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Database: UniProt
Entry: A0A151XF73_9HYME
LinkDB: A0A151XF73_9HYME
Original site: A0A151XF73_9HYME 
ID   A0A151XF73_9HYME        Unreviewed;       600 AA.
AC   A0A151XF73;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Moesin/ezrin/radixin homolog 1 {ECO:0000256|ARBA:ARBA00022025};
GN   ORFNames=ALC60_01992 {ECO:0000313|EMBL:KYQ58985.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ58985.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ58985.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ58985.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ58985.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000256|ARBA:ARBA00004536}. 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; KQ982205; KYQ58985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151XF73; -.
DR   STRING; 64791.A0A151XF73; -.
DR   Proteomes; UP000075809; Unassembled WGS sequence.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
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   GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR   GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13194; FERM_C_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:SF18; MOESIN/EZRIN/RADIXIN HOMOLOG 1; 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; 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; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT   DOMAIN          1..328
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          477..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..538
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         311
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   600 AA;  70905 MW;  8980904346B16E4F CRC64;
     MNVRVTTMDA ELEFAIQQTT TGKQLFDQVV KTIGLREVWF FGLQYTDTKG DLTWIKLYKK
     PESAIARVVK KEVKKKVRKL RGYSDSDTDD DEFDDGLVMN QEVKKETPLQ FKFRAKFYPE
     DVAEELIQDI TLRLFYLQVK NGILTDEIYC PPETSVLLAS YAVQARHGDY QKGNHPAGFL
     SNDRLLPQRV VDQHKMSKEE WDNSITNWWQ EHRGMLREDA MMEYLKIAQD LEMYGVNYFE
     IRNKKGTDLW LGVDALGLNI YEKDDKLTPK IGFPWSEIRN ISFNDKKFII KPIDKKAPDF
     VFFANRVKIN KRILALCMGN HELYMRRRKP DTIDVQQMKA QARDEKMAKQ QQREKLQLEI
     AARERAEKKQ QEYEERLKNM AEEMDRRNAE LNEAQEMIRR LEEQLKQLQA AKEELENRQK
     ELTAMMEKLE LSHEMEAAER AKLEQEIRAK QEEVQRIQSE VEAKDAEARR LQAELRQEEA
     DRQYQANQTP HHHHVEENEE GEEEGEDEVP QGDVTKDLLT DESIIDPVGE RRTLAERSER
     LNDQLKALKQ DLAQSRDESK ETVMDKIHRE NVRQGRDKYK TLREIRKGNT KRRVDQFENM
//
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