PIWL1_MOUSE
ID PIWL1_MOUSE Reviewed; 862 AA.
AC Q9JMB7; A1L324; A1L325; Q6NXX0;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Piwi-like protein 1 {ECO:0000305};
DE EC=3.1.26.- {ECO:0000269|PubMed:22121019};
GN Name=Piwil1 {ECO:0000312|MGI:MGI:1928897};
GN Synonyms=Miwi {ECO:0000303|PubMed:11578866, ECO:0000303|PubMed:28254886};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, FUNCTION, AND RNA-BINDING.
RC TISSUE=Testis;
RX PubMed=11578866; DOI=10.1016/s0925-4773(01)00499-3;
RA Kuramochi-Miyagawa S.K., Kimura T., Yomogida K., Kuroiwa A., Tadokoro Y.,
RA Fujita Y., Sato M., Matsuda Y., Nakano T.;
RT "Two mouse piwi-related genes: miwi and mili.";
RL Mech. Dev. 108:121-133(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12062093; DOI=10.1016/s1534-5807(02)00165-x;
RA Deng W., Lin H.;
RT "miwi, a murine homolog of piwi, encodes a cytoplasmic protein essential
RT for spermatogenesis.";
RL Dev. Cell 2:819-830(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=KM; TISSUE=Testis;
RA Zhang S., Li D., Li E., Lu J.;
RT "The clone of Miwi and research about its effect on self-proliferation of
RT SSCs.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP RNA-BINDING.
RX PubMed=16766680; DOI=10.1101/gad.1434406;
RA Grivna S.T., Beyret E., Wang Z., Lin H.;
RT "A novel class of small RNAs in mouse spermatogenic cells.";
RL Genes Dev. 20:1709-1714(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF17, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16787948; DOI=10.1242/jcs.03022;
RA Kotaja N., Lin H., Parvinen M., Sassone-Corsi P.;
RT "Interplay of PIWI/Argonaute protein MIWI and kinesin KIF17b in chromatoid
RT bodies of male germ cells.";
RL J. Cell Sci. 119:2819-2825(2006).
RN [7]
RP RNA-BINDING.
RX PubMed=16751776; DOI=10.1038/nature04917;
RA Girard A., Sachidanandam R., Hannon G.J., Carmell M.A.;
RT "A germline-specific class of small RNAs binds mammalian Piwi proteins.";
RL Nature 442:199-202(2006).
RN [8]
RP INTERACTION WITH MAEL.
RX PubMed=16787967; DOI=10.1093/hmg/ddl158;
RA Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A.,
RA Cooke H.J.;
RT "Mouse MAELSTROM: the link between meiotic silencing of unsynapsed
RT chromatin and microRNA pathway?";
RL Hum. Mol. Genet. 15:2324-2334(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH DICER1.
RX PubMed=16938833; DOI=10.1073/pnas.0605506103;
RA Grivna S.T., Pyhtila B., Lin H.;
RT "MIWI associates with translational machinery and PIWI-interacting RNAs
RT (piRNAs) in regulating spermatogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13415-13420(2006).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PABPC1.
RX PubMed=19020299; DOI=10.1095/biolreprod.108.072553;
RA Kimura M., Ishida K., Kashiwabara S., Baba T.;
RT "Characterization of two cytoplasmic poly(A)-binding proteins, PABPC1 and
RT PABPC2, in mouse spermatogenic cells.";
RL Biol. Reprod. 80:545-554(2009).
RN [11]
RP METHYLATION AT ARG-14; ARG-49 AND ARG-371, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH TDRD1; TDRKH; TDRD6; PRMT5 AND WDR77.
RX PubMed=19584108; DOI=10.1101/gad.1814809;
RA Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S.,
RA Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.;
RT "Proteomic analysis of murine Piwi proteins reveals a role for arginine
RT methylation in specifying interaction with Tudor family members.";
RL Genes Dev. 23:1749-1762(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND 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).
RN [13]
RP METHYLATION.
RX PubMed=19465913; DOI=10.1038/nsmb.1615;
RA Reuter M., Chuma S., Tanaka T., Franz T., Stark A., Pillai R.S.;
RT "Loss of the Mili-interacting Tudor domain-containing protein-1 activates
RT transposons and alters the Mili-associated small RNA profile.";
RL Nat. Struct. Mol. Biol. 16:639-646(2009).
RN [14]
RP METHYLATION AT ARG-53, AND INTERACTION WITH TDRKH.
RX PubMed=19918066; DOI=10.1073/pnas.0911640106;
RA Chen C., Jin J., James D.A., Adams-Cioaba M.A., Park J.G., Guo Y.,
RA Tenaglia E., Xu C., Gish G., Min J., Pawson T.;
RT "Mouse Piwi interactome identifies binding mechanism of Tdrkh Tudor domain
RT to arginine methylated Miwi.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20336-20341(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP INTERACTION WITH MOV10L1.
RX PubMed=20534472; DOI=10.1073/pnas.1003953107;
RA Zheng K., Xiol J., Reuter M., Eckardt S., Leu N.A., McLaughlin K.J.,
RA Stark A., Sachidanandam R., Pillai R.S., Wang P.J.;
RT "Mouse MOV10L1 associates with Piwi proteins and is an essential component
RT of the Piwi-interacting RNA (piRNA) pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11841-11846(2010).
RN [17]
RP INTERACTION WITH TDRD6, TISSUE SPECIFICITY, AND METHYLATION.
RX PubMed=19926723; DOI=10.1261/rna.1869710;
RA Kirino Y., Vourekas A., Sayed N., de Lima Alves F., Thomson T., Lasko P.,
RA Rappsilber J., Jongens T.A., Mourelatos Z.;
RT "Arginine methylation of Aubergine mediates Tudor binding and germ plasm
RT localization.";
RL RNA 16:70-78(2010).
RN [18]
RP INTERACTION WITH CLOCK.
RX PubMed=22900038; DOI=10.1371/journal.pone.0042695;
RA Peruquetti R.L., de Mateo S., Sassone-Corsi P.;
RT "Circadian proteins CLOCK and BMAL1 in the chromatoid body, a RNA
RT processing granule of male germ cells.";
RL PLoS ONE 7:E42695-E42695(2012).
RN [19]
RP INTERACTION WITH TDRKH.
RX PubMed=23714778; DOI=10.1038/emboj.2013.121;
RA Saxe J.P., Chen M., Zhao H., Lin H.;
RT "Tdrkh is essential for spermatogenesis and participates in primary piRNA
RT biogenesis in the germline.";
RL EMBO J. 32:1869-1885(2013).
RN [20]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF ASP-633.
RX PubMed=22121019; DOI=10.1038/nature10672;
RA Reuter M., Berninger P., Chuma S., Shah H., Hosokawa M., Funaya C.,
RA Antony C., Sachidanandam R., Pillai R.S.;
RT "Miwi catalysis is required for piRNA amplification-independent LINE1
RT transposon silencing.";
RL Nature 480:264-267(2011).
RN [21]
RP UBIQUITINATION, INTERACTION WITH ANAPC10, DOMAIN, AND MUTAGENESIS OF
RP 218-ARG--LEU-221; 330-LYS--LYS-335 AND 346-TYR-TYR-347.
RX PubMed=23328397; DOI=10.1016/j.devcel.2012.12.006;
RA Zhao S., Gou L.T., Zhang M., Zu L.D., Hua M.M., Hua Y., Shi H.J., Li Y.,
RA Li J., Li D., Wang E.D., Liu M.F.;
RT "piRNA-triggered MIWI ubiquitination and removal by APC/C in late
RT spermatogenesis.";
RL Dev. Cell 24:13-25(2013).
RN [22]
RP INDUCTION.
RX PubMed=23523368; DOI=10.1016/j.molcel.2013.02.016;
RA Li X.Z., Roy C.K., Dong X., Bolcun-Filas E., Wang J., Han B.W., Xu J.,
RA Moore M.J., Schimenti J.C., Weng Z., Zamore P.D.;
RT "An ancient transcription factor initiates the burst of piRNA production
RT during early meiosis in mouse testes.";
RL Mol. Cell 50:67-81(2013).
RN [23]
RP FUNCTION, UBIQUITINATION, INTERACTION WITH RNF8, AND MUTAGENESIS OF
RP 218-ARG--LEU-221.
RX PubMed=28552346; DOI=10.1016/j.cell.2017.04.034;
RA Gou L.T., Kang J.Y., Dai P., Wang X., Li F., Zhao S., Zhang M., Hua M.M.,
RA Lu Y., Zhu Y., Li Z., Chen H., Wu L.G., Li D., Fu X.D., Li J., Shi H.J.,
RA Liu M.F.;
RT "Ubiquitination-deficient mutations in human Piwi cause male infertility by
RT impairing histone-to-protamine exchange during spermiogenesis.";
RL Cell 169:1090-1104(2017).
RN [24]
RP RNA-BINDING, AND INTERACTION WITH TEX19.1.
RX PubMed=28254886; DOI=10.1242/jcs.188763;
RA Tarabay Y., Achour M., Teletin M., Ye T., Teissandier A., Mark M.,
RA Bourc'his D., Viville S.;
RT "Tex19 paralogs are new members of the piRNA pathway controlling
RT retrotransposon suppression.";
RL J. Cell Sci. 130:1463-1474(2017).
RN [25]
RP STRUCTURE BY NMR OF 276-395 IN COMPLEX WITH METHYLATED SMALL RNA, DOMAIN
RP PAZ, MUTAGENESIS OF PHE-343 AND MET-382, AND FUNCTION.
RX PubMed=21237665; DOI=10.1016/j.str.2010.11.015;
RA Simon B., Kirkpatrick J.P., Eckhardt S., Reuter M., Rocha E.A.,
RA Andrade-Navarro M.A., Sehr P., Pillai R.S., Carlomagno T.;
RT "Recognition of 2'-O-methylated 3'-end of piRNA by the PAZ domain of a Piwi
RT protein.";
RL Structure 19:172-180(2011).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 485-612, FUNCTION, AND DOMAIN.
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).
CC -!- FUNCTION: Endoribonuclease that plays a central role in postnatal germ
CC cells by repressing transposable elements and preventing their
CC mobilization, which is essential for the germline integrity
CC (PubMed:11578866, PubMed:22121019, PubMed:21237665). Acts via the piRNA
CC metabolic process, which mediates the repression of transposable
CC elements during meiosis by forming complexes composed of piRNAs and
CC Piwi proteins and governs the methylation and subsequent repression of
CC transposons (PubMed:11578866, PubMed:22121019, PubMed:21237665).
CC Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs
CC that are generated by a Dicer-independent mechanism and are primarily
CC derived from transposons and other repeated sequence elements
CC (PubMed:11578866, PubMed:22121019, PubMed:21237665). Strongly prefers a
CC uridine in the first position of their guide (g1U preference, also
CC named 1U-bias) (PubMed:24757166). Not involved in the piRNA
CC amplification loop, also named ping-pong amplification cycle
CC (PubMed:22121019). Acts as an endoribonuclease that cleaves transposon
CC messenger RNAs (PubMed:22121019). Besides their function in
CC transposable elements repression, piRNAs are probably involved in other
CC processes during meiosis such as translation regulation
CC (PubMed:16938833). Probable component of some RISC complex, which
CC mediates RNA cleavage and translational silencing (PubMed:16938833).
CC Also plays a role in the formation of chromatoid bodies and is required
CC for some miRNAs stability (PubMed:16787948). Required to sequester RNF8
CC in the cytoplasm until late spermatogenesis; RNF8 being released upon
CC ubiquitination and degradation of PIWIL1 (PubMed:28552346).
CC {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:16787948,
CC ECO:0000269|PubMed:16938833, ECO:0000269|PubMed:21237665,
CC ECO:0000269|PubMed:22121019, ECO:0000269|PubMed:24757166,
CC ECO:0000269|PubMed:28552346}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22121019};
CC -!- SUBUNIT: Interacts (via Piwi domain) with DICER1, suggesting that it
CC forms ribonucleoprotein RISC complexes; this interaction is regulated
CC by HSP90AB1 activity (PubMed:16938833). Interacts with MAEL, KIF17,
CC PABPC1, PRMT5 and WDR77 (PubMed:16787948, PubMed:16787967,
CC PubMed:19020299, PubMed:19584108). Interacts (when methylated on
CC arginine residues) with TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7
CC and TDRD9 (PubMed:19584108, PubMed:19918066, PubMed:19926723,
CC PubMed:23714778). Interacts with CLOCK (PubMed:22900038). Interacts
CC with MOV10L1 (PubMed:20534472). Interacts with ANAPC10; interaction oly
CC takes place following piRNA-binding (PubMed:23328397). Interacts with
CC RNF8; leading to sequester RNF8 in the cytoplasm (PubMed:28552346).
CC Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886).
CC {ECO:0000269|PubMed:16787948, ECO:0000269|PubMed:16787967,
CC ECO:0000269|PubMed:16938833, ECO:0000269|PubMed:19020299,
CC ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19918066,
CC ECO:0000269|PubMed:19926723, ECO:0000269|PubMed:20534472,
CC ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:23328397,
CC ECO:0000269|PubMed:23714778, ECO:0000269|PubMed:28254886,
CC ECO:0000269|PubMed:28552346}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11578866,
CC ECO:0000269|PubMed:12062093, ECO:0000269|PubMed:16787948,
CC ECO:0000269|PubMed:16938833, ECO:0000269|PubMed:19020299,
CC ECO:0000269|PubMed:19584108}. Note=Component of the meiotic nuage, also
CC named P granule, a germ-cell-specific organelle required to repress
CC transposon activity during meiosis. Also present in chromatoid body.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JMB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JMB7-2; Sequence=VSP_036663;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Expressed in testis,
CC specifically in spermatocytes (at protein level). Only detected in germ
CC lineage cells of adult testis. Expressed in male gonads 2 weeks after
CC birth at the initiation of spermatogenesis, but not expressed in female
CC gonads. {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:12062093,
CC ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19926723}.
CC -!- INDUCTION: Expression is activated by MYBL1/A-MYB.
CC {ECO:0000269|PubMed:23523368}.
CC -!- DOMAIN: The D-box (destruction box) acts as a recognition signal for
CC association with the APC/C complex, ubiquitination and degradation
CC (PubMed:23328397). {ECO:0000269|PubMed:23328397}.
CC -!- DOMAIN: The PAZ domain specifically recognizes binds the 2'-O-
CC methylated 3'-end of piRNAs (PubMed:21237665). The MID region is
CC required for recognition of uridine in the first position of piRNAs
CC (g1U preference, also named 1U-bias) (PubMed:24757166).
CC {ECO:0000269|PubMed:21237665, ECO:0000269|PubMed:24757166}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C)
CC in late spermatids, leading to its degradation (PubMed:23328397).
CC Ubiquitination only takes place following piRNA-binding in adult testis
CC (PubMed:23328397). Ubiquitination and degradation in late
CC spermatogenesis by APC/C is probably required to release RNF8 from the
CC cytoplasm and promote histone to protamine exchange by RNF8
CC (PubMed:28552346). {ECO:0000269|PubMed:23328397,
CC ECO:0000269|PubMed:28552346}.
CC -!- PTM: Arginine methylation by PRMT5 is required for the interaction with
CC Tudor domain-containing protein (TDRD1, TDRKH/TDRD2, RNF17/TDRD4,
CC TDRD6, TDRD7 and TDRD9) and subsequent localization to the meiotic
CC nuage, also named P granule. {ECO:0000269|PubMed:19377467,
CC ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108,
CC ECO:0000269|PubMed:19918066, ECO:0000269|PubMed:19926723}.
CC -!- DISRUPTION PHENOTYPE: Mice display spermatogenic arrest at the
CC beginning of the round spermatid stage, resembling the phenotype of
CC CREM, a master regulator of spermiogenesis; mRNAs of FHL5/activator of
CC CREM and CREM target genes are down-regulated in testes. Female are
CC fertile but male are completely sterile, no sperm is found in the
CC epididimus. Chromatoid bodies from round spermatids are not fully
CC compacted and remain as a diffuse chromatoid material.
CC {ECO:0000269|PubMed:12062093, ECO:0000269|PubMed:16787948}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH66846.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB032604; BAA93705.1; -; mRNA.
DR EMBL; AF438405; AAL31014.1; -; mRNA.
DR EMBL; EF196092; ABM69181.1; -; mRNA.
DR EMBL; BC066846; AAH66846.1; ALT_SEQ; mRNA.
DR EMBL; BC129857; AAI29858.1; -; mRNA.
DR EMBL; BC129858; AAI29859.1; -; mRNA.
DR CCDS; CCDS19690.1; -. [Q9JMB7-1]
DR RefSeq; NP_067286.1; NM_021311.3. [Q9JMB7-1]
DR RefSeq; XP_006504381.1; XM_006504318.1. [Q9JMB7-1]
DR PDB; 2XFM; NMR; -; A=276-425.
DR PDB; 4P1Z; X-ray; 2.30 A; A/B/C/D=485-612.
DR PDBsum; 2XFM; -.
DR PDBsum; 4P1Z; -.
DR AlphaFoldDB; Q9JMB7; -.
DR BMRB; Q9JMB7; -.
DR SMR; Q9JMB7; -.
DR BioGRID; 208311; 1.
DR DIP; DIP-59456N; -.
DR IntAct; Q9JMB7; 5.
DR MINT; Q9JMB7; -.
DR STRING; 10090.ENSMUSP00000083222; -.
DR iPTMnet; Q9JMB7; -.
DR PhosphoSitePlus; Q9JMB7; -.
DR PaxDb; Q9JMB7; -.
DR PeptideAtlas; Q9JMB7; -.
DR PRIDE; Q9JMB7; -.
DR ProteomicsDB; 287738; -. [Q9JMB7-1]
DR ProteomicsDB; 287739; -. [Q9JMB7-2]
DR Antibodypedia; 31942; 288 antibodies from 38 providers.
DR DNASU; 57749; -.
DR Ensembl; ENSMUST00000086056; ENSMUSP00000083222; ENSMUSG00000029423. [Q9JMB7-1]
DR Ensembl; ENSMUST00000195959; ENSMUSP00000142386; ENSMUSG00000029423. [Q9JMB7-2]
DR GeneID; 57749; -.
DR KEGG; mmu:57749; -.
DR UCSC; uc008zsi.1; mouse. [Q9JMB7-1]
DR UCSC; uc008zsj.1; mouse. [Q9JMB7-2]
DR CTD; 9271; -.
DR MGI; MGI:1928897; Piwil1.
DR VEuPathDB; HostDB:ENSMUSG00000029423; -.
DR eggNOG; KOG1042; Eukaryota.
DR GeneTree; ENSGT00950000183200; -.
DR HOGENOM; CLU_008813_0_0_1; -.
DR InParanoid; Q9JMB7; -.
DR OMA; NPTMSRW; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; Q9JMB7; -.
DR TreeFam; TF354206; -.
DR BioGRID-ORCS; 57749; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Piwil1; mouse.
DR PRO; PR:Q9JMB7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JMB7; protein.
DR Bgee; ENSMUSG00000029423; Expressed in spermatocyte and 14 other tissues.
DR ExpressionAtlas; Q9JMB7; baseline and differential.
DR Genevisible; Q9JMB7; MM.
DR GO; GO:0033391; C:chromatoid body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0097433; C:dense body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0140262; F:mRNA cap binding complex binding; IDA:UniProtKB.
DR GO; GO:0034584; F:piRNA binding; IDA:UniProtKB.
DR GO; GO:1905538; F:polysome binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:MGI.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; NAS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IDA:UniProtKB.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR031320; GAGE.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR031326; PIWIL1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR22891:SF46; PTHR22891:SF46; 1.
DR Pfam; PF08699; ArgoL1; 1.
DR Pfam; PF05831; GAGE; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01379; GAGE; 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 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Endonuclease; Hydrolase; Magnesium; Meiosis;
KW Metal-binding; Methylation; Nuclease; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Spermatogenesis; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..862
FT /note="Piwi-like protein 1"
FT /id="PRO_0000234568"
FT DOMAIN 278..392
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 556..848
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..319
FT /note="Required for binding 2'-O-methylated 3'-end of
FT piRNAs"
FT /evidence="ECO:0000269|PubMed:21237665"
FT REGION 480..616
FT /note="MID region"
FT /evidence="ECO:0000305|PubMed:24757166"
FT MOTIF 218..225
FT /note="D-box"
FT /evidence="ECO:0000269|PubMed:23328397"
FT ACT_SITE 633
FT /evidence="ECO:0000305|PubMed:22121019"
FT ACT_SITE 671
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 703
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 837
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT SITE 382
FT /note="Required for binding 2'-O-methylated 3'-end of
FT piRNAs"
FT MOD_RES 14
FT /note="Omega-N-methylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000269|PubMed:19584108"
FT MOD_RES 14
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000269|PubMed:19584108"
FT MOD_RES 49
FT /note="Omega-N-methylarginine; by PRMT5"
FT /evidence="ECO:0000269|PubMed:19584108"
FT MOD_RES 53
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:19918066"
FT MOD_RES 53
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000305|PubMed:19918066"
FT MOD_RES 371
FT /note="Omega-N-methylarginine; by PRMT5"
FT /evidence="ECO:0000269|PubMed:19584108"
FT VAR_SEQ 825..862
FT /note="GVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL -> VSVLLWTTYP
FT G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036663"
FT MUTAGEN 218..221
FT /note="RRLL->ARLA: Does not affect piRNA-binding but
FT abolishes ubiquitination by the APC/C. Causes male
FT sterility."
FT /evidence="ECO:0000269|PubMed:23328397,
FT ECO:0000269|PubMed:28552346"
FT MUTAGEN 330..335
FT /note="KSTFKK->ASTFAA: Abolishes ubiquitination by the
FT APC/C."
FT /evidence="ECO:0000269|PubMed:23328397"
FT MUTAGEN 343
FT /note="F->A: Impairs binding to 2'-O-methylated 3'-end of
FT piRNAs."
FT /evidence="ECO:0000269|PubMed:21237665"
FT MUTAGEN 346..347
FT /note="YY->AA: Abolishes piRNA-binding and ubiquitination
FT by the APC/C."
FT /evidence="ECO:0000269|PubMed:23328397"
FT MUTAGEN 382
FT /note="M->A: Impairs binding to 2'-O-methylated 3'-end of
FT piRNAs."
FT /evidence="ECO:0000269|PubMed:21237665"
FT MUTAGEN 633
FT /note="D->A: In DAH mutant; causes male infertility due to
FT derepression of LINE1 retrotransposons transcripts."
FT /evidence="ECO:0000269|PubMed:22121019"
FT CONFLICT 374
FT /note="G -> S (in Ref. 4; AAH66846)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="K -> R (in Ref. 4; AAH66846)"
FT /evidence="ECO:0000305"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:2XFM"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2XFM"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2XFM"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:2XFM"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:2XFM"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:4P1Z"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:4P1Z"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:4P1Z"
FT HELIX 506..519
FT /evidence="ECO:0007829|PDB:4P1Z"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:4P1Z"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:4P1Z"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:4P1Z"
FT HELIX 539..549
FT /evidence="ECO:0007829|PDB:4P1Z"
FT STRAND 557..563
FT /evidence="ECO:0007829|PDB:4P1Z"
FT HELIX 566..579
FT /evidence="ECO:0007829|PDB:4P1Z"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:4P1Z"
FT HELIX 589..592
FT /evidence="ECO:0007829|PDB:4P1Z"
FT HELIX 595..608
FT /evidence="ECO:0007829|PDB:4P1Z"
SQ SEQUENCE 862 AA; 98574 MW; 45588D13284CCC4C CRC64;
MTGRARARAR GRARGQETVQ HVGAAASQQP GYIPPRPQQS PTEGDLVGRG RQRGMVVGAT
SKSQELQISA GFQELSLAER GGRRRDFHDL GVNTRQNLDH VKESKTGSSG IIVKLSTNHF
RLTSRPQWAL YQYHIDYNPL MEARRLRSAL LFQHEDLIGR CHAFDGTILF LPKRLQHKVT
EVFSQTRNGE HVRITITLTN ELPPTSPTCL QFYNIIFRRL LKIMNLQQIG RNYYNPSDPI
DIPNHRLVIW PGFTTSILQY ENNIMLCTDV SHKVLRSETV LDFMFNLYQQ TEEHKFQEQV
SKELIGLIVL TKYNNKTYRV DDIDWDQNPK STFKKADGSE VSFLEYYRKQ YNQEITDLKQ
PVLVSQPKRR RGPGGTLPGP AMLIPELCYL TGLTDKMRND FNVMKDLAVH TRLTPEQRQR
EVGRLIDYIH KDDNVQRELR DWGLSFDSNL LSFSGRILQS EKIHQGGKTF DYNPQFADWS
KETRGAPLIS VKPLDNWLLI YTRRNYEAAN SLIQNLFKVT PAMGIQMKKA IMIEVDDRTE
AYLRALQQKV TSDTQIVVCL LSSNRKDKYD AIKKYLCTDC PTPSQCVVAR TLGKQQTVMA
IATKIALQMN CKMGGELWRV DMPLKLAMIV GIDCYHDTTA GRRSIAGFVA SINEGMTRWF
SRCVFQDRGQ ELVDGLKVCL QAALRAWSGC NEYMPSRVIV YRDGVGDGQL KTLVNYEVPQ
FLDCLKSVGR GYNPRLTVIV VKKRVNARFF AQSGGRLQNP LPGTVIDVEV TRPEWYDFFI
VSQAVRSGSV SPTHYNVIYD SSGLKPDHIQ RLTYKLCHVY YNWPGVIRVP APCQYAHKLA
FLVGQSIHRE PNLSLSNRLY YL
