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Protein

Lipopolysaccharide-binding protein

Gene

Lbp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:9144073). Acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarity). Promotes the release of cytokines in response to bacterial lipopolysaccharide (PubMed:24380872).By similarity2 Publications

GO - Molecular functioni

  • lipopolysaccharide binding Source: MGI
  • lipoteichoic acid binding Source: MGI
  • receptor binding Source: BHF-UCL

GO - Biological processi

  • acute-phase response Source: BHF-UCL
  • cellular response to lipopolysaccharide Source: UniProtKB
  • cellular response to lipoteichoic acid Source: MGI
  • defense response to Gram-negative bacterium Source: BHF-UCL
  • defense response to Gram-positive bacterium Source: BHF-UCL
  • detection of molecule of bacterial origin Source: MGI
  • innate immune response Source: BHF-UCL
  • leukocyte chemotaxis involved in inflammatory response Source: MGI
  • lipopolysaccharide-mediated signaling pathway Source: MGI
  • lipopolysaccharide transport Source: MGI
  • macrophage activation involved in immune response Source: BHF-UCL
  • negative regulation of growth of symbiont in host Source: MGI
  • negative regulation of tumor necrosis factor production Source: MGI
  • opsonization Source: BHF-UCL
  • positive regulation of chemokine production Source: MGI
  • positive regulation of interleukin-6 production Source: MGI
  • positive regulation of interleukin-8 production Source: MGI
  • positive regulation of macrophage activation Source: MGI
  • positive regulation of neutrophil chemotaxis Source: MGI
  • positive regulation of respiratory burst involved in inflammatory response Source: BHF-UCL
  • positive regulation of toll-like receptor 4 signaling pathway Source: MGI
  • positive regulation of tumor necrosis factor biosynthetic process Source: MGI
  • positive regulation of tumor necrosis factor production Source: UniProtKB
  • response to lipopolysaccharide Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Immunity, Innate immunity, Lipid transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-166020. Transfer of LPS from LBP carrier to CD14.
R-MMU-5686938. Regulation of TLR by endogenous ligand.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipopolysaccharide-binding protein
Short name:
LBP
Gene namesi
Name:Lbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1098776. Lbp.

Subcellular locationi

  • Secreted By similarity
  • Cytoplasmic granule membrane By similarity

  • Note: Membrane-associated in polymorphonuclear Leukocytes (PMN) granules.By similarity

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • extracellular exosome Source: MGI
  • extracellular space Source: BHF-UCL
  • membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001715925 – 481Lipopolysaccharide-binding proteinAdd BLAST457

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi159 ↔ 198Combined sources1 Publication
Glycosylationi300N-linked (GlcNAc...)Sequence analysis1
Glycosylationi355N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61805.
PaxDbiQ61805.
PeptideAtlasiQ61805.
PRIDEiQ61805.

PTM databases

iPTMnetiQ61805.
PhosphoSitePlusiQ61805.

Expressioni

Gene expression databases

BgeeiENSMUSG00000016024.
CleanExiMM_LBP.
ExpressionAtlasiQ61805. baseline and differential.
GenevisibleiQ61805. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000016168.

Structurei

Secondary structure

1481
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 35Combined sources7
Helixi36 – 54Combined sources19
Beta strandi62 – 68Combined sources7
Turni69 – 71Combined sources3
Beta strandi72 – 87Combined sources16
Beta strandi91 – 96Combined sources6
Turni97 – 99Combined sources3
Beta strandi100 – 119Combined sources20
Beta strandi127 – 146Combined sources20
Beta strandi152 – 162Combined sources11
Beta strandi166 – 170Combined sources5
Helixi175 – 184Combined sources10
Helixi186 – 207Combined sources22
Helixi209 – 213Combined sources5
Beta strandi218 – 221Combined sources4
Beta strandi223 – 225Combined sources3
Beta strandi227 – 229Combined sources3
Beta strandi232 – 235Combined sources4
Beta strandi240 – 247Combined sources8
Beta strandi254 – 256Combined sources3
Beta strandi274 – 281Combined sources8
Beta strandi285 – 287Combined sources3
Beta strandi300 – 304Combined sources5
Helixi305 – 307Combined sources3
Beta strandi310 – 312Combined sources3
Turni318 – 320Combined sources3
Turni322 – 324Combined sources3
Helixi328 – 331Combined sources4
Beta strandi336 – 345Combined sources10
Beta strandi350 – 352Combined sources3
Beta strandi355 – 358Combined sources4
Beta strandi361 – 369Combined sources9
Beta strandi373 – 394Combined sources22
Beta strandi397 – 417Combined sources21
Helixi421 – 434Combined sources14
Helixi436 – 446Combined sources11
Beta strandi456 – 465Combined sources10
Beta strandi467 – 478Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M4DX-ray2.91A/B25-481[»]
ProteinModelPortaliQ61805.
SMRiQ61805.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4160. Eukaryota.
ENOG410Z88E. LUCA.
GeneTreeiENSGT00730000110583.
HOGENOMiHOG000231250.
HOVERGENiHBG002797.
InParanoidiQ61805.
KOiK05399.
OMAiRVQGRWK.
OrthoDBiEOG091G08NV.
TreeFamiTF315617.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR030675. BPI/LBP.
IPR032942. BPI/LBP/Plunc.
IPR030180. LBP.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504. PTHR10504. 1 hit.
PTHR10504:SF66. PTHR10504:SF66. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002417. Lipid_binding_protein. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61805-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAGTGPLLS TLLGLLFLSI QGTGGVNPGV VARITDKGLA YAAKEGLVAL
60 70 80 90 100
QRELYKITLP DFSGDFKIKA VGRGQYEFHS LEIQNCELRG SSLKLLPGQG
110 120 130 140 150
LSLAISDSSI GVRGKWKVRK SFLKLHGSFD LDVKGVTISV DLLLGMDPSG
160 170 180 190 200
RPTVSASGCS SRICDLDVHI SGNVGWLLNL FHNQIESKLQ KVLENKVCEM
210 220 230 240 250
IQKSVTSDLQ PYLQTLPVTA EIDNVLGIDY SLVAAPQAKA QVLDVMFKGE
260 270 280 290 300
IFNRNHRSPV ATPTPTMSLP EDSKQMVYFA ISDYAFNIAS RVYHQAGYLN
310 320 330 340 350
FSITDDMLPH DSGIRLNTKA FRPFTPQIYK KYPDMKLELL GTVVSAPILN
360 370 380 390 400
VSPGNLSLAP QMEIEGFVIL PTSAREPVFR LGVVTNVFAS LTFNNSKVTG
410 420 430 440 450
MLHPDKAQVR LIESKVGMFN VNLFQAFLNY YLLNSLYPDV NAELAQGFPL
460 470 480
PLPRHIQLHD LDFQIRKDFL YLGANVQYMR V
Length:481
Mass (Da):53,055
Last modified:July 27, 2011 - v2
Checksum:iAC1D3FC2DA87FE9A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25G → C in CAA67727 (PubMed:9144073).Curated1
Sequence conflicti51Q → K in CAA67727 (PubMed:9144073).Curated1
Sequence conflicti102S → R in CAA67727 (PubMed:9144073).Curated1
Sequence conflicti280A → S in AAH04795 (Ref. 3) Curated1
Sequence conflicti284Y → H in CAA67727 (PubMed:9144073).Curated1
Sequence conflicti284Y → H in AAH04795 (Ref. 3) Curated1
Sequence conflicti310H → P in AAH04795 (Ref. 3) Curated1
Sequence conflicti313G → S in AAH04795 (Ref. 3) Curated1
Sequence conflicti341G → R in CAA67727 (PubMed:9144073).Curated1
Sequence conflicti382G → S in CAA67727 (PubMed:9144073).Curated1
Sequence conflicti395 – 396NS → TR in CAA67727 (PubMed:9144073).Curated2
Sequence conflicti418M → I in CAA67727 (PubMed:9144073).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99347 mRNA. Translation: CAA67727.1.
AL663063 Genomic DNA. Translation: CAM23528.1.
CH466551 Genomic DNA. Translation: EDL06262.1.
BC004795 mRNA. Translation: AAH04795.1.
CCDSiCCDS16988.1.
RefSeqiNP_032515.2. NM_008489.2.
UniGeneiMm.218846.

Genome annotation databases

EnsembliENSMUST00000016168; ENSMUSP00000016168; ENSMUSG00000016024.
GeneIDi16803.
KEGGimmu:16803.
UCSCiuc008npz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99347 mRNA. Translation: CAA67727.1.
AL663063 Genomic DNA. Translation: CAM23528.1.
CH466551 Genomic DNA. Translation: EDL06262.1.
BC004795 mRNA. Translation: AAH04795.1.
CCDSiCCDS16988.1.
RefSeqiNP_032515.2. NM_008489.2.
UniGeneiMm.218846.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M4DX-ray2.91A/B25-481[»]
ProteinModelPortaliQ61805.
SMRiQ61805.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000016168.

PTM databases

iPTMnetiQ61805.
PhosphoSitePlusiQ61805.

Proteomic databases

MaxQBiQ61805.
PaxDbiQ61805.
PeptideAtlasiQ61805.
PRIDEiQ61805.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016168; ENSMUSP00000016168; ENSMUSG00000016024.
GeneIDi16803.
KEGGimmu:16803.
UCSCiuc008npz.1. mouse.

Organism-specific databases

CTDi3929.
MGIiMGI:1098776. Lbp.

Phylogenomic databases

eggNOGiKOG4160. Eukaryota.
ENOG410Z88E. LUCA.
GeneTreeiENSGT00730000110583.
HOGENOMiHOG000231250.
HOVERGENiHBG002797.
InParanoidiQ61805.
KOiK05399.
OMAiRVQGRWK.
OrthoDBiEOG091G08NV.
TreeFamiTF315617.

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-166020. Transfer of LPS from LBP carrier to CD14.
R-MMU-5686938. Regulation of TLR by endogenous ligand.

Miscellaneous databases

ChiTaRSiLbp. mouse.
PROiQ61805.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000016024.
CleanExiMM_LBP.
ExpressionAtlasiQ61805. baseline and differential.
GenevisibleiQ61805. MM.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR030675. BPI/LBP.
IPR032942. BPI/LBP/Plunc.
IPR030180. LBP.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504. PTHR10504. 1 hit.
PTHR10504:SF66. PTHR10504:SF66. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002417. Lipid_binding_protein. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLBP_MOUSE
AccessioniPrimary (citable) accession number: Q61805
Secondary accession number(s): A2AC66, Q99KA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.