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Database: UniProt
Entry: B4QFF9_DROSI
LinkDB: B4QFF9_DROSI
Original site: B4QFF9_DROSI 
ID   B4QFF9_DROSI            Unreviewed;       410 AA.
AC   B4QFF9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=GD11040 {ECO:0000313|EMBL:EDX07069.1};
GN   Name=Dsim\GD11040 {ECO:0000313|EMBL:EDX07069.1};
GN   ORFNames=Dsim_GD11040 {ECO:0000313|EMBL:EDX07069.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX07069.1, ECO:0000313|Proteomes:UP000000304};
RN   [1] {ECO:0000313|EMBL:EDX07069.1, ECO:0000313|Proteomes:UP000000304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mosaic {ECO:0000313|Proteomes:UP000000304};
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: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the shroom family.
CC       {ECO:0000256|ARBA:ARBA00006469}.
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DR   EMBL; CM000362; EDX07069.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4QFF9; -.
DR   SMR; B4QFF9; -.
DR   STRING; 7240.B4QFF9; -.
DR   EnsemblMetazoa; FBtr0347853; FBpp0312841; FBgn0182798.
DR   HOGENOM; CLU_023224_0_0_1; -.
DR   OMA; AHLCDTS; -.
DR   PhylomeDB; B4QFF9; -.
DR   Proteomes; UP000000304; Chromosome 2r.
DR   Bgee; FBgn0182798; Expressed in adult organism and 3 other cell types or tissues.
DR   GO; GO:0005912; C:adherens junction; IEA:EnsemblMetazoa.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IEA:EnsemblMetazoa.
DR   GO; GO:0051015; F:actin filament binding; IEA:EnsemblMetazoa.
DR   GO; GO:0019900; F:kinase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR   GO; GO:0031032; P:actomyosin structure organization; IEA:EnsemblMetazoa.
DR   GO; GO:0003383; P:apical constriction; IEA:EnsemblMetazoa.
DR   GO; GO:0048598; P:embryonic morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IEA:EnsemblMetazoa.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IEA:EnsemblMetazoa.
DR   GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IEA:EnsemblMetazoa.
DR   GO; GO:0071896; P:protein localization to adherens junction; IEA:EnsemblMetazoa.
DR   Gene3D; 6.10.250.3120; -; 1.
DR   InterPro; IPR014799; ASD2_dom.
DR   InterPro; IPR027685; Shroom_fam.
DR   PANTHER; PTHR15012; APICAL PROTEIN/SHROOM-RELATED; 1.
DR   PANTHER; PTHR15012:SF32; PROTEIN SHROOM; 1.
DR   Pfam; PF08687; ASD2; 1.
DR   PROSITE; PS51307; ASD2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000304}.
FT   DOMAIN          139..406
FT                   /note="ASD2"
FT                   /evidence="ECO:0000259|PROSITE:PS51307"
FT   REGION          46..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          234..261
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          323..350
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   410 AA;  46185 MW;  3FE372EB87F53D45 CRC64;
     MNRQESLREN IEKITQLQSV LMSAHLCDTS LLSGYTTPLI TSPTASFANE PLMTPPLPPS
     PPPPLEPEEE QEENDMPDKQ PEIEELQLMQ RSELVLMVNP KPSTMDMACQ TDELEDRDTD
     LEAAREEHQT RTTLQPRQRQ PIELDYEQMS RELVKLLPPG DKIADILTPK ICKPTSQYVS
     NLYNPDVPLR LAKRDVGTST LMRMKSITSS AEIRVVSVEL QLAEPSEEPT NLIKQKMDEL
     IKHLNQKIVS LKREQQTISE ECSANDRLGQ DLFAKLAEKV RPSEASKFRT HVDAVGNITS
     LLLSLSERLA QTESSLETRQ QEKGALESKR DLLYEQLEEA QRLKSDIERR GVSIAGLLGK
     NLSADMCADY DYFINMKAKL IADARDLAVR IKGSEEQLSS LSDALVQSDC
//
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