Piwil2
entrez
57746
canonical
uniprot
Q8CDG1
canonical
ensembl
ENSMUSG00000033644
resolver
ensp
ENSMUSP00000047385
resolver
enst
ENSMUST00000048129
resolver
genesymbol
Piwil2
resolver
genesymbol_syn
Mili
resolver
uniprot
A6H617
resolver
uniprot
Q3TQE8
resolver
uniprot
Q99MV6
resolver
uniprot
Q9JMB6
resolver
uniprot_entry
PIWL2_MOUSE
resolver
uniprot_sec
A6H617
resolver
uniprot_sec
Q3TQE8
resolver
uniprot_sec
Q99MV6
resolver
uniprot_sec
Q9JMB6
resolver
amino_acid_sequence
MDPVRPLFRGPTPVHPSQCVRMPGCWPQAPRPLEPAWGRAGPAGRGLVFRKPEDSSPPLQPVQKDSVGLVSMFRGMGLDTAFRPPSKREVPPLGRGVLGRGLSANMVRKDREEPRSSLPDPSVLAAGDSKLAEASVGWSRMLGRGSSEVSLLPLGRAASSIGRGMDKPPSAFGLTARDPPRLPQPPALSPTSLHSADPPPVLTMERKEKELLVKQGSKGTPQSLGLNLIKIQCHNEAVYQYHVTFSPSVECKSMRFGMLKDHQSVTGNVTAFDGSILYLPVKLQQVVELKSQRKTDDAEISIKIQLTKILEPCSDLCIPFYNVVFRRVMKLLDMKLVGRNFYDPTSAMVLQQHRLQIWPGYAASIRRTDGGLFLLADVSHKVIRNDSVLDVMHAIYQQNKEHFQDECSKLLVGSIVITRYNNRTYRIDDVDWNKTPKDSFVMSDGKEITFLEYYSKNYGITVKEDDQPLLIHRPSERQNNHGMLLKGEILLLPELSFMTGIPEKMKKDFRAMKDLTQQINLSPKQHHGALECLLQRISQNETASNELTRWGLSLHKDVHKIEGRLLPMERINLRNTSFVTSEDLNWVKEVTRDASILTIPMHFWALFYPKRAMDQARELVNMLEKIAGPIGMRISPPAWVELKDDRIETYIRTIQSLLGVEGKIQMVVCIIMGTRDDLYGAIKKLCCVQSPVPSQVINVRTIGQPTRLRSVAQKILLQMNCKLGGELWGVDIPLKQLMVIGMDVYHDPSRGMRSVVGFVASINLTLTKWYSRVVFQMPHQEIVDSLKLCLVGSLKKYYEVNHCLPEKIVVYRDGVSDGQLKTVANYEIPQLQKCFEAFDNYHPKMVVFVVQKKISTNLYLAAPDHFVTPSPGTVVDHTITSCEWVDFYLLAHHVRQGCGIPTHYICVLNTANLSPDHMQRLTFKLCHMYWNWPGTIRVPAPCKYAHKLAFLSGQILHHEPAIQLCGNLFFL
uniprot
proteins
ec_number
3.1.26.-
uniprot
proteins
function
FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:11578866, PubMed:14736746, PubMed:17446352, PubMed:18381894, PubMed:18922463, PubMed:26669262). Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells (PubMed:11578866, PubMed:14736746, PubMed:17446352, PubMed:18381894, PubMed:18922463, PubMed:26669262). Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females (PubMed:11578866, PubMed:14736746, PubMed:17446352, PubMed:18381894, PubMed:18922463, PubMed:26669262). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (PubMed:11578866, PubMed:14736746, PubMed:17446352, PubMed:18381894, PubMed:18922463, PubMed:26669262). During piRNA biosynthesis, plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto 'slicer-incompetent' PIWIL4 (PubMed:22020280, PubMed:23706823, PubMed:26669262). PIWIL2 slicing produces a pre-miRNA intermediate, which is then processed in mature piRNAs, and as well as a 16 nucleotide by-product that is degraded (PubMed:28633017). Required for PIWIL4/MIWI2 nuclear localization and association with secondary piRNAs antisense (PubMed:18381894, PubMed:18922463, PubMed:26669262). Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (PubMed:19114715). Indirectly modulates expression of genes such as PDGFRB, SLC2A1, ITGA6, GJA7, THY1, CD9 and STRA8 (PubMed:16261612). Represses circadian rhythms by promoting the stability and activity of core clock components BMAL1 and CLOCK by inhibiting GSK3B-mediated phosphorylation and ubiquitination-dependent degradation of these proteins (PubMed:28903391). {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:14736746, ECO:0000269|PubMed:16261612, ECO:0000269|PubMed:17446352, ECO:0000269|PubMed:18381894, ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:19114715, ECO:0000269|PubMed:22020280, ECO:0000269|PubMed:23706823, ECO:0000269|PubMed:26669262, ECO:0000269|PubMed:28633017, ECO:0000269|PubMed:28903391}.
uniprot
proteins
mass_dalton
109488
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="R->K: Abolishes interaction with TDRD1; when associated with K-39; K-45 and K-74."; /evidence="ECO:0000269|PubMed:19584108"; MUTAGEN 39; /note="R->K: Abolishes interaction with TDRD1; when associated with K-9; K-45 and K-74."; /evidence="ECO:0000269|PubMed:19584108"; MUTAGEN 45; /note="R->K: Abolishes interaction with TDRD1; when associated with K-9; K-39 and K-74."; /evidence="ECO:0000269|PubMed:19584108"; MUTAGEN 74; /note="R->K: Abolishes interaction with TDRD1; when associated with K-9; K-39 and K-45."; /evidence="ECO:0000269|PubMed:19584108"; MUTAGEN 813; /note="D->A: In DAH mutant; leads to arrest in meiotic prophase due to a failure of transposon piRNA amplification, resulting in the marked reduction of piRNA-bound within PIWIL4."; /evidence="ECO:0000269|PubMed:22020280, ECO:0000269|PubMed:23706823
uniprot
proteins
post_translational_modification
PTM: Arginine methylation by PRMT5 is required for the interaction with Tudor domain-containing protein TDRD1 and subsequent localization to the meiotic nuage, also named P granule. {ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19918066, ECO:0000269|PubMed:22996915}.
uniprot
proteins
protein_family
Argonaute family
uniprot
proteins
protein_family
Piwi subfamily
uniprot
proteins
pubmed
11279525
uniprot
proteins
pubmed
11578866
uniprot
proteins
pubmed
12906857
uniprot
proteins
pubmed
14736746
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16261612
uniprot
proteins
pubmed
16751777
uniprot
proteins
pubmed
16787967
uniprot
proteins
pubmed
17446352
uniprot
proteins
pubmed
18381894
uniprot
proteins
pubmed
18404146
uniprot
proteins
pubmed
18922463
uniprot
proteins
pubmed
19114715
uniprot
proteins
pubmed
19345100
uniprot
proteins
pubmed
19377467
uniprot
proteins
pubmed
19465913
uniprot
proteins
pubmed
19584108
uniprot
proteins
pubmed
19918066
uniprot
proteins
pubmed
20439430
uniprot
proteins
pubmed
20534472
uniprot
proteins
pubmed
20547853
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22020280
uniprot
proteins
pubmed
22996915
uniprot
proteins
pubmed
23611983
uniprot
proteins
pubmed
23706823
uniprot
proteins
pubmed
24067652
uniprot
proteins
pubmed
26669262
uniprot
proteins
pubmed
28254886
uniprot
proteins
pubmed
28633017
uniprot
proteins
pubmed
28903391
uniprot
proteins
pubmed
32381626
uniprot
proteins
sequence_length
971
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:19114715, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20439430, ECO:0000269|PubMed:32381626}. Note=Present in chromatoid body. Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:20439430). {ECO:0000269|PubMed:20439430}.
uniprot
proteins