EZRI_MOUSE
ID EZRI_MOUSE Reviewed; 586 AA.
AC P26040; Q80ZT8; Q9DCI1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Ezrin;
DE AltName: Full=Cytovillin;
DE AltName: Full=Villin-2;
DE AltName: Full=p81;
GN Name=Ezr; Synonyms=Vil2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1955455; DOI=10.1083/jcb.115.4.1039;
RA Funayama N., Nagafuchi A., Sato N., Tsukita S., Tsukita S.;
RT "Radixin is a novel member of the band 4.1 family.";
RL J. Cell Biol. 115:1039-1048(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 264-273, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION AT THR-567, AND ACTIVITY REGULATION.
RX PubMed=9456324; DOI=10.1083/jcb.140.3.647;
RA Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K.,
RA Tsukita S., Tsukita S.;
RT "Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin
RT (ERM) proteins and regulates their head-to-tail association.";
RL J. Cell Biol. 140:647-657(1998).
RN [6]
RP INTERACTION WITH SPN/CD43 CYTOPLASMIC TAIL; CD44 AND ICAM2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9472040; DOI=10.1083/jcb.140.4.885;
RA Yonemura S., Hirao M., Doi Y., Takahashi N., Kondo T., Tsukita S.,
RA Tsukita S.;
RT "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino
RT acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and
RT ICAM-2.";
RL J. Cell Biol. 140:885-895(1998).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15797715; DOI=10.1016/j.mcn.2004.11.014;
RA Groenholm M., Teesalu T., Tyynelaa J., Piltti K., Boehling T.,
RA Wartiovaara K., Vaheri A., Carpen O.;
RT "Characterization of the NF2 protein merlin and the ERM protein ezrin in
RT human, rat, and mouse central nervous system.";
RL Mol. Cell. Neurosci. 28:683-693(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH PRX; AHNAK; BFSP1; BFSP2; ANK2; PLEC; VIM
RP AND SPECTRIN, AND TISSUE SPECIFICITY.
RX PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036;
RA Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J., Rao P.V.;
RT "Periaxin is required for hexagonal geometry and membrane organization of
RT mature lens fibers.";
RL Dev. Biol. 357:179-190(2011).
RN [10]
RP INTERACTION WITH SPN/CD43 CYTOPLASMIC TAIL.
RX PubMed=21289089; DOI=10.1091/mbc.e10-07-0586;
RA Cannon J.L., Mody P.D., Blaine K.M., Chen E.J., Nelson A.D., Sayles L.J.,
RA Moore T.V., Clay B.S., Dulin N.O., Shilling R.A., Burkhardt J.K.,
RA Sperling A.I.;
RT "CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell
RT trafficking and CD43 phosphorylation.";
RL Mol. Biol. Cell 22:954-963(2011).
CC -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC structures to the plasma membrane. In epithelial cells, required for
CC the formation of microvilli and membrane ruffles on the apical pole.
CC Along with PLEKHG6, required for normal macropinocytosis (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: A head-to-tail association, of the N-terminal and
CC C-terminal halves results in a closed conformation (inactive form)
CC which is incapable of actin or membrane-binding.
CC {ECO:0000269|PubMed:9456324}.
CC -!- SUBUNIT: Interacts with PALS1 and SLC9A3R2. Found in a complex with
CC EZR, PODXL and SLC9A3R2 (By similarity). Interacts with MCC, PLEKHG6,
CC PODXL, SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when
CC phosphorylated) with FES/FPS. Interacts with dimeric S100P, the
CC interaction may be activating through unmasking of F-actin binding
CC sites (By similarity). Identified in complexes that contain VIM, EZR,
CC AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462).
CC Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By
CC similarity). Interacts with PDPN (via cytoplasmic domain); activates
CC RHOA and promotes epithelial-mesenchymal transition (By similarity).
CC Interacts with SPN/CD43 cytoplasmic tail (PubMed:9472040,
CC PubMed:21289089). Interacts with CD44 and ICAM2 (PubMed:9472040).
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31976,
CC ECO:0000250|UniProtKB:P31977, ECO:0000250|UniProtKB:Q8HZQ5,
CC ECO:0000269|PubMed:21289089, ECO:0000269|PubMed:21745462,
CC ECO:0000269|PubMed:9472040}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P15311}. Cell projection
CC {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P15311}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus
CC {ECO:0000269|PubMed:9472040}. Note=Localization to the apical membrane
CC of parietal cells depends on the interaction with PALS1. Microvillar
CC peripheral membrane protein (cytoplasmic side). Localizes to cell
CC extensions and peripheral processes of astrocytes (By similarity).
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (PubMed:21745462).
CC Expressed in cerebrum and cerebellum (at protein level)
CC (PubMed:15797715). Component of the microvilli of intestinal epithelial
CC cells. {ECO:0000269|PubMed:15797715, ECO:0000269|PubMed:21745462}.
CC -!- DEVELOPMENTAL STAGE: Detected in whole embryo from 5 dpc with highest
CC expression at 8, 11, 12, and 18 dpc. Expressed at 18 dpc in brain, a
CC clear reduction occurs after birth followed by a transient increase
CC around 2 weeks to 1 month. Hardly detected in adult brain.
CC {ECO:0000269|PubMed:15797715}.
CC -!- DOMAIN: Has three main structural domains: an N-terminal FERM domain, a
CC central alpha-helical domain and a C-terminal actin-binding domain.
CC {ECO:0000250|UniProtKB:P15311}.
CC -!- DOMAIN: The FERM domain is organized in a clover-shaped structure that
CC comprises three subdomains identified as F1 (residues 2-82), F2
CC (residues 96-198), and F3 (residues 204-296). In the active form, the
CC subdomain F3 adopts two mutually exclusive conformational isomers where
CC a row of four phenylalanine side chains (Phe250, Phe255, Phe267 and
CC Phe269) must point in the same direction. In the autoinhibited form,
CC the F3 subdomain interacts with the C-terminal domain (residues 516-
CC 586) and stabilizes the structure, selecting only one possible
CC arrangement of phenylalanine side chains. The FERM domain mediates
CC binding to membrane lipids and signaling molecules.
CC {ECO:0000250|UniProtKB:P15311}.
CC -!- DOMAIN: The central alpha-helical domain is composed of two alpha
CC helices (residues 326-406 and 417-466) connected by a linker. It
CC protrudes from the FERM domain forming a coiled coil structure where
CC the linker can have either a loop or a helix conformation. The monomer
CC is predicted to form an intra-molecular helix-loop-helix coiled coil
CC structure. Whereas the dimer adopts an elongated dumbbell-shaped
CC configuration where continuous alpha helices from each protomer are
CC organized in a antiparallel coiled coil structure that connect FERM:C-
CC terminal domain swapped complex at each end. The dimer is predicted to
CC link actin filaments parallel to the plasma membrane.
CC {ECO:0000250|UniProtKB:P15311}.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P15311}.
CC -!- PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by
CC ROCK2 suppresses the head-to-tail association of the N-terminal and C-
CC terminal halves resulting in an opened conformation which is capable of
CC actin and membrane-binding. {ECO:0000269|PubMed:9456324}.
CC -!- PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-
CC modified low-densitity lipoprotein (LDL(ox)) possibly implicating the
CC iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P15311}.
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DR EMBL; X60671; CAA43086.1; -; mRNA.
DR EMBL; AK002766; BAB22341.1; -; mRNA.
DR EMBL; BC048181; AAH48181.2; -; mRNA.
DR CCDS; CCDS37428.1; -.
DR PIR; B41129; B41129.
DR RefSeq; NP_033536.2; NM_009510.2.
DR AlphaFoldDB; P26040; -.
DR BMRB; P26040; -.
DR SMR; P26040; -.
DR BioGRID; 204522; 37.
DR CORUM; P26040; -.
DR IntAct; P26040; 12.
DR MINT; P26040; -.
DR STRING; 10090.ENSMUSP00000063734; -.
DR ChEMBL; CHEMBL3102687; -.
DR TCDB; 8.A.25.1.1; the ezrin/radixin/moesin (ezrin) family.
DR iPTMnet; P26040; -.
DR PhosphoSitePlus; P26040; -.
DR SwissPalm; P26040; -.
DR REPRODUCTION-2DPAGE; P26040; -.
DR CPTAC; non-CPTAC-3807; -.
DR EPD; P26040; -.
DR jPOST; P26040; -.
DR PaxDb; P26040; -.
DR PeptideAtlas; P26040; -.
DR PRIDE; P26040; -.
DR ProteomicsDB; 275709; -.
DR Antibodypedia; 3417; 1513 antibodies from 46 providers.
DR DNASU; 22350; -.
DR Ensembl; ENSMUST00000064234; ENSMUSP00000063734; ENSMUSG00000052397.
DR GeneID; 22350; -.
DR KEGG; mmu:22350; -.
DR UCSC; uc008ahv.1; mouse.
DR CTD; 7430; -.
DR MGI; MGI:98931; Ezr.
DR VEuPathDB; HostDB:ENSMUSG00000052397; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; P26040; -.
DR OMA; HSGMLRE; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; P26040; -.
DR TreeFam; TF313935; -.
DR Reactome; R-MMU-373752; Netrin-1 signaling.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR BioGRID-ORCS; 22350; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Ezr; mouse.
DR PRO; PR:P26040; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P26040; protein.
DR Bgee; ENSMUSG00000052397; Expressed in epithelium of stomach and 325 other tissues.
DR ExpressionAtlas; P26040; baseline and differential.
DR Genevisible; P26040; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0097449; C:astrocyte projection; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0051286; C:cell tip; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0044393; C:microspike; ISO:MGI.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097454; C:Schwann cell microvillus; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0001931; C:uropod; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0051018; F:protein kinase A binding; ISO:MGI.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044548; F:S100 protein binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0030953; P:astral microtubule organization; ISO:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR GO; GO:0043622; P:cortical microtubule organization; ISO:MGI.
DR GO; GO:0051660; P:establishment of centrosome localization; ISO:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:MGI.
DR GO; GO:0046847; P:filopodium assembly; ISO:MGI.
DR GO; GO:0001951; P:intestinal D-glucose absorption; IGI:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IGI:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0010737; P:protein kinase A signaling; ISO:MGI.
DR GO; GO:0072697; P:protein localization to cell cortex; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; IMP:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0032532; P:regulation of microvillus length; IGI:UniProtKB.
DR GO; GO:1902115; P:regulation of organelle assembly; ISO:MGI.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; ISO:MGI.
DR GO; GO:1902896; P:terminal web assembly; IGI:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
DR InterPro; IPR041789; ERM_FERM_C.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR008954; Moesin_tail_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23281; PTHR23281; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PIRSF; PIRSF002305; ERM; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48678; SSF48678; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Cell shape; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; S-nitrosylation.
FT CHAIN 1..586
FT /note="Ezrin"
FT /id="PRO_0000219409"
FT DOMAIN 2..295
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 244..586
FT /note="Interaction with SCYL3"
FT /evidence="ECO:0000250"
FT REGION 306..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..462
FT /evidence="ECO:0000255"
FT MOTIF 115..120
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT COMPBIAS 540..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 146
FT /note="Phosphotyrosine; by PDGFR"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 354
FT /note="Phosphotyrosine; by PDGFR"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 478
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 567
FT /note="Phosphothreonine; by ROCK2 and PKC/PRKCI"
FT /evidence="ECO:0000305|PubMed:9456324"
FT CONFLICT 48
FT /note="Q -> P (in Ref. 1; CAA43086)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="T -> A (in Ref. 1; CAA43086)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="Q -> R (in Ref. 2; BAB22341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 69407 MW; 5B7728F575F6DE3E CRC64;
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK
LDKKVSAQEV RKENPVQFKF RAKFYPEDVA EELIQDITQK LFFLQVKDGI LSDEIYCPPE
TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR
GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR LQDYEQKTKR
AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK EELERQAQDQ IKSQEQLAAE
LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP
VNYHVQEGLQ DEGAEPMGYS AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ
ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM
