ID A0A0A0A6N7_CHAVO Unreviewed; 576 AA.
AC A0A0A0A6N7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Moesin {ECO:0000256|ARBA:ARBA00041051};
DE AltName: Full=Membrane-organizing extension spike protein {ECO:0000256|ARBA:ARBA00043042};
DE Flags: Fragment;
GN ORFNames=N301_11294 {ECO:0000313|EMBL:KGL89731.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL89731.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL89731.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL89731.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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; KL870849; KGL89731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0A6N7; -.
DR STRING; 50402.A0A0A0A6N7; -.
DR Proteomes; UP000053858; 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; 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:SF26; MOESIN; 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 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:UP000053858}.
FT DOMAIN 1..291
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 300..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56..59
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 274
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:KGL89731.1"
FT NON_TER 576
FT /evidence="ECO:0000313|EMBL:KGL89731.1"
SQ SEQUENCE 576 AA; 67988 MW; 68CE6FA464D28067 CRC64;
ISVRVTTMDA ELEFAIQPNT TGKQLFDQVV KTIGLREVWF FGLQYQDTKG FSTWLKLNKK
VTAQDVRKES PLLFKFRAKF YPEDVAEELI QDITQRLFFL QVKEAILNDD IYCPPETAVL
LASYAVQSKY GDFNKEVHKS GYLASDKLLP QRVLEQHKLN KDQWEERIQV WHEEHRGMIR
EDAVLEYLKI AQDLEMYGVN YFNIKNKKGS ELWLGVDALG LNIYEQNDRL TPKIGFPWSE
IRNISFNDKK FVIKPIDKKA PDFVFYAPRL RINKRILALC MGNHELYMRR RKPDTIEVQQ
MKAQAREEKH QKQMERALLE NEKKKRELAE KEKEKIEREK EELMERLKQI EEQTKKAQQE
LEEQTRRAME LEQERKRAQE EAEKLAKERR EAEEAKEALL KASHDQQKTQ EQLASEMAEL
TARITQLELA RQKKESEAQE WQQKAQMVQE DLEKTKEELK TAMSTPHVTE PMHSENEHDD
EQDENAAEAS AELRSEATIK DRSEEERTTE AEKNERVQKH LKALSSELAN ARDETKKTAN
DMIHAENMRL GRDKYKTLRQ IRQGNTKQRI DEFESM
//
