ID G1LS78_AILME Unreviewed; 593 AA.
AC G1LS78;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 80.
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:ENSAMEP00000009916.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000009916.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000009916.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000009916.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G1LS78; -.
DR STRING; 9646.ENSAMEP00000009916; -.
DR Ensembl; ENSAMET00000010350.2; ENSAMEP00000009916.2; ENSAMEG00000009395.2.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT01090000260082; -.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; G1LS78; -.
DR TreeFam; TF313935; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
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:0001931; C:uropod; IEA:Ensembl.
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:0097718; F:disordered domain specific 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: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:0035088; P:establishment or maintenance of apical/basal cell polarity; IEA:Ensembl.
DR GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR GO; GO:0001951; P:intestinal D-glucose absorption; 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:0040018; P:positive regulation of multicellular organism growth; 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:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; 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:0031623; P:receptor internalization; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0032532; P:regulation of microvillus length; IEA:Ensembl.
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 GO; GO:1902896; P:terminal web assembly; IEA:Ensembl.
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, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}.
FT DOMAIN 12..302
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 313..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 531..558
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 67..70
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 285
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 593 AA; 70303 MW; 6302CA11A5456145 CRC64;
MPISWKFMGS LINVRVTTMD AELEFAIQPN TTGKQLFDQV VKTIGLREVW YFGLQYVDNK
GFPTWLKLDK KVSAQEVRKE NPLQFKFRAK FYPEDVSEEL IQDITQKLFF LQVKEGILSD
EIYCPPETAV LLGSYAVQAK FGDYNKDTHK SGYLSSERLI PQRVMDQHKL TRDQWEDRIQ
VWHAEHRGML KDSAMLEYLK IAQDLEMYGI NYFEIKNKKG TDLWLGVDAL GLNIYEKEDK
LTPKIGFPWS EIRNISFNDK KFVIKPIDKK APDFVFYAPR LRINKRILQL CMGNHELYMR
RRKPDTIEVQ QMKAQAREEK HQKQLERQQL ETEKKRRETV EREKEQMMRE KEELMLRLQD
YEQKTKKAEK ELSDQIQRAL QLEEERKRAQ EEAERLENDR VAALRAKEEL ERQAADQIKS
QEQLAAELAE YTAKIALLEE ARRRKEDEVE EWQHRAKEAQ DDLVKTKEEL HLVMTAPPPP
PPPVYEPVSY HVQDNLQDEG TEYTGYSAEL SSEGILDDRN EEKRITEAEK NERVQRQLMT
LTNELSQARD ENKRTHNDII HNENMRQGRD KYKTLRQIRQ GNTKQRIDEF EAM
//
