Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q61805 (LBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipopolysaccharide-binding protein

Short name=LBP
Gene names
Name:Lbp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria, and acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide By similarity. Ref.5

Subunit structure

When bound to LPS, interacts (via C-terminus) with soluble CD14 By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
Lipid transport
Transport
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from mutant phenotype PubMed 12932360. Source: BHF-UCL

cellular response to lipoteichoic acid

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-negative bacterium

Inferred from mutant phenotype PubMed 9338787. Source: BHF-UCL

defense response to Gram-positive bacterium

Inferred from mutant phenotype PubMed 12932360. Source: BHF-UCL

detection of molecule of bacterial origin

Inferred from electronic annotation. Source: Ensembl

innate immune response

Inferred from mutant phenotype PubMed 12932360. Source: BHF-UCL

leukocyte chemotaxis involved in inflammatory response

Inferred from mutant phenotype PubMed 12055258. Source: MGI

lipopolysaccharide transport

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

macrophage activation involved in immune response

Inferred from direct assay PubMed 12932360. Source: BHF-UCL

negative regulation of growth of symbiont in host

Inferred from mutant phenotype PubMed 12055258. Source: MGI

negative regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

opsonization

Inferred by curator. Source: BHF-UCL

positive regulation of chemokine production

Inferred from mutant phenotype PubMed 12055258. Source: MGI

positive regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-8 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage activation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neutrophil chemotaxis

Inferred from mutant phenotype PubMed 12055258. Source: MGI

positive regulation of respiratory burst involved in inflammatory response

Inferred from mutant phenotype PubMed 9338787. Source: BHF-UCL

positive regulation of toll-like receptor 4 signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor biosynthetic process

Inferred from mutant phenotype PubMed 12055258. Source: MGI

positive regulation of tumor necrosis factor production

Inferred from direct assay PubMed 12932360. Source: BHF-UCL

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 9338787. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay PubMed 12932360. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 9338787. Source: BHF-UCL

   Molecular_functionlipopolysaccharide binding

Inferred from direct assay PubMed 11079463. Source: MGI

lipoteichoic acid binding

Inferred from electronic annotation. Source: Ensembl

receptor binding

Inferred from direct assay PubMed 9338787. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 481457Lipopolysaccharide-binding protein
PRO_0000017159

Amino acid modifications

Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Disulfide bond159 ↔ 198 Ref.5

Experimental info

Sequence conflict251G → C in CAA67727. Ref.1
Sequence conflict511Q → K in CAA67727. Ref.1
Sequence conflict1021S → R in CAA67727. Ref.1
Sequence conflict2801A → S in AAH04795. Ref.3
Sequence conflict2841Y → H in CAA67727. Ref.1
Sequence conflict2841Y → H in AAH04795. Ref.3
Sequence conflict3101H → P in AAH04795. Ref.3
Sequence conflict3131G → S in AAH04795. Ref.3
Sequence conflict3411G → R in CAA67727. Ref.1
Sequence conflict3821G → S in CAA67727. Ref.1
Sequence conflict395 – 3962NS → TR in CAA67727. Ref.1
Sequence conflict4181M → I in CAA67727. Ref.1

Secondary structure

....................................................................... 481
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61805 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: AC1D3FC2DA87FE9A

FASTA48153,055
        10         20         30         40         50         60 
MKAGTGPLLS TLLGLLFLSI QGTGGVNPGV VARITDKGLA YAAKEGLVAL QRELYKITLP 

        70         80         90        100        110        120 
DFSGDFKIKA VGRGQYEFHS LEIQNCELRG SSLKLLPGQG LSLAISDSSI GVRGKWKVRK 

       130        140        150        160        170        180 
SFLKLHGSFD LDVKGVTISV DLLLGMDPSG RPTVSASGCS SRICDLDVHI SGNVGWLLNL 

       190        200        210        220        230        240 
FHNQIESKLQ KVLENKVCEM IQKSVTSDLQ PYLQTLPVTA EIDNVLGIDY SLVAAPQAKA 

       250        260        270        280        290        300 
QVLDVMFKGE IFNRNHRSPV ATPTPTMSLP EDSKQMVYFA ISDYAFNIAS RVYHQAGYLN 

       310        320        330        340        350        360 
FSITDDMLPH DSGIRLNTKA FRPFTPQIYK KYPDMKLELL GTVVSAPILN VSPGNLSLAP 

       370        380        390        400        410        420 
QMEIEGFVIL PTSAREPVFR LGVVTNVFAS LTFNNSKVTG MLHPDKAQVR LIESKVGMFN 

       430        440        450        460        470        480 
VNLFQAFLNY YLLNSLYPDV NAELAQGFPL PLPRHIQLHD LDFQIRKDFL YLGANVQYMR 


V 

« Hide

References

« Hide 'large scale' references
[1]"Reactivity of murine and human recombinant LPS-binding protein (LBP) within LPS and Gram-negative bacteria."
Lengacher S., Jongeneel C.V., le Roy D., Lee J.D., Kravchenko V., Ulevitch R.J., Glauser M.P., Heumann D.
J. Inflamm. 47:165-172(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The crystal structure of lipopolysaccharide binding protein reveals the location of a frequent mutation that impairs innate immunity."
Eckert J.K., Kim Y.J., Kim J.I., Guertler K., Oh D.Y., Sur S., Lundvall L., Hamann L., van der Ploeg A., Pickkers P., Giamarellos-Bourboulis E., Kubarenko A.V., Weber A.N., Kabesch M., Kumpf O., An H.J., Lee J.O., Schumann R.R.
Immunity 39:647-660(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS), FUNCTION, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99347 mRNA. Translation: CAA67727.1.
AL663063 Genomic DNA. Translation: CAM23528.1.
CH466551 Genomic DNA. Translation: EDL06262.1.
BC004795 mRNA. Translation: AAH04795.1.
CCDSCCDS16988.1.
RefSeqNP_032515.2. NM_008489.2.
UniGeneMm.218846.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4M4DX-ray2.91A/B25-481[»]
ProteinModelPortalQ61805.
SMRQ61805. Positions 26-480.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ61805.

Proteomic databases

MaxQBQ61805.
PaxDbQ61805.
PRIDEQ61805.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016168; ENSMUSP00000016168; ENSMUSG00000016024.
GeneID16803.
KEGGmmu:16803.
UCSCuc008npz.1. mouse.

Organism-specific databases

CTD3929.
MGIMGI:1098776. Lbp.

Phylogenomic databases

eggNOGNOG262970.
GeneTreeENSGT00730000110583.
HOGENOMHOG000231250.
HOVERGENHBG002797.
InParanoidA2AC66.
KOK05399.
OMARNHRSPV.
OrthoDBEOG76739B.
TreeFamTF315617.

Gene expression databases

ArrayExpressQ61805.
BgeeQ61805.
CleanExMM_LBP.
GenevestigatorQ61805.

Family and domain databases

InterProIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PfamPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
SMARTSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMSSF55394. SSF55394. 2 hits.
PROSITEPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLBP. mouse.
NextBio290688.
PROQ61805.
SOURCESearch...

Entry information

Entry nameLBP_MOUSE
AccessionPrimary (citable) accession number: Q61805
Secondary accession number(s): A2AC66, Q99KA0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot