ID LBP_MOUSE Reviewed; 481 AA. AC Q61805; A2AC66; Q99KA0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 14-OCT-2015, entry version 120. DE RecName: Full=Lipopolysaccharide-binding protein; DE Short=LBP; DE Flags: Precursor; GN Name=Lbp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC STRAIN=BALB/c; RX PubMed=9144073; RA Lengacher S., Jongeneel C.V., le Roy D., Lee J.D., Kravchenko V., RA Ulevitch R.J., Glauser M.P., Heumann D.; RT "Reactivity of murine and human recombinant LPS-binding protein (LBP) RT within LPS and Gram-negative bacteria."; RL J. Inflamm. 47:165-172(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION. RX PubMed=24380872; DOI=10.1093/intimm/dxt071; RA Tanimura N., Saitoh S., Ohto U., Akashi-Takamura S., Fujimoto Y., RA Fukase K., Shimizu T., Miyake K.; RT "The attenuated inflammation of MPL is due to the lack of CD14- RT dependent tight dimerization of the TLR4/MD2 complex at the plasma RT membrane."; RL Int. Immunol. 26:307-314(2014). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS), AND DISULFIDE BOND. RX PubMed=24120359; DOI=10.1016/j.immuni.2013.09.005; RA Eckert J.K., Kim Y.J., Kim J.I., Guertler K., Oh D.Y., Sur S., RA Lundvall L., Hamann L., van der Ploeg A., Pickkers P., RA Giamarellos-Bourboulis E., Kubarenko A.V., Weber A.N., Kabesch M., RA Kumpf O., An H.J., Lee J.O., Schumann R.R.; RT "The crystal structure of lipopolysaccharide binding protein reveals RT the location of a frequent mutation that impairs innate immunity."; RL Immunity 39:647-660(2013). CC -!- FUNCTION: Plays a role in the innate immune response. Binds to the CC lipid A moiety of bacterial lipopolysaccharides (LPS), a CC glycolipid present in the outer membrane of all Gram-negative CC bacteria (PubMed:9144073). Acts as an affinity enhancer for CD14, CC facilitating its association with LPS (By similarity). Promotes CC the release of cytokines in response to bacterial CC lipopolysaccharide (PubMed:24380872). CC {ECO:0000250|UniProtKB:P18428, ECO:0000269|PubMed:24380872, CC ECO:0000269|PubMed:9144073}. CC -!- SUBUNIT: When bound to LPS, interacts (via C-terminus) with CC soluble and membrane-bound CD14. {ECO:0000250|UniProtKB:P18428}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P18428}. CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP CC family. {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; X99347; CAA67727.1; -; mRNA. DR EMBL; AL663063; CAM23528.1; -; Genomic_DNA. DR EMBL; CH466551; EDL06262.1; -; Genomic_DNA. DR EMBL; BC004795; AAH04795.1; -; mRNA. DR CCDS; CCDS16988.1; -. DR RefSeq; NP_032515.2; NM_008489.2. DR UniGene; Mm.218846; -. DR PDB; 4M4D; X-ray; 2.91 A; A/B=25-481. DR PDBsum; 4M4D; -. DR ProteinModelPortal; Q61805; -. DR SMR; Q61805; 26-480. DR STRING; 10090.ENSMUSP00000016168; -. DR PhosphoSite; Q61805; -. DR MaxQB; Q61805; -. DR PaxDb; Q61805; -. DR PRIDE; Q61805; -. DR Ensembl; ENSMUST00000016168; ENSMUSP00000016168; ENSMUSG00000016024. DR GeneID; 16803; -. DR KEGG; mmu:16803; -. DR UCSC; uc008npz.1; mouse. DR CTD; 3929; -. DR MGI; MGI:1098776; Lbp. DR eggNOG; NOG262970; -. DR GeneTree; ENSGT00730000110583; -. DR HOGENOM; HOG000231250; -. DR HOVERGEN; HBG002797; -. DR InParanoid; Q61805; -. DR KO; K05399; -. DR OMA; RVQGRWK; -. DR OrthoDB; EOG76739B; -. DR TreeFam; TF315617; -. DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade. DR Reactome; R-MMU-166020; Transfer of LPS from LBP carrier to CD14. DR ChiTaRS; Lbp; mouse. DR NextBio; 290688; -. DR PRO; PR:Q61805; -. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; Q61805; -. DR CleanEx; MM_LBP; -. DR ExpressionAtlas; Q61805; baseline and differential. DR Genevisible; Q61805; MM. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI. DR GO; GO:0070891; F:lipoteichoic acid binding; ISO:MGI. DR GO; GO:0005102; F:receptor binding; IDA:BHF-UCL. DR GO; GO:0006953; P:acute-phase response; IMP:BHF-UCL. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB. DR GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:MGI. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:BHF-UCL. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:BHF-UCL. DR GO; GO:0032490; P:detection of molecule of bacterial origin; ISO:MGI. DR GO; GO:0045087; P:innate immune response; IMP:BHF-UCL. DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IMP:MGI. DR GO; GO:0015920; P:lipopolysaccharide transport; ISO:MGI. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:MGI. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0002281; P:macrophage activation involved in immune response; IDA:BHF-UCL. DR GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI. DR GO; GO:0008228; P:opsonization; IC:BHF-UCL. DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:MGI. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI. DR GO; GO:0043032; P:positive regulation of macrophage activation; ISO:MGI. DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:MGI. DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl. DR GO; GO:0060265; P:positive regulation of respiratory burst involved in inflammatory response; IMP:BHF-UCL. DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISO:MGI. DR GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IMP:MGI. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB. DR GO; GO:0090559; P:regulation of membrane permeability; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:BHF-UCL. DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom. DR InterPro; IPR030675; BPI/LBP. DR InterPro; IPR030180; LBP. DR InterPro; IPR001124; Lipid-bd_serum_glycop_C. DR InterPro; IPR017954; Lipid-bd_serum_glycop_CS. DR InterPro; IPR017942; Lipid-bd_serum_glycop_N. DR PANTHER; PTHR10504:SF43; PTHR10504:SF43; 1. DR Pfam; PF01273; LBP_BPI_CETP; 1. DR Pfam; PF02886; LBP_BPI_CETP_C; 1. DR PIRSF; PIRSF002417; Lipid_binding_protein; 1. DR SMART; SM00328; BPI1; 1. DR SMART; SM00329; BPI2; 1. DR SUPFAM; SSF55394; SSF55394; 2. DR PROSITE; PS00400; LBP_BPI_CETP; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Complete proteome; KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; KW Lipid transport; Reference proteome; Secreted; Signal; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 481 Lipopolysaccharide-binding protein. FT /FTId=PRO_0000017159. FT CARBOHYD 300 300 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 355 355 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 159 198 {ECO:0000244|PDB:4M4D, FT ECO:0000269|PubMed:24120359}. FT CONFLICT 25 25 G -> C (in Ref. 1; CAA67727). FT {ECO:0000305}. FT CONFLICT 51 51 Q -> K (in Ref. 1; CAA67727). FT {ECO:0000305}. FT CONFLICT 102 102 S -> R (in Ref. 1; CAA67727). FT {ECO:0000305}. FT CONFLICT 280 280 A -> S (in Ref. 3; AAH04795). FT {ECO:0000305}. FT CONFLICT 284 284 Y -> H (in Ref. 1; CAA67727 and 3; FT AAH04795). {ECO:0000305}. FT CONFLICT 310 310 H -> P (in Ref. 3; AAH04795). FT {ECO:0000305}. FT CONFLICT 313 313 G -> S (in Ref. 3; AAH04795). FT {ECO:0000305}. FT CONFLICT 341 341 G -> R (in Ref. 1; CAA67727). FT {ECO:0000305}. FT CONFLICT 382 382 G -> S (in Ref. 1; CAA67727). FT {ECO:0000305}. FT CONFLICT 395 396 NS -> TR (in Ref. 1; CAA67727). FT {ECO:0000305}. FT CONFLICT 418 418 M -> I (in Ref. 1; CAA67727). FT {ECO:0000305}. FT STRAND 29 35 {ECO:0000244|PDB:4M4D}. FT HELIX 36 54 {ECO:0000244|PDB:4M4D}. FT STRAND 62 68 {ECO:0000244|PDB:4M4D}. FT TURN 69 71 {ECO:0000244|PDB:4M4D}. FT STRAND 72 87 {ECO:0000244|PDB:4M4D}. FT STRAND 91 96 {ECO:0000244|PDB:4M4D}. FT TURN 97 99 {ECO:0000244|PDB:4M4D}. FT STRAND 100 119 {ECO:0000244|PDB:4M4D}. FT STRAND 127 146 {ECO:0000244|PDB:4M4D}. FT STRAND 152 162 {ECO:0000244|PDB:4M4D}. FT STRAND 166 170 {ECO:0000244|PDB:4M4D}. FT HELIX 175 184 {ECO:0000244|PDB:4M4D}. FT HELIX 186 207 {ECO:0000244|PDB:4M4D}. FT HELIX 209 213 {ECO:0000244|PDB:4M4D}. FT STRAND 218 221 {ECO:0000244|PDB:4M4D}. FT STRAND 223 225 {ECO:0000244|PDB:4M4D}. FT STRAND 227 229 {ECO:0000244|PDB:4M4D}. FT STRAND 232 235 {ECO:0000244|PDB:4M4D}. FT STRAND 240 247 {ECO:0000244|PDB:4M4D}. FT STRAND 254 256 {ECO:0000244|PDB:4M4D}. FT STRAND 274 281 {ECO:0000244|PDB:4M4D}. FT STRAND 285 287 {ECO:0000244|PDB:4M4D}. FT STRAND 300 304 {ECO:0000244|PDB:4M4D}. FT HELIX 305 307 {ECO:0000244|PDB:4M4D}. FT STRAND 310 312 {ECO:0000244|PDB:4M4D}. FT TURN 318 320 {ECO:0000244|PDB:4M4D}. FT TURN 322 324 {ECO:0000244|PDB:4M4D}. FT HELIX 328 331 {ECO:0000244|PDB:4M4D}. FT STRAND 336 345 {ECO:0000244|PDB:4M4D}. FT STRAND 350 352 {ECO:0000244|PDB:4M4D}. FT STRAND 355 358 {ECO:0000244|PDB:4M4D}. FT STRAND 361 369 {ECO:0000244|PDB:4M4D}. FT STRAND 373 394 {ECO:0000244|PDB:4M4D}. FT STRAND 397 417 {ECO:0000244|PDB:4M4D}. FT HELIX 421 434 {ECO:0000244|PDB:4M4D}. FT HELIX 436 446 {ECO:0000244|PDB:4M4D}. FT STRAND 456 465 {ECO:0000244|PDB:4M4D}. FT STRAND 467 478 {ECO:0000244|PDB:4M4D}. SQ SEQUENCE 481 AA; 53055 MW; AC1D3FC2DA87FE9A CRC64; MKAGTGPLLS TLLGLLFLSI QGTGGVNPGV VARITDKGLA YAAKEGLVAL QRELYKITLP DFSGDFKIKA VGRGQYEFHS LEIQNCELRG SSLKLLPGQG LSLAISDSSI GVRGKWKVRK SFLKLHGSFD LDVKGVTISV DLLLGMDPSG RPTVSASGCS SRICDLDVHI SGNVGWLLNL FHNQIESKLQ KVLENKVCEM IQKSVTSDLQ PYLQTLPVTA EIDNVLGIDY SLVAAPQAKA QVLDVMFKGE IFNRNHRSPV ATPTPTMSLP EDSKQMVYFA ISDYAFNIAS RVYHQAGYLN FSITDDMLPH DSGIRLNTKA FRPFTPQIYK KYPDMKLELL GTVVSAPILN VSPGNLSLAP QMEIEGFVIL PTSAREPVFR LGVVTNVFAS LTFNNSKVTG MLHPDKAQVR LIESKVGMFN VNLFQAFLNY YLLNSLYPDV NAELAQGFPL PLPRHIQLHD LDFQIRKDFL YLGANVQYMR V //