Descriptions

The tumor suppressor gene Nf2 encodes the protein 4.1, Ezrin, Radixin, Moesin (FERM) domain-containing protein Merlin. The tumor suppressor Merlin/NF2 functions upstream of the core Hippo pathway kinases Lats1/2 and Mst1/2, as well as the nuclear E3 ubiquitin ligase CRL4.
Merlin’s autoinhibitory tail physically blocks the Lats1/2-binding site on the Merlin FERM domain. Angiomotin binding releases this autoinhibition, promoting Merlin’s binding to Lats1/2, leading to activation of Hippo pathway kinases.

Autoinhibitory domains (AIDs)

Target domain

14-304 (FERM domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

0 structures for Q6Q413

Entry ID Method Resolution Chain Position Source

No variants for Q6Q413

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6Q413

No associated diseases with Q6Q413

6 regional properties for Q6Q413

Type Name Position InterPro Accession
domain Peptidase S8/S53 domain 192 - 474 IPR000209
domain P domain 490 - 628 IPR002884
active_site Peptidase S8, subtilisin, His-active site 240 - 250 IPR022398
active_site Peptidase S8, subtilisin, Asp-active site 197 - 208 IPR023827
domain Peptidase S8, pro-domain 42 - 116 IPR032815
domain Kexin/furin catalytic domain 159 - 447 IPR034182

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Membrane ; Peripheral membrane protein ; Cytoplasmic side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
adherens junction A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules.
apical part of cell The region of a polarized cell that forms a tip or is distal to a base. For example, in a polarized epithelial cell, the apical region has an exposed surface and lies opposite to the basal lamina that separates the epithelium from other tissue.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
integrin binding Binding to an integrin.

7 GO annotations of biological process

Name Definition
negative regulation of cell population proliferation Any process that stops, prevents or reduces the rate or extent of cell proliferation.
positive regulation of early endosome to late endosome transport Any process that activates or increases the frequency, rate or extent of early endosome to late endosome transport.
positive regulation of protein localization to early endosome Any process that activates or increases the frequency, rate or extent of protein localization to early endosome.
regulation of cell shape Any process that modulates the surface configuration of a cell.
regulation of gliogenesis Any process that modulates the frequency, rate or extent of gliogenesis, the formation of mature glia.
regulation of hippo signaling Any process that modulates the frequency, rate or extent of hippo signaling.
regulation of organelle assembly Any process that modulates the frequency, rate or extent of organelle assembly.

21 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P31976 EZR Ezrin Bos taurus (Bovine) PR
Q2HJ49 MSN Moesin Bos taurus (Bovine) PR
Q32LP2 RDX Radixin Bos taurus (Bovine) SS
Q9PU45 RDX Radixin Gallus gallus (Chicken) PR
P46150 Moe Moesin/ezrin/radixin homolog 1 Drosophila melanogaster (Fruit fly) SS
Q24564 Mer Moesin/ezrin/radixin homolog 2 Drosophila melanogaster (Fruit fly) SS
Q3KP66 INAVA Innate immunity activator protein Homo sapiens (Human) PR
P15311 EZR Ezrin Homo sapiens (Human) EV
P26038 MSN Moesin Homo sapiens (Human) EV
P35240 NF2 Merlin Homo sapiens (Human) EV
P35241 RDX Radixin Homo sapiens (Human) SS
A2AD83 Frmd7 FERM domain-containing protein 7 Mus musculus (Mouse) PR
P26040 Ezr Ezrin Mus musculus (Mouse) SS
P26041 Msn Moesin Mus musculus (Mouse) SS
P26043 Rdx Radixin Mus musculus (Mouse) SS
P46662 Nf2 Merlin Mus musculus (Mouse) SS
P26042 MSN Moesin Sus scrofa (Pig) PR
P26044 RDX Radixin Sus scrofa (Pig) SS
Q63648 Nf2 Merlin Rattus norvegicus (Rat) SS
O35763 Msn Moesin Rattus norvegicus (Rat) SS
P31977 Ezr Ezrin Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MSILGLKKKQ PKTFKVKVST MDAEMEFSCE VKWKGKDLFD LVCRTIGLRE TWFFGLRYTV
70 80 90 100 110 120
KDTYAWLKPD KRVLDQEVPK DSPITFHFLA KFFPEKVEDE LVQEITQHLF FLQVKKQILD
130 140 150 160 170 180
EEIFCSPEAS VLLASYAVQA KYGDYDPNFH KPGFLAQDEL LPKRVLMQYQ MTPDMWEEKI
190 200 210 220 230 240
TAWYAEHRNI TRDEAEMEYL KIAQDLDMYG VSYFSITQNK RDTELLLGVD AQGLHIYNPN
250 260 270 280 290 300
NKLSPNKSFP WSGIRNISYS EKEFTIKPLD KKKEVFKFYS SQLRVNKLIL QLCIGNHDLF
310 320 330 340 350 360
MRRRKVDSIE VQQMKAQAKE EKARKKVERQ ILAREKQMRE EAERAKEEME RRMFQLQDEA
370 380 390 400 410 420
RMANEALLRS EETADLLAEK AQIAEEEAKL LAHKAAEAEQ ERQRLEVTAL KTKEEKRLME
430 440 450 460 470 480
QKMREAEQLA VKLVEQSERR LKEADHLKQD LNEAKDAERR AKQKLLEITK TTYPLIAAYS
490 500 510 520 530 540
NPPPPAGPES PEMAIEMGNP IQMDFKDSDM KRLSMEIERE RLEYMEKSKH LQDQLKELKS
550 560 570 580
EIESLKLEEQ QQAGVYNLRS YAEPPFIPPS NRNSAYMAQM AFYEEV