ID   MOEH_CULQU              Reviewed;         572 AA.
AC   B0WYY2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Moesin/ezrin/radixin homolog 1 {ECO:0000250|UniProtKB:P46150};
GN   Name=Moe {ECO:0000250|UniProtKB:P46150}; ORFNames=CPIJ012259;
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000312|EMBL:EDS37245.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000312|EMBL:EDS37245.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA   Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in connections of major cytoskeletal structures to
CC       the plasma membrane. {ECO:0000250|UniProtKB:P46150}.
CC   -!- SUBUNIT: Interacts with cytoskeletal actin. {ECO:0000250}.
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}.
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DR   EMBL; DS232201; EDS37245.1; -; Genomic_DNA.
DR   RefSeq; XP_001862607.1; XM_001862572.1.
DR   AlphaFoldDB; B0WYY2; -.
DR   SMR; B0WYY2; -.
DR   STRING; 7176.CPIJ012259-PA; -.
DR   PRIDE; B0WYY2; -.
DR   GeneID; 6045211; -.
DR   KEGG; cqu:CpipJ_CPIJ012259; -.
DR   VEuPathDB; VectorBase:CPIJ012259; -.
DR   VEuPathDB; VectorBase:CQUJHB004297; -.
DR   eggNOG; KOG3529; Eukaryota.
DR   HOGENOM; CLU_003623_6_2_1; -.
DR   InParanoid; B0WYY2; -.
DR   OMA; RISTWHA; -.
DR   OrthoDB; 627741at2759; -.
DR   PhylomeDB; B0WYY2; -.
DR   Proteomes; UP000002320; Partially assembled WGS sequence.
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..572
FT                   /note="Moesin/ezrin/radixin homolog 1"
FT                   /id="PRO_0000355094"
FT   DOMAIN          1..291
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   REGION          456..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  67748 MW;  C677CBEE39EA0085 CRC64;
     MNVRVTTMDA ELEFAIQQST TGKQLFDQVV KTIGLREVWF FGLQYTDSKG DLTWIKLYKK
     VMSQDVQKGD PLQFKFRAKF YPEDVAEELI QDITLRLFYL QVKNAILSDE IYCPPETSVL
     LASYAVQARH GDYNKTTHTP GFLVNDRLLP QRVIDQHKMS KDEWENSITT WWQEHRGMLR
     EDAMMEYLKI AQDLEMYGVN YFEIRNKKGT ELWLGVDALG LNIYEKDDRL TPKIGFPWSE
     IRNISFNDRK FIIKPIDKKA PDFVFFAPRV RINKRILALC MGNHELYMRR RKPDTIDVQQ
     MKAQAREEKN AKQQEREKLQ LALAARERAE KKQQEYEDRI RNMQEEMERS QANLIEAQDM
     IRRLEEQLKQ LQAAKDDLEQ RQNELQVMIT RLEETKNMEA AERAKLEDEI RMKQEEVHKI
     QEEVSVKDSE TKRLQEEVEE ARRKQTEAAA ALLAATTTPS HHHVEEEEEM DNEEELVNGE
     NGNQDFSKDF DTDEHIKDPV EERRTLAERN ERLHDQLKAL KQDLALSRDD TMETANDKIH
     RENVRQGRDK YKTLREIRKG NTKRRVDQFE NM