SRRT_DROME
ID SRRT_DROME Reviewed; 943 AA.
AC Q9V9K7; A4UZ50; Q53XG1; Q8SWW6; Q95TJ0;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=CG7843;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND SER-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-79; SER-81; THR-300; SER-303;
RP SER-309; SER-349; SER-352; SER-640 AND SER-642, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP FUNCTION, INTERACTION WITH PASHA; CBP20 AND DCR-2, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19632183; DOI=10.1016/j.cell.2009.04.045;
RA Sabin L.R., Zhou R., Gruber J.J., Lukinova N., Bambina S., Berman A.,
RA Lau C.-K., Thompson C.B., Cherry S.;
RT "Ars2 regulates both miRNA- and siRNA- dependent silencing and suppresses
RT RNA virus infection in Drosophila.";
RL Cell 138:340-351(2009).
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:0000269|PubMed:19632183}.
CC -!- SUBUNIT: Interacts with cbp20, Dcr-2 and pasha.
CC {ECO:0000269|PubMed:19632183}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Lethality. {ECO:0000269|PubMed:19632183}.
CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM11365.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM11365.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF57281.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68343.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68344.1; -; Genomic_DNA.
DR EMBL; AY058743; AAL13972.1; ALT_INIT; mRNA.
DR EMBL; AY095037; AAM11365.1; ALT_SEQ; mRNA.
DR EMBL; BT011368; AAR96160.1; -; mRNA.
DR RefSeq; NP_610203.2; NM_136359.3.
DR RefSeq; NP_724453.1; NM_165458.2.
DR RefSeq; NP_724454.1; NM_165459.2.
DR AlphaFoldDB; Q9V9K7; -.
DR SMR; Q9V9K7; -.
DR BioGRID; 61443; 13.
DR DIP; DIP-24057N; -.
DR IntAct; Q9V9K7; 8.
DR STRING; 7227.FBpp0085354; -.
DR iPTMnet; Q9V9K7; -.
DR PaxDb; Q9V9K7; -.
DR PRIDE; Q9V9K7; -.
DR DNASU; 35539; -.
DR EnsemblMetazoa; FBtr0086018; FBpp0085354; FBgn0033062.
DR EnsemblMetazoa; FBtr0086020; FBpp0085356; FBgn0033062.
DR EnsemblMetazoa; FBtr0086021; FBpp0085357; FBgn0033062.
DR GeneID; 35539; -.
DR KEGG; dme:Dmel_CG7843; -.
DR UCSC; CG7843-RA; d. melanogaster.
DR CTD; 35539; -.
DR FlyBase; FBgn0033062; Ars2.
DR VEuPathDB; VectorBase:FBgn0033062; -.
DR eggNOG; KOG2295; Eukaryota.
DR GeneTree; ENSGT00390000005492; -.
DR HOGENOM; CLU_008560_0_0_1; -.
DR InParanoid; Q9V9K7; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; Q9V9K7; -.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9V9K7; -.
DR BioGRID-ORCS; 35539; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 35539; -.
DR PRO; PR:Q9V9K7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033062; Expressed in eye disc (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q9V9K7; baseline and differential.
DR Genevisible; Q9V9K7; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:FlyBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; IMP:UniProtKB.
DR GO; GO:0030422; P:siRNA processing; IMP:FlyBase.
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 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..943
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000220968"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..886
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 284..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 943 AA; 107222 MW; 0C1AF09E02E8AB0B CRC64;
MGDSDDEYDR KRRDKFRGER ESYRTERRDD RRPVGGSAGA RDEWAERNPF RGGASAGGGG
ARHRPDYSDY RGPGARPRYG SPVRDLPPAK RMRPDWGDGD VRANPRFGGY DPYLMQAWND
HYQSMHSAYS HGGHAPPVRE SIGGGGGDTL TQPAMLNLKQ FLDTQDENIS DSEVMRKYTE
YKTDFKRQQL NEFFVAHKDE EWFKNKYHPE DSVKRSEEQR GFLQRRTDVF MELLENGTIG
SVKVDSSQAD ALIRVLDTCV IKLEGGTDED LKVLDEKPKD PVVYERKAEQ MQSVKEVEKT
INSPKEEMSE ADPVSTQRKP VRPVNSDGEN WDDDDAENSA PKKELAEDSK DSDSKPEDKQ
LNKKKTKKRK RNSSDDDSSS SESSSSSDEE KLKEKYDVED GLRAEQKTEA EKDRQEATKA
KQGPQSPKLD EDEGNENTEP KGLDSKINTY EEIDNTLKSP EISSNPIKNT DNGDGSKVEE
DGEKPSVGKD KVVETETIDL DKVKDGQPRA LHRTSSIFLR NLAPSITRSE IEAVCNRFSG
YLRVAIADPL VERRWYRRGW ITFMRDVNIK EICWGLNNQR LRDCEMGAIV NRDLSRRVRP
ANGITAHKQV VRSDIKLCAK IALNLDEKFR LWAEGPKDDS NSARANESSE NGSGSTYGFN
SQNPVLQNIT DYLIEEASAE EEELLGLTGE NKDTEGEPIE RDEQLISVLD RLVLYLRIVH
SVDYYNHCEY PYEDEMPNRC GIIHARGPPP VRVTNNDVQE YIKIYESKLQ QFLTKTVPLS
DEEIKNLGAK DAETEVEKFV QANTQELAKD KWLCPLSGKK FKGPEFIRKH IFNKHEEKVD
EVRKEVQYFN NYLRDPKRPQ LPEHPGTSKR PESESARGGG GGYRPPMYPP FSAMPYGFGP
PMMGGGRGGR NFPPARRELP LEHQRRLIGY HDLDAPANSD MFD
