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Protein

Merlin

Gene

Nf2

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

Functioni

Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium (By similarity).By similarity

GO - Molecular functioni

  • beta-catenin binding Source: RGD
  • integrin binding Source: RGD
  • protein domain specific binding Source: RGD

GO - Biological processi

  • negative regulation of cell growth Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Merlin
Alternative name(s):
Moesin-ezrin-radixin-like protein
Neurofibromin-2
Schwannomin
Gene namesi
Name:Nf2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3169. Nf2.

Subcellular locationi

  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cell projection By similarity
  • Cytoplasmcytoskeleton By similarity
  • Nucleus By similarity

  • Note: Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with VPRBP in the nucleus. The intramolecular association of the FERM domain with the C-terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions (By similarity).By similarity

GO - Cellular componenti

  • cell projection Source: UniProtKB-SubCell
  • cytoplasm Source: RGD
  • cytoskeleton Source: UniProtKB-SubCell
  • extrinsic component of membrane Source: InterPro
  • membrane raft Source: RGD
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • protein complex Source: RGD
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 586›586MerlinPRO_0000219415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei514 – 5141Phosphoserine; by PAKBy similarity

Post-translational modificationi

Phosphorylation of Ser-514 inhibits nuclear localization by disrupting the intramolecular association of the FERM domain with the C-terminal tail.By similarity
Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3 ubiquitin-protein ligase complex for ubiquitination and subsequent proteasome-dependent degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ63648.
PRIDEiQ63648.

PTM databases

iPTMnetiQ63648.
PhosphoSiteiQ63648.

Interactioni

Subunit structurei

Interacts with SLC9A3R1, HGS and AGAP2. Interacts with SGSM3. Interacts (via FERM domain) with MPP1 (By similarity). Interacts with LAYN and WWC1. Interacts with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The unphosphorylated form interacts (via FERM domain) with VPRBP/DCAF1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AmotD4A9Q24EBI-1013682,EBI-3892226

GO - Molecular functioni

  • beta-catenin binding Source: RGD
  • integrin binding Source: RGD
  • protein domain specific binding Source: RGD

Protein-protein interaction databases

IntActiQ63648. 3 interactions.
MINTiMINT-4571419.
STRINGi10116.ENSRNOP00000010690.

Structurei

3D structure databases

ProteinModelPortaliQ63648.
SMRiQ63648. Positions 14-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 307290FERMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi323 – 461139Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiQ63648.
KOiK16684.
PhylomeDBiQ63648.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. 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.
[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.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 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: Fragment.

Q63648-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
IASRMSFSSL KRKQPKTFTV RIVTMDAEME FNCEMKWKGK DLFDLVCRTL
60 70 80 90 100
GLRETWFFGL QYTIKDTVAW LKMDKKVLDH DVSKEEPVTF HFLAKFYPEN
110 120 130 140 150
AEEELVQEIT QHLFFLQVKK QILDEKVYCP PEASVLLASY AVQAKYGDYD
160 170 180 190 200
PSVHKRGFLA QEELLPKRVI NLYQMTPEMW EERITAWYAE HRGRARDEAE
210 220 230 240 250
MEYLKIAQDL EMYGVNYFTI RNKKGTELLL GVDALGLHIY DPENRLTPKI
260 270 280 290 300
SFPWNEIRNI SYSDKEFTIK PLDKKIDVFK FNSSKLRVNK LILQLCIGNH
310 320 330 340 350
DLFMRRRKAD SLEVQQMKAQ AREEKARKQM ERQRLAREKQ MREEAERSRD
360 370 380 390 400
EPERRVLHMK EEATMANEAL MRSEETADLL AEKAQITEEE AKLLAQKAAE
410 420 430 440 450
AEQEMQRIKA TAIRTEEEKR LMEQKVLEAE VLALKMAEES ERRAKEADQL
460 470 480 490 500
KQDLQEAREA ERRAKQKLLE IATKPTYPPM NPIPAPLPPD IPSFDIIGDS
510 520 530 540 550
LSFDFKDTDM KRLSMEIEKE KVEYMEKSKH LQEQLNELKT EIEALKLKER
560 570 580
ETALDILHSE HSDSGTSSKH NTIKKPQAQG RRPICI
Length:586
Mass (Da):68,712
Last modified:November 1, 1996 - v1
Checksum:i2385AF8461407B24
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61772 mRNA. Translation: AAC13318.1.
RefSeqiNP_037325.1. NM_013193.1.
UniGeneiRn.46695.

Genome annotation databases

GeneIDi25744.
KEGGirno:25744.
UCSCiRGD:3169. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61772 mRNA. Translation: AAC13318.1.
RefSeqiNP_037325.1. NM_013193.1.
UniGeneiRn.46695.

3D structure databases

ProteinModelPortaliQ63648.
SMRiQ63648. Positions 14-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ63648. 3 interactions.
MINTiMINT-4571419.
STRINGi10116.ENSRNOP00000010690.

PTM databases

iPTMnetiQ63648.
PhosphoSiteiQ63648.

Proteomic databases

PaxDbiQ63648.
PRIDEiQ63648.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25744.
KEGGirno:25744.
UCSCiRGD:3169. rat.

Organism-specific databases

CTDi4771.
RGDi3169. Nf2.

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiQ63648.
KOiK16684.
PhylomeDBiQ63648.

Miscellaneous databases

NextBioi607911.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. 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.
[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.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of the rat neurofibromatosis 2 gene and its involvement in asbestos-induced mesothelioma."
    Kleymenova E.V., Bianchi A.A., Kley N., Pylev L.N., Walker C.L.
    Mol. Carcinog. 18:54-60(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer.
    Tissue: Heart and Liver.

Entry informationi

Entry nameiMERL_RAT
AccessioniPrimary (citable) accession number: Q63648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.