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Database: UniProt
Entry: A6P7L8
LinkDB: A6P7L8
Original site: A6P7L8 
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   08-MAY-2019, entry version 45.
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;
OC   Salmoniformes; 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
RT   driven by 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
CC       spermatocytes, germ cell differentiation and in self-renewal of
CC       spermatogonial stem cells. Acts via the piRNA metabolic process,
CC       which mediates the repression of transposable elements during
CC       meiosis by forming complexes composed of piRNAs and Piwi proteins
CC       and govern the methylation and subsequent repression of
CC       transposons. During piRNA biosynthesis, plays a key role in the
CC       piRNA amplification loop, also named ping-pong amplification
CC       cycle, by acting as a 'slicer-competent' piRNA endoribonuclease
CC       that cleaves primary piRNAs, which are then loaded onto 'slicer-
CC       incompetent' piwil4. Piwil2 slicing produces a pre-miRNA
CC       intermediate, which is then processed in mature piRNAs, and as
CC       well as a 16 nucleotide by-product that is degraded. Required for
CC       piwil4/miwi2 nuclear localization and association with secondary
CC       piRNAs antisense. {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.
CC       {ECO:0000250|UniProtKB:Q8CDG1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2CEI6}.
CC       Nucleus {ECO:0000250|UniProtKB:A2CEI6}. Note=Probable component of
CC       the meiotic nuage, also named P granule, a germ-cell-specific
CC       organelle required to repress transposon activity during meiosis.
CC       {ECO:0000250|UniProtKB:Q8CDG1}.
CC   -!- PTM: Methylated on arginine residues; required for the interaction
CC       with Tudor domain-containing protein and subsequent localization
CC       to the meiotic nuage, also named P granule.
CC       {ECO:0000250|UniProtKB:Q8CDG1}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC       {ECO:0000305}.
DR   EMBL; AB331649; BAF69069.1; -; mRNA.
DR   RefSeq; NP_001117714.1; NM_001124242.1.
DR   SMR; A6P7L8; -.
DR   GeneID; 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:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
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;
KW   Hydrolase; Meiosis; Metal-binding; Methylation; Nuclease; Nucleus;
KW   RNA-binding; RNA-mediated gene silencing; Translation regulation.
FT   CHAIN         1   1054       Piwi-like protein 2.
FT                                /FTId=PRO_0000367288.
FT   DOMAIN      464    576       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      749   1040       Piwi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00150}.
FT   ACT_SITE    826    826       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE    864    864       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE    896    896       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE   1029   1029       {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
//
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