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Details on Person UniProt:P15311 EZR
| Class:Id | ReferenceGeneProduct:54558 |
|---|---|
| _chainChangeLog | initiator methionine:1 added on Fri February 6 2015;chain:2-586 added on Fri February 6 2015 |
| _displayName | UniProt:P15311 EZR |
| _timestamp | 2024-11-03 19:36:17 |
| chain | chain:1-586 |
| checksum | F1B592CF49A7CC46 |
| comment | FUNCTION Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis.ACTIVITY REGULATION A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding.SUBUNIT Monomer. Homodimer (PubMed:27364155). Interacts with PALS1 and NHERF2. Found in a complex with EZR, PODXL and NHERF2 (By similarity). Interacts with MCC, PLEKHG6, PODXL, SCYL3/PACE1, NHERF1 and TMEM8B (PubMed:12651155, PubMed:15498789, PubMed:17616675, PubMed:17881735, PubMed:19555689, PubMed:9314537). Interacts (when phosphorylated) with FES/FPS (PubMed:18046454). Interacts with dimeric S100P, the interaction may be activating through unmasking of F-actin binding sites (PubMed:12808036, PubMed:19111582). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By similarity). Interacts with PDPN (via cytoplasmic domain); activates RHOA and promotes epithelial-mesenchymal transition (PubMed:17046996). Interacts with SPN/CD43 cytoplasmic tail, CD44 and ICAM2 (By similarity). Interacts with SLC9A3; interaction targets SLC9A3 to the apical membrane (By similarity). Interacts with SLC9A1; regulates interactions of SLC9A1 with cytoskeletal and promotes stress fiber formation (By similarity). Interacts with CLIC5; may work together in a complex which also includes RDX and MYO6 to stabilize linkages between the plasma membrane and subjacent actin cytoskeleton at the base of stereocilia (By similarity).INTERACTION Localization to the apical membrane of parietal cells depends on the interaction with PALS1. Localizes to cell extensions and peripheral processes of astrocytes (By similarity). Microvillar peripheral membrane protein (cytoplasmic side).TISSUE SPECIFICITY Expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. Weakly expressed in brain stem and diencephalon. Stronger expression was detected in gray matter of frontal lobe compared to white matter (at protein level). Component of the microvilli of intestinal epithelial cells. Preferentially expressed in astrocytes of hippocampus, frontal cortex, thalamus, parahippocampal cortex, amygdala, insula, and corpus callosum. Not detected in neurons in most tissues studied.DEVELOPMENTAL STAGE Very strong staining is detected in the Purkinje cell layer and in part of the molecular layer of the infant brain compared to adult brain.DOMAIN Has three main structural domains: an N-terminal FERM domain, a central alpha-helical domain and a C-terminal actin-binding domain.DOMAIN The FERM domain is organized in a clover-shaped structure that comprises three subdomains identified as F1 (residues 2-82), F2 (residues 96-198), and F3 (residues 204-296). In the active form, the subdomain F3 adopts two mutually exclusive conformational isomers where a row of four phenylalanine side chains (Phe250, Phe255, Phe267 and Phe269) must point in the same direction. In the autoinhibited form, the F3 subdomain interacts with the C-terminal domain (residues 516-586) and stabilizes the structure, selecting only one possible arrangement of phenylalanine side chains. The FERM domain mediates binding to membrane lipids and signaling molecules.DOMAIN The central alpha-helical domain is composed of two alpha helices (residues 326-406 and 417-466) connected by a linker. It protrudes from the FERM domain forming a coiled coil structure where the linker can have either a loop or a helix conformation. The monomer is predicted to form an intra-molecular helix-loop-helix coiled coil structure. Whereas the dimer adopts an elongated dumbbell-shaped configuration where continuous alpha helices from each protomer are organized in a antiparallel coiled coil structure that connect FERM:C-terminal domain swapped complex at each end. The dimer is predicted to link actin filaments parallel to the plasma membrane.DOMAIN The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.PTM Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity).PTM S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Extended N-terminus. |
| description | recommendedName: Ezrin alternativeName: Cytovillin alternativeName: Villin-2 alternativeName: p81 |
| geneName | EZR VIL2 |
| identifier | P15311 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Cell membrane Cell projection Cell shape Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Membrane Phosphoprotein Proteomics identification Reference proteome S-nitrosylation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | EZR |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8987813] ENSEMBL:ENSG00000092820 EZR [Homo sapiens] |
| secondaryIdentifier | EZRI_HUMAN E1P5A8 P23714 Q4VX75 Q96CU8 Q9NSJ4 |
| sequenceLength | 586 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:374559] p-T567-EZR [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:374572] p-Y146,Y354-EZR [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:9020826] EZR [cytosol] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:374533] O-phospho-L-threonine at 567 [ModifiedResidue:443619] O4'-phospho-L-tyrosine at 354 [ModifiedResidue:443620] O4'-phospho-L-tyrosine at 146 |
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No pathways have been reviewed or authored by UniProt:P15311 EZR (54558)
