The domain within your query sequence starts at position 331 and ends at position 470; the E-value for the LBP_BPI_CETP_C domain shown below is 1.6e-8.

LGPTQMLKIFTHSTPHIVLNEGSARAAQSVVLEVFPTNTDVRPFFSLGIEASYEAQFFTE
DNRLMLNFNNVSIERIKLMISDIKLFDPEVLKDTLTKILEYTLLPNENGKLRTGVPMSMS
KALGYEKAMWSVSKGALKLT

LBP_BPI_CETP_C

LBP_BPI_CETP_C
PFAM accession number:PF02886
Interpro abstract (IPR001124):

This entry represents the C-terminal domain found in several lipid-binding serum glycoproteins. The N- and C-terminal domains share a similar two-layer alpha/beta structure, but they show little sequence identity. Proteins containing this C-terminal domain include:

  • Bactericidal permeability-increasing protein (BPI)
  • Lipopolysaccharide-binding protein (LBP)
  • Cholesteryl ester transfer protein (CETP)
  • Phospholipid transfer protein (PLTP)
  • Palate, lung and nasal epithelium carcinoma-associated protein (PLUNC)

Bactericidal permeability-increasing protein (BPI) is a potent antimicrobial protein of 456 residues that binds to and neutralises lipopolysaccharides from the outer membrane of Gram-negative bacteria [(PUBMED:9188532)]. BPI contains two domains that adopt the same structural fold, even though they have little sequence similarity [(PUBMED:10843855)].

Lipopolysaccharide-binding protein (LBP) is an endotoxin-binding protein that is closely related to, and functions in a co-ordinated manner with BPI to facilitate an integrated host response to invading Gram-negative bacteria [(PUBMED:12887306)].

Cholesteryl ester transfer protein (CETP) is a glycoprotein that facilitates the transfer of lipids (cholesteryl esters and triglycerides) between the different lipoproteins that transport them through plasma, including HDL, LDL, VLDL and chylomicrons. These lipoproteins shield the lipids from water by encapsulating them within a coating of polar lipids and proteins [(PUBMED:17277799)].

Phospholipid transfer protein (PLTP) exchanges phospholipids between lipoproteins and remodels high-density lipoproteins (HDLs) [(PUBMED:12693940)].

Palate, lung and nasal epithelium carcinoma-associated protein (PLUNC) is a potential host defensive protein that is secreted from the submucosal gland to the saliva and nasal lavage fluid. PLUNC aapears to be a secreted product of neutrophil granules that participates in an aspect of the inflammatory response that contributes to host defence [(PUBMED:18245229)]. Short palate, lung and nasal epithelium clone 1 (SPLUNC1) may bind the lipopolysaccharide of Gram-negative nanobacteria, thereby playing an important role in the host defence of nasopharyngeal epithelium [(PUBMED:16364440)].

GO function:lipid binding (GO:0008289)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry LBP_BPI_CETP_C