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Toll-like receptor 3 (CD antigen CD283)

 TLR3_MOUSE              Reviewed;         905 AA.
Q99MB1; Q91ZM4;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
31-JAN-2002, sequence version 2.
12-SEP-2018, entry version 164.
RecName: Full=Toll-like receptor 3;
AltName: CD_antigen=CD283;
Flags: Precursor;
Name=Tlr3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/Sv;
PubMed=11607032; DOI=10.1038/35099560;
Alexopoulou L., Holt A.C., Medzhitov R., Flavell R.A.;
"Recognition of double-stranded RNA and activation of NF-kappaB by
Toll-like receptor 3.";
Nature 413:732-738(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c X NIH; TISSUE=Macrophage;
Applequist S.E., Ljunggren H.G.;
"Molecular cloning of mouse Toll-like receptor 3 cDNA.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
FUNCTION IN CYTOMEGALOVIRUS INFECTION.
PubMed=14993594; DOI=10.1073/pnas.0400525101;
Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K.,
Mudd S., Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A.,
Beutler B.;
"Toll-like receptors 9 and 3 as essential components of innate immune
defense against mouse cytomegalovirus infection.";
Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH UNC93B1.
PubMed=17452530; DOI=10.1083/jcb.200612056;
Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L.,
Kim Y.M.;
"The interaction between the ER membrane protein UNC93B and TLR3, 7,
and 9 is crucial for TLR signaling.";
J. Cell Biol. 177:265-275(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH WDFY1 AND TICAM1.
PubMed=25736436; DOI=10.15252/embr.201439637;
Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
Liu Y.;
"WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
EMBO Rep. 16:447-455(2015).
[8]
X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 28-704 IN COMPLEX WITH
DS-RNA, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-71;
ASN-197; ASN-253; ASN-276; ASN-292; ASN-399; ASN-414; ASN-425;
ASN-508; ASN-663 AND ASN-668.
PubMed=18420935; DOI=10.1126/science.1155406;
Liu L., Botos I., Wang Y., Leonard J.N., Shiloach J., Segal D.M.,
Davies D.R.;
"Structural basis of toll-like receptor 3 signaling with double-
stranded RNA.";
Science 320:379-381(2008).
-!- FUNCTION: Key component of innate and adaptive immunity. TLRs
(Toll-like receptors) control host immune response against
pathogens through recognition of molecular patterns specific to
microorganisms. TLR3 is a nucleotide-sensing TLR which is
activated by double-stranded RNA, a sign of viral infection. Acts
via the adapter TRIF/TICAM1, leading to NF-kappa-B activation,
IRF3 nuclear translocation, cytokine secretion and the
inflammatory response (By similarity). {ECO:0000250,
ECO:0000269|PubMed:14993594}.
-!- SUBUNIT: Monomer and homodimer; dimerization is triggered by
ligand-binding, the signaling unit is composed of one ds-RNA of
around 40 bp and two TLR3 molecules, and lateral clustering of
signaling units along the length of the ds-RNA ligand is required
for TLR3 signal transduction. Interacts (via transmembrane domain)
with UNC93B1; the interaction is required for transport from the
ER to the endosomes. Interacts with SRC; upon binding of double-
stranded RNA (By similarity). Interacts with TICAM1 (via the TIR
domain) in response to poly(I:C) and this interaction is enhanced
in the presence of WDFY1 (PubMed:25736436). The tyrosine-
phosphorylated form (via TIR domain) interacts with WDFY1 (via WD
repeat 2) in response to poly(I:C) (PubMed:25736436).
{ECO:0000250|UniProtKB:O15455, ECO:0000269|PubMed:25736436}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type I membrane protein. Endosome membrane
{ECO:0000250|UniProtKB:O15455}. Early endosome
{ECO:0000250|UniProtKB:O15455}.
-!- TISSUE SPECIFICITY: Highly expressed in lung. After
intraperitoneal injection of lipopolysaccharide, highly expressed
in brain, heart, kidney, liver, lung and spleen.
-!- DOMAIN: ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to
18.
-!- PTM: TLR3 signaling requires a proteolytic cleavage mediated by
cathepsins CTSB and CTSH, the cleavage occurs between amino acids
252 and 346. The cleaved form of TLR3 is the predominant form
found in endosomes (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
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EMBL; AF420279; AAL27007.1; -; mRNA.
EMBL; AF355152; AAK26117.1; -; mRNA.
EMBL; AK083977; BAC39082.1; -; mRNA.
CCDS; CCDS22278.1; -.
RefSeq; NP_569054.2; NM_126166.4.
RefSeq; XP_006509341.1; XM_006509278.3.
RefSeq; XP_006509342.1; XM_006509279.2.
RefSeq; XP_006509343.1; XM_006509280.2.
RefSeq; XP_006509344.1; XM_006509281.3.
RefSeq; XP_006509345.1; XM_006509282.3.
RefSeq; XP_006509346.1; XM_006509283.3.
UniGene; Mm.33874; -.
PDB; 3CIG; X-ray; 2.66 A; A=28-704.
PDB; 3CIY; X-ray; 3.41 A; A/B=28-704.
PDBsum; 3CIG; -.
PDBsum; 3CIY; -.
ProteinModelPortal; Q99MB1; -.
SMR; Q99MB1; -.
BioGrid; 228338; 8.
IntAct; Q99MB1; 2.
MINT; Q99MB1; -.
STRING; 10090.ENSMUSP00000034056; -.
ChEMBL; CHEMBL2146340; -.
iPTMnet; Q99MB1; -.
PhosphoSitePlus; Q99MB1; -.
MaxQB; Q99MB1; -.
PaxDb; Q99MB1; -.
PRIDE; Q99MB1; -.
Ensembl; ENSMUST00000034056; ENSMUSP00000034056; ENSMUSG00000031639.
Ensembl; ENSMUST00000167106; ENSMUSP00000126556; ENSMUSG00000031639.
Ensembl; ENSMUST00000209772; ENSMUSP00000147738; ENSMUSG00000031639.
GeneID; 142980; -.
KEGG; mmu:142980; -.
UCSC; uc009loy.1; mouse.
CTD; 7098; -.
MGI; MGI:2156367; Tlr3.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000251618; -.
HOVERGEN; HBG023181; -.
InParanoid; Q99MB1; -.
KO; K05401; -.
OMA; HLLKDPL; -.
OrthoDB; EOG091G02Q2; -.
PhylomeDB; Q99MB1; -.
TreeFam; TF325595; -.
Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
EvolutionaryTrace; Q99MB1; -.
PRO; PR:Q99MB1; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031639; Expressed in 228 organ(s), highest expression level in cochlea.
CleanEx; MM_TLR3; -.
ExpressionAtlas; Q99MB1; baseline and differential.
Genevisible; Q99MB1; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071360; P:cellular response to exogenous dsRNA; ISO:MGI.
GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0006952; P:defense response; IMP:MGI.
GO; GO:0051607; P:defense response to virus; IGI:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0007252; P:I-kappaB phosphorylation; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0001774; P:microglial cell activation; ISO:MGI.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
GO; GO:0097527; P:necroptotic signaling pathway; ISO:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; IGI:BHF-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IMP:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
GO; GO:0045356; P:positive regulation of interferon-alpha biosynthetic process; ISS:UniProtKB.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; ISS:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:BHF-UCL.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; ISS:UniProtKB.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0032481; P:positive regulation of type I interferon production; IDA:MGI.
GO; GO:0034346; P:positive regulation of type III interferon production; IDA:MGI.
GO; GO:0002730; P:regulation of dendritic cell cytokine production; IDA:MGI.
GO; GO:0043331; P:response to dsRNA; ISO:MGI.
GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
GO; GO:0009615; P:response to virus; IMP:MGI.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IEA:InterPro.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISO:MGI.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027173; TLR3.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR44599; PTHR44599; 1.
Pfam; PF00560; LRR_1; 1.
Pfam; PF13855; LRR_8; 5.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 16.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 18.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; RNA-binding;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 905 Toll-like receptor 3.
/FTId=PRO_0000034716.
TOPO_DOM 26 705 Lumenal. {ECO:0000255}.
TRANSMEM 706 726 Helical. {ECO:0000255}.
TOPO_DOM 727 905 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 52 LRRNT.
REPEAT 53 74 LRR 1.
REPEAT 77 98 LRR 2.
REPEAT 101 122 LRR 3.
REPEAT 125 146 LRR 4.
REPEAT 149 170 LRR 5.
REPEAT 173 196 LRR 6.
REPEAT 199 220 LRR 7.
REPEAT 250 271 LRR 8.
REPEAT 276 297 LRR 9.
REPEAT 300 321 LRR 10.
REPEAT 324 345 LRR 11.
REPEAT 357 378 LRR 12.
REPEAT 381 401 LRR 13.
REPEAT 409 430 LRR 14.
REPEAT 433 454 LRR 15.
REPEAT 458 479 LRR 16.
REPEAT 482 502 LRR 17.
REPEAT 508 529 LRR 18.
REPEAT 532 553 LRR 19.
REPEAT 564 585 LRR 20.
REPEAT 588 609 LRR 21.
REPEAT 612 633 LRR 22.
DOMAIN 646 699 LRRCT.
DOMAIN 755 897 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
MOD_RES 760 760 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15455}.
MOD_RES 859 859 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15455}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 248 248 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 414 414 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 508 508 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 663 663 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
CARBOHYD 668 668 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420935}.
DISULFID 29 38 {ECO:0000269|PubMed:18420935}.
DISULFID 96 123 {ECO:0000269|PubMed:18420935}.
DISULFID 650 678 {ECO:0000269|PubMed:18420935}.
DISULFID 652 697 {ECO:0000269|PubMed:18420935}.
CONFLICT 670 670 S -> F (in Ref. 2; AAK26117).
{ECO:0000305}.
STRAND 33 37 {ECO:0000244|PDB:3CIY}.
STRAND 55 58 {ECO:0000244|PDB:3CIY}.
TURN 69 72 {ECO:0000244|PDB:3CIG}.
TURN 74 77 {ECO:0000244|PDB:3CIG}.
STRAND 79 82 {ECO:0000244|PDB:3CIG}.
HELIX 94 98 {ECO:0000244|PDB:3CIG}.
STRAND 104 106 {ECO:0000244|PDB:3CIG}.
HELIX 117 120 {ECO:0000244|PDB:3CIY}.
STRAND 128 130 {ECO:0000244|PDB:3CIG}.
TURN 143 146 {ECO:0000244|PDB:3CIG}.
STRAND 152 154 {ECO:0000244|PDB:3CIG}.
STRAND 167 169 {ECO:0000244|PDB:3CIG}.
STRAND 176 178 {ECO:0000244|PDB:3CIG}.
HELIX 190 195 {ECO:0000244|PDB:3CIG}.
STRAND 199 204 {ECO:0000244|PDB:3CIG}.
TURN 215 220 {ECO:0000244|PDB:3CIG}.
STRAND 221 224 {ECO:0000244|PDB:3CIG}.
STRAND 226 228 {ECO:0000244|PDB:3CIG}.
HELIX 236 246 {ECO:0000244|PDB:3CIG}.
STRAND 247 249 {ECO:0000244|PDB:3CIG}.
STRAND 253 255 {ECO:0000244|PDB:3CIG}.
STRAND 262 264 {ECO:0000244|PDB:3CIY}.
TURN 266 269 {ECO:0000244|PDB:3CIG}.
HELIX 270 272 {ECO:0000244|PDB:3CIG}.
STRAND 279 281 {ECO:0000244|PDB:3CIG}.
TURN 292 297 {ECO:0000244|PDB:3CIG}.
STRAND 303 305 {ECO:0000244|PDB:3CIG}.
TURN 316 321 {ECO:0000244|PDB:3CIG}.
STRAND 327 329 {ECO:0000244|PDB:3CIG}.
STRAND 339 341 {ECO:0000244|PDB:3CIG}.
TURN 349 354 {ECO:0000244|PDB:3CIG}.
STRAND 360 362 {ECO:0000244|PDB:3CIG}.
TURN 373 378 {ECO:0000244|PDB:3CIY}.
STRAND 384 386 {ECO:0000244|PDB:3CIG}.
STRAND 391 393 {ECO:0000244|PDB:3CIG}.
TURN 399 402 {ECO:0000244|PDB:3CIG}.
HELIX 403 405 {ECO:0000244|PDB:3CIG}.
STRAND 412 414 {ECO:0000244|PDB:3CIG}.
TURN 425 430 {ECO:0000244|PDB:3CIG}.
STRAND 436 438 {ECO:0000244|PDB:3CIG}.
STRAND 445 447 {ECO:0000244|PDB:3CIG}.
HELIX 451 453 {ECO:0000244|PDB:3CIY}.
STRAND 461 463 {ECO:0000244|PDB:3CIG}.
STRAND 468 471 {ECO:0000244|PDB:3CIG}.
TURN 474 479 {ECO:0000244|PDB:3CIG}.
STRAND 485 487 {ECO:0000244|PDB:3CIG}.
STRAND 493 495 {ECO:0000244|PDB:3CIG}.
STRAND 497 500 {ECO:0000244|PDB:3CIY}.
TURN 502 505 {ECO:0000244|PDB:3CIG}.
STRAND 511 513 {ECO:0000244|PDB:3CIG}.
TURN 524 529 {ECO:0000244|PDB:3CIG}.
STRAND 535 537 {ECO:0000244|PDB:3CIG}.
STRAND 567 569 {ECO:0000244|PDB:3CIG}.
TURN 580 585 {ECO:0000244|PDB:3CIG}.
STRAND 591 593 {ECO:0000244|PDB:3CIG}.
TURN 604 609 {ECO:0000244|PDB:3CIG}.
STRAND 615 617 {ECO:0000244|PDB:3CIG}.
HELIX 628 635 {ECO:0000244|PDB:3CIG}.
STRAND 639 642 {ECO:0000244|PDB:3CIG}.
HELIX 652 664 {ECO:0000244|PDB:3CIG}.
HELIX 672 675 {ECO:0000244|PDB:3CIG}.
STRAND 677 681 {ECO:0000244|PDB:3CIG}.
HELIX 682 684 {ECO:0000244|PDB:3CIG}.
HELIX 689 691 {ECO:0000244|PDB:3CIG}.
HELIX 694 696 {ECO:0000244|PDB:3CIY}.
SEQUENCE 905 AA; 103671 MW; 8EA6DBA9818E14B4 CRC64;
MKGCSSYLMY SFGGLLSLWI LLVSSTNQCT VRYNVADCSH LKLTHIPDDL PSNITVLNLT
HNQLRRLPPT NFTRYSQLAI LDAGFNSISK LEPELCQILP LLKVLNLQHN ELSQISDQTF
VFCTNLTELD LMSNSIHKIK SNPFKNQKNL IKLDLSHNGL SSTKLGTGVQ LENLQELLLA
KNKILALRSE ELEFLGNSSL RKLDLSSNPL KEFSPGCFQT IGKLFALLLN NAQLNPHLTE
KLCWELSNTS IQNLSLANNQ LLATSESTFS GLKWTNLTQL DLSYNNLHDV GNGSFSYLPS
LRYLSLEYNN IQRLSPRSFY GLSNLRYLSL KRAFTKQSVS LASHPNIDDF SFQWLKYLEY
LNMDDNNIPS TKSNTFTGLV SLKYLSLSKT FTSLQTLTNE TFVSLAHSPL LTLNLTKNHI
SKIANGTFSW LGQLRILDLG LNEIEQKLSG QEWRGLRNIF EIYLSYNKYL QLSTSSFALV
PSLQRLMLRR VALKNVDISP SPFRPLRNLT ILDLSNNNIA NINEDLLEGL ENLEILDFQH
NNLARLWKRA NPGGPVNFLK GLSHLHILNL ESNGLDEIPV GVFKNLFELK SINLGLNNLN
KLEPFIFDDQ TSLRSLNLQK NLITSVEKDV FGPPFQNLNS LDMRFNPFDC TCESISWFVN
WINQTHTNIS ELSTHYLCNT PHHYYGFPLK LFDTSSCKDS APFELLFIIS TSMLLVFILV
VLLIHIEGWR ISFYWNVSVH RILGFKEIDT QAEQFEYTAY IIHAHKDRDW VWEHFSPMEE
QDQSLKFCLE ERDFEAGVLG LEAIVNSIKR SRKIIFVITH HLLKDPLCRR FKVHHAVQQA
IEQNLDSIIL IFLQNIPDYK LNHALCLRRG MFKSHCILNW PVQKERINAF HHKLQVALGS
RNSAH


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