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Database: UniProt
Entry: A0A0Q9VZ78_DROVI
LinkDB: A0A0Q9VZ78_DROVI
Original site: A0A0Q9VZ78_DROVI 
ID   A0A0Q9VZ78_DROVI        Unreviewed;       575 AA.
AC   A0A0Q9VZ78;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Moesin/ezrin/radixin homolog 1 {ECO:0000256|ARBA:ARBA00022025};
GN   Name=Dvir\GJ15179 {ECO:0000313|EMBL:KRF78156.1};
GN   ORFNames=Dvir_GJ15179 {ECO:0000313|EMBL:KRF78156.1};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF78156.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:KRF78156.1, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000256|ARBA:ARBA00004536}. Cell projection, microvillus
CC       {ECO:0000256|ARBA:ARBA00004105}. Cell projection, rhabdomere
CC       {ECO:0000256|ARBA:ARBA00043944}. 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; CH940660; KRF78156.1; -; Genomic_DNA.
DR   RefSeq; XP_015024568.1; XM_015169082.1.
DR   AlphaFoldDB; A0A0Q9VZ78; -.
DR   SMR; A0A0Q9VZ78; -.
DR   EnsemblMetazoa; FBtr0435058; FBpp0392062; FBgn0202375.
DR   GeneID; 6635548; -.
DR   OrthoDB; 5476297at2759; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
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   GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR   GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
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:SF18; MOESIN_EZRIN_RADIXIN HOMOLOG 1; 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 junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792}.
FT   DOMAIN          6..296
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          459..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          303..456
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        489..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61..64
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         279
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"
SQ   SEQUENCE   575 AA;  67887 MW;  F32A3D3A224E56C0 CRC64;
     MSPKSLNVRV TTMDAELEFA IQSTTTGKQL FDQVVKTIGL REVWFFGLQY TDSKGDSTWI
     KLYKKVMNQD VKKENPLQFR FRAKFYPEDV AEELIQDITL RLFYLQVKNA ILTDEIYCPP
     ETSVLLASYA VQARHGDHNK TTHTAGFLAN DRLLPQRVID QHKMSKDEWE QSIMTWWQEH
     RSMLREDAMM EYLKIAQDLE MYGVNYFEIR NKKGTDLWLG VDALGLNIYE QDDRLTPKIG
     FPWSEIRNIS FSEKKFIIKP IDKKAPDFMF FAPRVRINKR ILALCMGNHE LYMRRRKPDT
     IDVQQMKAQA REEKNAKQQE REKLQLALAA RERAEKKQQE YEDRLKQMQE EMERSQRDLL
     EAQEMIRRLE EQLKQLQAAK DELELRQKEL QSMLQRLEEA KNMEAVEKAK LEEEIMAKQQ
     EVQRIQDEVN AKDEETKRLQ DEVEEARRKQ AEAAAALLAA STTPQHHHVA EDENENEEEL
     TNGDAGGDVS RDLDTDEHIK DPIEDRRTLA ERNERLHDQL KALKQDLAQS RDETKETAND
     KIHRENVRQG RDKYKTLREI RKGNTKRRVD QFENM
//
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