TLR3_MOUSE
ID TLR3_MOUSE Reviewed; 905 AA.
AC Q99MB1; Q91ZM4;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Toll-like receptor 3 {ECO:0000305};
DE AltName: CD_antigen=CD283;
DE Flags: Precursor;
GN Name=Tlr3 {ECO:0000312|MGI:MGI:2156367};
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].
RC STRAIN=129/Sv;
RX PubMed=11607032; DOI=10.1038/35099560;
RA Alexopoulou L., Holt A.C., Medzhitov R., Flavell R.A.;
RT "Recognition of double-stranded RNA and activation of NF-kappaB by Toll-
RT like receptor 3.";
RL Nature 413:732-738(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/c X NIH; TISSUE=Macrophage;
RA Applequist S.E., Ljunggren H.G.;
RT "Molecular cloning of mouse Toll-like receptor 3 cDNA.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION IN CYTOMEGALOVIRUS INFECTION.
RX PubMed=14993594; DOI=10.1073/pnas.0400525101;
RA Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K., Mudd S.,
RA Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A., Beutler B.;
RT "Toll-like receptors 9 and 3 as essential components of innate immune
RT defense against mouse cytomegalovirus infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH UNC93B1.
RX PubMed=17452530; DOI=10.1083/jcb.200612056;
RA Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L., Kim Y.M.;
RT "The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9
RT is crucial for TLR signaling.";
RL J. Cell Biol. 177:265-275(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH WDFY1 AND TICAM1.
RX PubMed=25736436; DOI=10.15252/embr.201439637;
RA Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
RA Liu Y.;
RT "WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
RL EMBO Rep. 16:447-455(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 28-704 IN COMPLEX WITH DS-RNA,
RP SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-71; ASN-197; ASN-253;
RP ASN-276; ASN-292; ASN-399; ASN-414; ASN-425; ASN-508; ASN-663 AND ASN-668.
RX PubMed=18420935; DOI=10.1126/science.1155406;
RA Liu L., Botos I., Wang Y., Leonard J.N., Shiloach J., Segal D.M.,
RA Davies D.R.;
RT "Structural basis of toll-like receptor 3 signaling with double-stranded
RT RNA.";
RL Science 320:379-381(2008).
RN [9] {ECO:0007744|PDB:7C77}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH UNC93B1,
RP AND INTERACTION WITH UNC93B1.
RX PubMed=33432245; DOI=10.1038/s41594-020-00542-w;
RA Ishida H., Asami J., Zhang Z., Nishizawa T., Shigematsu H., Ohto U.,
RA Shimizu T.;
RT "Cryo-EM structures of Toll-like receptors in complex with UNC93B1.";
RL Nat. Struct. Mol. Biol. 28:173-180(2021).
CC -!- FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-
CC like receptors) control host immune response against pathogens through
CC recognition of molecular patterns specific to microorganisms. TLR3 is a
CC nucleotide-sensing TLR which is activated by double-stranded RNA, a
CC sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to
CC NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion
CC and the inflammatory response (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:14993594}.
CC -!- SUBUNIT: Monomer and homodimer; dimerization is triggered by ligand-
CC binding, the signaling unit is composed of one ds-RNA of around 40 bp
CC and two TLR3 molecules, and lateral clustering of signaling units along
CC the length of the ds-RNA ligand is required for TLR3 signal
CC transduction. Interacts (via transmembrane domain) with UNC93B1; the
CC interaction is required for transport from the ER to the endosomes
CC (PubMed:33432245). Interacts with SRC; upon binding of double-stranded
CC RNA (By similarity). Interacts with TICAM1 (via the TIR domain) in
CC response to poly(I:C) and this interaction is enhanced in the presence
CC of WDFY1 (PubMed:25736436). The tyrosine-phosphorylated form (via TIR
CC domain) interacts with WDFY1 (via WD repeat 2) in response to poly(I:C)
CC (PubMed:25736436). {ECO:0000250|UniProtKB:O15455,
CC ECO:0000269|PubMed:25736436, ECO:0000269|PubMed:33432245}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein. Endosome membrane {ECO:0000250|UniProtKB:O15455}.
CC Early endosome {ECO:0000250|UniProtKB:O15455}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung. After intraperitoneal
CC injection of lipopolysaccharide, highly expressed in brain, heart,
CC kidney, liver, lung and spleen.
CC -!- DOMAIN: ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to 18.
CC -!- PTM: TLR3 signaling requires a proteolytic cleavage mediated by
CC cathepsins CTSB and CTSH, the cleavage occurs between amino acids 252
CC and 346. The cleaved form of TLR3 is the predominant form found in
CC endosomes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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DR EMBL; AF420279; AAL27007.1; -; mRNA.
DR EMBL; AF355152; AAK26117.1; -; mRNA.
DR EMBL; AK083977; BAC39082.1; -; mRNA.
DR CCDS; CCDS22278.1; -.
DR RefSeq; NP_569054.2; NM_126166.4.
DR RefSeq; XP_006509341.1; XM_006509278.3.
DR RefSeq; XP_006509342.1; XM_006509279.2.
DR RefSeq; XP_006509343.1; XM_006509280.2.
DR RefSeq; XP_006509344.1; XM_006509281.3.
DR RefSeq; XP_006509345.1; XM_006509282.3.
DR RefSeq; XP_006509346.1; XM_006509283.3.
DR PDB; 3CIG; X-ray; 2.66 A; A=28-704.
DR PDB; 3CIY; X-ray; 3.41 A; A/B=28-704.
DR PDB; 7C77; EM; 3.30 A; A=1-905.
DR PDB; 7DA7; EM; 3.47 A; A/B=28-698.
DR PDB; 7DAS; EM; 3.64 A; A/B=28-698.
DR PDBsum; 3CIG; -.
DR PDBsum; 3CIY; -.
DR PDBsum; 7C77; -.
DR PDBsum; 7DA7; -.
DR PDBsum; 7DAS; -.
DR AlphaFoldDB; Q99MB1; -.
DR SMR; Q99MB1; -.
DR BioGRID; 228338; 13.
DR IntAct; Q99MB1; 1.
DR STRING; 10090.ENSMUSP00000034056; -.
DR ChEMBL; CHEMBL2146340; -.
DR GlyGen; Q99MB1; 15 sites.
DR iPTMnet; Q99MB1; -.
DR PhosphoSitePlus; Q99MB1; -.
DR MaxQB; Q99MB1; -.
DR PaxDb; Q99MB1; -.
DR PRIDE; Q99MB1; -.
DR ProteomicsDB; 259207; -.
DR ABCD; Q99MB1; 10 sequenced antibodies.
DR Antibodypedia; 17502; 1121 antibodies from 48 providers.
DR DNASU; 142980; -.
DR Ensembl; ENSMUST00000034056; ENSMUSP00000034056; ENSMUSG00000031639.
DR Ensembl; ENSMUST00000167106; ENSMUSP00000126556; ENSMUSG00000031639.
DR Ensembl; ENSMUST00000209772; ENSMUSP00000147738; ENSMUSG00000031639.
DR GeneID; 142980; -.
DR KEGG; mmu:142980; -.
DR UCSC; uc009loy.1; mouse.
DR CTD; 7098; -.
DR MGI; MGI:2156367; Tlr3.
DR VEuPathDB; HostDB:ENSMUSG00000031639; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000159678; -.
DR HOGENOM; CLU_006000_4_1_1; -.
DR InParanoid; Q99MB1; -.
DR OMA; LFDTSPC; -.
DR OrthoDB; 737804at2759; -.
DR PhylomeDB; Q99MB1; -.
DR TreeFam; TF325595; -.
DR BioGRID-ORCS; 142980; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Tlr3; mouse.
DR EvolutionaryTrace; Q99MB1; -.
DR PRO; PR:Q99MB1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q99MB1; protein.
DR Bgee; ENSMUSG00000031639; Expressed in conjunctival fornix and 209 other tissues.
DR ExpressionAtlas; Q99MB1; baseline and differential.
DR Genevisible; Q99MB1; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISO:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IMP:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006952; P:defense response; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; IGI:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0007252; P:I-kappaB phosphorylation; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0001774; P:microglial cell activation; ISO:MGI.
DR GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0097527; P:necroptotic signaling pathway; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IGI:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:BHF-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IDA:MGI.
DR GO; GO:0034346; P:positive regulation of type III interferon production; IDA:MGI.
DR GO; GO:0002730; P:regulation of dendritic cell cytokine production; IDA:MGI.
DR GO; GO:0043331; P:response to dsRNA; ISO:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR GO; GO:0009615; P:response to virus; IMP:MGI.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IEA:InterPro.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; ISO:MGI.
DR GO; GO:0034343; P:type III interferon production; IDA:MGI.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR027173; TLR3.
DR InterPro; IPR041015; TLR3_TMD.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR PANTHER; PTHR24365:SF524; PTHR24365:SF524; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 6.
DR Pfam; PF01582; TIR; 1.
DR Pfam; PF17968; Tlr3_TMD; 1.
DR SMART; SM00369; LRR_TYP; 16.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 18.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; RNA-binding; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..905
FT /note="Toll-like receptor 3"
FT /id="PRO_0000034716"
FT TOPO_DOM 26..705
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 727..905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..52
FT /note="LRRNT"
FT REPEAT 53..74
FT /note="LRR 1"
FT REPEAT 77..98
FT /note="LRR 2"
FT REPEAT 101..122
FT /note="LRR 3"
FT REPEAT 125..146
FT /note="LRR 4"
FT REPEAT 149..170
FT /note="LRR 5"
FT REPEAT 173..196
FT /note="LRR 6"
FT REPEAT 199..220
FT /note="LRR 7"
FT REPEAT 250..271
FT /note="LRR 8"
FT REPEAT 276..297
FT /note="LRR 9"
FT REPEAT 300..321
FT /note="LRR 10"
FT REPEAT 324..345
FT /note="LRR 11"
FT REPEAT 357..378
FT /note="LRR 12"
FT REPEAT 381..401
FT /note="LRR 13"
FT REPEAT 409..430
FT /note="LRR 14"
FT REPEAT 433..454
FT /note="LRR 15"
FT REPEAT 458..479
FT /note="LRR 16"
FT REPEAT 482..502
FT /note="LRR 17"
FT REPEAT 508..529
FT /note="LRR 18"
FT REPEAT 532..553
FT /note="LRR 19"
FT REPEAT 564..585
FT /note="LRR 20"
FT REPEAT 588..609
FT /note="LRR 21"
FT REPEAT 612..633
FT /note="LRR 22"
FT DOMAIN 646..699
FT /note="LRRCT"
FT DOMAIN 755..898
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MOD_RES 760
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15455"
FT MOD_RES 859
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15455"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420935"
FT DISULFID 29..38
FT /evidence="ECO:0000269|PubMed:18420935"
FT DISULFID 96..123
FT /evidence="ECO:0000269|PubMed:18420935"
FT DISULFID 650..678
FT /evidence="ECO:0000269|PubMed:18420935"
FT DISULFID 652..697
FT /evidence="ECO:0000269|PubMed:18420935"
FT CONFLICT 670
FT /note="S -> F (in Ref. 2; AAK26117)"
FT /evidence="ECO:0000305"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3CIY"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 215..220
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3CIY"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 292..297
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 316..321
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 349..354
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 373..378
FT /evidence="ECO:0007829|PDB:3CIY"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:7DA7"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 425..430
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 474..479
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:3CIY"
FT TURN 502..505
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 524..529
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 580..585
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:3CIG"
FT TURN 604..609
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 628..635
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 639..642
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 652..664
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 668..671
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 672..675
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 677..681
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 682..684
FT /evidence="ECO:0007829|PDB:3CIG"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:3CIG"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 698..700
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 703..726
FT /evidence="ECO:0007829|PDB:7C77"
SQ 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
