SRRT_DROER
ID SRRT_DROER Reviewed; 947 AA.
AC B3N3F7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=GG10831;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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}.
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DR EMBL; CH954177; EDV59839.1; -; Genomic_DNA.
DR RefSeq; XP_001970780.1; XM_001970744.2.
DR AlphaFoldDB; B3N3F7; -.
DR SMR; B3N3F7; -.
DR STRING; 7220.FBpp0129377; -.
DR PRIDE; B3N3F7; -.
DR EnsemblMetazoa; FBtr0130885; FBpp0129377; FBgn0103136.
DR GeneID; 6541642; -.
DR KEGG; der:6541642; -.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_008560_0_0_1; -.
DR OMA; HLRMCEE; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; B3N3F7; -.
DR Proteomes; UP000008711; 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; RNA-mediated gene silencing.
FT CHAIN 1..947
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385217"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..890
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 295..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 354
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"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 947 AA; 107710 MW; AC2F92B82B782D77 CRC64;
MADSDDEYDR KRRDKFRGER SDSYRTERRD DRRPVGGSAG ARDEWAERNP FRGGASAGGG
GARHRPDYSD YRGPGARPRY GSPGRDLPPA KRMRPDWGDA DLRPNPRFGG YDPYLMQAWN
DHYQSMHSAY SHAGHAPPVR ESIGGGGDTL TQPAMLNLKQ FLDTQDENIS DSEVMRKYTE
YKTDFKRQQL NEFFVAHKDE EWFKNKYHPE DSVKRSDEQR GFLQRRTDVF VELLENGTIG
SVKVDSSQGD ALIRVLDTCV IKLEGGTDED LKVLDEKPKD PVVCERKAEP IESAKAVEKT
INSPKEEKIS EGDPLPAIVS PQRKTVKSVN SDEENWDDED AENATPKKEL GEDSKGTDSK
PEDKQLNKKK TKKRKRNSTD DDSSSSESSS SSDEEKLKEK YDVEDGLRAE QKADAEKDRH
EATKAKQEPE SPKLQELEGK EIVEPKELDS KSNTAENDDT LKSPEISPTP IKGTDNGDDN
KVEEDEKKPS VDEIKVVETE TIDLDKVKNG QPRALHRTSS IFLRNLAPSI TRAEIETVCN
RFTGYLRVAI ADPLVERRWY RRGWITFMRD VNIKEICWGL NNHRLRDCEM GAIVNRDLSR
RVRPANGITA HKQVVRSDIK LCAKIALNLD ERFRLWAEVP TDDSHPSRAD ESTENGSGST
YGFNSKNPVL QNITDYLIEE ASAEEEELLG LTGENKDTDG EPIERDEQLI SVLDRLVLYL
RIVHSVDYYN HCEYPYEDEM PNRCGIIHAR GPAPVRVTNN DVQEYIKTYE SKLQQFLTKT
VLLSDEEIKD LGAKDPETEV EKFVQANTQE LAKDKWLCPL SGKKFKGPEF IRKHIFNKHE
EKVDEVRKEV QYFNNYLRDP KRPQLPEHPG TSKRTESESA RGGGGGYRPP MYPPFSAMPY
GFGPPMMGGG RGGRNFPPAR RELPLEHQRR LIGYHDLDAP ANSDMFD
