ID TLR4_RAT Reviewed; 835 AA. AC Q9QX05; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 169. DE RecName: Full=Toll-like receptor 4; DE Short=Toll4; DE AltName: CD_antigen=CD284; DE Flags: Precursor; GN Name=Tlr4; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Heart; RX PubMed=10430608; DOI=10.1172/jci6709; RA Frantz S., Kobzik L., Kim Y.-D., Fukazawa R., Medzhitov R., Lee R.T., RA Kelly R.A.; RT "Toll4 (TLR4) expression in cardiac myocytes in normal and failing RT myocardium."; RL J. Clin. Invest. 104:271-280(1999). RN [2] RP INDUCTION BY LIPOPOLYSACCHARIDES. RX PubMed=30980393; DOI=10.1002/jcp.28614; RA Chao C.N., Lai C.H., Badrealam K.F., Lo J.F., Shen C.Y., Chen C.H., RA Chen R.J., Viswanadha V.P., Kuo W.W., Huang C.Y.; RT "CHIP attenuates lipopolysaccharide-induced cardiac hypertrophy and RT apoptosis by promoting NFATc3 proteasomal degradation."; RL J. Cell. Physiol. 234:20128-20138(2019). CC -!- FUNCTION: Transmembrane receptor that functions as a pattern CC recognition receptor recognizing pathogen- and damage-associated CC molecular patterns (PAMPs and DAMPs) to induce innate immune responses CC via downstream signaling pathways. At the plasma membrane, cooperates CC with LY96 to mediate the innate immune response to bacterial CC lipopolysaccharide (LPS). Also involved in LPS-independent inflammatory CC responses triggered by free fatty acids, such as palmitate, and Ni(2+). CC Mechanistically, acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B CC activation, cytokine secretion and the inflammatory response. CC Alternatively, CD14-mediated TLR4 internalization via endocytosis is CC associated with the initiation of a MYD88-independent signaling via the CC TICAM1-TBK1-IRF3 axis leading to type I interferon production. In CC addition to the secretion of proinflammatory cytokines, initiates the CC activation of NLRP3 inflammasome and formation of a positive feedback CC loop between autophagy and NF-kappa-B signaling cascade. In complex CC with TLR6, promotes inflammation in monocytes/macrophages by CC associating with TLR6 and the receptor CD86. Upon ligand binding, such CC as oxLDL or amyloid-beta 42, the TLR4:TLR6 complex is internalized and CC triggers inflammatory response, leading to NF-kappa-B-dependent CC production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling CC pathway, and CCL5 cytokine, via TICAM1 signaling pathway. In myeloid CC dendritic cells, vesicular stomatitis virus glycoprotein G but not LPS CC promotes the activation of IRF7, leading to type I IFN production in a CC CD14-dependent manner. {ECO:0000250|UniProtKB:O00206}. CC -!- SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a multi- CC protein complex containing at least CD14, LY96 and TLR4. Binding to CC bacterial LPS leads to homodimerization. Interacts with LY96 via the CC extracellular domain. Interacts with MYD88 and TIRAP via their CC respective TIR domains. Interacts with TICAM2. Interacts with NOX4. CC Interacts with CNPY3 and HSP90B1; this interaction is required for CC proper folding in the endoplasmic reticulum. Interacts with MAP3K21; CC this interaction leads to negative regulation of TLR4 signaling. CC Interacts with CD36, following CD36 stimulation by oxLDL or amyloid- CC beta 42, and forms a heterodimer with TLR6. The trimeric complex is CC internalized and triggers inflammatory response. LYN kinase activity CC facilitates TLR4-TLR6 heterodimerization and signal initiation. CC Interacts with TICAM1 in response to LPS in a WDFY1-dependent manner. CC Interacts with WDFY1 in response to LPS. Interacts with SMPDL3B. CC Interacts with CEACAM1; upon lipopolysaccharide stimulation, forms a CC complex including TLR4 and the phosphorylated form of SYK and CEACAM1, CC which in turn, recruits PTPN6 that dephosphorylates SYK, reducing the CC production of reactive oxygen species (ROS) and lysosome disruption, CC which in turn, reduces the activity of the inflammasome. Interacts with CC RFTN1; the interaction occurs in response to lipopolysaccharide CC stimulation. Interacts with SCIMP; the interaction occurs in response CC to lipopolysaccharide stimulation and is enhanced by phosphorylation of CC SCIMP by LYN (By similarity). This interaction facilitates the CC phosphorylation of TLR4 by LYN which elicits a selective cytokine CC response in macrophages (By similarity). Interacts with TRAF3IP3 (By CC similarity). Interacts with TREM1; this interaction enhances TLR4- CC mediated inflammatory response (By similarity). Interacts with CC ZG16B/PAUF (By similarity). {ECO:0000250|UniProtKB:O00206, CC ECO:0000250|UniProtKB:Q9QUK6}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00206}; CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O00206}. CC Early endosome {ECO:0000250|UniProtKB:O00206}. Cell projection, ruffle CC {ECO:0000250|UniProtKB:Q9QUK6}. Note=Upon complex formation with CD36 CC and TLR6, internalized through dynamin-dependent endocytosis. CC Colocalizes with RFTN1 at cell membrane and then together with RFTN1 CC moves to endosomes, upon lipopolysaccharide stimulation. CC {ECO:0000250|UniProtKB:O00206}. CC -!- INDUCTION: Induced by lipopolysaccharides. CC {ECO:0000269|PubMed:30980393}. CC -!- DOMAIN: The TIR domain mediates interaction with NOX4. CC {ECO:0000250|UniProtKB:O00206}. CC -!- PTM: Phosphorylated on tyrosine residues by LYN after binding CC lipopolysaccharide. {ECO:0000250|UniProtKB:Q9QUK6}. CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}. CC -!- CAUTION: In some plant proteins and in human SARM1, the TIR domain has CC NAD(+) hydrolase (NADase) activity (By similarity). However, despite CC the presence of the catalytic Asp residue, the isolated TIR domain of CC human TLR4 lacks NADase activity (By similarity). Based on this, it is CC unlikely that Toll-like receptors have NADase activity. CC {ECO:0000250|UniProtKB:O00206, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF057025; AAC13313.1; -; mRNA. DR RefSeq; NP_062051.1; NM_019178.1. DR AlphaFoldDB; Q9QX05; -. DR SMR; Q9QX05; -. DR BioGRID; 247933; 1. DR IntAct; Q9QX05; 1. DR MINT; Q9QX05; -. DR STRING; 10116.ENSRNOP00000014020; -. DR ChEMBL; CHEMBL4523480; -. DR GlyCosmos; Q9QX05; 15 sites, No reported glycans. DR GlyGen; Q9QX05; 15 sites. DR PhosphoSitePlus; Q9QX05; -. DR PaxDb; 10116-ENSRNOP00000014020; -. DR ABCD; Q9QX05; 2 sequenced antibodies. DR GeneID; 29260; -. DR KEGG; rno:29260; -. DR UCSC; RGD:3870; rat. DR AGR; RGD:3870; -. DR CTD; 7099; -. DR RGD; 3870; Tlr4. DR eggNOG; KOG4641; Eukaryota. DR InParanoid; Q9QX05; -. DR OrthoDB; 1207361at2759; -. DR PhylomeDB; Q9QX05; -. DR Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand. DR Reactome; R-RNO-936964; Activation of IRF3, IRF7 mediated by TBK1, IKBKE. DR Reactome; R-RNO-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex. DR PRO; PR:Q9QX05; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0009986; C:cell surface; IDA:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD. DR GO; GO:0046696; C:lipopolysaccharide receptor complex; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD. DR GO; GO:0001891; C:phagocytic cup; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0043235; C:receptor complex; ISO:RGD. DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:RGD. DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; ISS:UniProtKB. 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:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD. DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD. DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro. DR GO; GO:0002218; P:activation of innate immune response; ISO:RGD. DR GO; GO:0014002; P:astrocyte development; ISO:RGD. DR GO; GO:0042100; P:B cell proliferation; ISO:RGD. DR GO; GO:0002322; P:B cell proliferation involved in immune response; ISO:RGD. DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD. DR GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:RGD. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD. DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISO:RGD. DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:RGD. DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD. DR GO; GO:0071346; P:cellular response to type II interferon; ISO:RGD. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD. DR GO; GO:0032497; P:detection of lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:RGD. DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:RGD. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD. DR GO; GO:0010467; P:gene expression; ISO:RGD. DR GO; GO:0016064; P:immunoglobulin mediated immune response; IEP:RGD. DR GO; GO:0006954; P:inflammatory response; ISO:RGD. DR GO; GO:0002758; P:innate immune response-activating signaling pathway; IMP:RGD. DR GO; GO:0060729; P:intestinal epithelial structure maintenance; ISO:RGD. DR GO; GO:0007254; P:JNK cascade; ISO:RGD. DR GO; GO:0006691; P:leukotriene metabolic process; IDA:RGD. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD. DR GO; GO:0046651; P:lymphocyte proliferation; ISO:RGD. DR GO; GO:0042116; P:macrophage activation; ISO:RGD. DR GO; GO:0045342; P:MHC class II biosynthetic process; ISO:RGD. DR GO; GO:0014004; P:microglia differentiation; ISO:RGD. DR GO; GO:0001774; P:microglial cell activation; IDA:RGD. DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; ISO:RGD. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD. DR GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:RGD. DR GO; GO:0032707; P:negative regulation of interleukin-23 production; ISO:RGD. DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD. DR GO; GO:0032689; P:negative regulation of type II interferon production; ISO:RGD. DR GO; GO:0022008; P:neurogenesis; ISO:RGD. DR GO; GO:0006809; P:nitric oxide biosynthetic process; ISO:RGD. DR GO; GO:0002537; P:nitric oxide production involved in inflammatory response; ISO:RGD. DR GO; GO:0070427; P:nucleotide-binding oligomerization domain containing 1 signaling pathway; ISO:RGD. DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:RGD. DR GO; GO:0006909; P:phagocytosis; ISO:RGD. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD. DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:RGD. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:1903974; P:positive regulation of cellular response to macrophage colony-stimulating factor stimulus; ISO:RGD. DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISO:RGD. DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD. DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISO:RGD. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD. DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD. DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD. DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:RGD. DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:RGD. DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB. DR GO; GO:0032732; P:positive regulation of interleukin-1 production; ISO:RGD. DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD. DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:RGD. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD. DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD. DR GO; GO:0050671; P:positive regulation of lymphocyte proliferation; ISO:RGD. DR GO; GO:0043032; P:positive regulation of macrophage activation; ISO:RGD. DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISO:RGD. DR GO; GO:1904466; P:positive regulation of matrix metallopeptidase secretion; ISO:RGD. DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; ISO:RGD. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD. DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:RGD. DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:0070430; P:positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; ISO:RGD. DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:RGD. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD. DR GO; GO:0010572; P:positive regulation of platelet activation; ISO:RGD. DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:RGD. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:RGD. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD. DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD. DR GO; GO:0032729; P:positive regulation of type II interferon production; ISO:RGD. DR GO; GO:0002730; P:regulation of dendritic cell cytokine production; ISO:RGD. DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD. DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IMP:RGD. DR GO; GO:0014823; P:response to activity; IEP:RGD. DR GO; GO:0009617; P:response to bacterium; ISO:RGD. DR GO; GO:0045471; P:response to ethanol; IMP:RGD. DR GO; GO:0070542; P:response to fatty acid; IDA:RGD. DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD. DR GO; GO:1990268; P:response to gold nanoparticle; IEP:RGD. DR GO; GO:0001666; P:response to hypoxia; IEP:RGD. DR GO; GO:0032868; P:response to insulin; IEP:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:RGD. DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD. DR GO; GO:0032570; P:response to progesterone; IEP:RGD. DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD. DR GO; GO:0009636; P:response to toxic substance; IEP:RGD. DR GO; GO:0003009; P:skeletal muscle contraction; IEP:RGD. DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:RGD. DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:RGD. DR GO; GO:0002224; P:toll-like receptor signaling pathway; IDA:RGD. DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; ISO:RGD. DR GO; GO:0002246; P:wound healing involved in inflammatory response; ISO:RGD. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1. 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; IPR017241; Toll-like_receptor. DR InterPro; IPR035897; Toll_tir_struct_dom_sf. DR PANTHER; PTHR24365; TOLL-LIKE RECEPTOR; 1. DR PANTHER; PTHR24365:SF521; TOLL-LIKE RECEPTOR 4; 1. DR Pfam; PF13855; LRR_8; 3. DR Pfam; PF01582; TIR; 1. DR PIRSF; PIRSF037595; Toll-like_receptor; 1. DR SMART; SM00369; LRR_TYP; 9. DR SMART; SM00255; TIR; 1. DR SUPFAM; SSF52058; L domain-like; 3. DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1. DR PROSITE; PS51450; LRR; 13. DR PROSITE; PS50104; TIR; 1. PE 2: Evidence at transcript level; KW Cell membrane; Cell projection; Disulfide bond; Endosome; Glycoprotein; KW Immunity; Inflammatory response; Innate immunity; Leucine-rich repeat; KW Membrane; NAD; Receptor; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..835 FT /note="Toll-like receptor 4" FT /id="PRO_0000034728" FT TOPO_DOM 26..638 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 639..659 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 660..835 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 54..75 FT /note="LRR 1" FT REPEAT 78..99 FT /note="LRR 2" FT REPEAT 102..123 FT /note="LRR 3" FT REPEAT 126..147 FT /note="LRR 4" FT REPEAT 150..171 FT /note="LRR 5" FT REPEAT 175..198 FT /note="LRR 6" FT REPEAT 204..224 FT /note="LRR 7" FT REPEAT 226..247 FT /note="LRR 8" FT REPEAT 372..381 FT /note="LRR 9" FT REPEAT 398..420 FT /note="LRR 10" FT REPEAT 421..442 FT /note="LRR 11" FT REPEAT 446..467 FT /note="LRR 12" FT REPEAT 470..491 FT /note="LRR 13" FT REPEAT 495..516 FT /note="LRR 14" FT REPEAT 519..540 FT /note="LRR 15" FT REPEAT 543..564 FT /note="LRR 16" FT DOMAIN 576..627 FT /note="LRRCT" FT DOMAIN 670..813 FT /note="TIR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 43 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 75 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 172 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 204 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 237 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 248 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 281 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 307 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 492 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 495 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 524 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 572 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 575 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 622 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 28..39 FT /evidence="ECO:0000250|UniProtKB:O00206" FT DISULFID 280..304 FT /evidence="ECO:0000250|UniProtKB:O00206" FT DISULFID 388..389 FT /evidence="ECO:0000250|UniProtKB:O00206" FT DISULFID 580..606 FT /evidence="ECO:0000250|UniProtKB:O00206" FT DISULFID 582..625 FT /evidence="ECO:0000250|UniProtKB:O00206" SQ SEQUENCE 835 AA; 96072 MW; DF5E16A30851E3A0 CRC64; MMPLLHLAGT LIMALFLSCL RPGSLNPCIE VLPNITYQCM DQNLSKIPHD IPYSTKNLDL SFNPLKILRS YSFTNFSQLQ WLDLSRCEIE TIEDKAWHGL NQLSTLVLTG NPIKSFSPGS FSGLTNLENL VAVETKMTSL EGFHIGQLIS LKKLNVAHNL IHSFKLPEYF SNLTNLEHVD LSYNYIQTIS VKDLQFLREN PQVNLSLDLS LNPIDSIQAQ AFQGIRLHEL TLRSNFNSSN VLKMCLQNMT GLHVHRLILG EFKNERNLES FDRSVMEGLC NVSIDEFRLT YINHFSDDIY NLNCLANISA MSFTGVHIKH IADVPRHFKW QSLSIIRCHL KPFPKLSLPF LKSWTLTTNR EDISFGQLAL PSLRYLDLSR NAMSFRGCCS YSDFGTNNLK YLDLSFNGVI LMSANFMGLE ELEYLDFQHS TLKKVTEFSV FLSLEKLLYL DISYTNTKID FDGIFLGLIS LNTLKMAGNS FKDNTLSNVF TNTTNLTFLD LSKCQLEQIS RGVFDTLYRL QLLNMSHNNL LFLDPSHYKQ LYSLRTLDCS FNRIETSKGI LQHFPKSLAV FNLTNNSVAC ICEYQNFLQW VKDQKMFLVN VEQMKCASPI DMKASLVLDF TNSTCYIYKT IISVSVVSVL VVATVAFLIY HFYFHLILIA GCKKYSRGES IYDAFVIYSS QNEDWVRNEL VKNLEEGVPR FQLCLHYRDF IPGVAIAANI IQEGFHKSRK VIVVVSRHFI QSRWCIFEYE IAQTWQFLSS RSGIIFIVLE KVEKSLLRQQ VELYRLLSRN TYLEWEDNAL GRHIFWRRLK KALLDGKALN PDETSEEEQE ATTLT //