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Database: UniProt
Entry: A0A2K5XVI4_MANLE
LinkDB: A0A2K5XVI4_MANLE
Original site: A0A2K5XVI4_MANLE 
ID   A0A2K5XVI4_MANLE        Unreviewed;       588 AA.
AC   A0A2K5XVI4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 34.
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:ENSMLEP00000007290.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000007290.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000007290.1}
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; A0A2K5XVI4; -.
DR   STRING; 9568.ENSMLEP00000007290; -.
DR   Ensembl; ENSMLET00000030593.1; ENSMLEP00000007290.1; ENSMLEG00000027290.1.
DR   GeneTree; ENSGT01090000260082; -.
DR   OMA; EWQHRAI; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:Ensembl.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR   GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:Ensembl.
DR   GO; GO:0034237; F:protein kinase A regulatory subunit binding; IEA:Ensembl.
DR   GO; GO:0044548; F:S100 protein binding; IEA:Ensembl.
DR   GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl.
DR   GO; GO:0030953; P:astral microtubule organization; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0043622; P:cortical microtubule organization; IEA:Ensembl.
DR   GO; GO:0051660; P:establishment of centrosome localization; IEA:Ensembl.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR   GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR   GO; GO:0030033; P:microvillus assembly; IEA:Ensembl.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
DR   GO; GO:1903753; P:negative regulation of p38MAPK cascade; IEA:Ensembl.
DR   GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:1902966; P:positive regulation of protein localization to early endosome; IEA:Ensembl.
DR   GO; GO:0010737; P:protein kinase A signaling; IEA:Ensembl.
DR   GO; GO:0072697; P:protein localization to cell cortex; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0031503; P:protein-containing complex localization; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:1902115; P:regulation of organelle assembly; IEA:Ensembl.
DR   GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; IEA:Ensembl.
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:UP000233140};
KW   S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}.
FT   DOMAIN          7..297
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          308..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62..65
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         280
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   588 AA;  69572 MW;  8943F4ED6C8E69E2 CRC64;
     LPSPNTINVR VTTMDAELEF AIQPNTTGKQ LFDQVVKTIG LREVWYFGLQ YVDNKGFPTW
     LKLDKKVSAQ EVRKENPLQF KFRAKFFPED VAEELIQDIT QKLFFLQVKE GILSDEIYCP
     PETAVLLGSY AVQAKFGDYN KEVHKSGYLS SERLIPQRVM DQHKLTRDQW EDRIQVWHAE
     HRGMLKDNAM LEYLKIAQDL EMYGINYFEI KNKKGTELWL GVDALGLNIY EKDDKLTPKI
     GFPWSEIRNI SFNDKKFVIK PIDKKAPDFV FYAPRLRINK RILQLCMGNH ELYMRRRKPD
     TIEVQQMKAQ AREEKHQKQL ERQQLETEKK RRETVEREKE QMMREKEELM LRLQDYEEKT
     KKAERELSEQ IQRALQLEEE RKRAQEEAER LEADRMAALR AKEELERQAV DQIKSQEQLA
     AELAEYTAKI ALLEEARRRK EDEVEEWQHR AKEAQDDLVK TKEELHLVMT APPPPPPPVY
     EPLSYHVQES LQDEGAEPTG YSAELSSEGI RDDRNEEKRI TEAEKNERVQ RQLLTLSSEL
     SQARDENKRT HNDIIHNENM RQGRDKYKTL RQIRQGNTKQ RIDEFEAL
//
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