Skip Header

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

O35763

- MOES_RAT

UniProt

O35763 - MOES_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Moesin

Gene

Msn

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Probably involved in connections of major cytoskeletal structures to the plasma membrane.

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.By similarity

GO - Molecular functioni

  1. actin binding Source: RGD
  2. protein binding, bridging Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Moesin
Alternative name(s):
Membrane-organizing extension spike protein
Gene namesi
Name:Msn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621260. Msn.

Subcellular locationi

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

GO - Cellular componenti

  1. cell surface Source: RGD
  2. cell tip Source: RGD
  3. cytoplasmic side of plasma membrane Source: RGD
  4. cytoskeleton Source: UniProtKB-KW
  5. extrinsic component of membrane Source: InterPro
  6. filopodium membrane Source: RGD
  7. secretory granule membrane Source: RGD
  8. T-tubule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 577576MoesinPRO_0000219419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei116 – 1161PhosphotyrosineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei165 – 1651N6-acetyllysineBy similarity
Modified residuei558 – 5581Phosphothreonine; by ROCK2 and STK10By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO35763.
PRIDEiO35763.

2D gel databases

World-2DPAGE0004:O35763.

PTM databases

PhosphoSiteiO35763.

Expressioni

Gene expression databases

GenevestigatoriO35763.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi249518. 2 interactions.
IntActiO35763. 4 interactions.
MINTiMINT-4571444.
STRINGi10116.ENSRNOP00000043519.

Structurei

3D structure databases

ProteinModelPortaliO35763.
SMRiO35763. Positions 1-396, 488-577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 295294FERMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG236035.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiO35763.
KOiK05763.
PhylomeDBiO35763.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. 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.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35763-1 [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 MAELTARVSQ LEMARKKKES EAEECHQKAQ
460 470 480 490 500
MVQEDLEKTR AELKTAMSTP HVAEPAENEH DEQDENGAEA SAELRADAMA
510 520 530 540 550
KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTT NDMIHAENMR
560 570
LGRDKYKTLR QIRQGNTKQR IDEFESM
Length:577
Mass (Da):67,739
Last modified:January 23, 2007 - v3
Checksum:i49F47973D6C8FDC8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF004811 mRNA. Translation: AAB61666.1.
RefSeqiNP_110490.1. NM_030863.1.
UniGeneiRn.2762.

Genome annotation databases

GeneIDi81521.
KEGGirno:81521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF004811 mRNA. Translation: AAB61666.1 .
RefSeqi NP_110490.1. NM_030863.1.
UniGenei Rn.2762.

3D structure databases

ProteinModelPortali O35763.
SMRi O35763. Positions 1-396, 488-577.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249518. 2 interactions.
IntActi O35763. 4 interactions.
MINTi MINT-4571444.
STRINGi 10116.ENSRNOP00000043519.

PTM databases

PhosphoSitei O35763.

2D gel databases

World-2DPAGE 0004:O35763.

Proteomic databases

PaxDbi O35763.
PRIDEi O35763.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 81521.
KEGGi rno:81521.

Organism-specific databases

CTDi 4478.
RGDi 621260. Msn.

Phylogenomic databases

eggNOGi NOG236035.
HOGENOMi HOG000007113.
HOVERGENi HBG002185.
InParanoidi O35763.
KOi K05763.
PhylomeDBi O35763.

Miscellaneous databases

NextBioi 615037.

Gene expression databases

Genevestigatori O35763.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProi 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_tail.
IPR011993. PH_like_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF002305. ERM. 1 hit.
PRINTSi PR00935. BAND41.
PR00661. ERMFAMILY.
SMARTi SM00295. B41. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMOES_RAT
AccessioniPrimary (citable) accession number: O35763
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3