AGO3_BOMMO
ID AGO3_BOMMO Reviewed; 926 AA.
AC A9ZSZ2; A7BJS3; H9JHN9;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Piwi-like protein Ago3;
DE Short=BmAGO3 {ECO:0000303|PubMed:18191035};
DE EC=3.1.26.-;
GN Name=AGO3;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tatsuke T., Tsukioka H., Sakashita K., Mitsunobu H., Lee J., Kawaguchi Y.,
RA Kusakabe T.;
RT "Molecular cloning of Piwi and Aubergine homolog genes from the silkworm,
RT Bombyx mori.";
RL Entomotech 31:43-46(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18191035; DOI=10.1016/j.bbrc.2008.01.013;
RA Kawaoka S., Minami K., Katsuma S., Mita K., Shimada T.;
RT "Developmentally synchronized expression of two Bombyx mori Piwi subfamily
RT genes, SIWI and BmAGO3 in germ-line cells.";
RL Biochem. Biophys. Res. Commun. 367:755-760(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [4]
RP FUNCTION.
RX PubMed=19460866; DOI=10.1261/rna.1452209;
RA Kawaoka S., Hayashi N., Suzuki Y., Abe H., Sugano S., Tomari Y.,
RA Shimada T., Katsuma S.;
RT "The Bombyx ovary-derived cell line endogenously expresses PIWI/PIWI-
RT interacting RNA complexes.";
RL RNA 15:1258-1264(2009).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF TYR-633.
RX PubMed=24757166; DOI=10.1261/rna.044701.114;
RA Cora E., Pandey R.R., Xiol J., Taylor J., Sachidanandam R., McCarthy A.A.,
RA Pillai R.S.;
RT "The MID-PIWI module of Piwi proteins specifies nucleotide- and strand-
RT biases of piRNAs.";
RL RNA 20:773-781(2014).
RN [6]
RP INTERACTION WITH PAPI, AND DOMAIN.
RX PubMed=23970546; DOI=10.1261/rna.040428.113;
RA Honda S., Kirino Y., Maragkakis M., Alexiou P., Ohtaki A., Murali R.,
RA Mourelatos Z., Kirino Y.;
RT "Mitochondrial protein BmPAPI modulates the length of mature piRNAs.";
RL RNA 19:1405-1418(2013).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25558067; DOI=10.1016/j.celrep.2014.12.013;
RA Nishida K.M., Iwasaki Y.W., Murota Y., Nagao A., Mannen T., Kato Y.,
RA Siomi H., Siomi M.C.;
RT "Respective functions of two distinct Siwi complexes assembled during PIWI-
RT interacting RNA biogenesis in Bombyx germ cells.";
RL Cell Rep. 10:193-203(2015).
CC -!- FUNCTION: Endoribonuclease that plays a central role during
CC spermatogenesis by repressing transposable elements and preventing
CC their mobilization, which is essential for the germline integrity
CC (PubMed:19460866). Plays an essential role in meiotic differentiation
CC of spermatocytes, germ cell differentiation and in self-renewal of
CC spermatogonial stem cells (PubMed:19460866, PubMed:25558067). Its
CC presence in oocytes suggests that it may participate in similar
CC functions during oogenesis in females (PubMed:18191035). Acts via the
CC piRNA metabolic process, which mediates the repression of transposable
CC elements during meiosis by forming complexes composed of piRNAs and
CC Piwi proteins and govern the methylation and subsequent repression of
CC transposons (PubMed:19460866, PubMed:25558067). Directly binds piRNAs,
CC a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-
CC independent mechanism and are primarily derived from transposons and
CC other repeated sequence elements (PubMed:19460866, PubMed:25558067).
CC Strongly prefers a have adenine at position 10 of their guide (g10A
CC preference) (PubMed:24757166, PubMed:25558067). Plays a key role in the
CC piRNA amplification loop, also named ping-pong amplification cycle:
CC antisense piRNA-bound Siwi and sense piRNA-bound Ago3 reciprocally
CC cleave complementary transcripts, to couple the amplification of piRNAs
CC with the repression of transposable elements (PubMed:25558067).
CC {ECO:0000269|PubMed:18191035, ECO:0000269|PubMed:19460866,
CC ECO:0000269|PubMed:24757166, ECO:0000269|PubMed:25558067}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A8D8P8};
CC -!- SUBUNIT: Interacts (when symmetrically methylated) with Papi/TDRKH
CC (PubMed:23970546). Interacts with Vasa. {ECO:0000269|PubMed:23970546}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25558067}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. {ECO:0000269|PubMed:25558067}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the larval testis, pupal ovary
CC and adult eggs. {ECO:0000269|PubMed:18191035}.
CC -!- PTM: Arginine methylation is required for the interaction with Tudor
CC domain-containing protein Papi/TDRKH. {ECO:0000269|PubMed:23970546}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
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DR EMBL; AB332312; BAF73717.2; -; mRNA.
DR EMBL; AB372007; BAF98575.1; -; mRNA.
DR EMBL; BABH01012993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001098067.2; NM_001104597.2.
DR RefSeq; XP_012550549.1; XM_012695095.1.
DR AlphaFoldDB; A9ZSZ2; -.
DR SMR; A9ZSZ2; -.
DR GeneID; 100125337; -.
DR KEGG; bmor:100125337; -.
DR CTD; 192669; -.
DR eggNOG; KOG1042; Eukaryota.
DR HOGENOM; CLU_008813_0_0_1; -.
DR OrthoDB; 220258at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061980; F:regulatory RNA binding; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Endonuclease; Hydrolase;
KW Magnesium; Meiosis; Metal-binding; Methylation; Nuclease;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Spermatogenesis.
FT CHAIN 1..926
FT /note="Piwi-like protein Ago3"
FT /id="PRO_0000439354"
FT DOMAIN 332..455
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 620..912
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 697
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 735
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 767
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 901
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT BINDING 672
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT BINDING 926
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT MUTAGEN 633
FT /note="Y->L: Does not affect ability to recognize adenine
FT at position 10 of piRNAs (g10A preference)."
FT /evidence="ECO:0000269|PubMed:24757166"
FT CONFLICT 108
FT /note="N -> S (in Ref. 1; BAF73717)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="I -> V (in Ref. 1; BAF73717)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> T (in Ref. 1; BAF73717)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="H -> Y (in Ref. 2; BAF98575)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="V -> I (in Ref. 2; BAF98575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 104557 MW; A0399D0D09E2F2C8 CRC64;
MADPGKGRGR SLALLQALKK SQMMDSPSQS ESQSPESTPE QSTAPSTIAS ATPSTSGVSI
GGRGRAAALM LAKMQQKPGS TTPAIFVPPS STSAPTAGTG RGFKLLQNLQ ASQKASSQIA
SSQVTSSAQS DIKDLTEKMS ETSVSAQASS VAKNKYFREV KDTPPVVKKG ETGVPIEVTC
NYIYLNFKEN IVFEYEVKFE PDQDYKHLRF KLLNEHIEHF KEKTFDGTTL YVPHELPDAV
RNLVSTNPYD QSKVNVSIIF RRTRRLSEMI HIYNVMFKCI MKDLKLIRFG RQHYNEHAAI
QIPQHKLEVW PGYVTAVDEY EGGLMLTLDS THRVLRTQTV LSLIKEVVQT EGANWKRKMT
DILIGASVMT TYNKKLFRVD TIDDKMSPRS TFEKTEKGET VQISFIDYYK KNYGIEIMDW
DQPLLISRDT KRMPGSDTPT DFMICLIPEL CQLTGLTDDQ RSNFRLMKDV ATYTRITPNQ
RHAAFKKYIE SVMKNETAKS RLAGWGLSIA PETVNLTART LPPETLYFGD NVRVPGKPNA
EWNSEVTKHS VMQAVDIMRW VLLFTQRDKQ VAMDFLSTLK RNCRPMGIMV SDAELVPLAN
DRTDTYVLAL KKCITSSVQL VVAICSTKRD DRYAAIKKVC CADNPVPSQV INARTLMNTN
KIRSITQKIL LQLNCKLGGT LWSISIPFKS AMIVGIDSYH DPSRRNRSVC SFVASYNQSM
TLWYSKVIFQ EKGQEIVDGL KCCLVDALTH YLRSNGQLPD RIIIYRDGVG DGQLKLLQQY
EIPQMKICFT ILGSNYQPTL TYVVVQKRIN TRIFLKSRDG YDNPNPGTVV DHCITRRDWY
DFLIVSQKVT QGTVTPTHYV VVYDDSGITP DQCQRLTYKM CHLYYNWPGT VRVPAPCQYA
HKLSYLVGQC VHAQPSDVLV DKLFFL
