PIWL1_DANRE
ID PIWL1_DANRE Reviewed; 858 AA.
AC Q8UVX0; Q7ZWB5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Piwi-like protein 1;
DE EC=3.1.26.- {ECO:0000250|UniProtKB:Q9JMB7};
GN Name=piwil1; Synonyms=ziwi {ECO:0000303|PubMed:14516689};
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 {ECO:0000312|EMBL:AAL57170.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Gonad {ECO:0000269|PubMed:14516689};
RX PubMed=14516689; DOI=10.1016/s0925-4773(03)00120-5;
RA Tan C.H., Lee T.C., Weeraratne S.D., Korzh V., Lim T.M., Gong Z.;
RT "Ziwi, the zebrafish homologue of the Drosophila piwi: co-localization with
RT vasa at the embryonic genital ridge and gonad-specific expression in the
RT adults.";
RL Mech. Dev. 119:S221-S224(2002).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=AB {ECO:0000305};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RNA-BINDING, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASN-687 AND ILE-694.
RX PubMed=17418787; DOI=10.1016/j.cell.2007.03.026;
RA Houwing S., Kamminga L.M., Berezikov E., Cronembold D., Girard A.,
RA van den Elst H., Filippov D.V., Blaser H., Raz E., Moens C.B.,
RA Plasterk R.H.A., Hannon G.J., Draper B.W., Ketting R.F.;
RT "A role for Piwi and piRNAs in germ cell maintenance and transposon
RT silencing in Zebrafish.";
RL Cell 129:69-82(2007).
RN [4]
RP FUNCTION, AND RNA-BINDING.
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).
CC -!- FUNCTION: Plays a central role during gametogenesis by repressing
CC transposable elements and preventing their mobilization, which is
CC essential for the germline integrity (PubMed:14516689, PubMed:17418787,
CC PubMed:18833190). Acts via the piRNA metabolic process, which mediates
CC the repression of transposable elements during meiosis by forming
CC complexes composed of piRNAs and Piwi proteins and governs the
CC methylation and subsequent repression of transposons (PubMed:14516689,
CC PubMed:17418787, PubMed:18833190). Directly binds methylated piRNAs, a
CC class of 24 to 30 nucleotide RNAs that are generated by a Dicer-
CC independent mechanism and are primarily derived from transposons and
CC other repeated sequence elements (PubMed:14516689, PubMed:17418787,
CC PubMed:18833190). Has a strong preference for piRNAs with a uridine
CC nucleotide at their 5'-end (g1U preference, also named 1U-bias) and
CC binds piRNAs in an opposite direction compared to piwil2/zili
CC (PubMed:14516689, PubMed:17418787, PubMed:18833190). Participates in a
CC piRNA amplification loop with piwil2/zili (PubMed:14516689,
CC PubMed:17418787, PubMed:18833190). Not involved in the piRNA
CC amplification loop, also named ping-pong amplification cycle. Acts as
CC an endoribonuclease that cleaves transposon messenger RNAs (By
CC similarity). {ECO:0000250|UniProtKB:Q9JMB7,
CC ECO:0000269|PubMed:14516689, ECO:0000269|PubMed:17418787,
CC ECO:0000269|PubMed:18833190}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9JMB7};
CC -!- INTERACTION:
CC Q8UVX0; Q58EK5: tdrd1; NbExp=3; IntAct=EBI-7011759, EBI-7011788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17418787}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. {ECO:0000269|PubMed:17418787}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q8UVX0-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8UVX0-2; Sequence=VSP_050727, VSP_050728;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the adult gonads;
CC expression in the ovary weaker than in the testis (at protein level).
CC During neurogenesis and organogenesis, expression is detected in CNS
CC (midbrain and eye) and fin buds. Starting from 24 hours post-
CC fertilization, expression is found in the genital ridge.
CC {ECO:0000269|PubMed:14516689, ECO:0000269|PubMed:17418787}.
CC -!- DEVELOPMENTAL STAGE: Initially detected during embryonic segmentation
CC which persists for at least 4 weeks post hatching.
CC {ECO:0000269|PubMed:14516689}.
CC -!- DOMAIN: The PAZ domain specifically recognizes binds the 2'-O-
CC methylated 3'-end of piRNAs. The MID region is required for recognition
CC of uridine in the first position of piRNAs (g1U preference, also named
CC 1U-bias). {ECO:0000250|UniProtKB:Q9JMB7}.
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:Q9JMB7}.
CC -!- DISRUPTION PHENOTYPE: Progressive loss of germ cells due to apoptosis
CC during larval development. {ECO:0000269|PubMed:17418787}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
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DR EMBL; AF336369; AAL57170.1; -; mRNA.
DR EMBL; BC049495; AAH49495.1; -; mRNA.
DR RefSeq; NP_899181.1; NM_183338.1. [Q8UVX0-1]
DR AlphaFoldDB; Q8UVX0; -.
DR SMR; Q8UVX0; -.
DR IntAct; Q8UVX0; 2.
DR MINT; Q8UVX0; -.
DR STRING; 7955.ENSDARP00000121147; -.
DR PaxDb; Q8UVX0; -.
DR PRIDE; Q8UVX0; -.
DR Ensembl; ENSDART00000061115; ENSDARP00000061114; ENSDARG00000041699. [Q8UVX0-1]
DR Ensembl; ENSDART00000138019; ENSDARP00000121147; ENSDARG00000041699. [Q8UVX0-1]
DR GeneID; 368200; -.
DR KEGG; dre:368200; -.
DR CTD; 9271; -.
DR ZFIN; ZDB-GENE-030813-2; piwil1.
DR eggNOG; KOG1042; Eukaryota.
DR GeneTree; ENSGT00950000183200; -.
DR HOGENOM; CLU_008813_0_0_1; -.
DR InParanoid; Q8UVX0; -.
DR OMA; NPTMSRW; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; Q8UVX0; -.
DR TreeFam; TF354206; -.
DR PRO; PR:Q8UVX0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000041699; Expressed in testis and 28 other tissues.
DR ExpressionAtlas; Q8UVX0; baseline.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0043186; C:P granule; IDA: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:0009653; P:anatomical structure morphogenesis; IDA:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IDA:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
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; PF05831; GAGE; 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 Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Endonuclease; Hydrolase; Magnesium; Meiosis; Metal-binding; Methylation;
KW Nuclease; Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation.
FT CHAIN 1..858
FT /note="Piwi-like protein 1"
FT /id="PRO_0000194066"
FT DOMAIN 272..388
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 552..844
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..316
FT /note="Required for binding 2'-O-methylated 3'-end of
FT piRNAs"
FT /evidence="ECO:0000250|UniProtKB:Q9JMB7"
FT REGION 476..612
FT /note="MID region"
FT /evidence="ECO:0000250|UniProtKB:Q9JMB7"
FT ACT_SITE 629
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 667
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 699
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 833
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT SITE 378
FT /note="Required for binding 2'-O-methylated 3'-end of
FT piRNAs"
FT /evidence="ECO:0000250|UniProtKB:Q9JMB7"
FT VAR_SEQ 350..373
FT /note="DITDGNQVLLVSHVKRLGPSGRPP -> VIIRLLFFVIRCSNLKFLYLEIVN
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_050727"
FT VAR_SEQ 374..858
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_050728"
FT MUTAGEN 687
FT /note="N->K: In hu2410; induces germ cells apoptosis."
FT /evidence="ECO:0000269|PubMed:17418787"
FT MUTAGEN 694
FT /note="I->N: In fh222; induces germ cells apoptosis."
FT /evidence="ECO:0000269|PubMed:17418787"
FT CONFLICT 322
FT /note="W -> R (in Ref. 2; AAH49495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 97451 MW; 6A12F2E511465777 CRC64;
MTGRARARSR GRGRGQEPAA PGAQPPVSQE AAKPVVSTPS EGQLVGRGRQ KPAPGAMSEE
AMLQISAGFQ QVKIGERGGR RRDFHDSGVH TRQLMEHVKE SKTGVSGTAI ELRANFMRLL
SRPMWALYQY HVDYKPPMES RRLRSALLFQ HEETLGKAHT FDGAILFLPN KLRNAETVLC
SETRNGEKVE ITVTLTNELP PSSPVCLQFY NILFRRILRI LNMQQIGRHY YNPDDPFNIP
QHRLTIWPGF MTTILQYESS IMLCSDVSHK VLRSETVLDF MYSLRQQCGD QRFPEACTKE
LVGLIILTKY NNKTYRIDDI AWDHTPNNTF KKGDTEISFK NYFKSQYGLD ITDGNQVLLV
SHVKRLGPSG RPPPGPAMLV PEFCYLTGLT DKMRADFNIM KDLASHTRLS PEQREGRINR
LISNINRNGD VQNELTTWGL SFENKLLSLN GRVLPSERII QGGRAFEYNP WTADWSKEMR
GLPLISCMSL DNWLMFYTRR NADVAQSLLQ TLNKVSGPMG IRMQRAVMIE YEDRQESLLR
ALQQNVARET QMVVVILPTN RKDKYDCVKK YLCVDCPTPS QCVVSRTISK PQALMTVATK
IALQMNCKMG GELWSVEIPL RQLMIVGIDC YHDTAAGKRS IGAMVASLNQ GMSRWFSKCV
LQNRGQEIID ALKGSLQGAL KAYLKYNNSL PSRIIVYRDG VGDGMLQSVV DYEVPQIMQS
IKTMGQDYEP KLSVVVVKKR ISSRFFARID GKIANPPPGT VIDTEVTRPE WYDFFIVSQA
VRFGCVAPTH YNVVFDNSGL KPDHMQRLTY KLCHMYYNWQ GIVRVPAPCQ YAHKLAFLVG
QSIHKEPNMN LDDFLYYL
