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Database: UniProt
Entry: A0A0P7YAG9_SCLFO
LinkDB: A0A0P7YAG9_SCLFO
Original site: A0A0P7YAG9_SCLFO 
ID   A0A0P7YAG9_SCLFO        Unreviewed;       557 AA.
AC   A0A0P7YAG9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Moesin {ECO:0000256|ARBA:ARBA00041051};
DE   AltName: Full=Membrane-organizing extension spike protein {ECO:0000256|ARBA:ARBA00043042};
DE   Flags: Fragment;
GN   ORFNames=Z043_118754 {ECO:0000313|EMBL:KPP63015.1};
OS   Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX   NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP63015.1, ECO:0000313|Proteomes:UP000034805};
RN   [1] {ECO:0000313|EMBL:KPP63015.1, ECO:0000313|Proteomes:UP000034805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aro1 {ECO:0000313|EMBL:KPP63015.1};
RA   Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT   "The genome of the Asian arowana (Scleropages formosus).";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPP63015.1}.
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DR   EMBL; JARO02008211; KPP63015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7YAG9; -.
DR   STRING; 113540.ENSSFOP00015069486; -.
DR   Proteomes; UP000034805; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034805}.
FT   DOMAIN          1..274
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          455..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          283..427
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        479..495
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         257
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   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPP63015.1"
SQ   SEQUENCE   557 AA;  65573 MW;  7C681453E1B27C43 CRC64;
     LNVRVTTMDA ELDFAIQSNT TGKQLFNQVV LTVGLREVWF FGLQYQDSKG FSTWLKLDKK
     VTAQDMRKES PLPFKFRAKF YPEDVKEAIL NDDIYCPPET AVLLASYAVQ TKYGDHSPGI
     HLPGYLSNEK FLPQRVLEQH KLSKEQWEER IQVWHEEHKG MPREDSMLEY LKIAQDLEMY
     GVNYFCIKNK KGSELWLGVD ALGLNIYEQN DKMTPKIGFP WSEIRNISFS DKKFVIKPID
     KKAPDFVFYA ARLRINKRIL ALCMGNHELY MRRRKPDTIE VQQMKAQARE EKYQKQIERA
     LLENEKKKRE IAEKEKEKIE REKEELMERL MEIEEQTRKA QQALEEQTRR ALELEQEWRC
     AQEEAERLEK DRRMAEEAKA SLLQQSKNQM KNQELLATEL AELTSKISLL EDAKRKKEEE
     VTEWQKKCRS RQTDLVQEDL KKTKVELRSK VMSFTVENEH DENDESSAEA SAELTAVGSY
     RDRSEEDRLT EAEKNERVQK HLLALSSELA NARDETKKTA NDIIHAENVR SGRDKYKTLR
     QIRQGNTKQR IDEFESM
//
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