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56  structures 4462  species 4  interactions 9055  sequences 100  architectures

Family: PBP (PF01161)

Summary: Phosphatidylethanolamine-binding protein

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Phosphatidylethanolamine-binding protein Provide feedback

No Pfam abstract.

Literature references

  1. Banfield MJ, Barker JJ, Perry AC, Brady RL; , Structure 1998;6:1245-1254.: Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. PUBMED:9782050 EPMC:9782050

  2. Serre L, Vallee B, Bureaud N, Schoentgen F, Zelwer C; , Structure 1998;6:1255-1265.: Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins. PUBMED:9782057 EPMC:9782057


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008914

The PEBP (PhosphatidylEthanolamine-Binding Protein) family is a highly conserved group of proteins that have been identified in numerous tissues in a wide variety of organisms, including bacteria, yeast, nematodes, plants, drosophila and mammals. The various functions described for members of this family include lipid binding, neuronal development [PUBMED:12492898], serine protease inhibition [PUBMED:11034991], the control of the morphological switch between shoot growth and flower structures [PUBMED:10764580], and the regulation of several signalling pathways such as the MAP kinase pathway [PUBMED:12551925], and the NF-kappaB pathway [PUBMED:11585904]. The control of the latter two pathways involves the PEBP protein RKIP, which interacts with MEK and Raf-1 to inhibit the MAP kinase pathway, and with TAK1, NIK, IKKalpha and IKKbeta to inhibit the NF-kappaB pathway. Other PEBP-like proteins that show strong structural homology to PEBP include Escherichia coli YBHB and YBCL, the Rattus norvegicus (Rat) neuropeptide HCNP, and Antirrhinum majus (Garden snapdragon) protein centroradialis (CEN).

Structures have been determined for several members of the PEBP-like family, all of which show extensive fold conservation. The structure consists of a large central beta-sheet flanked by a smaller beta-sheet on one side, and an alpha helix on the other. Sequence alignments show two conserved central regions, CR1 and CR2, that form a consensus signature for the PEBP family. These two regions form part of the ligand-binding site, which can accommodate various anionic groups. The N- and C-terminal regions are the least conserved, and may be involved in interactions with different protein partners. The N-terminal residues 2-12 form the natural cleavage peptide HCNP involved in neuronal development. The C-terminal region is deleted in plant and bacterial PEBP homologues, and may help control accessibility to the active site.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(311)
Full
(9055)
Representative proteomes UniProt
(20526)
NCBI
(26501)
Meta
(240)
RP15
(2098)
RP35
(5336)
RP55
(8261)
RP75
(11423)
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PP/heatmap 1                

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(311)
Full
(9055)
Representative proteomes UniProt
(20526)
NCBI
(26501)
Meta
(240)
RP15
(2098)
RP35
(5336)
RP55
(8261)
RP75
(11423)
Alignment: