ID Q9YGW6_CHICK Unreviewed; 585 AA. AC Q9YGW6; F1P3H9; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 173. DE RecName: Full=Ezrin {ECO:0000256|ARBA:ARBA00039923}; DE AltName: Full=Cytovillin {ECO:0000256|ARBA:ARBA00042548}; DE AltName: Full=Villin-2 {ECO:0000256|ARBA:ARBA00042776}; DE AltName: Full=p81 {ECO:0000256|ARBA:ARBA00041750}; GN Name=EZR {ECO:0000313|Ensembl:ENSGALP00010007851.1}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|EMBL:BAA75497.1}; RN [1] {ECO:0000313|EMBL:BAA75497.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=White Leghorn {ECO:0000313|EMBL:BAA75497.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAA75497.1}; RX PubMed=10051754; DOI=10.1046/j.1460-9568.1999.00460.x; RA Takahashi M., Yamagata M., Noda M.; RT "Specific expression of ezrin, a cytoskeletal-membrane linker protein, in a RT subset of chick retinotectal and sensory projections."; RL Eur. J. Neurosci. 11:545-558(1999). RN [2] {ECO:0000313|Ensembl:ENSGALP00010007851.1} RP IDENTIFICATION. RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010007851.1}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00037857}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00037857}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00037857}. Cell projection, microvillus membrane CC {ECO:0000256|ARBA:ARBA00037837}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00037837}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00037837}. Cell projection, ruffle membrane CC {ECO:0000256|ARBA:ARBA00004599}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004599}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004599}. Cytoplasm, cell cortex CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton CC {ECO:0000256|ARBA:ARBA00004245}. Membrane CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB019790; BAA75497.1; -; mRNA. DR RefSeq; NP_990216.1; NM_204885.1. DR STRING; 9031.ENSGALP00000022293; -. DR PaxDb; 9031-ENSGALP00000022293; -. DR Ensembl; ENSGALT00010013289.1; ENSGALP00010007851.1; ENSGALG00010005548.1. DR GeneID; 395701; -. DR KEGG; gga:395701; -. DR CTD; 7430; -. DR VEuPathDB; HostDB:geneid_395701; -. DR eggNOG; KOG3529; Eukaryota. DR GeneTree; ENSGT01090000260082; -. DR HOGENOM; CLU_003623_6_2_1; -. DR OMA; EWQHRAI; -. DR OrthoDB; 5476297at2759; -. DR Reactome; R-GGA-373752; Netrin-1 signaling. DR Reactome; R-GGA-437239; Recycling pathway of L1. DR Proteomes; UP000000539; Chromosome 3. DR Bgee; ENSGALG00000013742; Expressed in ovary and 13 other cell types or tissues. 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; IBA:GO_Central. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0030175; C:filopodium; IBA:GO_Central. DR GO; GO:0005902; C:microvillus; IBA:GO_Central. DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IBA:GO_Central. DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB. DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB. DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB. DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IBA:GO_Central. DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central. DR GO; GO:1902115; P:regulation of organelle assembly; IBA:GO_Central. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd13194; FERM_C_ERM; 1. DR CDD; cd17239; FERM_F1_Ezrin; 1. DR Gene3D; 1.20.5.450; -; 1. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 6.10.360.10; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR046810; ERM_helical. 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:SF13; EZRIN; 1. DR PANTHER; PTHR23281; MERLIN/MOESIN/EZRIN/RADIXIN; 1. DR Pfam; PF00769; ERM_C; 1. DR Pfam; PF20492; ERM_helical; 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; SSF48678; Moesin tail domain; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF47031; Second domain of FERM; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 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 {ECO:0000256|ARBA:ARBA00022990}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9YGW6}; KW Reference proteome {ECO:0000313|Proteomes:UP000000539}; KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}. FT DOMAIN 5..295 FT /note="FERM" FT /evidence="ECO:0000259|PROSITE:PS50057" FT REGION 306..337 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 539..560 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 60..63 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol)" FT /ligand_id="ChEBI:CHEBI:57880" FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1" FT BINDING 278 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol)" FT /ligand_id="ChEBI:CHEBI:57880" FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1" SQ SEQUENCE 585 AA; 69367 MW; 854C6348F783CAEC CRC64; MPKPINVRVV TVDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFQTWLK LDKKVSAQEI RKENPLQFRF RAKFFPEDVA EELIQDITQK LFFLQVKEGI LSDEIYCPPE TAVLLGSYAV QAKFGDYNKD VHKPGYLNSE RLIPQRVMDQ HKLSRDQWEE RIQVWHAEHS GMLKENAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI EVQQMKAQAR EEKHQKQLER QQLENEKKKR ETIEREKEQM LREKEELLVR LQEYEVKTKR AEKELSDQIQ RALQLEEERR RAQEEAERLE ADRLAALQAK EELERQNIDQ IKSQEQLAAE LAEYTAKIAL LEEARKRKES EVEEWQIRAR EAQEDLVKTK EELHLVMTAP PPPPPIYEPV NYHVHDNLHD EGSEYSAYSA EFSSEGIRND RNEEKRITEA EKNERVQRQL KALTDELAQA RDEDKRTQND IIHSENVRQG RDKYKTLRQI RQGNTKQRID EFEAM //