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Protein

Moesin

Gene

Msn

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

Functioni

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

GO - Molecular functioni

  • actin binding Source: RGD
  • protein binding, bridging Source: RGD

GO - Biological processi

Names & Taxonomyi

Protein namesi
Recommended name:
MoesinBy similarity
Alternative name(s):
Membrane-organizing extension spike protein
Gene namesi
Name:MsnImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621260. 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194191 – 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 residuei116PhosphotyrosineBy similarity1
Modified residuei117S-nitrosocysteineBy similarity1
Modified residuei139N6-acetyllysineBy similarity1
Modified residuei146PhosphotyrosineBy similarity1
Modified residuei165N6-acetyllysineBy similarity1
Modified residuei407PhosphoserineCombined sources1
Modified residuei527PhosphoserineBy similarity1
Modified residuei558Phosphothreonine; by ROCK2 and STK10By similarity1

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
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

PaxDbiO35763.
PRIDEiO35763.

2D gel databases

World-2DPAGEi0004:O35763.

PTM databases

iPTMnetiO35763.
PhosphoSitePlusiO35763.

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

GO - Molecular functioni

  • actin binding Source: RGD
  • protein binding, bridging Source: RGD

Protein-protein interaction databases

BioGridi249518. 2 interactors.
CORUMiO35763.
IntActiO35763. 4 interactors.
MINTiMINT-4571444.
STRINGi10116.ENSRNOP00000043519.

Structurei

3D structure databases

ProteinModelPortaliO35763.
SMRiO35763.
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.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiO35763.
KOiK05763.
PhylomeDBiO35763.

Family and domain databases

CDDicd14473. FERM_B-lobe. 1 hit.
Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 1 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_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
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.
SSF50729. SSF50729. 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.

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:
EMBLi
GenBanki
DDBJi
Links Updated
AF004811 mRNA. Translation: AAB61666.1.
RefSeqiNP_110490.1. NM_030863.1.
UniGeneiRn.2762.

Genome annotation databases

GeneIDi81521.
KEGGirno:81521.

Similar proteinsi

Entry informationi

Entry nameiMOES_RAT
AccessioniPrimary (citable) accession number: O35763
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 141 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

Complete proteome, Direct protein sequencing, Reference proteome