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4  structures 487  species 0  interactions 3599  sequences 51  architectures

Family: ERM_helical (PF20492)

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
Identifiers
SymbolERM
PfamPF00769
SCOP21ef1 / SCOPe / SUPFAM

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]

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

  1. ^ 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. {{cite journal}}: Unknown parameter |month= ignored (help)
  2. ^ 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. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  3. ^ 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. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  4. ^ 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. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  5. ^ 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. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

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.

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

  1. 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

  2. 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

  3. 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

  4. 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

  5. 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

  6. 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

This tab holds annotation information from the InterPro database.

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Domain organisation

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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  Seed
(49)
Full
(3599)
Representative proteomes UniProt
(5958)
RP15
(332)
RP35
(898)
RP55
(2620)
RP75
(3632)
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Format an alignment

  Seed
(49)
Full
(3599)
Representative proteomes UniProt
(5958)
RP15
(332)
RP35
(898)
RP55
(2620)
RP75
(3632)
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(49)
Full
(3599)
Representative proteomes UniProt
(5958)
RP15
(332)
RP35
(898)
RP55
(2620)
RP75
(3632)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

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 View help on the curation process

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 , Chuguransky S
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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 26.8 26.8
Trusted cut-off 26.8 26.8
Noise cut-off 26.7 26.7
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.

Protein Predicted structure External Information
A0A044UA04 View 3D Structure Click here
A0A044UU54 View 3D Structure Click here
A0A077ZEL8 View 3D Structure Click here
A0A077ZIT0 View 3D Structure Click here
A0A0K0DUV9 View 3D Structure Click here
A0A0K0J3J0 View 3D Structure Click here
A0A0N4U1L3 View 3D Structure Click here
A0A0N4U7I1 View 3D Structure Click here
A0A2R8QLR0 View 3D Structure Click here
A0A3P7DKW2 View 3D Structure Click here
B0WYY2 View 3D Structure Click here
B3DGL5 View 3D Structure Click here
E9PT65 View 3D Structure Click here
G5EBK3 View 3D Structure Click here
O35763 View 3D Structure Click here
P15311 View 3D Structure Click here
P26038 View 3D Structure Click here
P26040 View 3D Structure Click here
P26041 View 3D Structure Click here
P26042 View 3D Structure Click here
P26043 View 3D Structure Click here
P26044 View 3D Structure Click here
P31976 View 3D Structure Click here
P31977 View 3D Structure Click here
P35240 View 3D Structure Click here
P35241 View 3D Structure Click here
P46150 View 3D Structure Click here
P46662 View 3D Structure Click here
P59750 View 3D Structure Click here
Q170J7 View 3D Structure Click here
Q24564 View 3D Structure Click here
Q29GR8 View 3D Structure Click here
Q2HJ49 View 3D Structure Click here
Q32LP2 View 3D Structure Click here
Q503E6 View 3D Structure Click here
Q5TZG5 View 3D Structure Click here
Q63648 View 3D Structure Click here
Q66I42 View 3D Structure Click here
Q6Q413 View 3D Structure Click here
Q7PS12 View 3D Structure Click here