Moesin - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

O35763 (MOES_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Moesin

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

Gene names

Name:

Msn

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 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. 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. 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.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	T-tubule Inferred from direct assay PubMed 19028724. Source: RGD apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell surface Inferred from direct assay Ref.1. Source: RGD cell tip Inferred from direct assay PubMed 17061246. Source: RGD cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: InterPro filopodium membrane Inferred from direct assay Ref.1. Source: RGD internal side of plasma membrane Inferred from direct assay Ref.1. Source: RGD microvillus membrane Inferred from electronic annotation. Source: UniProtKB-SubCell secretory granule membrane Inferred from direct assay Ref.1. Source: RGD
Molecular_function	actin binding Inferred from direct assay Ref.1. Source: RGD protein binding, bridging Traceable author statement PubMed 12900915. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 577

576

Moesin

PRO_0000219419

Regions

Domain

2 – 295

294

FERM

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

116

Phosphotyrosine By similarity

Modified residue

139

N6-acetyllysine By similarity

Modified residue

558

Phosphothreonine; by ROCK2 and STK10 By similarity

Modified residue

576

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O35763 [UniParc].

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

FASTA

577

67,739

        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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF004811 mRNA. Translation: AAB61666.1.
IPI	IPI00212314.
RefSeq	NP_110490.1. NM_030863.1.
UniGene	Rn.2762.
3D structure databases
ProteinModelPortal	O35763.
SMR	O35763. Positions 1-396, 488-577.
ModBase	Search...
Protein-protein interaction databases
IntAct	O35763. 3 interactions.
MINT	MINT-4571444.
STRING	10116.ENSRNOP00000043519.
PTM databases
PhosphoSite	O35763.
2D gel databases
World-2DPAGE	0004:O35763.
Proteomic databases
PaxDb	O35763.
PRIDE	O35763.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	81521.
KEGG	rno:81521.
Organism-specific databases
CTD	4478.
RGD	621260. Msn.
Phylogenomic databases
eggNOG	NOG236035.
HOGENOM	HOG000007113.
HOVERGEN	HBG002185.
InParanoid	O35763.
KO	K05763.
OrthoDB	EOG4C5CJJ.
Gene expression databases
ArrayExpress	O35763.
Genevestigator	O35763.
GermOnline	ENSRNOG00000030118. Rattus norvegicus.
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
NextBio	615037.

Entry information

Entry name

MOES_RAT

Accession

Primary (citable) accession number: O35763

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents