SRRT_DROSE
ID SRRT_DROSE Reviewed; 947 AA.
AC B4II37;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=GM16482;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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 -!- SEQUENCE CAUTION:
CC Sequence=EDW49563.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH480841; EDW49563.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002043397.1; XM_002043361.1.
DR AlphaFoldDB; B4II37; -.
DR SMR; B4II37; -.
DR STRING; 7238.B4II37; -.
DR EnsemblMetazoa; FBtr0199467; FBpp0197959; FBgn0171397.
DR Proteomes; UP000001292; 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..947
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385222"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..666
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..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..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 460..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..666
FT /note="Polar 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 79
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 81
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 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 947 AA; 107857 MW; 5EF5EBDDC0F2C78C CRC64;
MADSDDEYDR KRRDKFRGER DSYRTERRDD RRPVGGSAGA RDEWAERNPF RGAASAGGGG
ARHRPDYSDY RGPGARPRYG SPGRDLPPAK RMRPDWGDGD VRANPRFGGY DPYLMQAWND
HYQSMHSAYS HAGHAPPVRE SIGGGGSDTL TQPAMLNLKQ FLDTQDENIS DSEVMRKYTD
YKTDFKRQQL NEFFVAHKDE EWFKNKYHPE DSVKRNEEQR GFLQRRTDVF MELLENGTIG
SVKVDSSQAD ALIRVLDTCV IKLEGGTDED LKVLDEKPKD PVVYERKAEP MQSVKEVEKT
INSPKDEISE ADPLPAVVST QRKPVGPVNS DEENWDDDND AENSTPKKEL AEDSKDSDSK
PEEKQLNKKK TKKRKRNSSD DDSSSSESSS SSDEEKLKEK YDVEDGLRTE QKIEAEKDRQ
EATKAKQEPQ SPKLDEVEGN DTTEPKGLDS KINTVEIDDT LKSPEISSNP IKNTDNGDSS
KVEEDEEKPS VGKDKVVETE TIDLDKVKDC QPRALHRTSS IFLRNLAPSI TRSEIEAMCN
RFTGYLRVAI ADPLVERRWY RRGWITFMRD VNIKEICWGL NNQRLRDCEM GAIVNRDLSR
RVRPANGITA HKQVVRSDIK LCAKIALNLD EKFRLWAEVP KDDPNSARAN ESSENGSGST
YGFNSQNPVL QNITDYLIEE ASAEEEELLG LTGENKDTEG EPIERDEQLI SVLDRLVLYL
RIVHSVDYYN HCEYPYEDEM PNRCGIIHAR GPPPVRVTNN DVQEYIKMYE TKLQQFLTKT
VPLSDEEIKN LGAKDAETEV EKFVQANTQE LAKDKWLCPL SGKKFKGPEF IRKHIFNKHE
EKVDEVRKEV QYFNNYLRDP KRPQLPEHPG TSKRPESESA RGGGGGYRPP MYPPFSAMPY
GFGPPMMGGG RGGRNFPPAR RELPLEHQRR LIGYHDLDAP ANSDMFD
