Summary: Meiotic cell cortex C-terminal pleckstrin homology
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Meiotic cell cortex C-terminal pleckstrin homology Provide feedback
The PH domain of these largely fungal proteins is necessary for the cortical localisation of the protein during meiosis, since the overall function of the protein is to anchor dynein at the cell cortex during the horsetail phase. During prophase I of fission yeast, horsetail nuclear movement occurs, and this starts when all the telomeres become bundled at the spindle pole body - SPB. Subsequent to this, the nucleus undergoes a dynamic oscillation, resulting in elongated nuclear morphology. Horsetail nuclear movement is thought to be predominantly due to the pulling of astral microtubules that link the SPB to cortical microtubule-attachment sites at the opposite end of the cell; the pulling force is believed to be provided by cytoplasmic dynein and dynactin.
Saito TT, Okuzaki D, Nojima H;, J Cell Biol. 2006;173:27-33.mcp5 C terminal domain: Mcp5, a meiotic cell cortex protein, is required for nuclear movement mediated by dynein and microtubules in fission yeast. PUBMED:16585273 EPMC:16585273
Internal database links
|SCOOP:||PH_3 PH_4 PH_6 PH_8 PH_9 PH_11 PH_2|
|Similarity to PfamA using HHSearch:||PH|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR024774
This pleckstrin homology domain is found in eukaryotic proteins, including Mcp5, a fungal protein that anchors dynein at the cell cortex during the horsetail phase (prophase I) of meiosis. During prophase I of fission yeast all the telomeres become bundled at the spindle pole body and subsequently the nucleus undergoes a dynamic oscillation, resulting in elongated nuclear morphology known as "horsetail" nucleus. The pleckstrin homology domain is necessary for the cortical localisation of the Mcp5 protein during meiosis [PUBMED:16585273].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cell cortex (GO:0005938)|
|Molecular function||protein binding (GO:0005515)|
|phospholipid binding (GO:0005543)|
|Biological process||cortical protein anchoring (GO:0032065)|
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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 33 members:bPH_1 bPH_2 bPH_3 bPH_4 bPH_5 bPH_6 DCP1 DUF1448 FERM_C GRAM ICAP-1_inte_bdg Mcp5_PH PH PH_10 PH_11 PH_2 PH_3 PH_4 PH_5 PH_6 PH_7 PH_8 PH_9 PH_BEACH PID PID_2 PTB Ran_BP1 Rtt106 SSrecog Voldacs Vps36_ESCRT-II WH1
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Curation and family details
|Seed source:||Pfam-B_1220 (release 24.0)|
|Author:||Wood V, Coggill P|
|Number in seed:||26|
|Number in full:||320|
|Average length of the domain:||121.30 aa|
|Average identity of full alignment:||30 %|
|Average coverage of the sequence by the domain:||9.25 %|
|HMM build commands:||
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||2|
|Download:||download the raw HMM for this family|
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