Summary: Exocyst complex component SEC3 N-terminal PIP2 binding PH
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Exocyst complex component SEC3 N-terminal PIP2 binding PH Provide feedback
This is the N-terminal domain of fungal and eukaryotic Sec3 proteins. Sec3 is a component of the exocyst complex that is involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.This N-terminal domain contains a cryptic pleckstrin homology (PH) fold, and all six positively charged lysine and arginine residues in the PH domain predicted to bind the PIP2 head group are conserved. The exocyst complex is essential for many exocytic events, by tethering vesicles at the plasma membrane for fusion. In fission yeast, polarised exocytosis for growth relies on the combined action of the exocyst at cell poles and myosin-driven transport along actin cables .
Bendezu FO, Vincenzetti V, Martin SG;, PLoS One. 2012;7:e40248.: Fission yeast sec3 and exo70 are transported on actin cables and localize the exocyst complex to cell poles. PUBMED:22768263 EPMC:22768263
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This family is new in this Pfam release.
|Author:||Wood V, Coggill P|
|Number in seed:||101|
|Number in full:||335|
|Average length of the domain:||91.70 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||10.66 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||1|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Sec3-PIP2_bind domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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