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
This tab holds annotation information from the InterPro database.
InterPro entry IPR028258
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 targeting and tethering of post-Golgi secretory vesicles to fusion sites on the plasma membrane prior to SNARE-mediated fusion. 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 phosphatidylinositol 4,5-bisphosphate (PIP2) head group are conserved. 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 [PUBMED:22768263].
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Members of this clan share a PH-like fold. Many families in this clan bind to short peptide motifs in proteins and are involved in signalling.
The clan contains the following 56 members:BBL5 bPH_1 bPH_2 bPH_3 bPH_4 bPH_5 bPH_6 CARM1 DCP1 DUF1126 DUF1681 DUF3203 FERM_C Glycoprot_B_PH1 Glycoprot_B_PH2 GRAM hSac2 ICAP-1_inte_bdg INPP5B_PH IQ_SEC7_PH IRS Mcp5_PH Myosin_TH1 OCRL_clath_bd PH PH_10 PH_11 PH_12 PH_13 PH_2 PH_3 PH_4 PH_5 PH_6 PH_8 PH_9 PH_BEACH PH_TFIIH PID PID_2 POB3_N Proteasom_Rpn13 PTB Ran_BP1 Rtt106 Sec3-PIP2_bind Sharpin_PH SIN1_PH SPT16 SSrecog UCH_N Voldacs Vps36_ESCRT-II WH1 YcxB ZFYVE21_C
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Curation and family details
|Author:||Wood V, Coggill P|
|Number in seed:||125|
|Number in full:||856|
|Average length of the domain:||90.60 aa|
|Average identity of full alignment:||30 %|
|Average coverage of the sequence by the domain:||9.93 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 sequence.
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