MOES_MOUSE
ID MOES_MOUSE Reviewed; 577 AA.
AC P26041; B1AX70; Q3UL28; Q8BSN4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Moesin {ECO:0000303|PubMed:1429901};
DE AltName: Full=Membrane-organizing extension spike protein;
GN Name=Msn {ECO:0000312|MGI:MGI:97167};
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=1429901; DOI=10.1242/jcs.103.1.131;
RA Sato N., Funayama N., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S.;
RT "A gene family consisting of ezrin, radixin and moesin. Its specific
RT localization at actin filament/plasma membrane association sites.";
RL J. Cell Sci. 103:131-143(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Forelimb, and Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-577.
RX PubMed=1573844; DOI=10.1038/ki.1992.102;
RA Furthmayr H., Lankes W.T., Amieva M.R.;
RT "Moesin, a new cytoskeletal protein and constituent of filopodia: its role
RT in cellular functions.";
RL Kidney Int. 41:665-670(1992).
RN [6]
RP PHOSPHORYLATION AT THR-558, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-558.
RX PubMed=9856983; DOI=10.1074/jbc.273.52.34663;
RA Oshiro N., Fukata Y., Kaibuchi K.;
RT "Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a
RT crucial role in the formation of microvilli-like structures.";
RL J. Biol. Chem. 273:34663-34666(1998).
RN [7]
RP PHOSPHORYLATION AT THR-558, 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 [8]
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 [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=9890997; DOI=10.1074/jbc.274.4.2315;
RA Doi Y., Itoh M., Yonemura S., Ishihara S., Takano H., Noda T., Tsukita S.;
RT "Normal development of mice and unimpaired cell adhesion/cell
RT motility/actin-based cytoskeleton without compensatory up-regulation of
RT ezrin or radixin in moesin gene knockout.";
RL J. Biol. Chem. 274:2315-2321(1999).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH SLC9A3R1 AND PAG1.
RX PubMed=11777944; DOI=10.4049/jimmunol.168.2.541;
RA Itoh K., Sakakibara M., Yamasaki S., Takeuchi A., Arase H., Miyazaki M.,
RA Nakajima N., Okada M., Saito T.;
RT "Negative regulation of immune synapse formation by anchoring lipid raft to
RT cytoskeleton through Cbp-EBP50-ERM assembly.";
RL J. Immunol. 168:541-544(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, 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 [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22875842; DOI=10.1093/intimm/dxs077;
RA Hirata T., Nomachi A., Tohya K., Miyasaka M., Tsukita S., Watanabe T.,
RA Narumiya S.;
RT "Moesin-deficient mice reveal a non-redundant role for moesin in lymphocyte
RT homeostasis.";
RL Int. Immunol. 24:705-717(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28978692; DOI=10.4049/jimmunol.1700074;
RA Satooka H., Nagakubo D., Sato T., Hirata T.;
RT "The ERM Protein Moesin Regulates CD8+ Regulatory T Cell Homeostasis and
RT Self-Tolerance.";
RL J. Immunol. 199:3418-3426(2017).
RN [16]
RP FUNCTION, AND INTERACTION WITH PTPN6.
RX PubMed=29247647; DOI=10.1016/j.bbrc.2017.12.061;
RA Gomez C.P., Descoteaux A.;
RT "Moesin and myosin IIA modulate phagolysosomal biogenesis in macrophages.";
RL Biochem. Biophys. Res. Commun. 495:1964-1971(2018).
CC -!- FUNCTION: Ezrin-radixin-moesin (ERM) family protein that connects the
CC actin cytoskeleton to the plasma membrane and thereby regulates the
CC structure and function of specific domains of the cell cortex. Tethers
CC actin filaments by oscillating between a resting and an activated state
CC providing transient interactions between moesin and the actin
CC cytoskeleton (By similarity). Once phosphorylated on its C-terminal
CC threonine, moesin is activated leading to interaction with F-actin and
CC cytoskeletal rearrangement (By similarity). These rearrangements
CC regulate many cellular processes, including cell shape determination,
CC membrane transport, and signal transduction (By similarity). The role
CC of moesin is particularly important in immunity acting on both T and B-
CC cells homeostasis and self-tolerance, regulating lymphocyte egress from
CC lymphoid organs (PubMed:22875842). Modulates phagolysosomal biogenesis
CC in macrophages (PubMed:28978692). Participates also in immunologic
CC synapse formation (By similarity). {ECO:0000250|UniProtKB:P26038,
CC ECO:0000269|PubMed:22875842, ECO:0000269|PubMed:28978692}.
CC -!- SUBUNIT: In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which
CC is disrupted upon TCR activation (PubMed:11777944). Interacts with
CC SLC9A3R1 (PubMed:11777944). Interacts with PPP1R16B (By similarity).
CC Interacts with PDZD8 (By similarity). Interacts with SELPLG and SYK;
CC these interaction mediate the activation of SYK by SELPLG (By
CC similarity). Interacts with PDPN (via cytoplasmic domain); this
CC interaction activates RHOA and promotes epithelial-mesenchymal
CC transition (By similarity). Interacts with SPN/CD43 cytoplasmic tail
CC (PubMed:9472040). Interacts with CD44 (PubMed:9472040). Interacts with
CC ICAM2 (PubMed:9472040). Interacts with ICAM3 (via C-terminus) (By
CC similarity). Interacts with PDZD8 (By similarity). Interacts with F-
CC actin (By similarity). Interacts with CD46 (By similarity). Interacts
CC with PTPN6 (PubMed:29247647). {ECO:0000250|UniProtKB:P26038,
CC ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:29247647,
CC ECO:0000269|PubMed:9472040}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9856983};
CC Peripheral membrane protein {ECO:0000269|PubMed:9856983}; Cytoplasmic
CC side {ECO:0000269|PubMed:9856983}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9856983}. Apical cell membrane
CC {ECO:0000269|PubMed:9856983}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9856983}; Cytoplasmic side
CC {ECO:0000269|PubMed:9856983}. Cell projection, microvillus membrane
CC {ECO:0000269|PubMed:9856983}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9856983}; Cytoplasmic side
CC {ECO:0000269|PubMed:9856983}. Cell projection, microvillus
CC {ECO:0000269|PubMed:9472040}. Note=Phosphorylated form is enriched in
CC microvilli-like structures at apical membrane. Increased cell membrane
CC localization of both phosphorylated and non-phosphorylated forms seen
CC after thrombin treatment (By similarity). Localizes at the uropods of T
CC lymphoblasts (By similarity). {ECO:0000250|UniProtKB:P26038,
CC ECO:0000269|PubMed:9856983}.
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:P26038}.
CC -!- PTM: Phosphorylation on Thr-558 by STK10 negatively regulates
CC lymphocyte migration and polarization (By similarity). Phosphorylation
CC on Thr-558 is crucial for the formation of microvilli-like structures.
CC Phosphorylation by ROCK2 suppresses the head-to-tail association of the
CC N-terminal and C-terminal halves resulting in an opened conformation
CC which is capable of actin and membrane-binding. {ECO:0000250,
CC ECO:0000269|PubMed:9456324, ECO:0000269|PubMed:9856983}.
CC -!- PTM: S-nitrosylation of Cys-117 is induced by interferon-gamma and
CC oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating
CC the iNOS-S100A8/9 transnitrosylase complex.
CC {ECO:0000250|UniProtKB:P26038}.
CC -!- DISRUPTION PHENOTYPE: Moesin-deficient mice exhibit no obvious
CC abnormalities in appearance or fertility, but display altered humoral
CC immune responses. {ECO:0000269|PubMed:22875842,
CC ECO:0000269|PubMed:28978692, ECO:0000269|PubMed:9890997}.
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DR EMBL; S47577; AAA11762.1; -; mRNA.
DR EMBL; AK031171; BAC27288.1; -; mRNA.
DR EMBL; AK088336; BAC40290.1; -; mRNA.
DR EMBL; AK133819; BAE21861.1; -; mRNA.
DR EMBL; AK145746; BAE26623.1; -; mRNA.
DR EMBL; AK150869; BAE29920.1; -; mRNA.
DR EMBL; AK153210; BAE31809.1; -; mRNA.
DR EMBL; AL805963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047366; AAH47366.1; -; mRNA.
DR EMBL; M86390; AAA39728.1; -; mRNA.
DR CCDS; CCDS53139.1; -.
DR RefSeq; NP_034963.2; NM_010833.2.
DR PDB; 4YL8; X-ray; 1.50 A; A=1-297.
DR PDBsum; 4YL8; -.
DR AlphaFoldDB; P26041; -.
DR SMR; P26041; -.
DR BioGRID; 201534; 52.
DR IntAct; P26041; 22.
DR MINT; P26041; -.
DR STRING; 10090.ENSMUSP00000113071; -.
DR CarbonylDB; P26041; -.
DR iPTMnet; P26041; -.
DR PhosphoSitePlus; P26041; -.
DR SwissPalm; P26041; -.
DR CPTAC; non-CPTAC-3594; -.
DR EPD; P26041; -.
DR jPOST; P26041; -.
DR MaxQB; P26041; -.
DR PaxDb; P26041; -.
DR PeptideAtlas; P26041; -.
DR PRIDE; P26041; -.
DR ProteomicsDB; 290094; -.
DR Antibodypedia; 2774; 1022 antibodies from 43 providers.
DR DNASU; 17698; -.
DR Ensembl; ENSMUST00000117399; ENSMUSP00000113071; ENSMUSG00000031207.
DR GeneID; 17698; -.
DR KEGG; mmu:17698; -.
DR UCSC; uc009tug.1; mouse.
DR CTD; 4478; -.
DR MGI; MGI:97167; Msn.
DR VEuPathDB; HostDB:ENSMUSG00000031207; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; P26041; -.
DR OMA; WADHKNT; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; P26041; -.
DR TreeFam; TF313935; -.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR BioGRID-ORCS; 17698; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Msn; mouse.
DR PRO; PR:P26041; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P26041; protein.
DR Bgee; ENSMUSG00000031207; Expressed in right lung and 244 other tissues.
DR Genevisible; P26041; MM.
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:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0051286; C:cell tip; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0031527; C:filopodium membrane; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
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; ISO:MGI.
DR GO; GO:0031143; C:pseudopodium; ISO:MGI.
DR GO; GO:0030667; C:secretory granule membrane; 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:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; ISO:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISO:MGI.
DR GO; GO:0022612; P:gland morphogenesis; ISO:MGI.
DR GO; GO:0001771; P:immunological synapse formation; ISS:UniProtKB.
DR GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
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:0071803; P:positive regulation of podosome assembly; IDA:MGI.
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:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:2000401; P:regulation of lymphocyte migration; ISO:MGI.
DR GO; GO:1902115; P:regulation of organelle assembly; ISO:MGI.
DR GO; GO:0070489; P:T cell aggregation; ISS:UniProtKB.
DR GO; GO:0072678; P:T cell migration; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; ISS: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 3D-structure; Acetylation; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
KW S-nitrosylation.
FT CHAIN 1..577
FT /note="Moesin"
FT /id="PRO_0000219417"
FT DOMAIN 2..295
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 322..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 115..120
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT COMPBIAS 358..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 83
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26043"
FT MOD_RES 116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 117
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 558
FT /note="Phosphothreonine; by ROCK2 and STK10"
FT /evidence="ECO:0000269|PubMed:9456324,
FT ECO:0000269|PubMed:9856983"
FT MUTAGEN 558
FT /note="T->A: Diminishes the number of microvilli-like
FT structures."
FT /evidence="ECO:0000269|PubMed:9856983"
FT MUTAGEN 558
FT /note="T->D: No effect on microvilli-like structures."
FT /evidence="ECO:0000269|PubMed:9856983"
FT CONFLICT 331..332
FT /note="EL -> DV (in Ref. 5; AAA39728)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..372
FT /note="RA -> SP (in Ref. 5; AAA39728)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:4YL8"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:4YL8"
FT TURN 144..149
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:4YL8"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:4YL8"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:4YL8"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 274..294
FT /evidence="ECO:0007829|PDB:4YL8"
SQ SEQUENCE 577 AA; 67767 MW; 4E9B5521313EF5B5 CRC64;
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKAFSTWLK
LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE
TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR
GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK LKQIEEQTKK
AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLASE
MAELTARISQ LEMARKKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEH
DEQDENGAEA SAELRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM
