Summary: Exo70 exocyst complex subunit
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EXOC7 Edit Wikipedia article
|, 2-5-3p, EX070, EXO70, EXOC1, Exo70p, YJL085W, exocyst complex component 7, BLOM4|
|Exo70 exocyst complex subunit|
crystal structure of the s. cerevisiae exocyst component exo70p
It forms one subunit of the exocyst complex. First discovered in Saccharomyces cerevisiae, this and other exocyst proteins have been observed in several other eukaryotes, including humans. In S. cerevisiae, the exocyst complex is involved in the late stages of exocytosis, and is localised at the tip of the bud, the major site of exocytosis in yeast. It interacts with the Rho3 GTPase. This interaction mediates one of the three known functions of Rho3 in cell polarity: vesicle docking and fusion with the plasma membrane (the other two functions are regulation of actin polarity and transport of exocytic vesicles from the mother cell to the bud). In humans, the functions of this protein and the exocyst complex are less well characterised: this protein is expressed in several tissues and is thought to also be involved in exocytosis.
- GRCh38: Ensembl release 89: ENSG00000182473 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000020792 - Ensembl, May 2017
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- Robinson NG, Guo L, Imai J, Toh-E A, Matsui Y, Tamanoi F (May 1999). "Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70". Mol. Cell. Biol. 19 (5): 3580–7. PMC . PMID 10207081.
- Adamo JE, Rossi G, Brennwald P (December 1999). "The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity". Mol. Biol. Cell. 10 (12): 4121–33. PMC . PMID 10588647. doi:10.1091/mbc.10.12.4121.
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- Kee Y, Yoo JS, Hazuka CD, Peterson KE, Hsu SC, Scheller RH (1998). "Subunit structure of the mammalian exocyst complex". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14438–14443. PMC . PMID 9405631. doi:10.1073/pnas.94.26.14438.
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Exo70 exocyst complex subunit Provide feedback
The Exo70 protein forms one subunit of the exocyst complex. First discovered in S. cerevisiae  Exo70 and other exocyst proteins have been observed in several other eukaryotes, including humans. In S. cerevisiae, the exocyst complex is involved in the late stages of exocytosis, and is localised at the tip of the bud, the major site of exocytosis in yeast . Exo70 interacts with the Rho3 GTPase . This interaction mediates one of the three known functions of Rho3 in cell polarity: vesicle docking and fusion with the plasma membrane (the other two functions are regulation of actin polarity and transport of exocytic vesicles from the mother cell to the bud) . In humans, the functions of Exo70 and the exocyst complex are less well characterised: Exo70 is expressed in several tissues and is thought to also be involved in exocytosis .
Robinson NG, Guo L, Imai J, Toh-E A, Matsui Y, Tamanoi F; , Mol Cell Biol 1999;19:3580-3587.: Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. PUBMED:10207081 EPMC:10207081
This tab holds annotation information from the InterPro database.
InterPro entry IPR004140The Exo70 protein forms one subunit of the exocyst complex (consist of (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70, and Exo84 in budding yeast). First discovered in Saccharomyces cerevisiae [PUBMED:8978675], Exo70 and other exocyst proteins have been observed in several other eukaryotes, including humans. In S. cerevisiae, the exocyst complex is involved in the late stages of exocytosis, and is localized at the tip of the bud, the major site of exocytosis in yeast [PUBMED:8978675]. Exo70 interacts with the Rho3 GTPase [PUBMED:10207081]. This interaction mediates one of the three known functions of Rho3 in cell polarity: vesicle docking and fusion with the plasma membrane (the other two functions are regulation of actin polarity and transport of exocytic vesicles from the mother cell to the bud) [PUBMED:10588647]. In humans, the functions of Exo70 and the exocyst complex are less well characterised: Exo70 is expressed in several tissues and is thought to also be involved in exocytosis [PUBMED:9405631].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||exocyst (GO:0000145)|
|Biological process||exocytosis (GO:0006887)|
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This clan includes an N-terminal domain from several vesicle transport proteins that are related to Vps51.
The clan contains the following 18 members:COG2 COG5 COG6 Dor1 Dsl1_N Exo70 Exo84_C Sec15 Sec3_C Sec3_C_2 Sec5 Sec6 Sec8_exocyst Vps51 Vps52 Vps53_N Vps54_N Zw10
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|Seed source:||Pfam-B_2462 (release 6.4)|
|Number in seed:||271|
|Number in full:||3612|
|Average length of the domain:||324.40 aa|
|Average identity of full alignment:||23 %|
|Average coverage of the sequence by the domain:||56.65 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
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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 Exo70 domain has been found. There are 10 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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