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7  structures 263  species 0  interactions 882  sequences 11  architectures

Family: Exo70 (PF03081)

Summary: Exo70 exocyst complex subunit

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This is the Wikipedia entry entitled "EXOC7". More...

EXOC7 Edit Wikipedia article

Exocyst complex component 7

PDB rendering based on 2pft.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols EXOC7; 2-5-3p; EX070; EXO70; EXOC1; Exo70p; YJL085W
External IDs OMIM608163 MGI1859270 HomoloGene41019 GeneCards: EXOC7 Gene
RNA expression pattern
PBB GE EXOC7 212026 s at tn.png
PBB GE EXOC7 212034 s at tn.png
PBB GE EXOC7 212035 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 23265 53413
Ensembl ENSG00000182473 ENSMUSG00000020792
UniProt Q9UPT5 O35250
RefSeq (mRNA) NM_001013839 NM_001162872
RefSeq (protein) NP_001013861 NP_001156344
Location (UCSC) Chr 17:
74.08 – 74.12 Mb
Chr 11:
116.29 – 116.31 Mb
PubMed search [1] [2]
Exo70 exocyst complex subunit
PDB 2b7m EBI.jpg
crystal structure of the s. cerevisiae exocyst component exo70p
Identifiers
Symbol Exo70
Pfam PF03081
Pfam clan CL0295
InterPro IPR004140

Exocyst complex component 7 is a protein that in humans is encoded by the EXOC7 gene.[1][2] It was formerly known as Exo70.

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.[3] 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.[3] It interacts with the Rho3 GTPase.[4] 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).[5] 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.[6]


Interactions[edit]

EXOC7 has been shown to interact with EXOC4[7][8] and RHOQ.[8]

References[edit]

  1. ^ Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA (Dec 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc Natl Acad Sci U S A 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
  2. ^ "Entrez Gene: EXOC7 exocyst complex component 7". 
  3. ^ a b TerBush DR, Maurice T, Roth D, Novick P (December 1996). "The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae". EMBO J. 15 (23): 6483–94. PMC 452473. PMID 8978675. 
  4. ^ 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 84150. PMID 10207081. 
  5. ^ 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 25747. PMID 10588647. 
  6. ^ Kee Y, Yoo JS, Hazuka CD, Peterson KE, Hsu SC, Scheller RH (December 1997). "Subunit structure of the mammalian exocyst complex". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14438–43. doi:10.1073/pnas.94.26.14438. PMC 25013. PMID 9405631. 
  7. ^ Sans, Nathalie; Prybylowski Kate, Petralia Ronald S, Chang Kai, Wang Ya-Xian, Racca Claudia, Vicini Stefano, Wenthold Robert J (Jun 2003). "NMDA receptor trafficking through an interaction between PDZ proteins and the exocyst complex". Nat. Cell Biol. (England) 5 (6): 520–530. doi:10.1038/ncb990. ISSN 1465-7392. PMID 12738960. 
  8. ^ a b Inoue, Mayumi; Chang Louise, Hwang Joseph, Chiang Shian-Huey, Saltiel Alan R (Apr 2003). "The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin". Nature (England) 422 (6932): 629–633. doi:10.1038/nature01533. ISSN 0028-0836. PMID 12687004. 

Further reading[edit]


This article incorporates text from the public domain Pfam and InterPro IPR004140


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Exo70 exocyst complex subunit Provide feedback

The Exo70 protein forms one subunit of the exocyst complex. First discovered in S. cerevisiae [1] 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 [1]. Exo70 interacts with the Rho3 GTPase [4]. 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) [3]. 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 [2].

Literature references

  1. TerBush DR, Maurice T, Roth D, Novick P; , EMBO J 1996;15:6483-6494.: The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. PUBMED:8978675 EPMC:8978675

  2. Kee Y, Yoo JS, Hazuka CD, Peterson KE, Hsu SC, Scheller RH; , Proc Natl Acad Sci U S A 1997;94:14438-14443.: Subunit structure of the mammalian exocyst complex. PUBMED:9405631 EPMC:9405631

  3. Adamo JE, Rossi G, Brennwald P; , Mol Biol Cell 1999;10:4121-4133.: The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity. PUBMED:10588647 EPMC:10588647

  4. 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

  5. Hamburger ZA, Hamburger AE, West AP Jr, Weis WI; , J Mol Biol. 2005; [Epub ahead of print]: Crystal Structure of the S.cerevisiae Exocyst Component Exo70p. PUBMED:16359701 EPMC:16359701


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004140

The Exo70 protein forms one subunit of the exocyst complex. 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].

Gene Ontology

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Domain organisation

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

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Pfam Clan

This family is a member of clan Vps51 (CL0295), which has the following description:

This clan includes an N-terminal domain from several vesicle transport proteins that are related to Vps51.

The clan contains the following 16 members:

COG2 COG5 COG6 Dor1 DUF2450 Exo70 Sec15 Sec3_C Sec3_C_2 Sec5 Sec6 Sec8_exocyst Vps51 Vps52 Vps53_N Zw10

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Full
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Representative proteomes NCBI
(852)
Meta
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RP15
(109)
RP35
(289)
RP55
(425)
RP75
(540)
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  Seed
(58)
Full
(882)
Representative proteomes NCBI
(852)
Meta
(0)
RP15
(109)
RP35
(289)
RP55
(425)
RP75
(540)
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External links

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_2462 (release 6.4)
Previous IDs: none
Type: Family
Author: Mifsud W
Number in seed: 58
Number in full: 882
Average length of the domain: 323.30 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 57.29 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.7 23.7
Trusted cut-off 24.3 23.8
Noise cut-off 23.3 23.6
Model length: 371
Family (HMM) version: 10
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Species distribution

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Structures

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 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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