ID A0A0P8XRT0_DROAN Unreviewed; 940 AA.
AC A0A0P8XRT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Serrate RNA effector molecule homolog {ECO:0000256|ARBA:ARBA00017364};
DE AltName: Full=Arsenite-resistance protein 2 homolog {ECO:0000256|ARBA:ARBA00030701};
GN Name=Dana\GF13819 {ECO:0000313|EMBL:KPU77297.1};
GN Synonyms=dana_GLEANR_13826 {ECO:0000313|EMBL:KPU77297.1};
GN ORFNames=GF13819 {ECO:0000313|EMBL:KPU77297.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:KPU77297.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:KPU77297.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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 -!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and
CC RNA-mediated gene silencing (RNAi). Involved in innate immunity via the
CC short interfering RNAs (siRNAs) processing machinery by restricting the
CC viral RNA production. Also involved microRNA (miRNA)-mediated silencing
CC by contributing to the stability and delivery of primary miRNA
CC transcripts to the primary miRNA processing complex containing drosha
CC and pasha. {ECO:0000256|ARBA:ARBA00025002}.
CC -!- SUBUNIT: Interacts with cbp20, Dcr-2 and pasha.
CC {ECO:0000256|ARBA:ARBA00011796}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ARS2 family.
CC {ECO:0000256|ARBA:ARBA00005407}.
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DR EMBL; CH902619; KPU77297.1; -; Genomic_DNA.
DR RefSeq; XP_014763904.1; XM_014908418.1.
DR AlphaFoldDB; A0A0P8XRT0; -.
DR SMR; A0A0P8XRT0; -.
DR EnsemblMetazoa; FBtr0383571; FBpp0343692; FBgn0090846.
DR GeneID; 6496655; -.
DR OrthoDB; 4174205at2759; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR InterPro; IPR039727; SE/Ars2.
DR InterPro; IPR007042; SERRATE/Ars2_C.
DR InterPro; IPR021933; SERRATE/Ars2_N.
DR PANTHER; PTHR13165; ARSENITE-RESISTANCE PROTEIN 2; 1.
DR PANTHER; PTHR13165:SF0; SERRATE RNA EFFECTOR MOLECULE HOMOLOG; 1.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801}.
FT DOMAIN 157..266
FT /note="SERRATE/Ars2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12066"
FT DOMAIN 747..912
FT /note="SERRATE/Ars2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04959"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 106699 MW; D85492B597EE46B2 CRC64;
MADSDDEYDR KRRDKFRGER SDSYRTERRD DRRPLGGSGS ARDEWSDRGG ASAGGGGGGA
RHRPDYSDYR GPGPRARYGS PGRDLPPAKR MRPDWGDGDV RPNPRFGGYD PYLMQAWNDH
YQSIHSAYSH GSHMPPVRES GGSGGDSLTQ PAMLNLKQFL DTQDENISDS EVMRKYTEYK
TDFKRQQLNE FFVAHKDEEW FKNKYHPEDS VRRAEEQRGF LKRRTDVFVE LLENGTIGSV
KVDSVQGDAL IRVLDTCVIK LEGGTDEDLK ALDEKPKETP VYERKHDPAP VKAVDEVKSP
KKETEKEASP VIVSPQRKSV KPLNSDDENW DEEVAAPPKK DVEEEPKALE SGSEDKSRRK
KSAKRKRVNS GDDSSSESDS SSSSDDEDEE KLKKKYDVED GLRSEQKAEA EKDKEMQDAK
VIEAPESPKE ATENSAEEVK ASDAAETPAE EAEQEKPEVA EEVNRPKQDQ ENGDKITTED
GETKSDSEEN KVMETETIDL DKVRDGQPRA LHRTSSIFLR NLAPSITKAE IEAVCTRFSG
YLRVAIADPL VERRWYRRGW ITFTRDVNIK EICWSLNNQR LRDCEMGAIV NRDLSRRVRP
ANGITAHKQV VRSDIKLCAK IILNLDERFR LWPEPTSDDS IPFDRAGESS ANGNTSTYGI
KSKNPVLQNI TDYLIEEASA EEEELLGLTG ENKDAEGEPI ERDEHLLAVL DRLVLYLRIV
HSVDYYNHCE YPYEDEMPNR CGIIHARGPA PSRVTSNDIH EYVKTYESKL QQFLTKTALL
SDEETKDLGA KDAETEVEKF VQANTQELAK DKWLCPLSGK KFKGPEFIRK HIFNKHEEKV
DEVRKEVQYF NNYLRDPKRP QLPEHPGSSK RPESESGRGG GSGYRPPMYP PFSGMPYGFS
PSMMGGGRGG RNFPPVRRPG GFDYRPRSHY RDLDAPQEPY
//
