MOEH_AEDAE
ID MOEH_AEDAE Reviewed; 583 AA.
AC Q170J7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Moesin/ezrin/radixin homolog 1 {ECO:0000250|UniProtKB:P46150};
GN Name=Moe {ECO:0000250|UniProtKB:P46150}; ORFNames=AAEL007915;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT40344.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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; CH477473; EAT40344.1; -; Genomic_DNA.
DR RefSeq; XP_001652975.1; XM_001652925.1.
DR AlphaFoldDB; Q170J7; -.
DR SMR; Q170J7; -.
DR STRING; 7159.AAEL007915-PA; -.
DR PRIDE; Q170J7; -.
DR VEuPathDB; VectorBase:AAEL007915; -.
DR eggNOG; KOG3529; Eukaryota.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; Q170J7; -.
DR OMA; SREDSMM; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; Q170J7; -.
DR Proteomes; UP000008820; Unassembled 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..583
FT /note="Moesin/ezrin/radixin homolog 1"
FT /id="PRO_0000355092"
FT DOMAIN 11..301
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 466..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 69067 MW; 9F815317AA02AAE5 CRC64;
MGRPRTARVF MNVRVTTMDA ELEFAIQQST TGKQLFDQVV KTIGLREVWF FGLQYTDSKG
DLTWIKLYKK VMSQDVQKGD PLQFKFRAKF YPEDVAEELI QDITLRLFYL QVKNAILSDE
IYCPPETSVL LASYAVQARH GDYNKTTHVP GFLVNDRLLP QRVIDQHKMS KDEWENSITT
WWQEHRGMLR EDAMMEYLKI AQDLEMYGVN YFEIRNKKGT ELWLGVDALG LNIYEKDDRL
TPKIGFPWSE IRNISFNDRK FIIKPIDKKA PDFVFFAPRV RINKRILALC MGNHELYMRR
RKPDTIDVQQ MKAQAREEKN AKQQEREKLQ LALAARERAE KKQQEYEDRL RTMQEEMERS
QANLIEAQEM IRRLEDQLKQ LQFAKDELEA RQNELQVMIK RLEESKNMEV AERQKLEDEI
RAKQEEVQKI QEEVSVKDTE TKRLQEEVEE ARRKQNEAAA ALLAATTTPN HHHVDEEEED
NEEELTNGAE NGTSRDYSKD FDTDEHIKDP VEERRTLAER NERLHDQLKA LKQDLALSRD
DTMETANDKI HRENVRQGRD KYKTLREIRK GNTKRRVDQF ENM
