(data stored in ACNUC9306 zone)

HOGENOM: MOUSE11_PE124

ID   MOUSE11_PE124                        STANDARD;      PRT;   596 AA.
AC   MOUSE11_PE124; P46662; Q8BR03;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Merlin;AltName: Full=Moesin-ezrin-radixin-like
DE   protein;AltName: Full=Neurofibromin-2;AltName: Full=Schwannomin;
DE   (MOUSE11.PE124).
GN   Name=Nf2; Synonyms=Nf-2;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE11.PE124.
CC       Mus musculus chromosome 11 NCBIM37  sequence 1..121843856 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:MERL_MOUSE
CC   -!- FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo)
CC       signaling pathway, a signaling pathway that plays a pivotal role
CC       in tumor suppression by restricting proliferation and promoting
CC       apoptosis. Along with WWC1 can synergistically induce the
CC       phosphorylation of LATS1 and LATS2 and can probably function in
CC       the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway.
CC       May act as a membrane stabilizing protein. May inhibit PI3 kinase
CC       by binding to AGAP2 and impairing its stimulating activity.
CC       Suppresses cell proliferation and tumorigenesis by inhibiting the
CC       CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex
CC       (By similarity). Plays a role in lens development and is required
CC       for complete fiber cell terminal differentiation, maintenance of
CC       cell polarity and separation of the lens vesicle from the corneal
CC       epithelium.
CC   -!- SUBUNIT: Interacts with SLC9A3R1, HGS and AGAP2. Interacts with
CC       SGSM3. Interacts (via FERM domain) with MPP1 (By similarity).
CC       Interacts with LAYN and WWC1. Interacts with the CUL4A-RBX1-DDB1-
CC       VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The
CC       unphosphorylated form interacts (via FERM domain) with VPRBP/DCAF1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cell projection (By similarity).
CC       Cytoplasm, cytoskeleton (By similarity). Nucleus (By similarity).
CC       Note=Colocalizes with MPP1 in non-myelin-forming Schwann cells.
CC       Binds with VPRBP in the nucleus. The intramolecular association of
CC       the FERM domain with the C-terminal tail promotes nuclear
CC       accumulation. The unphosphorylated form accumulates predominantly
CC       in the nucleus while the phosphorylated form is largely confined
CC       to the non-nuclear fractions (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=P46662-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P46662-2; Sequence=VSP_000493;
CC   -!- PTM: Phosphorylation of Ser-518 inhibits nuclear localization by
CC       disrupting the intramolecular association of the FERM domain with
CC       the C-terminal tail (By similarity).
CC   -!- PTM: Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3
CC       ubiquitin-protein ligase complex for ubiquitination and subsequent
CC       proteasome-dependent degradation (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are born with abnormally small lenses
CC       with serious structural defects. Failure of lens vesicle
CC       separation and the resulting changes in cell organization causes
CC       lenses to herniate, leading to expulsion of lens fiber cells
CC       through a perforation in the cornea. Developing lenses show loss
CC       of cell apical-basal polarity, failure of the lens vesicle to
CC       separate from the surface ectoderm, failure to properly exit the
CC       cell cycle during fiber cell differentiation and incomplete
CC       terminal differentiation of fiber cells.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- GENE_FAMILY: HOG000007113 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000009073;ENSMUST00000109910;ENSMUSP00000105536.
DR   EMBL; AK045998; - ;
DR   EMBL; AK167685; - ;
DR   EMBL; AL606521; - ;
DR   EMBL; AL645603; - ;
DR   EMBL; BC005442; - ;
DR   EMBL; CH466574; - ;
DR   EMBL; L27090; - ;
DR   EMBL; L27105; - ;
DR   EMBL; L28176; - ;
DR   EMBL; X74671; - ;
DR   EMBL; X75759; - ;
DR   UniProtKB/Swiss-Prot; P46662; Q8BR03; -.
DR   EMBL; X74671; CAA52737.1; -; mRNA.
DR   EMBL; L27105; AAA39807.1; -; mRNA.
DR   EMBL; L27090; AAA63648.1; -; mRNA.
DR   EMBL; L28176; AAA39808.1; -; mRNA.
DR   EMBL; AK045998; BAC32567.1; -; mRNA.
DR   EMBL; X75759; CAA53386.1; -; mRNA.
DR   IPI; IPI00135968; -.
DR   IPI; IPI00228063; -.
DR   PIR; I48683; I48683.
DR   PIR; I54368; I54368.
DR   PIR; I68664; I68664.
DR   RefSeq; NP_035028.2; NM_010898.3.
DR   UniGene; Mm.297109; -.
DR   PDB; 1ISN; X-ray; 2.90 A; A=18-340.
DR   PDBsum; 1ISN; -.
DR   ProteinModelPortal; P46662; -.
DR   SMR; P46662; 18-596.
DR   IntAct; P46662; 5.
DR   STRING; P46662; -.
DR   PhosphoSite; P46662; -.
DR   PRIDE; P46662; -.
DR   Ensembl; ENSMUST00000053079; ENSMUSP00000055033; ENSMUSG00000009073.
DR   Ensembl; ENSMUST00000056290; ENSMUSP00000055061; ENSMUSG00000009073.
DR   Ensembl; ENSMUST00000109910; ENSMUSP00000105536; ENSMUSG00000009073.
DR   GeneID; 18016; -.
DR   KEGG; mmu:18016; -.
DR   CTD; 4771; -.
DR   MGI; MGI:97307; Nf2.
DR   eggNOG; roNOG08559; -.
DR   InParanoid; P46662; -.
DR   OMA; VNYFTIR; -.
DR   OrthoDB; EOG4NVZK5; -.
DR   PhylomeDB; P46662; -.
DR   NextBio; 293053; -.
DR   ArrayExpress; P46662; -.
DR   Bgee; P46662; -.
DR   CleanEx; MM_NF2; -.
DR   Genevestigator; P46662; -.
DR   GermOnline; ENSMUSG00000009073; Mus musculus.
DR   GO; GO:0005912; C:adherens junction; IMP:MGI.
DR   GO; GO:0032154; C:cleavage furrow; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR   GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR   GO; GO:0070306; P:lens fiber cell differentiation; IMP:UniProtKB.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0043409; P:negative regulation of MAPKKK cascade; IMP:MGI.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR008954; Moesin.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00769; ERM; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PIRSF; PIRSF002305; ERM; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF48678; Moesin; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   HOGENOMDNA; MOUSE11.PE124; -.
KW   ENSMUSG000000090735old_1320000031; ENSMUSP000001055361old_1320000031;
KW   Q3TIW4_MOUSE; Q5NCK4_MOUSE; Q99K59_MOUSE; AK045998; AK167685; AL606521;
KW   BC005442; CH466574; L27090; L27105; L28176; X74671; X75759;
KW   3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Tumor suppressor; Ubl conjugation.
SQ   SEQUENCE   596 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAGAIASRMS FSSLKRKQPK TFTVRIVTMD AEMEFNCEMK WKGKDLFDLV CRTLGLRETW
     FFGLQYTIKD TVAWLKMDKK VLDHDVSKEE PVTFHFLAKF YPENAEEELV QEITQHLFFL
     QVKKQILDEK VYCPPEASVL LASYAVQAKY GDYDPSVHKR GFLAQEELLP KRVINLYQMT
     PEMWEERITA WYAEHRGRAR DEAEMEYLKI AQDLEMYGVN YFTIRNKKGT ELLLGVDALG
     LHIYDPENRL TPKISFPWNE IRNISYSDKE FTIKPLDKKI DVFKFNSSKL RVNKLILQLC
     IGNHDLFMRR RKADSLEVQQ MKAQAREEKA RKQMERQRLA REKQMREEAE RTRDELERRL
     LQMKEEATMA NEALMRSEET ADLLAEKAQI TEEEAKLLAQ KAAEAEQEMQ RIKATAIRTE
     EEKRLMEQKV LEAEVLALKM AEESERRAKE ADQLKQDLQE AREAERRAKQ KLLEIATKPT
     YPPMNPIPPP LPPDIPSFDI IADSLSFDFK DTDMKRLSME IEKEKVEYME KSKHLQEQLN
     ELKTEIEALK LKERETALDV LHSESSDRGG PSSKHNTIKK LTLQSAKSRV AFFEEL
//

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