SRRT_DROAN
ID SRRT_DROAN Reviewed; 948 AA.
AC B3MJ69;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=GF13819;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with cbp20, Dcr-2 and pasha. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH902619; EDV38163.1; -; Genomic_DNA.
DR RefSeq; XP_001961341.1; XM_001961305.2.
DR AlphaFoldDB; B3MJ69; -.
DR SMR; B3MJ69; -.
DR STRING; 7217.FBpp0117011; -.
DR PRIDE; B3MJ69; -.
DR EnsemblMetazoa; FBtr0118519; FBpp0117011; FBgn0090846.
DR GeneID; 6496655; -.
DR KEGG; dan:6496655; -.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_008560_0_0_1; -.
DR InParanoid; B3MJ69; -.
DR OMA; HLRMCEE; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; B3MJ69; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:EnsemblMetazoa.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR GO; GO:0030422; P:siRNA processing; IEA:EnsemblMetazoa.
DR InterPro; IPR039727; SE/Ars2.
DR InterPro; IPR007042; SERRATE/Ars2_C.
DR InterPro; IPR021933; SERRATE/Ars2_N.
DR PANTHER; PTHR13165; PTHR13165; 1.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
PE 3: Inferred from homology;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..948
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385216"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..893
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 274..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 948 AA; 107630 MW; 6132FC6780ECFBC7 CRC64;
MADSDDEYDR KRRDKFRGER SDSYRTERRD DRRPLGGSGS ARDEWSDRNP FRGGASAGGG
GGGARHRPDY SDYRGPGPRA RYGSPGRDLP PAKRMRPDWG DGDVRPNPRF GGYDPYLMQA
WNDHYQSIHS AYSHGSHMPP VRESGGSGGD SLTQPAMLNL KQFLDTQDEN ISDSEVMRKY
TEYKTDFKRQ QLNEFFVAHK DEEWFKNKYH PEDSVRRAEE QRGFLKRRTD VFVELLENGT
IGSVKVDSVQ GDALIRVLDT CVIKLEGGTD EDLKALDEKP KETPVYERKH DPAPVKAVDE
VKSPKKETEK EASPVIVSPQ RKSVKPLNSD DENWDEEVAA PPKKDVEEEP KALESGSEDK
SRRKKSAKRK RVNSGDDSSS ESDSSSSSDD EDEEKLKKKY DVEDGLRSEQ KAEAEKDKEM
QDAKVIEAPE SPKEATENSA EEVKASDAAE TPAEEAEQEK PEVAEEVNRP KQDQENGDKI
TTEDGETKSD SEENKVMETE TIDLDKVRDG QPRALHRTSS IFLRNLAPSI TKAEIEAVCT
RFSGYLRVAI ADPLVERRWY RRGWITFTRD VNIKEICWSL NNQRLRDCEM GAIVNRDLSR
RVRPANGITA HKQVVRSDIK LCAKIILNLD ERFRLWPEPT SDDSIPFDRA GESSANGNTS
TYGIKSKNPV LQNITDYLIE EASAEEEELL GLTGENKDAE GEPIERDEHL LAVLDRLVLY
LRIVHSVDYY NHCEYPYEDE MPNRCGIIHA RGPAPSRVTS NDIHEYVKTY ESKLQQFLTK
TALLSDEETK DLGAKDAETE VEKFVQANTQ ELAKDKWLCP LSGKKFKGPE FIRKHIFNKH
EEKVDEVRKE VQYFNNYLRD PKRPQLPEHP GSSKRPESES GRGGGSGYRP PMYPPFSGMP
YGFSPSMMGG GRGGRNFPPV RRELPLEHQR RLIGYHDLDA PANSDMFD