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
//