MOEH_ANOGA
ID MOEH_ANOGA Reviewed; 581 AA.
AC Q7PS12; F5HJF6; F5HJF7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 5.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Moesin/ezrin/radixin homolog 1 {ECO:0000250|UniProtKB:P46150};
GN Name=Moe {ECO:0000250|UniProtKB:P46150}; ORFNames=AGAP000562;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C {ECO:0000269|PubMed:12364791};
CC IsoId=Q7PS12-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:12364791};
CC IsoId=Q7PS12-2; Sequence=VSP_042863;
CC Name=B {ECO:0000269|PubMed:12364791};
CC IsoId=Q7PS12-3; Sequence=VSP_042864;
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DR EMBL; AAAB01008846; EAA06305.6; -; Genomic_DNA.
DR EMBL; AAAB01008846; EGK96417.1; -; Genomic_DNA.
DR EMBL; AAAB01008846; EGK96418.1; -; Genomic_DNA.
DR RefSeq; XP_003437028.1; XM_003436980.1.
DR RefSeq; XP_003437029.1; XM_003436981.1.
DR RefSeq; XP_310518.5; XM_310518.5.
DR AlphaFoldDB; Q7PS12; -.
DR SMR; Q7PS12; -.
DR STRING; 7165.AGAP000562-PC; -.
DR PaxDb; Q7PS12; -.
DR PRIDE; Q7PS12; -.
DR GeneID; 4575958; -.
DR KEGG; aga:AgaP_AGAP000562; -.
DR CTD; 4575958; -.
DR VEuPathDB; VectorBase:AGAP000562; -.
DR eggNOG; KOG3529; Eukaryota.
DR InParanoid; Q7PS12; -.
DR OMA; WADHKNT; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; Q7PS12; -.
DR Proteomes; UP000007062; Chromosome X.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
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 GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IBA:GO_Central.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:1902115; P:regulation of organelle assembly; IBA:GO_Central.
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; Alternative splicing; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Membrane; Reference proteome.
FT CHAIN 1..581
FT /note="Moesin/ezrin/radixin homolog 1"
FT /id="PRO_0000355093"
FT DOMAIN 8..298
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 452..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..7
FT /note="MVASSKM -> MPKS (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12364791"
FT /id="VSP_042863"
FT VAR_SEQ 453..458
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12364791"
FT /id="VSP_042864"
SQ SEQUENCE 581 AA; 68611 MW; 5D7DFA7E20C6074A CRC64;
MVASSKMMNV RVTTMDAELE FAIQQGTTGK QLFDQVVKTI GLREVWFFGL QYTDSKGDNT
WIKLYKKVMS QDVQKGDPLL FKFRAKFYPE DVAEELIQDI TLRLFYLQVK NAILSDEIYC
PPETSVLLAS YAVQARHGDY NKGTHVPGFL AKDRLLPQRV IDQHKMSKDE WENSITTWWQ
EHRGLLREDA MMEYLKIAQD LEMYGVNYFE IRNKKGTELW LGVDALGLNI YEKEDRLTPK
IGFPWSEIRN ISFNDRKFII KPIDKKAPDF VFFAPRVRIN KRILALCMGN HELYMRRRKP
DTIDVQQMKA QARDEKNAKQ QEREKLQLAL AARERAEKKQ QEYEDRLRSM QEEMERKQAN
LSEAQDTIRR LQEQLNQVQA AKEELEQRQN ELHEMMQRLE ETKNMEATER AKLEEEIRVK
QLEMQKIQEE VTLKDSETKR LHEEVEEAIR KQVAKGSRAA AALQAATTTP KHHHVEEEEE
NEEELINGEN GTQDFSKDFD TDEHIKDPVE ERRTLAERNE RLQDQLKALK QDLALSRDDT
METPNDKIHR ENVRQGRDKY KTLREIRKGN TKRRVDQFEN M
