ID B3RY21_TRIAD Unreviewed; 553 AA.
AC B3RY21;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Moesin/ezrin/radixin homolog 1 {ECO:0000256|ARBA:ARBA00022025};
GN ORFNames=TRIADDRAFT_25177 {ECO:0000313|EMBL:EDV24958.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV24958.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV24958.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV24958.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SUBCELLULAR LOCATION: 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; DS985245; EDV24958.1; -; Genomic_DNA.
DR RefSeq; XP_002112848.1; XM_002112812.1.
DR AlphaFoldDB; B3RY21; -.
DR STRING; 10228.B3RY21; -.
DR EnsemblMetazoa; TriadT25177; TriadP25177; TriadG25177.
DR GeneID; 6754061; -.
DR KEGG; tad:TRIADDRAFT_25177; -.
DR CTD; 6754061; -.
DR eggNOG; KOG3529; Eukaryota.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; B3RY21; -.
DR OMA; XALEMAE; -.
DR OrthoDB; 5476297at2759; -.
DR PhylomeDB; B3RY21; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IBA:GO_Central.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:1902115; P:regulation of organelle assembly; IBA:GO_Central.
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; 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; 2.
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 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:UP000009022}.
FT DOMAIN 1..291
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 442..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV24958.1"
SQ SEQUENCE 553 AA; 64607 MW; E407E22822646485 CRC64;
VNVRVTSLDS ELEFAIQPNT SGKQLFDQVC KTLGIREVWY FGLRFLDSKG QLSWLRLEKK
VSAQDIKKEV PLQFKFRVEF FPEDVSEELI EDVTQKLFFL QVKEGIINDD VYCPPETAVL
LASYAVQAKF GDYDKDTHKD GYLSNEKLLP KRVLDQHKLD SRQWEERISN WHSEHKNMLK
EEAMMEYLKI AQDLEMYGVN YYDIKNKKGS DLWLGVDALG INVYEHEDRL TPKIGFPWSE
IRNISFSEKK FVIKPIDRKS PDFNFYVPRV KLNKHILALC MGNHELFIRR RKPDTVEIQQ
MKTTAKDLRN AKRSEKAQFL REQQARLDAE KQRLELEEKM KKFEEDQKIV QNSLKKTEEG
SKELAEKARK AEEETRRLEE IKKQIEEEKK KLEKIAAEDR ERLLEKNEEI KRLSEAAARA
EEAVAMAEEA AAKAAEEARA RAAEEAYQNN NLAEPQYEEG TDAGSSQLID DETDEVPMTQ
EIDRVALAER NKRLMEQLKL LGNELIGIRD NSKDTTMDHL HAENVKQGRD KYKTLKQIRQ
GNTKKRVNDF EQL
//
