MOEH_DROME
ID MOEH_DROME Reviewed; 578 AA.
AC P46150; A4V458; P91930; Q24053; Q24435; Q7KVS6; Q7KVS7; Q9W3B4; Q9W3B5;
AC Q9W3B6; Q9W3B7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Moesin/ezrin/radixin homolog 1;
DE Short=Ezrin-moesin-radixin 1;
DE AltName: Full=Moesin;
DE Short=dMoesin;
DE AltName: Full=Protein D17;
GN Name=Moe; Synonyms=EMR1; ORFNames=CG10701;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM J), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8666669; DOI=10.1083/jcb.133.4.843;
RA McCartney B.M., Fehon R.G.;
RT "Distinct cellular and subcellular patterns of expression imply distinct
RT functions for the Drosophila homologues of moesin and the neurofibromatosis
RT 2 tumor suppressor, merlin.";
RL J. Cell Biol. 133:843-852(1996).
RN [2]
RP SEQUENCE REVISION TO 183-184.
RA Fehon R.G.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 208-296.
RC TISSUE=Embryo;
RA Winge P., Fleming J.T., Gobel V.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 256-578 (ISOFORM D).
RC TISSUE=Embryo;
RX PubMed=8183953; DOI=10.1073/pnas.91.10.4589;
RA Edwards K.A., Montague R.A., Shepard S., Edgar B.A., Erikson R.L.,
RA Kiehart D.P.;
RT "Identification of Drosophila cytoskeletal proteins by induction of
RT abnormal cell shape in fission yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4589-4593(1994).
RN [8]
RP FUNCTION, AND INTERACTION WITH WGN.
RX PubMed=23544124; DOI=10.1371/journal.pone.0060091;
RA Ruan W., Unsain N., Desbarats J., Fon E.A., Barker P.A.;
RT "Wengen, the sole tumour necrosis factor receptor in Drosophila,
RT collaborates with moesin to control photoreceptor axon targeting during
RT development.";
RL PLoS ONE 8:E60091-E60091(2013).
RN [9]
RP FUNCTION, INTERACTION WITH PCID2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=28554770; DOI=10.1016/j.bbamcr.2017.05.020;
RA Kristo I., Bajusz C., Borsos B.N., Pankotai T., Dopie J., Jankovics F.,
RA Vartiainen M.K., Erdelyi M., Vilmos P.;
RT "The actin binding cytoskeletal protein Moesin is involved in nuclear mRNA
RT export.";
RL Biochim. Biophys. Acta 1864:1589-1604(2017).
CC -!- FUNCTION: Involved in connections of major cytoskeletal structures to
CC the plasma membrane (PubMed:8666669). Together with wgn, involved in
CC control of axon targeting of R8 and R2-R5 photoreceptors, independent
CC of egr (PubMed:23544124). In the nucleus, recruited to sites of active
CC transcription by RNA polymerase II where it has a role in nuclear mRNA
CC export together with the mRNA export factor PCID2 and other messenger
CC ribonucleoprotein (mRNP) particles (PubMed:28554770).
CC {ECO:0000269|PubMed:23544124, ECO:0000269|PubMed:28554770,
CC ECO:0000269|PubMed:8666669}.
CC -!- SUBUNIT: Interacts with wgn (PubMed:23544124). Interacts with Mer and
CC arm at the adherens junction (PubMed:8666669). Interacts with
CC cytoskeletal actin at apical buds of microvilli in the precellularised
CC embryo (PubMed:8666669). Interacts with PCID2 (possibly via FERM
CC domain) (PubMed:28554770). {ECO:0000269|PubMed:23544124,
CC ECO:0000269|PubMed:28554770, ECO:0000269|PubMed:8666669}.
CC -!- INTERACTION:
CC P46150-2; Q6XK19: btsz; NbExp=3; IntAct=EBI-206152, EBI-2890448;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:8666669}. Cell membrane
CC {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P26041}. Cytoplasm
CC {ECO:0000269|PubMed:28554770}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:28554770}. Chromosome
CC {ECO:0000269|PubMed:28554770}. Note=Nuclear localization is dependent
CC on Nup98 and Rae1. Associated with the active ecdysone-regulated loci
CC on polytene chromosomes and heat shock-induced puffs. Colocalizes with
CC messenger ribonucleoprotein (mRNP) particles probably through
CC interaction with the mRNA export factor PCID2.
CC {ECO:0000269|PubMed:28554770}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=J;
CC IsoId=P46150-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P46150-3; Sequence=VSP_035864, VSP_035866;
CC Name=B;
CC IsoId=P46150-4; Sequence=VSP_035865, VSP_035866;
CC Name=C;
CC IsoId=P46150-5; Sequence=VSP_035863;
CC Name=D; Synonyms=E, F, G, H, I;
CC IsoId=P46150-2; Sequence=VSP_007499;
CC -!- DEVELOPMENTAL STAGE: Expressed in apical and basolateral ends of
CC follicular epithelium during oogenesis (PubMed:8666669). In embryonic
CC CNS, expression is seen in the neuropil, developing brain and neuronal
CC cell bodies (PubMed:8666669). In embryonic PNS, expression is seen at
CC the cell membrane (PubMed:8666669). In third instar larvae, eye
CC imaginal disk expression is seen at the membranes of developing
CC photoreceptors posterior to the morphogenetic furrow (PubMed:8666669).
CC In pupal eyes, expression is at the membrane of cone cells, secondary
CC and tertiary pigment cells, bristle precursor cells and rhabdomeres
CC (PubMed:8666669). Expressed in the salivary glands of third instar
CC larvae (at protein level) (PubMed:28554770).
CC {ECO:0000269|PubMed:28554770, ECO:0000269|PubMed:8666669}.
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DR EMBL; L38909; AAB48934.1; -; mRNA.
DR EMBL; AE014298; AAF46415.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF46416.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46417.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46418.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65294.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65295.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65296.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65297.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65298.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65299.1; -; Genomic_DNA.
DR EMBL; AY069855; AAL40000.1; -; mRNA.
DR EMBL; U23798; AAA65059.1; -; mRNA.
DR EMBL; U08218; AAA19857.1; -; mRNA.
DR RefSeq; NP_001245584.1; NM_001258655.1. [P46150-1]
DR RefSeq; NP_525082.2; NM_080343.4. [P46150-2]
DR RefSeq; NP_727290.1; NM_167168.4. [P46150-4]
DR RefSeq; NP_727291.1; NM_167169.2. [P46150-3]
DR RefSeq; NP_727292.1; NM_167170.2. [P46150-5]
DR RefSeq; NP_996387.1; NM_206664.3. [P46150-1]
DR RefSeq; NP_996388.1; NM_206665.3. [P46150-2]
DR RefSeq; NP_996389.1; NM_206666.3. [P46150-2]
DR RefSeq; NP_996390.1; NM_206667.3. [P46150-2]
DR RefSeq; NP_996391.1; NM_206668.3. [P46150-2]
DR RefSeq; NP_996392.1; NM_206669.2. [P46150-2]
DR AlphaFoldDB; P46150; -.
DR SMR; P46150; -.
DR BioGRID; 58274; 144.
DR DIP; DIP-52150N; -.
DR IntAct; P46150; 15.
DR STRING; 7227.FBpp0071213; -.
DR TCDB; 8.A.25.1.4; the ezrin/radixin/moesin (ezrin) family.
DR iPTMnet; P46150; -.
DR PRIDE; P46150; -.
DR EnsemblMetazoa; FBtr0071269; FBpp0071212; FBgn0011661. [P46150-2]
DR EnsemblMetazoa; FBtr0071270; FBpp0071213; FBgn0011661. [P46150-4]
DR EnsemblMetazoa; FBtr0071271; FBpp0071214; FBgn0011661. [P46150-3]
DR EnsemblMetazoa; FBtr0071272; FBpp0071215; FBgn0011661. [P46150-5]
DR EnsemblMetazoa; FBtr0071273; FBpp0089231; FBgn0011661. [P46150-2]
DR EnsemblMetazoa; FBtr0071274; FBpp0089232; FBgn0011661. [P46150-2]
DR EnsemblMetazoa; FBtr0071275; FBpp0089233; FBgn0011661. [P46150-2]
DR EnsemblMetazoa; FBtr0071276; FBpp0089234; FBgn0011661. [P46150-2]
DR EnsemblMetazoa; FBtr0071277; FBpp0089235; FBgn0011661. [P46150-2]
DR EnsemblMetazoa; FBtr0071278; FBpp0089236; FBgn0011661. [P46150-1]
DR EnsemblMetazoa; FBtr0308194; FBpp0300514; FBgn0011661. [P46150-1]
DR GeneID; 31816; -.
DR KEGG; dme:Dmel_CG10701; -.
DR UCSC; CG10701-RA; d. melanogaster.
DR UCSC; CG10701-RB; d. melanogaster.
DR UCSC; CG10701-RC; d. melanogaster.
DR UCSC; CG10701-RE; d. melanogaster.
DR CTD; 31816; -.
DR FlyBase; FBgn0011661; Moe.
DR VEuPathDB; VectorBase:FBgn0011661; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR InParanoid; P46150; -.
DR PhylomeDB; P46150; -.
DR Reactome; R-DME-373752; Netrin-1 signaling.
DR SignaLink; P46150; -.
DR BioGRID-ORCS; 31816; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Moe; fly.
DR GenomeRNAi; 31816; -.
DR PRO; PR:P46150; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0011661; Expressed in embryonic/larval hemocyte (Drosophila) and 55 other tissues.
DR ExpressionAtlas; P46150; baseline and differential.
DR Genevisible; P46150; DM.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0035003; C:subapical complex; TAS:FlyBase.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0030029; P:actin filament-based process; NAS:FlyBase.
DR GO; GO:0009952; P:anterior/posterior pattern specification; TAS:FlyBase.
DR GO; GO:0060446; P:branching involved in open tracheal system development; IMP:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:FlyBase.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:FlyBase.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP:FlyBase.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; TAS:FlyBase.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IDA:UniProtKB.
DR GO; GO:0016336; P:establishment or maintenance of polarity of larval imaginal disc epithelium; IMP:FlyBase.
DR GO; GO:0042462; P:eye photoreceptor cell development; TAS:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
DR GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
DR GO; GO:0002009; P:morphogenesis of an epithelium; TAS:FlyBase.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0007315; P:pole plasm assembly; TAS:FlyBase.
DR GO; GO:0007318; P:pole plasm protein localization; TAS:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:FlyBase.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IBA:GO_Central.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
DR GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IMP:UniProtKB.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; TAS:FlyBase.
DR GO; GO:1990146; P:protein localization to rhabdomere; IMP:FlyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0016057; P:regulation of membrane potential in photoreceptor cell; IDA:FlyBase.
DR GO; GO:1902115; P:regulation of organelle assembly; IBA:GO_Central.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0045313; P:rhabdomere membrane biogenesis; IMP:FlyBase.
DR GO; GO:0006405; P:RNA export from nucleus; IMP: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 Actin-binding; Alternative splicing; Cell junction; Cell membrane;
KW Chromosome; Cytoplasm; Cytoskeleton; Membrane; Neurogenesis; Nucleus;
KW Reference proteome.
FT CHAIN 1..578
FT /note="Moesin/ezrin/radixin homolog 1"
FT /id="PRO_0000219425"
FT DOMAIN 1..296
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 463..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_035863"
FT VAR_SEQ 2..5
FT /note="SPKA -> GVNFLLFFFSIWL (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_035864"
FT VAR_SEQ 2..5
FT /note="SPKA -> VVVSDSRVRLPRYGGVSVKRKT (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_035865"
FT VAR_SEQ 65
FT /note="K -> KPESPAIKTIKYLKRVKKYVDKKTADSNGVNHLETSEEDDDADDMTG
FT SMPFSTW (in isoform A and isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_035866"
FT VAR_SEQ 451..453
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8183953"
FT /id="VSP_007499"
FT CONFLICT 217..219
FT /note="LWL -> SLV (in Ref. 6; AAA65059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 68141 MW; 24FBA67A3CDF3809 CRC64;
MSPKALNVRV TTMDAELEFA IQSTTTGKQL FDQVVKTIGL REVWFFGLQY TDSKGDSTWI
KLYKKVMNQD VKKENPLQFR FRAKFYPEDV AEELIQDITL RLFYLQVKNA ILTDEIYCPP
ETSVLLASYA VQARHGDHNK TTHTAGFLAN DRLLPQRVID QHKMSKDEWE QSIMTWWQEH
RSMLREDAMM EYLKIAQDLE MYGVNYFEIR NKKGTDLWLG VDALGLNIYE QDDRLTPKIG
FPWSEIRNIS FSEKKFIIKP IDKKAPDFMF FAPRVRINKR ILALCMGNHE LYMRRRKPDT
IDVQQMKAQA REEKNAKQQE REKLQLALAA RERAEKKQQE YEDRLKQMQE DMERSQRDLL
EAQDMIRRLE EQLKQLQAAK DELELRQKEL QAMLQRLEEA KNMEAVEKLK LEEEIMAKQM
EVQRIQDEVN AKDEETKRLQ DEVEDARRKQ VIAAEAAAAL LAASTTPQHH HVAEDENENE
EELTNGDAGG DVSRDLDTDE HIKDPIEDRR TLAERNERLH DQLKALKQDL AQSRDETKET
ANDKIHRENV RQGRDKYKTL REIRKGNTKR RVDQFENM
