PIWL2_DANRE
ID PIWL2_DANRE Reviewed; 1046 AA.
AC A2CEI6; A1Z661; B5A7D8; B5U367;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Piwi-like protein 2;
DE EC=3.1.26.- {ECO:0000250|UniProtKB:Q8CDG1};
GN Name=piwil2; Synonyms=zili {ECO:0000303|PubMed:18833190};
GN ORFNames=si:dkey-88f5.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING,
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-590.
RC STRAIN=TL;
RX PubMed=18833190; DOI=10.1038/emboj.2008.204;
RA Houwing S., Berezikov E., Ketting R.F.;
RT "Zili is required for germ cell differentiation and meiosis in zebrafish.";
RL EMBO J. 27:2702-2711(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Tuebingen;
RA Sun H., Li N., Yan N., Zhang L., Liu Y., Wang X., Ma Y.;
RT "Identification of zebrafish Piwil2-Zili gene.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AB;
RA Honda J., Beh L., Wong Q.Y., Orban L., Kai T.;
RT "Expression and localization of zebrafish piwi-like 2.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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:18833190). Plays an essential role in germ cell differentiation
CC and meiosis, independently of the function in transposable elements
CC repression (PubMed:18833190). Acts via the piRNA metabolic process,
CC which mediates the repression of transposable elements during meiosis
CC by forming complexes composed of piRNAs and Piwi proteins and govern
CC the methylation and subsequent repression of transposons
CC (PubMed:18833190). During piRNA biosynthesis, plays a key role in the
CC piRNA amplification loop, also named ping-pong amplification cycle, by
CC acting as a 'slicer-competent' piRNA endoribonuclease that cleaves
CC primary piRNAs, which are then loaded onto 'slicer-incompetent' piwil4
CC (By similarity). Piwil2 slicing produces a pre-miRNA intermediate,
CC which is then processed in mature piRNAs, and as well as a 16
CC nucleotide by-product that is degraded (By similarity). Required for
CC piwil4/miwi2 nuclear localization and association with secondary piRNAs
CC antisense (By similarity). Represses circadian rhythms by promoting the
CC stability and activity of core clock components ARNTL/BMAL1 and CLOCK
CC (By similarity). {ECO:0000250|UniProtKB:Q8CDG1,
CC ECO:0000269|PubMed:18833190}.
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 A2CEI6; Q58EK5: tdrd1; NbExp=9; IntAct=EBI-7011808, EBI-7011788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18833190}. Nucleus
CC {ECO:0000269|PubMed:18833190}. 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 (By similarity). In mitotic
CC and early meiotic cells of ovary, it is predominantly cytoplasmic. In
CC primary oocytes, it is found in a granular distribution around the
CC nucleus. Later, in maturing oocytes, it localizes to the nucleus. In
CC testis, it is present in the cytoplasm of mitotic and meiotic germ
CC cells, where a distinct granular distribution around the nucleus is
CC observed. {ECO:0000250|UniProtKB:Q8CDG1}.
CC -!- TISSUE SPECIFICITY: Detected in primordial germ cells (PGCs) from 3
CC dpf. In adult, it is found in both the female and male gonad. In the
CC ovary, it is present in all stages of germ cell differentiation. In
CC testis, it is present in mitotic and meiotic germ cells. No protein has
CC been detected in the fully differentiated sperm cell.
CC {ECO:0000269|PubMed:18833190}.
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 -!- DISRUPTION PHENOTYPE: Progressive loss of germ cells due to apoptosis
CC from 6 weeks of age. {ECO:0000269|PubMed:18833190}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM16455.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ168029; ACH96370.1; -; mRNA.
DR EMBL; EF186090; ABM46842.2; -; mRNA.
DR EMBL; EU817487; ACF35261.1; -; mRNA.
DR EMBL; CR450719; CAM16455.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001073668.2; NM_001080199.3.
DR RefSeq; XP_017211652.1; XM_017356163.1.
DR AlphaFoldDB; A2CEI6; -.
DR SMR; A2CEI6; -.
DR IntAct; A2CEI6; 21.
DR MINT; A2CEI6; -.
DR STRING; 7955.ENSDARP00000114406; -.
DR PaxDb; A2CEI6; -.
DR PeptideAtlas; A2CEI6; -.
DR Ensembl; ENSDART00000090695; ENSDARP00000085128; ENSDARG00000062601.
DR Ensembl; ENSDART00000162071; ENSDARP00000139021; ENSDARG00000062601.
DR GeneID; 572134; -.
DR CTD; 55124; -.
DR ZFIN; ZDB-GENE-060526-345; piwil2.
DR eggNOG; KOG1042; Eukaryota.
DR GeneTree; ENSGT00950000183200; -.
DR InParanoid; A2CEI6; -.
DR OMA; CLPFYNV; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; A2CEI6; -.
DR TreeFam; TF354206; -.
DR PRO; PR:A2CEI6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000062601; Expressed in testis and 23 other tissues.
DR ExpressionAtlas; A2CEI6; baseline.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IDA: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; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010991; P:negative regulation of SMAD protein complex assembly; IPI:ZFIN.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ZFIN.
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; 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; Oogenesis; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..1046
FT /note="Piwi-like protein 2"
FT /id="PRO_0000367287"
FT DOMAIN 457..569
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 741..1032
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 818
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 856
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 888
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 1021
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT MUTAGEN 590
FT /note="L->P: In hu2087; males develop normally and are
FT fertile but females are sterile due to defects in meiosis."
FT /evidence="ECO:0000269|PubMed:18833190"
FT CONFLICT 59
FT /note="P -> L (in Ref. 2; ABM46842 and 3; ACF35261)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="M -> V (in Ref. 1; ACH96370)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="A -> V (in Ref. 1; ACH96370)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="E -> Q (in Ref. 1; ACH96370)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> S (in Ref. 2; ABM46842 and 3; ACF35261)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="T -> A (in Ref. 2; ABM46842)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="N -> D (in Ref. 2; ABM46842)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="H -> R (in Ref. 2; ABM46842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1046 AA; 116207 MW; A71D25E1EF5A4E4D CRC64;
MDPKRPTFPS PPGVIRAPWQ QSTEDQSQLL DQPSLGRARG LIMPIDEPLP GRGRAFSVPG
EMPVRFGRGI TQSIAAEPLV GMARGVRLPM EEGGFGRGRG FLLPTPEPTV GIGRGAAIGP
VPTLDIQKAE VEEKMPELQA EVAPTVAKVG SPGTGSSLVS MFRGLGIEPG KTWGRGAAPV
GRGAAGDMGA DLQPKPTIIG ASLTPEREEV RSEESISFLG RGFTGFGRAA MPHMTVGRGP
IGPLSPSPSV AAPFSLISAS SASEDAPVAP GTPPKVEVKI ETVKEPLQKI GTKGSPIPIG
SNYIPICCKN DAVFQYHVTF TPNVESLSMR FGMMKEHRPT TGEVVAFDGS ILYLPKRLEE
VVHLKAERKT DNQEIDIKIQ LTKILPPSSD LCIPFYNVVL RRVMKILGLK LVGRNHYDPN
AVVILGKHRL QVWPGYSTSI KHTDGGLYLV VDVSHKVLRN DSVLDVMNLI YQGSRESFQD
ECTKEFVGSI VITRYNNRTY RIDDIEWSKS PKDTFTLADG SVTTFVDYYR KNYGITIKEL
DQPLLIHRPK ERSRPGGKVI TGEILLLPEL SFMTGIPEKM RKDFRAMKDL TMHINVGAQQ
HTQSLKQLLH NINSNNEALS ELGRWGLSIS QEILVTQGRT LPSETICLHS ASFVTSPAVD
WSRELVRDPS ISTVPLNCWA VFYPRRATDQ AEELVTTFSR VAGPMGMRVE RPIRVELRDD
RTETFVKSIH SQLTSEPRVQ LVVCIMTGNR DDLYSAIKKL CCIQSPVPSQ AINVRTISQP
QKLRSVAQKI LLQINCKLGG ELWTVNVPLK YLMVIGVDVH HDTSKKSRSV MGFVASLNSM
LTKWYSRVTF QMPNEEIING FRVCLLAALQ KYYEVNHAFP EKIVIYRDGV SDGQLKTVEH
YEIPQILKCF ETIPNYEPKL AFIVVQKRIS TTLYSYGSDH FGTPSPGTVL DHTVTNRDWV
DFYLMAHSIR QGCGLPTHYI TVYNTANLTP DHLQRLTFKM CHLYWNWPGT IRVPAPCKYA
HKLAFLSGQY LHSEPAIQLS EKLFFL
