P26041 (MOES_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Moesin

Alternative name(s):
Membrane-organizing extension spike protein

Gene names

Name:

Msn

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in connections of major cytoskeletal structures to the plasma membrane.
Enzyme regulation	A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding. Ref.7
Subunit structure	Binds SLC9A3R1 By similarity. In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation. Interacts with PPP1R16B By similarity. Interacts with PDZD8 By similarity. Interacts with SELPLG and SYK; mediates the activation of SYK by SELPLG By similarity. Ref.8
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection › microvillus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment By similarity. Ref.6
Post-translational modification	Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization By similarity. Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding.
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	leukocyte cell-cell adhesion Inferred from electronic annotation. Source: Compara leukocyte migration Inferred from electronic annotation. Source: Compara membrane to membrane docking Inferred from electronic annotation. Source: Compara regulation of lymphocyte migration Inferred from electronic annotation. Source: Compara
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 14625387. Source: MGI basolateral plasma membrane Inferred from direct assay PubMed 14625387. Source: MGI cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: InterPro filopodium Inferred from electronic annotation. Source: Compara focal adhesion Inferred from electronic annotation. Source: Compara microvillus membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: Compara uropod Inferred from direct assay PubMed 11728336. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 577	576	Moesin		PRO_0000219417
Regions
	Domain	2 – 295	294	FERM
Amino acid modifications
	Modified residue	79	1	N6-acetyllysine By similarity
	Modified residue	116	1	Phosphotyrosine Ref.10
	Modified residue	139	1	N6-acetyllysine By similarity
	Modified residue	558	1	Phosphothreonine; by ROCK2 and STK10 Ref.6 Ref.7 Ref.12
	Modified residue	576	1	Phosphoserine Ref.9 Ref.11
Experimental info
	Mutagenesis	558	1	T → A: Diminishes the number of microvilli-like structures. Ref.6
	Mutagenesis	558	1	T → D: No effect on microvilli-like structures. Ref.6
	Sequence conflict	331 – 332	2	EL → DV in AAA39728. Ref.5
	Sequence conflict	371 – 372	2	RA → SP in AAA39728. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P26041 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4E9B5521313EF5B5	FASTA	577	67,767
	10 20 30 40 50 60 MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKAFSTWLK 70 80 90 100 110 120 LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE 130 140 150 160 170 180 TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR 190 200 210 220 230 240 GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF 250 260 270 280 290 300 PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI 310 320 330 340 350 360 EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK LKQIEEQTKK 370 380 390 400 410 420 AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLASE 430 440 450 460 470 480 MAELTARISQ LEMARKKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEH 490 500 510 520 530 540 DEQDENGAEA SAELRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA 550 560 570 NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites." Sato N., Funayama N., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S. J. Cell Sci. 103:131-143(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Forelimb and Thymus.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[5]	"Moesin, a new cytoskeletal protein and constituent of filopodia: its role in cellular functions." Furthmayr H., Lankes W.T., Amieva M.R. Kidney Int. 41:665-670(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-577.
[6]	"Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures." Oshiro N., Fukata Y., Kaibuchi K. J. Biol. Chem. 273:34663-34666(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-558, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-558.
[7]	"Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association." Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K., Tsukita S., Tsukita S. J. Cell Biol. 140:647-657(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-558, ENZYME REGULATION.
[8]	"Negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly." Itoh K., Sakakibara M., Yamasaki S., Takeuchi A., Arase H., Miyazaki M., Nakajima N., Okada M., Saito T. J. Immunol. 168:541-544(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SLC9A3R1 AND PAG1.
[9]	"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line." Shu H., Chen S., Bi Q., Mumby M., Brekken D.L. Mol. Cell. Proteomics 3:279-286(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[10]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, MASS SPECTROMETRY. Tissue: Mast cell.
[11]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY. Tissue: Melanoma.
[12]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-558, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S47577 mRNA. Translation: AAA11762.1. AK031171 mRNA. Translation: BAC27288.1. AK088336 mRNA. Translation: BAC40290.1. AK133819 mRNA. Translation: BAE21861.1. AK145746 mRNA. Translation: BAE26623.1. AK150869 mRNA. Translation: BAE29920.1. AK153210 mRNA. Translation: BAE31809.1. AL805963 Genomic DNA. Translation: CAM27501.1. BC047366 mRNA. Translation: AAH47366.1. M86390 mRNA. Translation: AAA39728.1.
IPI	IPI00110588.
RefSeq	NP_034963.2. NM_010833.2.
UniGene	Mm.138876.
3D structure databases
ProteinModelPortal	P26041.
SMR	P26041. Positions 3-577.
ModBase	Search...
PTM databases
PhosphoSite	P26041.
Proteomic databases
PaxDb	P26041.
PRIDE	P26041.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000117399; ENSMUSP00000113071; ENSMUSG00000031207.
GeneID	17698.
KEGG	mmu:17698.
UCSC	uc009tug.1. mouse.
Organism-specific databases
CTD	4478.
MGI	MGI:97167. Msn.
Phylogenomic databases
eggNOG	NOG236035.
GeneTree	ENSGT00650000092953.
HOGENOM	HOG000007113.
HOVERGEN	HBG002185.
InParanoid	B1AX70.
KO	K05763.
OrthoDB	EOG4C5CJJ.
Gene expression databases
ArrayExpress	P26041.
Bgee	P26041.
CleanEx	MM_MSN.
Genevestigator	P26041.
GermOnline	ENSMUSG00000031207. Mus musculus.
Family and domain databases
Gene3D	1.20.80.10. 1 hit. 2.30.29.30. 1 hit.
InterPro	IPR019749. Band_41_domain. IPR019750. Band_41_fam. IPR011174. ERM. IPR011259. ERM_C_dom. IPR000798. Ez/rad/moesin_like. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR019747. FERM_CS. IPR000299. FERM_domain. IPR018979. FERM_N. IPR018980. FERM_PH-like_C. IPR008954. Moesin. IPR011993. PH_like_dom. [Graphical view]
Pfam	PF00769. ERM. 1 hit. PF09380. FERM_C. 1 hit. PF00373. FERM_M. 1 hit. PF09379. FERM_N. 1 hit. [Graphical view]
PIRSF	PIRSF002305. ERM. 1 hit.
PRINTS	PR00935. BAND41. PR00661. ERMFAMILY.
SMART	SM00295. B41. 1 hit. [Graphical view]
SUPFAM	SSF47031. FERM_3-hlx. 1 hit. SSF48678. Moesin. 1 hit.
PROSITE	PS00660. FERM_1. 1 hit. PS00661. FERM_2. 1 hit. PS50057. FERM_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MSN. mouse.
NextBio	292286.
SOURCE	Search...

Entry information

Entry name

MOES_MOUSE

Accession

Primary (citable) accession number: P26041
Secondary accession number(s): B1AX70, Q3UL28, Q8BSN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program