ID   PIWL2_ONCMY             Reviewed;        1054 AA.
AC   A6P7L8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Piwi-like protein 2;
DE            EC=3.1.26.- {ECO:0000250|UniProtKB:Q8CDG1};
GN   Name=piwil2; Synonyms=rtili;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17901070; DOI=10.1095/biolreprod.107.064667;
RA   Yano A., Suzuki K., Yoshizaki G.;
RT   "Flow-cytometric isolation of testicular germ cells from rainbow trout
RT   (Oncorhynchus mykiss) carrying the green fluorescent protein gene driven by
RT   trout vasa regulatory regions.";
RL   Biol. Reprod. 78:151-158(2008).
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       {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   -!- 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   -!- 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:0000250|UniProtKB:Q8CDG1}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB331649; BAF69069.1; -; mRNA.
DR   RefSeq; NP_001117714.1; NM_001124242.1.
DR   AlphaFoldDB; A6P7L8; -.
DR   SMR; A6P7L8; -.
DR   GeneID; 100135857; -.
DR   KEGG; omy:100135857; -.
DR   CTD; 55124; -.
DR   OrthoDB; 220258at2759; -.
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: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: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; 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   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Differentiation; Endonuclease; Hydrolase;
KW   Meiosis; Metal-binding; Methylation; Nuclease; Nucleus; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation.
FT   CHAIN           1..1054
FT                   /note="Piwi-like protein 2"
FT                   /id="PRO_0000367288"
FT   DOMAIN          464..576
FT                   /note="PAZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT   DOMAIN          749..1040
FT                   /note="Piwi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT   ACT_SITE        826
FT                   /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT   ACT_SITE        864
FT                   /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT   ACT_SITE        896
FT                   /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT   ACT_SITE        1029
FT                   /evidence="ECO:0000250|UniProtKB:A8D8P8"
SQ   SEQUENCE   1054 AA;  117141 MW;  BAA8E82F58F5A944 CRC64;
     MDPKKPCFPG LPGATRIPWL QQQAWGRGLR SDEPAIGRAR GLMFATDGSA SLGRARGFTT
     AGDTLLMQYG RGVPFPVSDP SIGFARGIPM PTSEDGGINR PRGWLLSTAD PTVGVARGEP
     LLGLGPHLGQ ATPGQLAKQD LPEEMPSLQA EEEVVAKQVD MSTQGQGSSL VSMFRGMGID
     PSKTWGRGGL PVGRGVFGAE LQPQTAPVGA VAVAGPGGDR FPEDMMGQGN SFLGRGVPSQ
     MVGMGRASMH PLGAGRGPTV PPTLPPSLHK EAHMTPGCSL TKGELKMEAT CETLHKTGTK
     GTPLPIGSNH ITIHCRNEAV YQYHVTFTPN VESMGMRFGM MKDHRPTTGE VVAFDGSILY
     LPVKMEEVVH LKSVRRTDNQ EVDIKVQMTK ILPPNSDLCI PFYNVVLRRV MKILGLKLVG
     RNHYDPKSAV ILGKHRLQVW PGYSTCIKHT DGGLYLQVDV SHKVLRNDSV LDCMNVIYQQ
     SRESFQDECT KELIGSIVIT RYNNRTYRID DIEWGKSPKD TFTMADGSTT TFVEYYSKNY
     GITIKEMDQP MLIHRPKERS KPGGKQVITG EILLLPELSF TTGIPDKMRK DFRAMKDLTM
     HINVSSEQHT HSLKQLLKNI NTNPEAQTEL ARWGLEISQD ILVTIGRILP LETICLQSVS
     FVTGADVSWS REVIRDASIS CIPMNCWAIF YPRRCAEQAE ELVSCFGKVA GPMGLRLDRP
     IRVELKDDRT ETYVKSIHSQ LTSEPNVQLV VCIMTGNRDD LYSAIKKLCC VQSPVPSQAI
     NVRTISQPQK LRSVAQKILL QMNCKLGGEL WTVNVPLKHL MVIGVDVHHD TSKKNRSVMG
     FVASLNSLLT RWYSRVTFQM PNEEIINGFR VCLLAALQKY YGVNHNFPEK IVVYRDGVSD
     GQLKTVELYE IPQLLKCFET FPNYEPKLAF IVVQKRVSTN LYSCSGDRFG TPPPGTVLDH
     TVTNREWVDF YLMAHHVRQG CGLPTRNISV YNTANLSPDH LQRLTFKMCH MYWNWPGTIR
     VPAPCKYAHK LAFLSGQYLH SEPAIQLADK LYFL