LBP
Lipopolysaccharide-binding protein
Also known as: BPIFD2, LBP_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P18428
- Gene
- LBP
- Ensembl
- ENSG00000129988
- Chromosome
- 20
- Canonical length
- 481 aa
- Protein class
- Plasma proteins, Predicted secreted proteins, Transporters
- Secretome location
- Secreted to blood
OverviewNCBI Gene
The protein encoded by this gene is involved in the acute-phase immunologic response to gram-negative bacterial infections. Gram-negative bacteria contain a glycolipid, lipopolysaccharide (LPS), on their outer cell wall. Together with bactericidal permeability-increasing protein (BPI), the encoded protein binds LPS and interacts with the CD14 receptor, probably playing a role in regulating LPS-dependent monocyte responses. Studies in mice suggest that the encoded protein is necessary for the rapid acute-phase response to LPS but not for the clearance of LPS from circulation. This protein is part of a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). [provided by RefSeq, Apr 2012]
Canonical amino-acid sequenceUniProt
481 residues, UniProt reviewed canonical sequence.
>P18428|LBP
1 MGALARALPS ILLALLLTST PEALGANPGL VARITDKGLQ YAAQEGLLAL QSELLRITLP
61 DFTGDLRIPH VGRGRYEFHS LNIHSCELLH SALRPVPGQG LSLSISDSSI RVQGRWKVRK
121 SFFKLQGSFD VSVKGISISV NLLLGSESSG RPTVTASSCS SDIADVEVDM SGDLGWLLNL
181 FHNQIESKFQ KVLESRICEM IQKSVSSDLQ PYLQTLPVTT EIDSFADIDY SLVEAPRATA
241 QMLEVMFKGE IFHRNHRSPV TLLAAVMSLP EEHNKMVYFA ISDYVFNTAS LVYHEEGYLN
301 FSITDDMIPP DSNIRLTTKS FRPFVPRLAR LYPNMNLELQ GSVPSAPLLN FSPGNLSVDP
361 YMEIDAFVLL PSSSKEPVFR LSVATNVSAT LTFNTSKITG FLKPGKVKVE LKESKVGLFN
421 AELLEALLNY YILNTFYPKF NDKLAEGFPL PLLKRVQLYD LGLQIHKDFL FLGANVQYMR
481 VLocalizationUniProt · AlphaFold · HPA
Whether an antibody against LBP can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.28
- Highest tissue expression
- 1,321 nTPM
Expression across tissuesHPA
Tissue
- liver: 1,321 nTPM
- adipose tissue: 55 nTPM
- appendix: 23 nTPM
- skeletal muscle: 23 nTPM
- kidney: 9.1 nTPM
- breast: 6.4 nTPM
Single-cell type
- hepatocytes: 514 nCPM
- hepatic stellate cells: 26 nCPM
- adipocytes: 24 nCPM
- myonuclei: 18 nCPM
- fibroblasts: 10 nCPM
- kupffer cells: 5.1 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- medulla oblongata: 2.2 nTPM
- thalamus: 0.9 nTPM
- cerebral cortex: 0.5 nTPM
- white matter: 0.5 nTPM
- basal ganglia: 0.2 nTPM
- cerebellum: 0.2 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.33
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.15
- DepMap mean gene effect
- 0.06
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 2% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- acute-phase response
- cell surface pattern recognition receptor signaling pathway
- cellular defense response
- cellular response to lipopolysaccharide
- cellular response to lipoteichoic acid
- defense response to Gram-negative bacterium
- defense response to Gram-positive bacterium
- detection of molecule of bacterial origin
- innate immune response
- leukocyte chemotaxis involved in inflammatory response
- lipopolysaccharide transport
- lipopolysaccharide-mediated signaling pathway
- macrophage activation involved in immune response
- negative regulation of tumor necrosis factor production
- neutrophil chemotaxis
- opsonization
- positive regulation of chemokine production
- positive regulation of interleukin-6 production
- positive regulation of interleukin-8 production
- positive regulation of macrophage activation
- positive regulation of neutrophil chemotaxis
- positive regulation of respiratory burst involved in inflammatory response
- positive regulation of toll-like receptor 4 signaling pathway
- positive regulation of tumor necrosis factor production
- response to lipopolysaccharide
Molecular functions
- coreceptor activity
- lipopeptide binding
- lipopolysaccharide binding
- lipoteichoic acid binding
- signaling receptor binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Lipid-binding serum glycoprotein, C-terminal
- Lipid-binding serum glycoprotein, N-terminal
- Bactericidal permeability-increasing protein, alpha/beta domain superfamily
- Lipid-binding serum glycoprotein, conserved site
- Lipid binding protein BPI/LBP
- BPI/LBP/Plunc family
- LBP / BPI / CETP family, N-terminal domain
- LBP / BPI / CETP family, C-terminal domain
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads LBP as an antibody target. Whether an autoantibody or antibody against LBP could matter depends on whether native LBP is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
LBP is annotated as secreted, so native LBP circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label LBP as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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