SRRT_DROPS
ID SRRT_DROPS Reviewed; 951 AA.
AC Q28WQ8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=GA20626;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CM000071; EAL26609.2; -; Genomic_DNA.
DR RefSeq; XP_001362029.2; XM_001361992.4.
DR RefSeq; XP_015040780.1; XM_015185294.1.
DR AlphaFoldDB; Q28WQ8; -.
DR SMR; Q28WQ8; -.
DR STRING; 7237.FBpp0278776; -.
DR PRIDE; Q28WQ8; -.
DR EnsemblMetazoa; FBtr0280338; FBpp0278776; FBgn0080620.
DR EnsemblMetazoa; FBtr0372149; FBpp0334198; FBgn0080620.
DR GeneID; 4805668; -.
DR KEGG; dpo:Dpse_GA20626; -.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_008560_0_0_1; -.
DR InParanoid; Q28WQ8; -.
DR OMA; HLRMCEE; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0080620; Expressed in insect adult head and 2 other tissues.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR035979; RBD_domain_sf.
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.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 3: Inferred from homology;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..951
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385221"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..893
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 300..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..880
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 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 951 AA; 107827 MW; 5DF1B34EC0BE5568 CRC64;
MADSDDEYDR KRRDKFRGER ESYRTERRDE RRPIGGAGGG RDEWSERNPF RGGGAGGGGA
PRHRPDYSDY RGPGPRARYG SPVRDMPPPK RMRSDWGDGD GRPGPRYGGY DPYLMQAWTD
HYQSMHSAYH HASHPPPVRE LPIIGGDTLT QPAMLNLKQF LDTQDENISD SEVMRKYTEY
KTDFKRQQLN EFFVAHKDEE WFKNKYHPED SVNRSEEQRG FLRRRTDVFV ELLENGTIGS
VKVDSSHGDA LIRVLDTCVI KLEGGTDEDL KVLDEKPKEA LVFDRKPESV DPTTVVENTP
KSPKKEKEED ELPLIVSPQR IALKPVNSDD ENWDDAEVED APPKKPEEEE PKESEPIPEI
KQKQKKEKKK KIKKRKRNSS SDEESSSSES ESSSSSSEEE EEDDEKLKAK YDVEDGLRAE
QKAEAEKDQA EAAKAKLGSV SPKEEISPEK SAADPEVEGE AKEDGKQAEK SPKCDDEKKQ
ENGDAAKVES AAEPATGDAQ GEVKPVTIDL DKVNPPRAMH RTSSIFLRNL APSITKAEIE
ALCSRFSGYL RTAIADPLVE RRWYRRGWIT FTRDVNIKEI CWSLNNQRLR DCEMGAIVNR
DLSRRVRPAN GITAHKQVVR SDIKLCARIV MNLDEKFKLW SEGPLSKPSP ASDSEATAAN
GSGSSYGFNS KNPVLQNITD YLIEEASAEE EELLGLSGDR KDGEGEPIER DEQLLSVLDR
LVLYLRIVHS VDYYNHCEYP YEDEMPNRCG IIHARGPAPS RVTSNELNEY IKSYEGKLLQ
FLTKTALLSE DQIKDLGAKN ADTEVEKFVQ ANTQELAKDK WLCPLSGKKF KGPEFIRKHI
FNKHEEKVDE VRKEVQYFNN YLRDPKRPQL PEHPGSVKRP ETESVRGPGG YRPPMYTPMS
GMPYSFGGHM MGGGRGGRHF PPARRELPLE HHRRLVGYHD LDAPSNSDIF D
