ID A0A1I8J2Y3_9PLAT Unreviewed; 571 AA.
AC A0A1I8J2Y3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=FERM domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0045758-snap-gene-1.4-mRNA-1};
GN ORFNames=BOX15_Mlig007381g1 {ECO:0000313|EMBL:PAA88157.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0045758-snap-gene-1.4-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0045758-snap-gene-1.4-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:PAA88157.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA88157.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA88157.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; NIVC01000200; PAA88157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I8J2Y3; -.
DR STRING; 282301.A0A1I8J2Y3; -.
DR WBParaSite; maker-uti_cns_0045758-snap-gene-1.4-mRNA-1; maker-uti_cns_0045758-snap-gene-1.4-mRNA-1; maker-uti_cns_0045758-snap-gene-1.4.
DR Proteomes; UP000095280; Unplaced.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
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; 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; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {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:UP000215902}.
FT DOMAIN 5..297
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT COILED 308..464
FT /evidence="ECO:0000256|SAM:Coils"
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 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 571 AA; 67203 MW; 2E3BE5542FF2509A CRC64;
MGKPINVKVT TMDAELEFAI QPSTTGKQLF DQVVKTIGLR EIWYFGLRYT DVKGFATWLK
LNKKVLQQDV PKDTLLVFEF RVKFFPEDAC EELVQEVTQR MFYLQVKESI LRGEVYCPPE
TAVLLASIAC QVKFGDYNPD VHQQGFLANE THFPISQAIL NQHTLSRQDW EDKIVNWYRE
LKGKMKEDAM LEYLKVAQDL EMYGVNYFEI KNKKGTDLFL GIDALGLNIY AQEDKLTPKI
GFPWSEIRNI SFNDRKFVIK PIDRKAPDFV FFAPRLRINK RILALCMGNH ELYMRRRKPD
TIEVQQMKAQ AKEDRANKQY EKIRLERERA AREEAESRRK ELEDRLAELE GLQESYARER
EEQSTRMAEM SRQMEEIQRQ RDEIEAARLR AEEIKNQLES EVQMSAEERA RLQEENERVQ
AMVRAKEEEA QAASNELTSM RGELETVRKD LDQTTNRMQD LQTKAAVIVT PHLAELDDEA
AGDKKYNFES QENGDMVARD DYREEYMQSH TIKTRLDEMR DEFKTSRKED QVQTIDRLHE
SNVKEGRSKF KTLQKIRMGN TKKRIDEFES M
//
