Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Moesin

Gene

Msn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Probably involved in connections of major cytoskeletal structures to the plasma membrane. Plays a role in regulating the proliferation, migration, and adhesion of human lymphoid cells and participates in immunologic synapse formation.By similarity

Enzyme regulationi

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.1 Publication

GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-MMU-437239 Recycling pathway of L1

Names & Taxonomyi

Protein namesi
Recommended name:
Moesin1 Publication
Alternative name(s):
Membrane-organizing extension spike protein
Gene namesi
Name:MsnImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:97167 Msn

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi558T → A: Diminishes the number of microvilli-like structures. 1 Publication1
Mutagenesisi558T → D: No effect on microvilli-like structures. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194171 – 577MoesinAdd BLAST577

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei74PhosphoserineBy similarity1
Modified residuei79N6-acetyllysineBy similarity1
Modified residuei83N6-succinyllysineBy similarity1
Modified residuei116PhosphotyrosineCombined sources1
Modified residuei117S-nitrosocysteineBy similarity1
Modified residuei139N6-acetyllysineBy similarity1
Modified residuei146PhosphotyrosineBy similarity1
Modified residuei165N6-acetyllysineCombined sources1
Modified residuei407PhosphoserineBy similarity1
Modified residuei527PhosphoserineCombined sources1
Modified residuei558Phosphothreonine; by ROCK2 and STK102 Publications1

Post-translational modificationi

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.By similarity2 Publications
S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP26041
MaxQBiP26041
PaxDbiP26041
PeptideAtlasiP26041
PRIDEiP26041

PTM databases

CarbonylDBiP26041
iPTMnetiP26041
PhosphoSitePlusiP26041
SwissPalmiP26041

Expressioni

Gene expression databases

BgeeiENSMUSG00000031207
CleanExiMM_MSN
GenevisibleiP26041 MM

Interactioni

Subunit structurei

Binds SLC9A3R1 (By similarity). In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation (PubMed:11777944). Interacts with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK; mediates the activation of SYK by SELPLG. Interacts with PDPN (via cytoplasmic domain); activates RHOA and promotes epithelial-mesenchymal transition (By similarity). Interacts with SPN, CD44 and ICAM2 (PubMed:9472040).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi20153423 interactors.
IntActiP26041 26 interactors.
MINTiP26041
STRINGi10090.ENSMUSP00000113071

Structurei

Secondary structure

1577
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Beta strandi15 – 20Combined sources6
Helixi26 – 37Combined sources12
Helixi42 – 44Combined sources3
Beta strandi45 – 51Combined sources7
Beta strandi56 – 58Combined sources3
Helixi65 – 67Combined sources3
Beta strandi74 – 84Combined sources11
Helixi89 – 92Combined sources4
Helixi96 – 111Combined sources16
Helixi119 – 134Combined sources16
Turni139 – 141Combined sources3
Turni144 – 149Combined sources6
Helixi155 – 160Combined sources6
Helixi165 – 178Combined sources14
Turni179 – 181Combined sources3
Helixi184 – 195Combined sources12
Turni199 – 202Combined sources4
Beta strandi204 – 209Combined sources6
Beta strandi215 – 221Combined sources7
Beta strandi224 – 229Combined sources6
Beta strandi233 – 235Combined sources3
Beta strandi237 – 241Combined sources5
Helixi242 – 244Combined sources3
Beta strandi245 – 251Combined sources7
Beta strandi254 – 261Combined sources8
Beta strandi267 – 270Combined sources4
Helixi274 – 294Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YL8X-ray1.50A1-297[»]
ProteinModelPortaliP26041
SMRiP26041
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 295FERMPROSITE-ProRule annotationAdd BLAST294

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi115 – 120[IL]-x-C-x-x-[DE] motifBy similarity6

Domaini

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.By similarity

Phylogenomic databases

eggNOGiKOG3529 Eukaryota
ENOG410XQFP LUCA
GeneTreeiENSGT00890000139341
HOGENOMiHOG000007113
HOVERGENiHBG002185
InParanoidiP26041
KOiK05763
OMAiMKNQEHL
OrthoDBiEOG091G06UO
PhylomeDBiP26041
TreeFamiTF313935

Family and domain databases

CDDicd14473 FERM_B-lobe, 1 hit
Gene3Di1.20.80.101 hit
1.25.40.10201 hit
2.30.29.301 hit
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR011174 ERM
IPR011259 ERM_C_dom
IPR000798 Ez/rad/moesin-like
IPR014352 FERM/acyl-CoA-bd_prot_sf
IPR035963 FERM_2
IPR019748 FERM_central
IPR019747 FERM_CS
IPR000299 FERM_domain
IPR018979 FERM_N
IPR018980 FERM_PH-like_C
IPR008954 Moesin_tail_sf
IPR011993 PH-like_dom_sf
IPR029071 Ubiquitin-like_domsf
PfamiView protein in Pfam
PF00769 ERM, 1 hit
PF09380 FERM_C, 1 hit
PF00373 FERM_M, 1 hit
PF09379 FERM_N, 1 hit
PIRSFiPIRSF002305 ERM, 1 hit
PRINTSiPR00935 BAND41
PR00661 ERMFAMILY
SMARTiView protein in SMART
SM00295 B41, 1 hit
SM01196 FERM_C, 1 hit
SUPFAMiSSF47031 SSF47031, 1 hit
SSF48678 SSF48678, 1 hit
SSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS00660 FERM_1, 1 hit
PS00661 FERM_2, 1 hit
PS50057 FERM_3, 1 hit

Sequencei

Sequence statusi: Complete.

P26041-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ
60 70 80 90 100
DTKAFSTWLK LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR
110 120 130 140 150
LFFLQVKEGI LNDDIYCPPE TAVLLASYAV QSKYGDFNKE VHKSGYLAGD
160 170 180 190 200
KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR GMLREDAVLE YLKIAQDLEM
210 220 230 240 250
YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF PWSEIRNISF
260 270 280 290 300
NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
310 320 330 340 350
EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK
360 370 380 390 400
LKQIEEQTKK AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK
410 420 430 440 450
EALLQASRDQ KKTQEQLASE MAELTARISQ LEMARKKKES EAVEWQQKAQ
460 470 480 490 500
MVQEDLEKTR AELKTAMSTP HVAEPAENEH DEQDENGAEA SAELRADAMA
510 520 530 540 550
KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA NDMIHAENMR
560 570
LGRDKYKTLR QIRQGNTKQR IDEFESM
Length:577
Mass (Da):67,767
Last modified:January 23, 2007 - v3
Checksum:i4E9B5521313EF5B5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti331 – 332EL → DV in AAA39728 (PubMed:1573844).Curated2
Sequence conflicti371 – 372RA → SP in AAA39728 (PubMed:1573844).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 No translation available.
BC047366 mRNA Translation: AAH47366.1
M86390 mRNA Translation: AAA39728.1
CCDSiCCDS53139.1
RefSeqiNP_034963.2, NM_010833.2
UniGeneiMm.138876

Genome annotation databases

EnsembliENSMUST00000117399; ENSMUSP00000113071; ENSMUSG00000031207
GeneIDi17698
KEGGimmu:17698
UCSCiuc009tug.1 mouse

Similar proteinsi

Entry informationi

Entry nameiMOES_MOUSE
AccessioniPrimary (citable) accession number: P26041
Secondary accession number(s): B1AX70, Q3UL28, Q8BSN4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 166 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome