PIWL2_XENTR
ID PIWL2_XENTR Reviewed; 949 AA.
AC A8KBF3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Piwi-like protein 2;
DE EC=3.1.26.- {ECO:0000250|UniProtKB:Q8CDG1};
GN Name=piwil2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING, TISSUE SPECIFICITY, AND
RP METHYLATION.
RX PubMed=19377467; DOI=10.1038/ncb1872;
RA Kirino Y., Kim N., de Planell-Saguer M., Khandros E., Chiorean S.,
RA Klein P.S., Rigoutsos I., Jongens T.A., Mourelatos Z.;
RT "Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for
RT Ago3 and Aub stability.";
RL Nat. Cell Biol. 11:652-658(2009).
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 Plays an essential role in meiotic differentiation of spermatocytes,
CC germ cell differentiation and in self-renewal of spermatogonial stem
CC cells. Acts via the piRNA metabolic process, which mediates the
CC repression of transposable elements during meiosis by forming complexes
CC composed of piRNAs and Piwi proteins and govern the methylation and
CC subsequent repression of transposons. During piRNA biosynthesis, plays
CC a key role in the piRNA amplification loop, also named ping-pong
CC amplification cycle, by acting as a 'slicer-competent' piRNA
CC endoribonuclease that cleaves primary piRNAs, which are then loaded
CC onto 'slicer-incompetent' piwil4. Piwil2 slicing produces a pre-miRNA
CC intermediate, which is then processed in mature piRNAs, and as well as
CC a 16 nucleotide by-product that is degraded. Required for piwil4/miwi2
CC nuclear localization and association with secondary piRNAs antisense.
CC Represses circadian rhythms by promoting the stability and activity of
CC core clock components ARNTL/BMAL1 and CLOCK (By similarity).
CC {ECO:0000250|UniProtKB:Q8CDG1}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9JMB7};
CC -!- SUBUNIT: Component of the PET complex. {ECO:0000250|UniProtKB:Q8CDG1}.
CC -!- INTERACTION:
CC A8KBF3; Q98SP8: epabp-a; Xeno; NbExp=3; IntAct=EBI-7191401, EBI-7191347;
CC A8KBF3; Q7ZYV9: sympk; Xeno; NbExp=3; IntAct=EBI-7191401, EBI-7191476;
CC A8KBF3; Q90WE3: tdrd6; Xeno; NbExp=4; IntAct=EBI-7191401, EBI-7191460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2CEI6}. Nucleus
CC {ECO:0000250|UniProtKB:A2CEI6}. Note=Probable component of the meiotic
CC nuage, also named P granule, a germ-cell-specific organelle required to
CC repress transposon activity during meiosis.
CC {ECO:0000250|UniProtKB:Q8CDG1}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes, testis and liver (at protein
CC level). {ECO:0000269|PubMed:19377467}.
CC -!- PTM: Methylated on arginine residues; required for the interaction with
CC Tudor domain-containing protein and subsequent localization to the
CC meiotic nuage, also named P granule. {ECO:0000269|PubMed:19377467}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
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DR EMBL; BC154090; AAI54091.1; -; mRNA.
DR RefSeq; NP_001106470.1; NM_001112999.1.
DR AlphaFoldDB; A8KBF3; -.
DR SMR; A8KBF3; -.
DR IntAct; A8KBF3; 7.
DR MINT; A8KBF3; -.
DR PaxDb; A8KBF3; -.
DR GeneID; 100127654; -.
DR KEGG; xtr:100127654; -.
DR CTD; 55124; -.
DR Xenbase; XB-GENE-982236; piwil2.
DR eggNOG; KOG1042; Eukaryota.
DR InParanoid; A8KBF3; -.
DR OrthoDB; 220258at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:1990923; C:PET complex; ISS:UniProtKB.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034584; F:piRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0007276; P:gamete generation; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0000966; P:RNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
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; PF08699; ArgoL1; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01163; DUF1785; 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 Biological rhythms; Cytoplasm; Developmental protein; Differentiation;
KW Endonuclease; Hydrolase; Meiosis; Metal-binding; Methylation; Nuclease;
KW Nucleus; Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation.
FT CHAIN 1..949
FT /note="Piwi-like protein 2"
FT /id="PRO_0000367289"
FT DOMAIN 365..478
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 644..935
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 721
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 759
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 791
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 924
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
SQ SEQUENCE 949 AA; 106966 MW; 2257DC7720E3D672 CRC64;
MDPTRPPFRG SPFHTPLGVR PPVLETKEEG PHGRAVLLPR GRALLGASAP SSDTTQRDPS
DSRNVLPALF RGMGIETKPS GIPGRGGPVF GRGFLSTMSS GDGPDQPLSE PSIRPSLSTR
VQQASDFSTE RVALGRARFP IPPVSMEKPH VPTGRGLLFP SVLPTLTSDP VPKESPIATL
QIEKEEKWEP LPKKGSKGSP CQLGLNLIKI NFQNEAVYQY HVTFTPIVEC RSMRFGMMKD
HRSVTGPVTA FDGSILYLPV KLAQTVELES ERRTDGQKIK ITIQMTKILD PSSDLCLPFY
NVVMRRVFKI LDLKLVGRNF YDPASSTVLQ QYRLQVWPGY AANIRKTDGG LFLLVDITHK
IIRSDSVLDI MNILYQQSPE NFQDEVTKQL VGSIVITRYN NRTYRIDDIE WNMSPKDSFS
MSDGSKISFI DYYSKNYGIT VKELDQPLLL HRPSERKAPK GKALDIVLLL PELAFMTGIP
EKMRKDFRAM KDLTQQIHLS PKQHHISLGK LLKRIESSAD AKNELQRWGL FLDTDIHMTT
GRILPIEKIN LRNNSFPAGE DLNWNREVTR EACRSSVHLL YWAMIYPKRA SAQAQELSSM
LERIGGPIGI RVNHPNCVEL RDDRVETYAR SIKSLLEGEG KVQLLVCLIS GTRDDLYGAI
KKLCCVQNPV PSQVINTRTI SQPQKLRSIA QKILLQINCK LGGELWGVDI PLKSVMVIGM
DVYHDPSRGM RSVLGFVASI NSCLTAWYSR VVFQLPNQEI MDSLKLCLVA ALQKFFEVNH
SLPEKIVVYR DGVSDGQLNT VENYEIPQLQ TCFQTFDNYN PRMVVIVVQK RVSTNLYSTA
TGQFLTPQPG TVIDHTVTNR KWIDFFLMSH HVRQGCGIPT HYICVMNTAN LGPDHLQRLT
FKLCHMYWNW PGTIRVPAPC KYAHKLAFLS GQFLHHEPSI KLCDKLFFL
