MOES_HUMAN
ID MOES_HUMAN Reviewed; 577 AA.
AC P26038;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Moesin {ECO:0000303|PubMed:1924289};
DE AltName: Full=Membrane-organizing extension spike protein;
GN Name=MSN {ECO:0000312|HGNC:HGNC:7373};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-16; 54-60 AND
RP 414-435.
RC TISSUE=Placenta;
RX PubMed=1924289; DOI=10.1073/pnas.88.19.8297;
RA Lankes W.T., Furthmayr H.;
RT "Moesin: a member of the protein 4.1-talin-ezrin family of proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8297-8301(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP INTERACTION WITH CD46, AND SUBCELLULAR LOCATION.
RX PubMed=7884872; DOI=10.1128/jvi.69.4.2248-2256.1995;
RA Schneider-Schaulies J., Dunster L.M., Schwartz-Albiez R., Krohne G.,
RA ter Meulen V.;
RT "Physical association of moesin and CD46 as a receptor complex for measles
RT virus.";
RL J. Virol. 69:2248-2256(1995).
RN [6]
RP INTERACTION WITH SLC9A3R1.
RX PubMed=9314537; DOI=10.1083/jcb.139.1.169;
RA Reczek D., Berryman M., Bretscher A.;
RT "Identification of EBP50: a PDZ-containing phosphoprotein that associates
RT with members of the ezrin-radixin-moesin family.";
RL J. Cell Biol. 139:169-179(1997).
RN [7]
RP INTERACTION WITH HIV-1 ENVELOPE PROTEIN GP120.
RX PubMed=9213396; DOI=10.1016/s0168-1702(97)00039-7;
RA Hecker C., Weise C., Schneider-Schaulies J., Holmes H.C., ter Meulen V.;
RT "Specific binding of HIV-1 envelope protein gp120 to the structural
RT membrane proteins ezrin and moesin.";
RL Virus Res. 49:215-223(1997).
RN [8]
RP FUNCTION, INTERACTION WITH ICAM3 AND CD44, AND SUBCELLULAR LOCATION.
RX PubMed=9298994; DOI=10.1083/jcb.138.6.1409;
RA Serrador J.M., Alonso-Lebrero J.L., del Pozo M.A., Furthmayr H.,
RA Schwartz-Albiez R., Calvo J., Lozano F., Sanchez-Madrid F.;
RT "Moesin interacts with the cytoplasmic region of intercellular adhesion
RT molecule-3 and is redistributed to the uropod of T lymphocytes during cell
RT polarization.";
RL J. Cell Biol. 138:1409-1423(1997).
RN [9]
RP FUNCTION, AND INTERACTION WITH SPN/CD43 CYTOPLASMIC TAIL.
RX PubMed=9616160;
RA Serrador J.M., Nieto M., Alonso-Lebrero J.L., del Pozo M.A., Calvo J.,
RA Furthmayr H., Schwartz-Albiez R., Lozano F., Gonzalez-Amaro R.,
RA Sanchez-Mateos P., Sanchez-Madrid F.;
RT "CD43 interacts with moesin and ezrin and regulates its redistribution to
RT the uropods of T lymphocytes at the cell-cell contacts.";
RL Blood 91:4632-4644(1998).
RN [10]
RP FUNCTION, MUTAGENESIS OF THR-558, AND INTERACTION WITH F-ACTIN.
RX PubMed=10212266; DOI=10.1074/jbc.274.18.12803;
RA Huang L., Wong T.Y., Lin R.C., Furthmayr H.;
RT "Replacement of threonine 558, a critical site of phosphorylation of moesin
RT in vivo, with aspartate activates F-actin binding of moesin. Regulation by
RT conformational change.";
RL J. Biol. Chem. 274:12803-12810(1999).
RN [11]
RP FUNCTION, INTERACTION WITH SPN/CD43 CYTOPLASMIC TAIL, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11728332; DOI=10.1016/s1074-7613(01)00231-x;
RA Delon J., Kaibuchi K., Germain R.N.;
RT "Exclusion of CD43 from the immunological synapse is mediated by
RT phosphorylation-regulated relocation of the cytoskeletal adaptor moesin.";
RL Immunity 15:691-701(2001).
RN [12]
RP INTERACTION WITH SELPLG AND SYK, AND FUNCTION.
RX PubMed=12387735; DOI=10.1016/s1074-7613(02)00420-x;
RA Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A.,
RA Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J.,
RA Sanchez-Madrid F.;
RT "ITAM-based interaction of ERM proteins with Syk mediates signaling by the
RT leukocyte adhesion receptor PSGL-1.";
RL Immunity 17:401-412(2002).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15039356; DOI=10.1128/iai.72.4.2312-2320.2004;
RA Iontcheva I., Amar S., Zawawi K.H., Kantarci A., Van Dyke T.E.;
RT "Role for moesin in lipopolysaccharide-stimulated signal transduction.";
RL Infect. Immun. 72:2312-2320(2004).
RN [14]
RP INTERACTION WITH PDPN.
RX PubMed=17046996; DOI=10.1242/jcs.03218;
RA Martin-Villar E., Megias D., Castel S., Yurrita M.M., Vilaro S.,
RA Quintanilla M.;
RT "Podoplanin binds ERM proteins to activate RhoA and promote epithelial-
RT mesenchymal transition.";
RL J. Cell Sci. 119:4541-4553(2006).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1R16B.
RX PubMed=18586956; DOI=10.1152/ajplung.00325.2007;
RA Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G.,
RA Verin A.D.;
RT "TIMAP is a positive regulator of pulmonary endothelial barrier function.";
RL Am. J. Physiol. 295:L440-L450(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP PHOSPHORYLATION AT THR-558, AND MUTAGENESIS OF TYR-556 AND THR-558.
RX PubMed=19255442; DOI=10.1073/pnas.0805963106;
RA Belkina N.V., Liu Y., Hao J.J., Karasuyama H., Shaw S.;
RT "LOK is a major ERM kinase in resting lymphocytes and regulates
RT cytoskeletal rearrangement through ERM phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4707-4712(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-139, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP FUNCTION, AND INTERACTION WITH PDZD8.
RX PubMed=21549406; DOI=10.1016/j.virol.2011.04.006;
RA Henning M.S., Stiedl P., Barry D.S., McMahon R., Morham S.G., Walsh D.,
RA Naghavi M.H.;
RT "PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that
RT suppresses infection by herpes simplex virus type 1.";
RL Virology 415:114-121(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-407 AND SER-527, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP S-NITROSYLATION AT CYS-117, MUTAGENESIS OF ILE-115 AND GLU-120, AND DOMAIN.
RX PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
RA Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L., Fox P.L.;
RT "Target-selective protein S-nitrosylation by sequence motif recognition.";
RL Cell 159:623-634(2014).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-577.
RX PubMed=10847681; DOI=10.1016/s0092-8674(00)80836-3;
RA Pearson M.A., Reczek D., Bretscher A., Karplus P.A.;
RT "Structure of the ERM protein moesin reveals the FERM domain fold masked by
RT an extended actin binding tail domain.";
RL Cell 101:259-270(2000).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-346.
RX PubMed=11401550; DOI=10.1021/bi010419h;
RA Edwards S.D., Keep N.H.;
RT "The 2.7 A crystal structure of the activated FERM domain of moesin: an
RT analysis of structural changes on activation.";
RL Biochemistry 40:7061-7068(2001).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-297 IN COMPLEX WITH SLC9A3R1.
RX PubMed=15020681; DOI=10.1242/jcs.01038;
RA Finnerty C.M., Chambers D., Ingraffea J., Faber H.R., Karplus P.A.,
RA Bretscher A.;
RT "The EBP50-moesin interaction involves a binding site regulated by direct
RT masking on the FERM domain.";
RL J. Cell Sci. 117:1547-1552(2004).
RN [30]
RP VARIANT IMD50 TRP-171, CHARACTERIZATION OF VARIANT IMD50 TRP-171, AND
RP FUNCTION.
RX PubMed=27405666; DOI=10.1016/j.jaci.2016.04.032;
RA Lagresle-Peyrou C., Luce S., Ouchani F., Soheili T.S., Sadek H.,
RA Chouteau M., Durand A., Pic I., Majewski J., Brouzes C., Lambert N.,
RA Bohineust A., Verhoeyen E., Cosset F.L., Magerus-Chatinet A.,
RA Rieux-Laucat F., Gandemer V., Monnier D., Heijmans C., van Gijn M.,
RA Dalm V.A., Mahlaoui N., Stephan J.L., Picard C., Durandy A., Kracker S.,
RA Hivroz C., Jabado N., de Saint Basile G., Fischer A., Cavazzana M.,
RA Andre-Schmutz I.;
RT "X-linked primary immunodeficiency associated with hemizygous mutations in
RT the moesin (MSN) gene.";
RL J. Allergy Clin. Immunol. 138:1681-1689(2016).
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 (PubMed:10212266). Once phosphorylated on its C-terminal
CC threonine, moesin is activated leading to interaction with F-actin and
CC cytoskeletal rearrangement (PubMed:10212266). These rearrangements
CC regulate many cellular processes, including cell shape determination,
CC membrane transport, and signal transduction (PubMed:12387735,
CC PubMed:15039356). The role of moesin is particularly important in
CC immunity acting on both T and B-cells homeostasis and self-tolerance,
CC regulating lymphocyte egress from lymphoid organs (PubMed:9298994,
CC PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By
CC similarity). Participates also in immunologic synapse formation
CC (PubMed:27405666). {ECO:0000250|UniProtKB:P26041,
CC ECO:0000269|PubMed:10212266, ECO:0000269|PubMed:12387735,
CC ECO:0000269|PubMed:15039356, ECO:0000269|PubMed:27405666,
CC ECO:0000269|PubMed:9298994, ECO:0000269|PubMed:9616160}.
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:10212266}.
CC -!- SUBUNIT: In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which
CC is disrupted upon TCR activation. Interacts with SLC9A3R1
CC (PubMed:9314537, PubMed:15020681). Interacts with PPP1R16B
CC (PubMed:18586956). Interacts with PDZD8. Interacts with SELPLG and SYK;
CC these interaction mediate the activation of SYK by SELPLG
CC (PubMed:12387735). Interacts with PDPN (via cytoplasmic domain); this
CC interaction activates RHOA and promotes epithelial-mesenchymal
CC transition (PubMed:17046996). Interacts with SPN/CD43 cytoplasmic tail
CC (PubMed:9616160, PubMed:11728332). Interacts with CD44
CC (PubMed:9298994). Interacts with ICAM2 (By similarity). Interacts with
CC ICAM3 (via C-terminus) (PubMed:9298994). Interacts with PDZD8
CC (PubMed:21549406). Interacts with F-actin (PubMed:10212266). Interacts
CC with CD46 (PubMed:7884872). Interacts with PTPN6 (By similarity).
CC {ECO:0000250|UniProtKB:P26041, ECO:0000269|PubMed:10212266,
CC ECO:0000269|PubMed:11728332, ECO:0000269|PubMed:12387735,
CC ECO:0000269|PubMed:15020681, ECO:0000269|PubMed:17046996,
CC ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:21549406,
CC ECO:0000269|PubMed:7884872, ECO:0000269|PubMed:9298994,
CC ECO:0000269|PubMed:9314537, ECO:0000269|PubMed:9616160}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 envelope protein
CC gp120. {ECO:0000269|PubMed:9213396}.
CC -!- INTERACTION:
CC P26038; P16070: CD44; NbExp=6; IntAct=EBI-528768, EBI-490245;
CC P26038; P25791-3: LMO2; NbExp=3; IntAct=EBI-528768, EBI-11959475;
CC P26038; Q5S007: LRRK2; NbExp=19; IntAct=EBI-528768, EBI-5323863;
CC P26038; O14745: SLC9A3R1; NbExp=4; IntAct=EBI-528768, EBI-349787;
CC P26038; P54274: TERF1; NbExp=2; IntAct=EBI-528768, EBI-710997;
CC P26038; Q5S006: Lrrk2; Xeno; NbExp=2; IntAct=EBI-528768, EBI-2693710;
CC P26038; P97820: Map4k4; Xeno; NbExp=2; IntAct=EBI-528768, EBI-644181;
CC P26038; P0DTC2: S; Xeno; NbExp=20; IntAct=EBI-528768, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11728332,
CC ECO:0000269|PubMed:15039356, ECO:0000269|PubMed:18586956,
CC ECO:0000269|PubMed:7884872, ECO:0000269|PubMed:9298994}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P26041}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:P26041}. 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. {ECO:0000250|UniProtKB:P26041,
CC ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:9298994}.
CC -!- TISSUE SPECIFICITY: In all tissues and cultured cells studied.
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:0000305|PubMed:25417112}.
CC -!- PTM: Phosphorylation on Thr-558 is crucial for the formation of
CC microvilli-like structures. Phosphorylation by ROCK2 suppresses the
CC head-to-tail association of the N-terminal and C-terminal halves
CC resulting in an opened conformation which is capable of actin and
CC membrane-binding (By similarity). Phosphorylation on Thr-558 by STK10
CC negatively regulates lymphocyte migration and polarization.
CC {ECO:0000250, ECO:0000269|PubMed:19255442}.
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:0000269|PubMed:25417112}.
CC -!- DISEASE: Immunodeficiency 50 (IMD50) [MIM:300988]: A primary
CC immunodeficiency disorder characterized by onset of recurrent bacterial
CC or varicella zoster virus infections in early childhood, profound
CC lymphopenia, hypogammaglobulinemia, fluctuating monocytopenia and
CC neutropenia, and a poor immune response to vaccine antigens.
CC {ECO:0000269|PubMed:27405666}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MSNID363.html";
CC ---------------------------------------------------------------------------
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DR EMBL; M69066; AAA36322.1; -; mRNA.
DR EMBL; Z98946; CAB46379.1; -; Genomic_DNA.
DR EMBL; BC017293; AAH17293.1; -; mRNA.
DR CCDS; CCDS14382.1; -.
DR PIR; A41289; A41289.
DR RefSeq; NP_002435.1; NM_002444.2.
DR PDB; 1E5W; X-ray; 2.70 A; A=2-346.
DR PDB; 1EF1; X-ray; 1.90 A; A/B=4-297, C/D=488-577.
DR PDB; 1SGH; X-ray; 3.50 A; A=1-297.
DR PDB; 6TXQ; X-ray; 1.73 A; AAA=1-346.
DR PDB; 6TXS; X-ray; 2.20 A; AAA=1-346.
DR PDBsum; 1E5W; -.
DR PDBsum; 1EF1; -.
DR PDBsum; 1SGH; -.
DR PDBsum; 6TXQ; -.
DR PDBsum; 6TXS; -.
DR AlphaFoldDB; P26038; -.
DR SMR; P26038; -.
DR BioGRID; 110584; 176.
DR DIP; DIP-33841N; -.
DR IntAct; P26038; 50.
DR MINT; P26038; -.
DR STRING; 9606.ENSP00000353408; -.
DR ChEMBL; CHEMBL4295733; -.
DR GlyGen; P26038; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P26038; -.
DR MetOSite; P26038; -.
DR PhosphoSitePlus; P26038; -.
DR SwissPalm; P26038; -.
DR BioMuta; MSN; -.
DR DMDM; 127234; -.
DR OGP; P26038; -.
DR CPTAC; CPTAC-94; -.
DR EPD; P26038; -.
DR jPOST; P26038; -.
DR MassIVE; P26038; -.
DR PaxDb; P26038; -.
DR PeptideAtlas; P26038; -.
DR PRIDE; P26038; -.
DR ProteomicsDB; 54311; -.
DR TopDownProteomics; P26038; -.
DR Antibodypedia; 2774; 1022 antibodies from 43 providers.
DR CPTC; P26038; 3 antibodies.
DR DNASU; 4478; -.
DR Ensembl; ENST00000360270.7; ENSP00000353408.5; ENSG00000147065.17.
DR GeneID; 4478; -.
DR KEGG; hsa:4478; -.
DR MANE-Select; ENST00000360270.7; ENSP00000353408.5; NM_002444.3; NP_002435.1.
DR CTD; 4478; -.
DR DisGeNET; 4478; -.
DR GeneCards; MSN; -.
DR HGNC; HGNC:7373; MSN.
DR HPA; ENSG00000147065; Low tissue specificity.
DR MalaCards; MSN; -.
DR MIM; 300988; phenotype.
DR MIM; 309845; gene.
DR neXtProt; NX_P26038; -.
DR OpenTargets; ENSG00000147065; -.
DR Orphanet; 504530; Combined immunodeficiency due to Moesin deficiency.
DR PharmGKB; PA31178; -.
DR VEuPathDB; HostDB:ENSG00000147065; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; P26038; -.
DR OMA; WADHKNT; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; P26038; -.
DR TreeFam; TF313935; -.
DR PathwayCommons; P26038; -.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; P26038; -.
DR SIGNOR; P26038; -.
DR BioGRID-ORCS; 4478; 16 hits in 709 CRISPR screens.
DR ChiTaRS; MSN; human.
DR EvolutionaryTrace; P26038; -.
DR GeneWiki; Moesin; -.
DR GenomeRNAi; 4478; -.
DR Pharos; P26038; Tbio.
DR PRO; PR:P26038; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P26038; protein.
DR Bgee; ENSG00000147065; Expressed in lower lobe of lung and 210 other tissues.
DR ExpressionAtlas; P26038; baseline and differential.
DR Genevisible; P26038; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:BHF-UCL.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0031143; C:pseudopodium; IDA:UniProtKB.
DR GO; GO:0001931; C:uropod; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IDA:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; IGI:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0022612; P:gland morphogenesis; IMP:UniProtKB.
DR GO; GO:0001771; P:immunological synapse formation; IDA:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEP:BHF-UCL.
DR GO; GO:0050900; P:leukocyte migration; IEP:BHF-UCL.
DR GO; GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IGI:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:UniProtKB.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IGI:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; IMP:UniProtKB.
DR GO; GO:2000401; P:regulation of lymphocyte migration; IMP:UniProtKB.
DR GO; GO:1902115; P:regulation of organelle assembly; IGI:UniProtKB.
DR GO; GO:0070489; P:T cell aggregation; IDA:UniProtKB.
DR GO; GO:0072678; P:T cell migration; IDA:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; IDA: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 IDEAL; IID00344; -.
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; Direct protein sequencing; Disease variant;
KW Host-virus interaction; Membrane; Phosphoprotein; Reference proteome;
KW S-nitrosylation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:1924289"
FT CHAIN 2..577
FT /note="Moesin"
FT /id="PRO_0000219416"
FT DOMAIN 2..295
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 323..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..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:0000305|PubMed:25417112"
FT COMPBIAS 488..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
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:19690332"
FT MOD_RES 117
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:25417112"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26041"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 558
FT /note="Phosphothreonine; by ROCK2 and STK10"
FT /evidence="ECO:0000269|PubMed:19255442"
FT VARIANT 171
FT /note="R -> W (in IMD50; decreased protein abundance in T
FT cell; loss of T cell proliferation after T cell activation;
FT does not affect immunologic synapses formation; decreased T
FT cell migration in response to activation by chemokines;
FT increased T cell adhesion in response to activation by
FT integrins; dbSNP:rs1057519074)"
FT /evidence="ECO:0000269|PubMed:27405666"
FT /id="VAR_078026"
FT MUTAGEN 115
FT /note="I->M: Inhibits S-nitrosylation of Cys-117; when
FT associated with M-120."
FT /evidence="ECO:0000269|PubMed:25417112"
FT MUTAGEN 120
FT /note="E->M: Inhibits S-nitrosylation of Cys-117; when
FT associated with M-115."
FT /evidence="ECO:0000269|PubMed:25417112"
FT MUTAGEN 556
FT /note="Y->R: Impairs phosphorylation by STK10."
FT /evidence="ECO:0000269|PubMed:19255442"
FT MUTAGEN 558
FT /note="T->A: Abolishes phosphorylation by STK10."
FT /evidence="ECO:0000269|PubMed:19255442"
FT MUTAGEN 558
FT /note="T->D: Completely abolishes the interaction between
FT N- and C-terminal domains."
FT /evidence="ECO:0000269|PubMed:10212266"
FT MUTAGEN 558
FT /note="T->D: Phosphomimetic mutant."
FT /evidence="ECO:0000269|PubMed:19255442"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:1EF1"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1EF1"
FT TURN 144..149
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:1EF1"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:1EF1"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:1EF1"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 274..295
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 301..343
FT /evidence="ECO:0007829|PDB:1E5W"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 516..530
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 540..550
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 555..562
FT /evidence="ECO:0007829|PDB:1EF1"
FT HELIX 567..575
FT /evidence="ECO:0007829|PDB:1EF1"
SQ SEQUENCE 577 AA; 67820 MW; 865A6C5CB14AE586 CRC64;
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKGFSTWLK
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 AMLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK
AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLALE
MAELTARISQ LEMARQKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEQ
DEQDENGAEA SADLRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM
