Flags: Precursor;
Name=IL1R1; Synonyms=IL1R, IL1RA, IL1RT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2532321; DOI=10.1093/nar/17.23.10114;
Chua A.O., Gubler U.;
"Sequence of the cDNA for the human fibroblast type interleukin-1
receptor.";
Nucleic Acids Res. 17:10114-10114(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell;
PubMed=2530587; DOI=10.1073/pnas.86.22.8946;
Sims J.E., Acres R.B., Grubin C.E., McMahan C.J., Wignall J.M.,
March C.J., Dower S.K.;
"Cloning the interleukin 1 receptor from human T cells.";
Proc. Natl. Acad. Sci. U.S.A. 86:8946-8950(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-124.
SeattleSNPs variation discovery resource;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
PubMed=8142597; DOI=10.1016/1043-4666(93)90032-Z;
Svenson M., Hansen M.B., Heegaard P., Abell K., Bendtzen K.;
"Specific binding of interleukin 1 (IL-1) beta and IL-1 receptor
antagonist (IL-1ra) to human serum. High-affinity binding of IL-1ra to
soluble IL-1 receptor type I.";
Cytokine 5:427-435(1993).
[8]
LIGAND-BINDING.
PubMed=7989776;
Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J.,
Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.;
"Elevated levels of shed type II IL-1 receptor in sepsis. Potential
role for type II receptor in regulation of IL-1 responses.";
J. Immunol. 153:5802-5809(1994).
[9]
INTERACTION WITH IL1RAP AND IRAK1.
TISSUE=Placenta;
PubMed=9371760; DOI=10.1073/pnas.94.24.12829;
Huang J., Gao X., Li S., Cao Z.;
"Recruitment of IRAK to the interleukin 1 receptor complex requires
interleukin 1 receptor accessory protein.";
Proc. Natl. Acad. Sci. U.S.A. 94:12829-12832(1997).
[10]
PHOSPHORYLATION AT TYR-496, AND INTERACTION WITH PIK3R1.
PubMed=9821957; DOI=10.1016/S0014-5793(98)01270-8;
Marmiroli S., Bavelloni A., Faenza I., Sirri A., Ognibene A.,
Cenni V., Tsukada J., Koyama Y., Ruzzene M., Ferri A., Auron P.E.,
Toker A., Maraldi N.M.;
"Phosphatidylinositol 3-kinase is recruited to a specific site in the
activated IL-1 receptor I.";
FEBS Lett. 438:49-54(1998).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10653850;
Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K.,
Hada T., Okamura H., Nakanishi K.;
"IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from
human T cells.";
Int. Immunol. 12:151-160(2000).
[12]
FUNCTION, AND MUTAGENESIS OF ASP-369 AND ARG-428.
PubMed=10671496; DOI=10.1074/jbc.275.7.4670;
Slack J.L., Schooley K., Bonnert T.P., Mitcham J.L., Qwarnstrom E.E.,
Sims J.E., Dower S.K.;
"Identification of two major sites in the type I interleukin-1
receptor cytoplasmic region responsible for coupling to pro-
inflammatory signaling pathways.";
J. Biol. Chem. 275:4670-4678(2000).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-332 IN COMPLEX WITH IL1B.
PubMed=9062193; DOI=10.1038/386190a0;
Vigers G.P.A., Anderson L.J., Caffes P., Brandhuber B.J.;
"Crystal structure of the type-I interleukin-1 receptor complexed with
interleukin-1beta.";
Nature 386:190-194(1997).
[14]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-331 IN COMPLEX WITH IL1RA.
PubMed=9062194; DOI=10.1038/386194a0;
Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A.,
Sarubbi E., Akeson A., Bowlin T., Yanofsky S., Barrett R.W.;
"A new cytokine-receptor binding mode revealed by the crystal
structure of the IL-1 receptor with an antagonist.";
Nature 386:194-200(1997).
[15]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 4-315 IN COMPLEX WITH THE
ANTAGONIST PEPTIDE AF10847.
PubMed=10903327; DOI=10.1074/jbc.M006071200;
Vigers G.P.A., Dripps D.J., Edwards C.K. III, Brandhuber B.J.;
"X-ray crystal structure of a small antagonist peptide bound to
interleukin-1 receptor type 1.";
J. Biol. Chem. 275:36927-36933(2000).
-!- FUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to
interleukin-1 associates with the coreceptor IL1RAP to form the
high affinity interleukin-1 receptor complex which mediates
interleukin-1-dependent activation of NF-kappa-B, MAPK and other
pathways. Signaling involves the recruitment of adapter molecules
such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR
domains of the receptor/coreceptor subunits. Binds ligands with
comparable affinity and binding of antagonist IL1RN prevents
association with IL1RAP to form a signaling complex. Involved in
IL1B-mediated costimulation of IFNG production from T-helper 1
(Th1) cells (PubMed:10653850). {ECO:0000269|PubMed:10653850,
ECO:0000269|PubMed:10671496}.
-!- SUBUNIT: The interleukin-1 receptor complex is a heterodimer of
IL1R1 and IL1RAP. Interacts with PIK3R1.
{ECO:0000269|PubMed:10903327, ECO:0000269|PubMed:9062193,
ECO:0000269|PubMed:9062194, ECO:0000269|PubMed:9371760,
ECO:0000269|PubMed:9821957}.
-!- INTERACTION:
P09619:PDGFRB; NbExp=2; IntAct=EBI-525905, EBI-641237;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-525905, EBI-359276;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8142597};
Single-pass type I membrane protein {ECO:0000269|PubMed:8142597}.
Cell membrane {ECO:0000305|PubMed:8142597}. Secreted
{ECO:0000269|PubMed:8142597}.
-!- TISSUE SPECIFICITY: Expressed in T-helper cell subsets.
Preferentially expressed in T-helper 1 (Th1) cells.
{ECO:0000269|PubMed:10653850}.
-!- PTM: A soluble form (sIL1R1) is probably produced by proteolytic
cleavage at the cell surface (shedding).
{ECO:0000269|PubMed:8142597}.
-!- PTM: Rapidly phosphorylated on Tyr-496 in response to IL-1, which
creates a SH2 binding site for the PI 3-kinase regulatory subunit
PIK3R1. {ECO:0000269|PubMed:9821957}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il1r1/";
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EMBL; X16896; CAA34773.1; -; mRNA.
EMBL; M27492; AAA59137.1; -; mRNA.
EMBL; AF531102; AAM88423.1; -; Genomic_DNA.
EMBL; AC007271; AAX81988.1; -; Genomic_DNA.
EMBL; CH471127; EAX01799.1; -; Genomic_DNA.
EMBL; BC067506; AAH67506.1; -; mRNA.
EMBL; BC075062; AAH75062.1; -; mRNA.
EMBL; BC075063; AAH75063.1; -; mRNA.
CCDS; CCDS2055.1; -.
PIR; A36187; A36187.
RefSeq; NP_000868.1; NM_000877.3.
RefSeq; NP_001275635.1; NM_001288706.1.
RefSeq; NP_001307907.1; NM_001320978.1.
RefSeq; NP_001307909.1; NM_001320980.1.
RefSeq; NP_001307910.1; NM_001320981.1.
RefSeq; NP_001307911.1; NM_001320982.1.
RefSeq; NP_001307912.1; NM_001320983.1.
RefSeq; NP_001307913.1; NM_001320984.1.
RefSeq; NP_001307914.1; NM_001320985.1.
RefSeq; XP_005263987.1; XM_005263930.4.
RefSeq; XP_005263991.1; XM_005263934.4.
RefSeq; XP_011509417.1; XM_011511115.2.
RefSeq; XP_011509418.1; XM_011511116.1.
RefSeq; XP_011509419.1; XM_011511117.1.
RefSeq; XP_011509420.1; XM_011511118.2.
RefSeq; XP_016859478.1; XM_017003989.1.
UniGene; Hs.701982; -.
PDB; 1G0Y; X-ray; 3.00 A; R=21-332.
PDB; 1IRA; X-ray; 2.70 A; Y=18-336.
PDB; 1ITB; X-ray; 2.50 A; B=18-332.
PDB; 4DEP; X-ray; 3.10 A; B/E=18-336.
PDB; 4GAF; X-ray; 2.15 A; B=18-336.
PDBsum; 1G0Y; -.
PDBsum; 1IRA; -.
PDBsum; 1ITB; -.
PDBsum; 4DEP; -.
PDBsum; 4GAF; -.
ProteinModelPortal; P14778; -.
SMR; P14778; -.
BioGrid; 109770; 23.
DIP; DIP-93N; -.
IntAct; P14778; 7.
STRING; 9606.ENSP00000233946; -.
ChEMBL; CHEMBL1959; -.
DrugBank; DB00026; Anakinra.
DrugBank; DB05303; OMS-103HP.
DrugBank; DB05207; SD118.
GuidetoPHARMACOLOGY; 1734; -.
TCDB; 8.A.23.1.11; the basigin (basigin) family.
iPTMnet; P14778; -.
PhosphoSitePlus; P14778; -.
BioMuta; IL1R1; -.
DMDM; 124308; -.
MaxQB; P14778; -.
PaxDb; P14778; -.
PeptideAtlas; P14778; -.
PRIDE; P14778; -.
ProteomicsDB; 53081; -.
Ensembl; ENST00000410023; ENSP00000386380; ENSG00000115594.
GeneID; 3554; -.
KEGG; hsa:3554; -.
UCSC; uc002tbq.5; human.
CTD; 3554; -.
DisGeNET; 3554; -.
EuPathDB; HostDB:ENSG00000115594.11; -.
GeneCards; IL1R1; -.
HGNC; HGNC:5993; IL1R1.
HPA; CAB007779; -.
HPA; HPA005823; -.
HPA; HPA029560; -.
MIM; 147810; gene.
neXtProt; NX_P14778; -.
OpenTargets; ENSG00000115594; -.
PharmGKB; PA29809; -.
eggNOG; ENOG410IQBC; Eukaryota.
eggNOG; ENOG410Z3W1; LUCA.
GeneTree; ENSGT00940000153278; -.
HOGENOM; HOG000253916; -.
HOVERGEN; HBG052103; -.
InParanoid; P14778; -.
KO; K04386; -.
OMA; AYIQLIH; -.
OrthoDB; EOG091G03IT; -.
PhylomeDB; P14778; -.
TreeFam; TF325519; -.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
SignaLink; P14778; -.
SIGNOR; P14778; -.
ChiTaRS; IL1R1; human.
EvolutionaryTrace; P14778; -.
GeneWiki; Interleukin_1_receptor,_type_I; -.
GenomeRNAi; 3554; -.
PRO; PR:P14778; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115594; Expressed in 228 organ(s), highest expression level in palpebral conjunctiva.
CleanEx; HS_IL1R1; -.
ExpressionAtlas; P14778; baseline and differential.
Genevisible; P14778; HS.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019966; F:interleukin-1 binding; IEA:Ensembl.
GO; GO:0004908; F:interleukin-1 receptor activity; IDA:BHF-UCL.
GO; GO:0004909; F:interleukin-1, type I, activating receptor activity; TAS:ProtInc.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:2000661; P:positive regulation of interleukin-1-mediated signaling pathway; IEA:Ensembl.
GO; GO:2000391; P:positive regulation of neutrophil extravasation; IEA:Ensembl.
GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IDA:BHF-UCL.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR004076; IL-1_rcpt_I-typ.
InterPro; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF01582; TIR; 1.
PRINTS; PR01538; INTRLEUKN1R1.
PRINTS; PR01536; INTRLKN1R12F.
SMART; SM00409; IG; 3.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Inflammatory response; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 17
CHAIN 18 569 Interleukin-1 receptor type 1, membrane
form.
/FTId=PRO_0000015435.
CHAIN 18 ? Interleukin-1 receptor type 1, soluble
form.
/FTId=PRO_0000415344.
TOPO_DOM 18 336 Extracellular. {ECO:0000255}.
TRANSMEM 337 356 Helical. {ECO:0000255}.
TOPO_DOM 357 569 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 110 Ig-like C2-type 1.
DOMAIN 118 210 Ig-like C2-type 2.
DOMAIN 226 328 Ig-like C2-type 3.
DOMAIN 383 541 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
MOD_RES 496 496 Phosphotyrosine.
{ECO:0000269|PubMed:9821957}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 193 193 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 263 263 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 23 104
DISULFID 44 96
DISULFID 121 164
DISULFID 142 196
DISULFID 248 312
VARIANT 124 124 A -> G (in dbSNP:rs2228139).
{ECO:0000269|Ref.3}.
/FTId=VAR_019131.
VARIANT 344 344 T -> M (in dbSNP:rs28362304).
/FTId=VAR_029189.
MUTAGEN 369 369 D->A: Reduces NF-kappa-B activation.
{ECO:0000269|PubMed:10671496}.
MUTAGEN 428 428 R->A: Reduces NF-kappa-B activation and
receptor-associated kinase activation.
{ECO:0000269|PubMed:10671496}.
STRAND 24 27 {ECO:0000244|PDB:4GAF}.
STRAND 32 35 {ECO:0000244|PDB:4GAF}.
STRAND 40 43 {ECO:0000244|PDB:4GAF}.
HELIX 48 50 {ECO:0000244|PDB:1IRA}.
STRAND 56 59 {ECO:0000244|PDB:4GAF}.
STRAND 72 77 {ECO:0000244|PDB:4GAF}.
STRAND 80 83 {ECO:0000244|PDB:4GAF}.
HELIX 88 90 {ECO:0000244|PDB:4GAF}.
STRAND 92 97 {ECO:0000244|PDB:4GAF}.
STRAND 100 102 {ECO:0000244|PDB:1ITB}.
STRAND 105 114 {ECO:0000244|PDB:4GAF}.
STRAND 120 122 {ECO:0000244|PDB:4GAF}.
HELIX 124 126 {ECO:0000244|PDB:4GAF}.
STRAND 127 133 {ECO:0000244|PDB:4GAF}.
STRAND 135 137 {ECO:0000244|PDB:1G0Y}.
STRAND 138 141 {ECO:0000244|PDB:4GAF}.
HELIX 146 148 {ECO:0000244|PDB:4GAF}.
TURN 151 153 {ECO:0000244|PDB:4GAF}.
STRAND 159 162 {ECO:0000244|PDB:4GAF}.
STRAND 171 177 {ECO:0000244|PDB:4GAF}.
STRAND 180 183 {ECO:0000244|PDB:4GAF}.
HELIX 188 190 {ECO:0000244|PDB:4GAF}.
STRAND 192 202 {ECO:0000244|PDB:4GAF}.
STRAND 205 218 {ECO:0000244|PDB:4GAF}.
STRAND 227 230 {ECO:0000244|PDB:4GAF}.
STRAND 233 237 {ECO:0000244|PDB:4GAF}.
STRAND 240 242 {ECO:0000244|PDB:1ITB}.
STRAND 244 252 {ECO:0000244|PDB:4GAF}.
STRAND 256 262 {ECO:0000244|PDB:4GAF}.
STRAND 272 281 {ECO:0000244|PDB:4GAF}.
HELIX 287 289 {ECO:0000244|PDB:4GAF}.
STRAND 290 300 {ECO:0000244|PDB:4GAF}.
HELIX 303 306 {ECO:0000244|PDB:4GAF}.
STRAND 310 316 {ECO:0000244|PDB:4GAF}.
STRAND 319 328 {ECO:0000244|PDB:4GAF}.
SEQUENCE 569 AA; 65402 MW; 5BAA83F8F0225C25 CRC64;
MKVLLRLICF IALLISSLEA DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD
DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL
CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR
LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL
GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE
IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKHMIG ICVTLTVIIV CSVFIYKIFK
IDIVLWYRDS CYDFLPIKAS DGKTYDAYIL YPKTVGEGST SDCDIFVFKV LPEVLEKQCG
YKLFIYGRDD YVGEDIVEVI NENVKKSRRL IIILVRETSG FSWLGGSSEE QIAMYNALVQ
DGIKVVLLEL EKIQDYEKMP ESIKFIKQKH GAIRWSGDFT QGPQSAKTRF WKNVRYHMPV
QRRSPSSKHQ LLSPATKEKL QREAHVPLG


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