MOEH_DROPS
ID MOEH_DROPS Reviewed; 593 AA.
AC Q29GR8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Moesin/ezrin/radixin homolog 1 {ECO:0000250|UniProtKB:P46150};
GN Name=Moe {ECO:0000250|UniProtKB:P46150}; ORFNames=GA10507;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Involved in connections of major cytoskeletal structures to
CC the plasma membrane. {ECO:0000250|UniProtKB:P46150}.
CC -!- SUBUNIT: Interacts with Mer and arm at the adherens junction. Interacts
CC with cytoskeletal actin at apical buds of microvilli in the
CC precellularised embryo (By similarity). {ECO:0000250|UniProtKB:P46150}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q24564}. Cell membrane
CC {ECO:0000250|UniProtKB:Q24564}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q24564}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q24564}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q24564}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL32041.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH379064; EAL32041.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015041867.1; XM_015186381.1.
DR AlphaFoldDB; Q29GR8; -.
DR SMR; Q29GR8; -.
DR STRING; 7237.FBpp0280425; -.
DR EnsemblMetazoa; FBtr0372580; FBpp0334538; FBgn0070564.
DR GeneID; 4815377; -.
DR KEGG; dpo:Dpse_GA10507; -.
DR eggNOG; KOG3529; Eukaryota.
DR InParanoid; Q29GR8; -.
DR ChiTaRS; Moe; fly.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0070564; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
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-SubCell.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
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; PTHR23281; 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48678; SSF48678; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Membrane; Reference proteome.
FT CHAIN 1..593
FT /note="Moesin/ezrin/radixin homolog 1"
FT /id="PRO_0000355095"
FT DOMAIN 24..314
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 477..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 69991 MW; 4850FF531FBAAF28 CRC64;
MVVVSDSRVR MPRYGGVSVK RKTLNVRVTT MDAELEFAIQ STTTGKQLFD QVVKTIGLRE
VWFFGLQYTD SKGDSTWIKL YKKVMNQDVK KENPLQFRFR AKFYPEDVAE ELIQDITLRL
FYLQVKNAIL TDEIYCPPET SVLLASYAVQ ARHGDHNKTT HTAGFLANDR LLPQRVIDQH
KMSKDEWEQS IMTWWQEHRS MLREDAMMEY LKIAQDLEMY GVNYFEIRNK KGTDLWLGVD
ALGLNIYEQD DRLTPKIGFP WSEIRNISFS EKKFIIKPID KKAPDFMFFA PRVRINKRIL
ALCMGNHELY MRRRKPDTID VQQMKAQARE EKNAKQQERE KLQLALAARE RAEKKQQEYE
DRLKQMQEEM ERSQRDLLEA QEMIRRLEEQ LKQLQAAKDE LELRQKELQS MLQRLEEAKN
MEAVEKIKLE EEIMAKQMEV QRIQDEVNAK DEETKRLQDE VEEARRKQAE AAAALLAAST
TPQHHHVAED ENENEEELTN GDAGGDVSRD LDTDEHIKDP IEDRRTLAER NERLHDQLKA
LKQDLAQSRD ETKETANDKI HRENVRQGRD KYKTLREIRK GNTKRRVDQF ENM
