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10  structures 479  species 0  interactions 3552  sequences 46  architectures

Family: ERM_C (PF00769)

Summary: Ezrin/radixin/moesin family C terminal

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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 family C terminal Provide feedback

This entry represents the C-terminal domain of the ERM family of proteins which consists of three closely-related proteins, ezrin, radixin and moesin [1]. These proteins link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain (PF00373), a common membrane binding module [1,2]. Ezrin was first identified as a constituent of microvilli [3] radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions [4] and moesin as a heparin binding protein [5]. 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). This entry represents the C-terminal actin-binding tail domain [6,7]. This entry also includes Ermin proteins, oligodendrocyte-specific proteins associated with the cytoskeleton whose C-terminal domain is similar to that in ERM family [8].

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. Pearson MA, Reczek D, Bretscher A, Karplus PA;, Cell. 2000;101:259-270.: Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. PUBMED:10847681 EPMC:10847681

  3. Bretscher A;, J Cell Biol. 1983;97:425-432.: Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. PUBMED:6885906 EPMC:6885906

  4. Lankes W, Griesmacher A, Grunwald J, Schwartz-Albiez R, Keller R;, Biochem J. 1988;251:831-842.: A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation. PUBMED:3046603 EPMC:3046603

  5. 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

  6. 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

  7. 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

  8. Wang S, Wang T, Liu T, Xie RG, Zhao XH, Wang L, Yang Q, Jia LT, Han J;, Glia. 2020;68:2264-2276.: Ermin is a p116(RIP) -interacting protein promoting oligodendroglial differentiation and myelin maintenance. PUBMED:32530539 EPMC:32530539


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR011259

The ERM family consists of three closely-related proteins, ezrin, radixin and moesin [ PUBMED:9048483 ]. Ezrin was first identified as a constituent of microvilli [ PUBMED:6885906 ], radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions [ PUBMED:2500445 ], and moesin as a heparin binding protein [ PUBMED:3046603 ]. 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) [ PUBMED:21167305 ]. ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain [ PUBMED:9048483 ]. Ezrin, radixin and merlin also contain a polyproline 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 [ PUBMED:27405666 ]. 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 [ PUBMED:9048483 ].

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 Moesin_tail (CL0719), which has the following description:

This superfamily includes the C-terminal actin-binding tail domain found in ERM (ezrin, radixin and moesin) family members, merlin (moesin-ezrin-radixin-like protein) and ermin [1,2,3].

The clan contains the following 2 members:

ERM_C Ermin

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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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(49)
Full
(3552)
Representative proteomes UniProt
(5787)
RP15
(365)
RP35
(901)
RP55
(2587)
RP75
(3573)
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  Seed
(49)
Full
(3552)
Representative proteomes UniProt
(5787)
RP15
(365)
RP35
(901)
RP55
(2587)
RP75
(3573)
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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
(3552)
Representative proteomes UniProt
(5787)
RP15
(365)
RP35
(901)
RP55
(2587)
RP75
(3573)
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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.

Note: You can also download the data file for the tree.

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_851 (release 2.1)
Previous IDs: ERM;
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Chuguransky S
Number in seed: 49
Number in full: 3552
Average length of the domain: 73.2 aa
Average identity of full alignment: 50 %
Average coverage of the sequence by the domain: 12.74 %

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 23.4 23.4
Trusted cut-off 23.5 23.5
Noise cut-off 23.2 23.2
Model length: 77
Family (HMM) version: 22
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_C 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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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
A0A0K0E8A0 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
A0A3P7DEP8 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
G4VND1 View 3D Structure Click here
G5EBK3 View 3D Structure Click here
H2KYX3 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