ID B4Q510_DROSI Unreviewed; 859 AA.
AC B4Q510;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE SubName: Full=GD22547 {ECO:0000313|EMBL:EDX04002.1};
GN Name=Dsim\GD22547 {ECO:0000313|EMBL:EDX04002.1};
GN ORFNames=Dsim_GD22547 {ECO:0000313|EMBL:EDX04002.1};
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:EDX04002.1, ECO:0000313|Proteomes:UP000000304};
RN [1] {ECO:0000313|EMBL:EDX04002.1, 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 {ECO:0000256|ARBA:ARBA00004496}.
CC Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the Homer family.
CC {ECO:0000256|ARBA:ARBA00023606}.
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DR EMBL; CM000361; EDX04002.1; -; Genomic_DNA.
DR AlphaFoldDB; B4Q510; -.
DR SMR; B4Q510; -.
DR STRING; 7240.B4Q510; -.
DR EnsemblMetazoa; FBtr0354659; FBpp0319019; FBgn0193948.
DR HOGENOM; CLU_332965_0_0_1; -.
DR Proteomes; UP000000304; Chromosome 2l.
DR Bgee; FBgn0193948; Expressed in embryo and 3 other cell types or tissues.
DR GO; GO:0030425; C:dendrite; IEA:EnsemblMetazoa.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblMetazoa.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:EnsemblMetazoa.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0035256; F:G protein-coupled glutamate receptor binding; IEA:InterPro.
DR GO; GO:0070737; F:protein-glycine ligase activity, elongating; IEA:EnsemblMetazoa.
DR GO; GO:0070736; F:protein-glycine ligase activity, initiating; IEA:EnsemblMetazoa.
DR GO; GO:0048149; P:behavioral response to ethanol; IEA:EnsemblMetazoa.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IEA:InterPro.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
DR GO; GO:0018094; P:protein polyglycylation; IEA:EnsemblMetazoa.
DR GO; GO:0040012; P:regulation of locomotion; IEA:EnsemblMetazoa.
DR CDD; cd01206; EVH1_Homer_Vesl; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR045027; Homer.
DR InterPro; IPR044100; Homer_EVH1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR10918; HOMER; 1.
DR PANTHER; PTHR10918:SF5; HOMER, ISOFORM E; 1.
DR Pfam; PF03133; TTL; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
DR PROSITE; PS50229; WH1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000000304};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 463..575
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 706..822
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 96612 MW; 915DD164AC9C2C66 CRC64;
MQTRPSSEPH RSRDQVTDGD RNRDQPQKCA SATLAKKPKC ERNIMSRFLE HMPVDFLWTN
RKEKCDYIDQ AKNPGMTINK FHRAPFTSKE GLCSQLRDFH WFFEEGTAEM YFPRCYNVWS
PEELGEFIEN FKLTACVAFL RAMLCKYHKQ GSDAVFSCSG KIPYSAIDFA YKRLVEFIDS
CQHNDIDFED PPKIWEHEWD AFLFQHQQLV NEDGRIQHDG GQRLEPMVKS CLSLVDKMKV
HWPQYSLDGY QNLWIVKPAN KCRGRGIILM DNLKKILGVV NPSIASKSRY VVQKYIERPL
ILFQTKFDIR QWFLITNTQP LVVWFYRESY LRFSSQEYSL SNHHESVHLT NYAHQKSTPM
ESGTAPAQRE HVGLLLLPGV PPSNWQVQHV VGAYISRNAQ GHRWLYAGLP GEHGPTAQHL
RVFRRGLHDL REFLSLAHRD QLQSGSRSHH ECDGAHVSPV FGGCCQGEQP IFTCQAHVFH
IDPKTKRTWI TASMKAVNVS FFYDSSRNLY RIISVEGTKA VINSTITPNM TFTQTSQKFG
QWSDVRANTV YGLGFASEAE LTKFVEKFQE VKEATKNAMK SANGSNAVTP TTSANTSPIS
GRAVGSMQND NTAIDPHTVE PPNMSNTNTQ NANPDSPSHK LLNTSDVKAD IGSATPSPQP
TSGVTGGGGV TISSGGSIVG MHTGPGAGAT AEQQLKYENE RLKMALAQSC ANAKKWEIEL
ATLKNNNIRL TSALQESTAN VDEWKRQLHT YKEENIRLKR DMEQLCVGGG GVAAAGGGAT
EDELRREVAT LKARTEQLQK ELMQQELELK SANISLREKS NDQTLAKLSE VNGVFAKHLS
ELYGVQKDME SIIQLAKCT
//