ID H0WVR4_OTOGA Unreviewed; 573 AA.
AC H0WVR4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Moesin {ECO:0000256|ARBA:ARBA00041051};
DE AltName: Full=Membrane-organizing extension spike protein {ECO:0000256|ARBA:ARBA00043042};
GN Name=MSN {ECO:0000313|Ensembl:ENSOGAP00000006414.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000006414.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000006414.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; AAQR03183749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WVR4; -.
DR STRING; 30611.ENSOGAP00000006414; -.
DR Ensembl; ENSOGAT00000007164.2; ENSOGAP00000006414.2; ENSOGAG00000007159.2.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT01090000260082; -.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; H0WVR4; -.
DR OMA; QWEDRIH; -.
DR TreeFam; TF313935; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0031143; C:pseudopodium; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0022612; P:gland morphogenesis; IEA:Ensembl.
DR GO; GO:0001771; P:immunological synapse formation; IEA:Ensembl.
DR GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:2000401; P:regulation of lymphocyte migration; IEA:Ensembl.
DR GO; GO:1902115; P:regulation of organelle assembly; IEA:Ensembl.
DR GO; GO:0070489; P:T cell aggregation; IEA:Ensembl.
DR GO; GO:0072678; P:T cell migration; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR CDD; cd17187; FERM_F1_ERM; 1.
DR Gene3D; 1.20.5.450; -; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
DR InterPro; IPR011259; ERM_C_dom.
DR InterPro; IPR041789; ERM_FERM_C.
DR InterPro; IPR046810; ERM_helical.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
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_tail_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23281; MERLIN/MOESIN/EZRIN/RADIXIN; 1.
DR PANTHER; PTHR23281:SF26; MOESIN; 1.
DR Pfam; PF00769; ERM_C; 1.
DR Pfam; PF20492; ERM_helical; 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 SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF48678; Moesin tail domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225}.
FT DOMAIN 1..291
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 319..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56..59
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1"
FT BINDING 274
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1"
SQ SEQUENCE 573 AA; 67298 MW; FA2DA5C29898DD6D CRC64;
ISVRVTTMDA ELEFAIQPNT TGKQLFDQVV KTIGLREVWF FGLQYQDTKG FSTWLKLNKK
VTAQDVRKES PLLFKFRAKF YPEDVSEELI QDITQRLFFL QVKEGILNDD IYCPPETAVL
LASYAVQSKY GDFNKEVHKS GYLAGDKLLP QRVLEQHKLN KDQWEERIQV WHEEHRGMLR
EDAVLEYLKI AQDLEMYGVN YFSIKNKKGS ELWLGVDALG LNIYEQNDRL TPKIGFPWSE
IRNISFNDKK FVIKPIDKKA PDFVFYAPRL RINKRILALC MGNHELYMRR RKPDTIEVQQ
MKAQAREEKH QKQMERALLE NEKKKREMAE KEKEKIEREK EELMERLKQI EEQTKKAQQE
LEEQTRRALE LEQERKRAQS EAEKLAKERQ EAEEAKDALL QASRDQKKTQ EQLALEMAEL
TARISQLEMA RQKKESEAVE WQQKAQMVQE DLEKTRAELK TAMSTPHVAE PAENEQDEQD
ENGAEASADL RADAMAKDRS EEERTTEAEK NERVQKHLKA LTSELANARD ESKKTANDMI
HAENVRLGRD KYKTLRQIRQ GNTKQRIDEF ESM
//
