ID A0A2K5CHS5_AOTNA Unreviewed; 608 AA.
AC A0A2K5CHS5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN Name=EZR {ECO:0000313|Ensembl:ENSANAP00000008263.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000008263.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000008263.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A2K5CHS5; -.
DR Ensembl; ENSANAT00000026044.1; ENSANAP00000008263.1; ENSANAG00000022176.1.
DR GeneTree; ENSGT01090000260082; -.
DR Proteomes; UP000233020; Unplaced.
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; 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: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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}.
FT DOMAIN 27..317
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 328..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82..85
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 300
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 608 AA; 71724 MW; 46C6CC2262B07CA1 CRC64;
MATAMGGNVQ RRTLTSGVDV CQVYCQINVR VTTMDAELEF AIQPNTTGKQ LFDQVVKTIG
LREVWYFGLQ YVDNKGFPTW LKLDKKVSAQ EVRKENPLQF KFRAKFYPED VAEELIQDIT
QKLFFLQVKE GILSDEIYCP PETAVLLGSY AVQAKFGDYN KDVHKSGYLS SERLIPQRVM
DQHKLTRDQW EDRIQVWHAE HRGMLKDNAM LEYLKIAQDL EMYGINYFEI KNKKGTDLWL
GVDALGLNIY EKDDKLTPKI GFPWSEIRNI SFNDKKFVIK PIDKKAPDFV FYAPRLRINK
RILQLCMGNH ELYMRRRKPD TIEVQQMKAQ AREEKHQKQL ERQQLETEKK RRETVEREKE
QMMREKEELM LRLQDYEEKT KKAERELSEQ IQRALQLEEE RKRAQEEAER LEADRMAALR
AKEELERQAV DQIKSQEQLA AELAEYTAKI ALLEEARRRK ENEVEEWQHR AKEAQDDLVK
TKEELHLVMT APPPPPPPVY EPVSYHVQES LQDEGAEPTG YSAELSSEGI RDDRNEEKRI
TEAEKNERVQ RQLLTLSSEL SQARDENKRT HNDIIHNENM RQGRDKYKTL RQIRQGNTKQ
RIDEFEAM
//
