P26038 (MOES_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. May inhibit herpes simplex virus 1 infection at an early stage. Ref.13
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 By similarity.
Subunit structure	In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation By similarity. Binds SLC9A3R1. Interacts with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK; mediates the activation of SYK by SELPLG. Ref.5 Ref.6 Ref.7 Ref.13
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton By similarity. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection › microvillus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Phosphorylated form is enriched in microvilli-like structures at apical membrane By similarity. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment. Ref.7
Tissue specificity	In all tissues and cultured cells studied.
Post-translational modification	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 By similarity. Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization.
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	leukocyte cell-cell adhesion Inferred from expression pattern PubMed 12082081. Source: BHF-UCL leukocyte migration Inferred from expression pattern PubMed 12082081. Source: BHF-UCL membrane to membrane docking Inferred from expression pattern PubMed 12082081. Source: BHF-UCL regulation of lymphocyte migration Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular_component	apical part of cell Inferred from direct assay PubMed 12082081. Source: BHF-UCL apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell basolateral plasma membrane Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay. Source: HPA cytoskeleton Traceable author statement PubMed 16130169. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB extrinsic to membrane Inferred from electronic annotation. Source: InterPro filopodium Inferred from direct assay PubMed 12082081. Source: BHF-UCL microvillus Inferred from direct assay PubMed 12082081. Source: BHF-UCL microvillus membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA uropod Inferred from electronic annotation. Source: Compara
Molecular_function	structural constituent of cytoskeleton Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LRRK2	Q5S007	5	EBI-528768,EBI-5323863
SLC9A3R1	O14745	5	EBI-528768,EBI-349787

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1 Ref.4

Chain

2 – 577

576

Moesin

PRO_0000219416

Regions

Domain

2 – 295

294

FERM

Amino acid modifications

Modified residue

79

1

N6-acetyllysine Ref.11

Modified residue

116

1

Phosphotyrosine Ref.10

Modified residue

139

1

N6-acetyllysine Ref.11

Modified residue

558

1

Phosphothreonine; by ROCK2 and STK10 Ref.9

Modified residue

576

1

Phosphoserine By similarity

Experimental info

Mutagenesis

556

1

Y → R: Impairs phosphorylation by STK10. Ref.9

Mutagenesis

558

1

T → A: Abolishes phosphorylation by STK10. Ref.9

Mutagenesis

558

1

T → D: Phosphomimetic mutant. Ref.9

Secondary structure

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577

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Beta strand

16 – 20

5

Helix

26 – 37

12

Helix

42 – 44

3

Beta strand

45 – 50

6

Beta strand

56 – 58

3

Beta strand

61 – 64

4

Helix

65 – 67

3

Beta strand

74 – 82

9

Helix

89 – 92

4

Helix

96 – 111

16

Helix

119 – 133

15

Turn

139 – 141

3

Beta strand

144 – 147

4

Turn

155 – 159

5

Helix

165 – 177

13

Turn

178 – 181

4

Helix

184 – 195

12

Turn

199 – 202

4

Beta strand

204 – 210

7

Beta strand

215 – 221

7

Beta strand

224 – 229

6

Beta strand

233 – 235

3

Beta strand

237 – 241

5

Helix

242 – 244

3

Beta strand

245 – 259

15

Beta strand

260 – 264

5

Beta strand

267 – 270

4

Helix

274 – 295

22

Helix

301 – 343

43

Sequences

	Sequence		Length	Mass (Da)
	P26038 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 865A6C5CB14AE586	FASTA	577	67,820
	10 20 30 40 50 60 MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKGFSTWLK 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 AMLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK 370 380 390 400 410 420 AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLALE 430 440 450 460 470 480 MAELTARISQ LEMARQKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEQ 490 500 510 520 530 540 DEQDENGAEA SADLRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA 550 560 570 NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Moesin: a member of the protein 4.1-talin-ezrin family of proteins." Lankes W.T., Furthmayr H. Proc. Natl. Acad. Sci. U.S.A. 88:8297-8301(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-16; 54-60 AND 414-435. Tissue: Placenta.
[2]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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]. Tissue: Pancreas.
[4]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8. Tissue: Platelet.
[5]	"Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family." Reczek D., Berryman M., Bretscher A. J. Cell Biol. 139:169-179(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SLC9A3R1.
[6]	"ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1." Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A., Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J., Sanchez-Madrid F. Immunity 17:401-412(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SELPLG AND SYK.
[7]	"TIMAP is a positive regulator of pulmonary endothelial barrier function." Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G., Verin A.D. Am. J. Physiol. 295:L440-L450(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R16B.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation." Belkina N.V., Liu Y., Hao J.J., Karasuyama H., Shaw S. Proc. Natl. Acad. Sci. U.S.A. 106:4707-4712(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-558, MUTAGENESIS OF TYR-556 AND THR-558.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-139, MASS SPECTROMETRY.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1." Henning M.S., Stiedl P., Barry D.S., McMahon R., Morham S.G., Walsh D., Naghavi M.H. Virology 415:114-121(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MSN.
[14]	"Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain." Pearson M.A., Reczek D., Bretscher A., Karplus P.A. Cell 101:259-270(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-577.
[15]	"The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation." Edwards S.D., Keep N.H. Biochemistry 40:7061-7068(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-346.
[16]	"The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain." Finnerty C.M., Chambers D., Ingraffea J., Faber H.R., Karplus P.A., Bretscher A. J. Cell Sci. 117:1547-1552(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-297 IN COMPLEX WITH SLC9A3R1.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M69066 mRNA. Translation: AAA36322.1.
Z98946 Genomic DNA. Translation: CAB46379.1.
BC017293 mRNA. Translation: AAH17293.1.

IPI

IPI00219365.

PIR

A41289.

RefSeq

NP_002435.1. NM_002444.2.

UniGene

Hs.87752.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E5W	X-ray	2.70	A	1-346	[»]
1EF1	X-ray	1.90	A/B	4-297	[»]
			C/D	488-577	[»]
1SGH	X-ray	3.50	A	1-297	[»]

ProteinModelPortal

P26038.

ModBase

Search...

Protein-protein interaction databases

IntAct

P26038. 11 interactions.

STRING

9606.ENSP00000353408.

PTM databases

PhosphoSite

P26038.

Polymorphism databases

DMDM

127234.

2D gel databases

OGP

P26038.

Proteomic databases

PaxDb

P26038.

PeptideAtlas

P26038.

PRIDE

P26038.

Protocols and materials databases

DNASU

4478.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360270; ENSP00000353408; ENSG00000147065.

GeneID

4478.

KEGG

hsa:4478.

UCSC

uc004dwf.3. human.

Organism-specific databases

CTD

4478.

GeneCards

GC0XP064887.

HGNC

HGNC:7373. MSN.

HPA

CAB010898.
CAB047338.
HPA000263.
HPA000763.
HPA011135.
HPA011227.

MIM

309845. gene.

neXtProt

NX_P26038.

PharmGKB

PA31178.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG236035.

HOGENOM

HOG000007113.

HOVERGEN

HBG002185.

InParanoid

P26038.

KO

K05763.

OMA

PHVTEPM.

OrthoDB

EOG4C5CJJ.

PhylomeDB

P26038.

Enzyme and pathway databases

Pathway_Interaction_DB

er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

Bgee

P26038.

CleanEx

HS_MSN.

Genevestigator

P26038.

GermOnline

ENSG00000147065. Homo sapiens.

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. human.

EvolutionaryTrace

P26038.

GenomeRNAi

4478.

NextBio

17331.

PMAP-CutDB

P26038.

SOURCE

Search...

Entry information

Entry name

MOES_HUMAN

Accession

Primary (citable) accession number: P26038

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.