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Protein

Piwi-like protein 2

Gene

Piwil2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells. Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females. 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. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Associates with primary piRNAs in the cytoplasm and is required for PIWIL4/MIWI2 nuclear localization and association with secondary piRNAs antisense. The piRNA process acts upstream of known mediators of DNA methylation. Participates in a piRNA amplification loop. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Indirectly modulates expression of genes such as PDGFRB, SLC2A1, ITGA6, GJA7, THY1, CD9 and STRA8. Inhibits tumor cell growth when repressed.8 Publications

GO - Molecular functioni

  • mRNA binding Source: UniProtKB
  • piRNA binding Source: UniProtKB

GO - Biological processi

  • DNA methylation involved in gamete generation Source: UniProtKB
  • gene silencing by RNA Source: UniProtKB
  • germ-line stem cell population maintenance Source: UniProtKB
  • meiotic cell cycle Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • oogenesis Source: UniProtKB
  • piRNA metabolic process Source: UniProtKB
  • positive regulation of histone H3-K14 acetylation Source: CACAO
  • positive regulation of histone H3-K9 acetylation Source: CACAO
  • positive regulation of meiosis I Source: MGI
  • positive regulation of translation Source: UniProtKB
  • RNA 5'-end processing Source: UniProtKB
  • spermatogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Meiosis, Oogenesis, RNA-mediated gene silencing, Spermatogenesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-5601884. PIWI-interacting RNA (piRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Piwi-like protein 2
Gene namesi
Name:Piwil2
Synonyms:Mili
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1930036. Piwil2.

Subcellular locationi

GO - Cellular componenti

  • chromatoid body Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • dense body Source: MGI
  • perinucleolar chromocenter Source: MGI
  • PET complex Source: UniProtKB
  • P granule Source: UniProtKB
  • pi-body Source: UniProtKB
  • polysome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice exhibit blocked spermatogenesis at the early prophase of the first meiosis due to transposable elements derepression, and apoptosis occurs subsequently. Female mice are fertile, while male are sterile.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9R → K: Abolishes interaction with TDRD1; when associated with K-39; K-45 and K-74. 1 Publication1
Mutagenesisi39R → K: Abolishes interaction with TDRD1; when associated with K-9; K-45 and K-74. 1 Publication1
Mutagenesisi45R → K: Abolishes interaction with TDRD1; when associated with K-9; K-39 and K-74. 1 Publication1
Mutagenesisi74R → K: Abolishes interaction with TDRD1; when associated with K-9; K-39 and K-45. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002345701 – 971Piwi-like protein 2Add BLAST971

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei45Symmetric dimethylarginine2 Publications1
Modified residuei74Omega-N-methylarginine; by PRMT5; alternate4 Publications1
Modified residuei74Symmetric dimethylarginine; by PRMT5; alternate4 Publications1
Modified residuei83Omega-N-methylarginine; alternate1 Publication1
Modified residuei83Symmetric dimethylarginine; alternate1 Publication1
Modified residuei95Omega-N-methylarginine; by PRMT5; alternate2 Publications1
Modified residuei95Symmetric dimethylarginine; alternate2 Publications1
Modified residuei100Omega-N-methylarginine; alternate2 Publications1
Modified residuei100Symmetric dimethylarginine; by PRMT5; alternate2 Publications1
Modified residuei144Symmetric dimethylarginine1 Publication1
Modified residuei156Symmetric dimethylarginine1 Publication1
Modified residuei163Symmetric dimethylarginine; by PRMT52 Publications1
Modified residuei549Symmetric dimethylarginine; by PRMT51 Publication1

Post-translational modificationi

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.5 Publications

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiQ8CDG1.
PRIDEiQ8CDG1.

PTM databases

iPTMnetiQ8CDG1.
PhosphoSitePlusiQ8CDG1.

Expressioni

Tissue specificityi

Expressed in adult testis, specifically in spermatocytes and in spermatogonia. Only detected in primordial germ cells of both sexes. Widely expressed in tumors. Also present at early stages of oocyte growth. Expressed in brain (at protein level).7 Publications

Developmental stagei

Expressed from E12.5 until adult in male gonads. In female gonads, detected since E12.5, then begins to cease after birth and disappears until the development of adult ovary.1 Publication

Gene expression databases

BgeeiENSMUSG00000033644.
CleanExiMM_PIWIL2.
GenevisibleiQ8CDG1. MM.

Interactioni

Subunit structurei

Interacts with DDX4, MAEL, EIF3A, EIF4E, EIF4G, PRMT5 and WDR77. Associates with EIF4E- and EIF4G-containing m7G cap-binding complexes. Interacts (when methylated on arginine residues) with TDRD1 and TDRKH/TDRD2. Interacts with TDRD12 (PubMed:24067652). Component of the PET complex, at least composed of EXD1, PIWIL2, TDRD12 and piRNAs (PubMed:26669262). Interacts with MOV10L1 (PubMed:20534472, PubMed:20547853).12 Publications

Protein-protein interaction databases

BioGridi208309. 1 interactor.
DIPiDIP-48522N.
IntActiQ8CDG1. 3 interactors.
MINTiMINT-8174116.
STRINGi10090.ENSMUSP00000047385.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B9WX-ray2.10P/S38-50[»]
ProteinModelPortaliQ8CDG1.
SMRiQ8CDG1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini386 – 494PAZPROSITE-ProRule annotationAdd BLAST109
Domaini666 – 957PiwiPROSITE-ProRule annotationAdd BLAST292

Sequence similaritiesi

Belongs to the argonaute family. Piwi subfamily.Curated
Contains 1 PAZ domain.PROSITE-ProRule annotation
Contains 1 Piwi domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1042. Eukaryota.
ENOG410XNRH. LUCA.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000254789.
HOVERGENiHBG049411.
InParanoidiQ8CDG1.
KOiK02156.
OMAiDVMHAIY.
OrthoDBiEOG091G020J.
PhylomeDBiQ8CDG1.
TreeFamiTF354206.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR014811. ArgoL1.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF08699. ArgoL1. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM01163. DUF1785. 1 hit.
SM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]
SUPFAMiSSF101690. SSF101690. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CDG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPVRPLFRG PTPVHPSQCV RMPGCWPQAP RPLEPAWGRA GPAGRGLVFR
60 70 80 90 100
KPEDSSPPLQ PVQKDSVGLV SMFRGMGLDT AFRPPSKREV PPLGRGVLGR
110 120 130 140 150
GLSANMVRKD REEPRSSLPD PSVLAAGDSK LAEASVGWSR MLGRGSSEVS
160 170 180 190 200
LLPLGRAASS IGRGMDKPPS AFGLTARDPP RLPQPPALSP TSLHSADPPP
210 220 230 240 250
VLTMERKEKE LLVKQGSKGT PQSLGLNLIK IQCHNEAVYQ YHVTFSPSVE
260 270 280 290 300
CKSMRFGMLK DHQSVTGNVT AFDGSILYLP VKLQQVVELK SQRKTDDAEI
310 320 330 340 350
SIKIQLTKIL EPCSDLCIPF YNVVFRRVMK LLDMKLVGRN FYDPTSAMVL
360 370 380 390 400
QQHRLQIWPG YAASIRRTDG GLFLLADVSH KVIRNDSVLD VMHAIYQQNK
410 420 430 440 450
EHFQDECSKL LVGSIVITRY NNRTYRIDDV DWNKTPKDSF VMSDGKEITF
460 470 480 490 500
LEYYSKNYGI TVKEDDQPLL IHRPSERQNN HGMLLKGEIL LLPELSFMTG
510 520 530 540 550
IPEKMKKDFR AMKDLTQQIN LSPKQHHGAL ECLLQRISQN ETASNELTRW
560 570 580 590 600
GLSLHKDVHK IEGRLLPMER INLRNTSFVT SEDLNWVKEV TRDASILTIP
610 620 630 640 650
MHFWALFYPK RAMDQARELV NMLEKIAGPI GMRISPPAWV ELKDDRIETY
660 670 680 690 700
IRTIQSLLGV EGKIQMVVCI IMGTRDDLYG AIKKLCCVQS PVPSQVINVR
710 720 730 740 750
TIGQPTRLRS VAQKILLQMN CKLGGELWGV DIPLKQLMVI GMDVYHDPSR
760 770 780 790 800
GMRSVVGFVA SINLTLTKWY SRVVFQMPHQ EIVDSLKLCL VGSLKKYYEV
810 820 830 840 850
NHCLPEKIVV YRDGVSDGQL KTVANYEIPQ LQKCFEAFDN YHPKMVVFVV
860 870 880 890 900
QKKISTNLYL AAPDHFVTPS PGTVVDHTIT SCEWVDFYLL AHHVRQGCGI
910 920 930 940 950
PTHYICVLNT ANLSPDHMQR LTFKLCHMYW NWPGTIRVPA PCKYAHKLAF
960 970
LSGQILHHEP AIQLCGNLFF L
Length:971
Mass (Da):109,488
Last modified:May 16, 2006 - v2
Checksum:i01E143C6513310FB
GO

Sequence cautioni

The sequence AAK31965 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti517Q → E in BAE37436 (PubMed:16141072).Curated1
Sequence conflicti542T → A in BAC26791 (PubMed:16141072).Curated1
Sequence conflicti583D → G in AAK31965 (PubMed:11279525).Curated1
Sequence conflicti634I → T in AAK31965 (PubMed:11279525).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032605 mRNA. Translation: BAA93706.1.
AK030116 mRNA. Translation: BAC26791.1.
AK163647 mRNA. Translation: BAE37436.1.
CH466535 Genomic DNA. Translation: EDL35904.1.
BC138444 mRNA. Translation: AAI38445.1.
BC145717 mRNA. Translation: AAI45718.1.
AF285586 mRNA. Translation: AAK31965.1. Different initiation.
CCDSiCCDS27252.1.
RefSeqiNP_067283.1. NM_021308.1.
XP_006519392.1. XM_006519329.3.
UniGeneiMm.85253.

Genome annotation databases

EnsembliENSMUST00000048129; ENSMUSP00000047385; ENSMUSG00000033644.
GeneIDi57746.
KEGGimmu:57746.
UCSCiuc007unx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032605 mRNA. Translation: BAA93706.1.
AK030116 mRNA. Translation: BAC26791.1.
AK163647 mRNA. Translation: BAE37436.1.
CH466535 Genomic DNA. Translation: EDL35904.1.
BC138444 mRNA. Translation: AAI38445.1.
BC145717 mRNA. Translation: AAI45718.1.
AF285586 mRNA. Translation: AAK31965.1. Different initiation.
CCDSiCCDS27252.1.
RefSeqiNP_067283.1. NM_021308.1.
XP_006519392.1. XM_006519329.3.
UniGeneiMm.85253.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B9WX-ray2.10P/S38-50[»]
ProteinModelPortaliQ8CDG1.
SMRiQ8CDG1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208309. 1 interactor.
DIPiDIP-48522N.
IntActiQ8CDG1. 3 interactors.
MINTiMINT-8174116.
STRINGi10090.ENSMUSP00000047385.

PTM databases

iPTMnetiQ8CDG1.
PhosphoSitePlusiQ8CDG1.

Proteomic databases

PaxDbiQ8CDG1.
PRIDEiQ8CDG1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048129; ENSMUSP00000047385; ENSMUSG00000033644.
GeneIDi57746.
KEGGimmu:57746.
UCSCiuc007unx.1. mouse.

Organism-specific databases

CTDi55124.
MGIiMGI:1930036. Piwil2.

Phylogenomic databases

eggNOGiKOG1042. Eukaryota.
ENOG410XNRH. LUCA.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000254789.
HOVERGENiHBG049411.
InParanoidiQ8CDG1.
KOiK02156.
OMAiDVMHAIY.
OrthoDBiEOG091G020J.
PhylomeDBiQ8CDG1.
TreeFamiTF354206.

Enzyme and pathway databases

ReactomeiR-MMU-5601884. PIWI-interacting RNA (piRNA) biogenesis.

Miscellaneous databases

PROiQ8CDG1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000033644.
CleanExiMM_PIWIL2.
GenevisibleiQ8CDG1. MM.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR014811. ArgoL1.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF08699. ArgoL1. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM01163. DUF1785. 1 hit.
SM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]
SUPFAMiSSF101690. SSF101690. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPIWL2_MOUSE
AccessioniPrimary (citable) accession number: Q8CDG1
Secondary accession number(s): A6H617
, Q3TQE8, Q99MV6, Q9JMB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: November 30, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.