Summary: Ezrin/radixin/moesin, alpha-helical domain
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This is the Wikipedia entry entitled "ERM protein family". More...
ERM protein family Edit Wikipedia article
Ezrin/radixin/moesin family | |||||||||||
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Identifiers | |||||||||||
Symbol | ERM | ||||||||||
Pfam | PF00769 | ||||||||||
SCOP2 | 1ef1 / SCOPe / SUPFAM | ||||||||||
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The ERM protein family consists of three closely-related proteins, ezrin,[1] radixin[2] and moesin.[3][4]
Structure
ERM molecules contain the following three domains:[4]
- an N-terminal globular domain
- an extended alpha-helical domain
- charged C-terminal domain
Ezrin, radixin and merlin also contain a polyproline region between the central helical and C-terminal domains.
Function
ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament-plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains.[4][5]
References
- ^ Bretscher A (1983). "Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells". J. Cell Biol. 97 (2): 425–32. doi:10.1083/jcb.97.2.425. PMC 2112519. PMID 6885906.
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ignored (help) - ^ Tsukita S, Hieda Y, Tsukita S (1989). "A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization". J. Cell Biol. 108 (6): 2369–82. doi:10.1083/jcb.108.6.2369. PMC 2115614. PMID 2500445.
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ Lankes W, Griesmacher A, Grünwald J, Schwartz-Albiez R, Keller R (1988). "A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation". Biochem. J. 251 (3): 831–42. PMC 1149078. PMID 3046603.
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ a b c Tsukita S, Yonemura S, Tsukita S (1997). "ERM proteins: head-to-tail regulation of actin-plasma membrane interaction". Trends Biochem. Sci. 22 (2): 53–8. doi:10.1016/S0968-0004(96)10071-2. PMID 9048483.
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S (1998). "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2". J. Cell Biol. 140 (4): 885–95. doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040.
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ignored (help)CS1 maint: multiple names: authors list (link)
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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.
Ezrin/radixin/moesin, alpha-helical domain Provide feedback
The ERM family consists of three closely-related proteins, ezrin, radixin and moesin [1,2]. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein [4]. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein) [3]. ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (PF00769) [2]. Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localise with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains [2]. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins [5,6].
Literature references
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Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S; , J Cell Biol 1998;140:885-895.: Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. PUBMED:9472040 EPMC:9472040
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Tsukita S, Yonemura S, Tsukita S;, Trends Biochem Sci. 1997;22:53-58.: ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. PUBMED:9048483 EPMC:9048483
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Chen H, Mei L, Zhou L, Zhang X, Guo C, Li J, Wang H, Zhu Y, Zheng Y, Huang L;, Int J Biochem Cell Biol. 2011;43:545-555.: Moesin-ezrin-radixin-like protein (merlin) mediates protein interacting with the carboxyl terminus-1 (PICT-1)-induced growth inhibition of glioblastoma cells in the nucleus. PUBMED:21167305 EPMC:21167305
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Lagresle-Peyrou C, Luce S, Ouchani F, Soheili TS, Sadek H, Chouteau M, Durand A, Pic I, Majewski J, Brouzes C, Lambert N, Bohineust A, Verhoeyen E, Cosset FL, Magerus-Chatinet A, Rieux-Laucat F, Gandemer V, Monnier D, Heijmans C, van Gijn M, Dalm VA, Mahlaoui N, Stephan JL, Picard C, Durandy A, Kracker S, Hivroz C, Jabado N, de Saint Basile G, Fischer A, Cavazzana M, Andre-Schmutz I;, J Allergy Clin Immunol. 2016;138:1681-1689.: X-linked primary immunodeficiency associated with hemizygous mutations in the moesin (MSN) gene. PUBMED:27405666 EPMC:27405666
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Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ;, J Mol Biol. 2007;365:1446-1459.: Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain. PUBMED:17134719 EPMC:17134719
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Phang JM, Harrop SJ, Duff AP, Sokolova AV, Crossett B, Walsh JC, Beckham SA, Nguyen CD, Davies RB, Glockner C, Bromley EH, Wilk KE, Curmi PM;, Biochem J. 2016;473:2763-2782.: Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin. PUBMED:27364155 EPMC:27364155
Internal database links
External database links
HOMSTRAD: | Band_41_NME ERM |
PRINTS: | PR00661 |
SCOP: | 1ef1 |
This tab holds annotation information from the InterPro database.
No InterPro data for this Pfam family.
Domain organisation
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Alignments
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Seed (49) |
Full (3599) |
Representative proteomes | UniProt (5958) |
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RP15 (332) |
RP35 (898) |
RP55 (2620) |
RP75 (3632) |
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HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (49) |
Full (3599) |
Representative proteomes | UniProt (5958) |
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---|---|---|---|---|---|---|---|
RP15 (332) |
RP35 (898) |
RP55 (2620) |
RP75 (3632) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
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
This family is new in this Pfam release.
Seed source: | Pfam-B_851 (release 2.1) |
Previous IDs: | none |
Type: | Coiled-coil |
Sequence Ontology: | SO:0001080 |
Author: |
Bateman A |
Number in seed: | 49 |
Number in full: | 3599 |
Average length of the domain: | 118 aa |
Average identity of full alignment: | 41 % |
Average coverage of the sequence by the domain: | 20.45 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 120 | ||||||||||||
Family (HMM) version: | 1 | ||||||||||||
Download: | download the raw HMM for this family |
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 ERM_helical domain has been found. There are 4 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.