SRRT_AEDAE
ID SRRT_AEDAE Reviewed; 937 AA.
AC Q17FR9; Q17FS0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=AAEL003287;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT45432.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH477268; EAT45431.1; -; Genomic_DNA.
DR EMBL; CH477268; EAT45432.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001663544.1; XM_001663494.1.
DR RefSeq; XP_001663545.1; XM_001663495.1.
DR AlphaFoldDB; Q17FR9; -.
DR SMR; Q17FR9; -.
DR STRING; 7159.AAEL003287-PA; -.
DR PRIDE; Q17FR9; -.
DR GeneID; 5577779; -.
DR KEGG; aag:5577779; -.
DR VEuPathDB; VectorBase:AAEL003287; -.
DR eggNOG; KOG2295; Eukaryota.
DR InParanoid; Q17FR9; -.
DR OMA; HLRMCEE; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; Q17FR9; -.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
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; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..937
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385214"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 107294 MW; 917BE908B263DF3B CRC64;
MGDSDDEYDR KRRDKFRGER SAGESYARGA DRADRSRGRD EWAERGRPRQ DYRDYRPPPR
DRGYSPTREG PPMKRMRGDG WGDDARPRFG GHEPYGMYGG YNHDHFGMHP AGPYGHPGGL
HPREQQSAGD MQTQPCMMTL KQFLATQDDS ISDSEAIQKY NDYKLEFKRQ QLNEFFVAHK
DEEWFKMKYH PEESLKRKEE QFGFLKRRCD VFVELLDHGD ISKVSVDTSN TDPLLRLLDT
VVIKLEGGTD EDLKVLDEKP VEIVKILPEK PKVEVKKEPT LEDTIKKEKI SIKEEKVEEA
DKPKEEKDDD KEKPAAEGEE PEGEKNDAEK EVTAEREDMD AEPAAKEPEP EEEPSRKKDR
RKRSRSDSGS SSSSSSSSSS SDSEDEKEKE KEDKEEEEEK KETEEEAAPK SPKPVEEGEK
EPQEEVENNG HKSGDEEEAT KKDQAEPEKM DTDEAVVENN KESEEAEKEK DTSKDEEEAN
KESNEDKQES EKTETIDLVK DTTVGNSPRA LHRTSSIFLR NLAPSITKAE VEAMCKRYNG
FLRVAIADPL LERRWFRRGW VTFRRDVNIK EICWNLNNIR LRDCELGAIV NKDLSRRVRP
VNGLTCHKTI VRSDIKLCAK IAHNLDDKVG LWKEQEDNGE KNGESFGLQS KNPVLQNITD
YLIEEASAEE DELLGLSTEA AKKSNDGELV ERDTQLIEVL DKLILYLRVV HSIDFYNHCE
YPYEDEMPNR CGIIHARGPP PQNKVTSNEI QEYIRTFEGK MGSFLARAVD LEEEEMKKLG
AKDAEAEVEK FIQANTQELA KDKWLCPLSG KKFKGPDFVR KHIFNKHNEK VDEVRKEVEY
FNNYLKDTKR PQLPEHPGNT KKAPSDAAPP TAGYRPPYGM AHAYAPMYAP YAQPMMAPAG
RARPGFGRGG REPMGEIRRP IIAYSDLDMP NFSDSFL