LBP_MOUSE
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 03-AUG-2022, entry version 158.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=BALB/cJ;
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT 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-dependent
RT tight dimerization of the TLR4/MD2 complex at the plasma 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., Lundvall L.,
RA Hamann L., van der Ploeg A., Pickkers P., Giamarellos-Bourboulis E.,
RA Kubarenko A.V., Weber A.N., Kabesch M., Kumpf O., An H.J., Lee J.O.,
RA Schumann R.R.;
RT "The crystal structure of lipopolysaccharide binding protein reveals the
RT 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 glycolipid
CC present in the outer membrane of all Gram-negative bacteria
CC (PubMed:9144073). Acts as an affinity enhancer for CD14, facilitating
CC its association with LPS (By similarity). Promotes the release of
CC cytokines in response to bacterial lipopolysaccharide
CC (PubMed:24380872). {ECO:0000250|UniProtKB:P18428,
CC ECO:0000269|PubMed:24380872, ECO:0000269|PubMed:9144073}.
CC -!- SUBUNIT: When bound to LPS, interacts (via C-terminus) with soluble and
CC membrane-bound CD14. {ECO:0000250|UniProtKB:P18428}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P18428}.
CC Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}.
CC Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
CC granules. {ECO:0000250|UniProtKB:P17213}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; X99347; CAA67727.1; -; mRNA.
DR EMBL; AL663063; -; NOT_ANNOTATED_CDS; 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 PDB; 4M4D; X-ray; 2.91 A; A/B=25-481.
DR PDBsum; 4M4D; -.
DR AlphaFoldDB; Q61805; -.
DR SMR; Q61805; -.
DR STRING; 10090.ENSMUSP00000016168; -.
DR GlyGen; Q61805; 2 sites.
DR iPTMnet; Q61805; -.
DR PhosphoSitePlus; Q61805; -.
DR CPTAC; non-CPTAC-3555; -.
DR CPTAC; non-CPTAC-3836; -.
DR MaxQB; Q61805; -.
DR PaxDb; Q61805; -.
DR PeptideAtlas; Q61805; -.
DR PRIDE; Q61805; -.
DR ProteomicsDB; 264845; -.
DR Antibodypedia; 777; 406 antibodies from 37 providers.
DR DNASU; 16803; -.
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 VEuPathDB; HostDB:ENSMUSG00000016024; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230353; -.
DR HOGENOM; CLU_028970_3_2_1; -.
DR InParanoid; Q61805; -.
DR OMA; NPYMEID; -.
DR OrthoDB; 1242894at2759; -.
DR PhylomeDB; Q61805; -.
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 Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR BioGRID-ORCS; 16803; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Lbp; mouse.
DR PRO; PR:Q61805; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61805; protein.
DR Bgee; ENSMUSG00000016024; Expressed in gastrula and 175 other tissues.
DR ExpressionAtlas; Q61805; baseline and differential.
DR Genevisible; Q61805; MM.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071723; F:lipopeptide binding; ISO:MGI.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
DR GO; GO:0070891; F:lipoteichoic acid binding; ISO:MGI.
DR GO; GO:0005102; F:signaling 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:0033036; P:macromolecule localization; ISO:MGI.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IDA:BHF-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP: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:0045919; P:positive regulation of cytolysis; ISO: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; ISO:MGI.
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:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0090559; P:regulation of membrane permeability; ISO:MGI.
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; IPR032942; BPI/LBP/Plunc.
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; PTHR10504; 1.
DR PANTHER; PTHR10504:SF66; PTHR10504:SF66; 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; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Lipid transport; Membrane; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..481
FT /note="Lipopolysaccharide-binding protein"
FT /id="PRO_0000017159"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 159..198
FT /evidence="ECO:0000269|PubMed:24120359,
FT ECO:0007744|PDB:4M4D"
FT CONFLICT 25
FT /note="G -> C (in Ref. 1; CAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="Q -> K (in Ref. 1; CAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> R (in Ref. 1; CAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="A -> S (in Ref. 3; AAH04795)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Y -> H (in Ref. 1; CAA67727 and 3; AAH04795)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="H -> P (in Ref. 3; AAH04795)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="G -> S (in Ref. 3; AAH04795)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="G -> R (in Ref. 1; CAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="G -> S (in Ref. 1; CAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..396
FT /note="NS -> TR (in Ref. 1; CAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="M -> I (in Ref. 1; CAA67727)"
FT /evidence="ECO:0000305"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4M4D"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:4M4D"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 72..87
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4M4D"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 100..119
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 127..146
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4M4D"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:4M4D"
FT HELIX 186..207
FT /evidence="ECO:0007829|PDB:4M4D"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:4M4D"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4M4D"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:4M4D"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:4M4D"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 336..345
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 373..394
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 397..417
FT /evidence="ECO:0007829|PDB:4M4D"
FT HELIX 421..434
FT /evidence="ECO:0007829|PDB:4M4D"
FT HELIX 436..446
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 456..465
FT /evidence="ECO:0007829|PDB:4M4D"
FT STRAND 467..478
FT /evidence="ECO:0007829|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
