ID A4F2N4_MOLTE Unreviewed; 588 AA.
AC A4F2N4;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Mt-ezrin/radixin/moesin {ECO:0000313|EMBL:BAF49215.1};
DE Flags: Fragment;
GN Name=ERMc {ECO:0000313|EMBL:BAF49215.1};
OS Molgula tectiformis (Ascidian).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Molgulidae; Molgula.
OX NCBI_TaxID=30286 {ECO:0000313|EMBL:BAF49215.1};
RN [1] {ECO:0000313|EMBL:BAF49215.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17540363; DOI=10.1016/j.ydbio.2007.03.035;
RA Gyoja F., Satou Y., Shin-i T., Kohara Y., Swalla B.J., Satoh N.;
RT "Analysis of large scale expression sequenced tags (ESTs) from the anural
RT ascidian, Molgula tectiformis.";
RL Dev. Biol. 307:460-482(2007).
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; AB297458; BAF49215.1; -; mRNA.
DR AlphaFoldDB; A4F2N4; -.
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 2: Evidence at transcript level;
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}.
FT DOMAIN 5..295
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 505..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 330..487
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 505..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 278
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 NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAF49215.1"
SQ SEQUENCE 588 AA; 69485 MW; F2978FAAAF611998 CRC64;
MPKSINVRVT TMDAELEFAI QQSTTGKQLF DQVVKTVGLR EIWYFGLQYI DSKGYPTWLK
LNKKVTQQDV RKESTLNFKF RCKFYPEDVG EELIQEATQK LFFLQVKEAI LNDDVYCPPE
TSVLLASFAV LAKFGPYDCE MHNTKYLSNE KLLPQRVVEQ HKLQREQWEE RIKTWHDEHG
DMLKDEAMIE YLKIAQDLEM YGVNYFEIQN KKKTQLFLGV DALGLNIYEK SDKLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY VERLRINKRI LALCMGNHEL YMRRRKPDSI
EVQQMKAQAK EVKYQKRRDK ERLGKEREQK IEAVNQRQKM LEENAKLKKQ LDNERIAREE
LAKASEEAHE KMLQMAKDEE KREKERKEIE EARRIAEEEM RRLAIISQQE SERTTAMEAQ
IAENLLEVER LREAEEEKKR EAIEYQKMLE TIRKQNEEQQ EELTRAREEA QQKALEASRA
MEEALQQELP PPIEEEIIDA TSHDMHAAPG ENDRSEEDRL TAAEKNNKLQ SQLKSLQEEL
SSMHDQTQDT TLDILHKQNV KAGRDKYKTL KQIRCGNTKQ RIDEFEAL
//
