Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O35763 (MOES_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Moesin
Alternative name(s):
Membrane-organizing extension spike protein
Gene names
Name:Msn
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity.

Subunit structure

Binds SLC9A3R1. In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation. Interacts with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK; mediates the activation of SYK by SELPLG By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionmicrovillus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. 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.

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. Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization By similarity.

Sequence similarities

Contains 1 FERM domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 577576Moesin
PRO_0000219419

Regions

Domain2 – 295294FERM

Amino acid modifications

Modified residue791N6-acetyllysine By similarity
Modified residue1161Phosphotyrosine By similarity
Modified residue1391N6-acetyllysine By similarity
Modified residue1651N6-acetyllysine By similarity
Modified residue5581Phosphothreonine; by ROCK2 and STK10 By similarity

Sequences

Sequence LengthMass (Da)Tools
O35763 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 49F47973D6C8FDC8

FASTA57767,739
        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 
MAELTARVSQ LEMARKKKES EAEECHQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEH 

       490        500        510        520        530        540 
DEQDENGAEA SAELRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTT 

       550        560        570 
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM 

« Hide

References

[1]"Cloning and cellular localization of the rat mast cell 78-kDa protein phosphorylated in response to the mast cell 'stabilizer' cromolyn."
Theoharides T.C., Wang L., Pang X., Letourneau R., Culm K.E., Basu S., Wang Y., Correia I.
J. Pharmacol. Exp. Ther. 294:810-821(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION.
[2]Lubec G., Afjehi-Sadat L.
Submitted (DEC-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 262-272, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004811 mRNA. Translation: AAB61666.1.
RefSeqNP_110490.1. NM_030863.1.
UniGeneRn.2762.

3D structure databases

ProteinModelPortalO35763.
SMRO35763. Positions 1-396, 488-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249518. 2 interactions.
IntActO35763. 4 interactions.
MINTMINT-4571444.
STRING10116.ENSRNOP00000043519.

PTM databases

PhosphoSiteO35763.

2D gel databases

World-2DPAGE0004:O35763.

Proteomic databases

PaxDbO35763.
PRIDEO35763.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81521.
KEGGrno:81521.

Organism-specific databases

CTD4478.
RGD621260. Msn.

Phylogenomic databases

eggNOGNOG236035.
HOGENOMHOG000007113.
HOVERGENHBG002185.
InParanoidO35763.
KOK05763.
PhylomeDBO35763.

Gene expression databases

GenevestigatorO35763.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. 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_tail.
IPR011993. PH_like_dom.
[Graphical view]
PfamPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFPIRSF002305. ERM. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615037.

Entry information

Entry nameMOES_RAT
AccessionPrimary (citable) accession number: O35763
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families