(data stored in ACNUC9306 zone)

SWISSPROT: 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   11-DEC-2019, entry version 191.
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; CD44 AND ICAM2, AND SUBCELLULAR 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.
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 MPP5 and SLC9A3R2. Found in a complex with EZR,
CC       PODXL and SLC9A3R2 (By similarity). Interacts with MCC, PLEKHG6, PODXL,
CC       SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when phosphorylated) with
CC       FES/FPS. Interacts with dimeric S100P, the interaction may be
CC       activating through unmasking of F-actin binding sites (By similarity).
CC       Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2,
CC       ANK2, PLEC, PRX and spectrin (PubMed:21745462). Detected in a complex
CC       composed of at least EZR, AHNAK, PPL and PRX (By similarity). Interacts
CC       with PDPN (via cytoplasmic domain); activates RHOA and promotes
CC       epithelial-mesenchymal transition (By similarity). Interacts with SPN
CC       (PubMed:9472040, PubMed:21289089). Interacts with CD44 and ICAM2
CC       (PubMed:9472040). {ECO:0000250|UniProtKB:P15311,
CC       ECO:0000250|UniProtKB:P31976, ECO:0000250|UniProtKB:P31977,
CC       ECO:0000250|UniProtKB:Q8HZQ5, ECO:0000269|PubMed:21289089,
CC       ECO:0000269|PubMed:21745462, 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 MPP5. 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: 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}.
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   SMR; P26040; -.
DR   BioGrid; 204522; 13.
DR   CORUM; P26040; -.
DR   IntAct; P26040; 14.
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   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   eggNOG; KOG3529; Eukaryota.
DR   eggNOG; ENOG410XQFP; LUCA.
DR   GeneTree; ENSGT00960000186596; -.
DR   HOGENOM; HOG000007113; -.
DR   InParanoid; P26040; -.
DR   KO; K08007; -.
DR   OMA; NYHVHDN; -.
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   ChiTaRS; Ezr; mouse.
DR   PRO; PR:P26040; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P26040; protein.
DR   Bgee; ENSMUSG00000052397; Expressed in 375 organ(s), highest expression level in epithelium of stomach.
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: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:0005623; C:cell; IEA:GOC.
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; IEA:Ensembl.
DR   GO; GO:0001772; C:immunological synapse; ISO:MGI.
DR   GO; GO:0071437; C:invadopodium; ISS:UniProtKB.
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:BHF-UCL.
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:0034629; P:cellular protein-containing complex localization; 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:1900041; P:negative regulation of interleukin-2 secretion; 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:1903364; P:positive regulation of cellular protein catabolic process; 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: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: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; 1.25.40.1020; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C_dom.
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   Pfam; PF00769; ERM; 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;
DR   PRODOM; P26040.
DR   SWISS-2DPAGE; P26040.
KW   Acetylation; Cell membrane; Cell projection; Cell shape; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein;
KW   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   MOTIF           115..120
FT                   /note="[IL]-x-C-x-x-[DE] motif"
FT                   /evidence="ECO:0000250|UniProtKB:P15311"
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:0000244|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
//

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