ID B2R6J2_HUMAN Unreviewed; 586 AA.
AC B2R6J2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Ezrin {ECO:0000256|ARBA:ARBA00039923};
DE AltName: Full=Cytovillin {ECO:0000256|ARBA:ARBA00042548};
DE AltName: Full=Villin-2 {ECO:0000256|ARBA:ARBA00042776};
DE AltName: Full=p81 {ECO:0000256|ARBA:ARBA00041750};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG35489.1};
RN [1] {ECO:0000313|EMBL:BAG35489.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:BAG35489.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA Isogai T.;
RT "NEDO functional analysis of protein and research application project.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00037857}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00037857}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00037857}. Cell projection, microvillus membrane
CC {ECO:0000256|ARBA:ARBA00037837}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00037837}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00037837}. Cell projection, ruffle membrane
CC {ECO:0000256|ARBA:ARBA00004599}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004599}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004599}. Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. 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; AK312597; BAG35489.1; -; mRNA.
DR AlphaFoldDB; B2R6J2; -.
DR IntAct; B2R6J2; 1.
DR PeptideAtlas; B2R6J2; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR CDD; cd17239; FERM_F1_Ezrin; 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:SF13; EZRIN; 1.
DR PANTHER; PTHR23281; MERLIN/MOESIN/EZRIN/RADIXIN; 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 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}.
FT DOMAIN 5..295
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 306..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..63
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 278
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 586 AA; 69401 MW; C3FCB65D0459AE30 CRC64;
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLHYV DNKGFPTWLK
LDKKVSAQEV RKENPLQFKF RAKFYPEDVA EELTQDITQK LFFLQVKEGI LSDEIYCPPE
TAVLLGSYAV QAKFGDYNKE VHKSGYLSSE RLIPQRVMDQ HKLTRDQWED RIQVWHAEHR
GMLKDNAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM MREKEELMLR LQDYEEKTKK
AERELSEQIQ RALQLEEERK RAQEEAERLE ADRMAALRAK EELERQAVDQ IKSQEQLAAE
LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP
VSYHVQESLQ DEGAEPTGYS AELSSEGIRD DRNEEKRITE AEKNERVQRQ LLTLSSELSQ
ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAL
//
