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Database: UniProt
Entry: A9ZSZ2
LinkDB: A9ZSZ2
Original site: A9ZSZ2 
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   11-DEC-2019, entry version 44.
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; Holometabola; 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}.
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   SMR; A9ZSZ2; -.
DR   STRING; 7091.BGIBMGA009037-TA; -.
DR   PRIDE; A9ZSZ2; -.
DR   GeneID; 100125337; -.
DR   KEGG; bmor:100125337; -.
DR   CTD; 192669; -.
DR   eggNOG; KOG1042; Eukaryota.
DR   eggNOG; ENOG410XNRH; LUCA.
DR   KO; K02156; -.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0007275; P:multicellular organism development; 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   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   METAL           672
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT   METAL           926
FT                   /note="Magnesium; via carboxylate"
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
//
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