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Database: UniProt
Entry: Q8UVX0
LinkDB: Q8UVX0
Original site: Q8UVX0 
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   16-OCT-2019, entry version 123.
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   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000312|EMBL:AAL57170.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND 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
RT   with vasa at the embryonic genital ridge and gonad-specific expression
RT   in the 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,
RP   DISRUPTION 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
RT   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,
CC       PubMed:17418787, PubMed:18833190). Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements
CC       during meiosis by forming complexes composed of piRNAs and Piwi
CC       proteins and governs the methylation and subsequent repression of
CC       transposons (PubMed:14516689, PubMed:17418787, PubMed:18833190).
CC       Directly binds methylated piRNAs, a class of 24 to 30 nucleotide
CC       RNAs that are generated by a Dicer-independent mechanism and are
CC       primarily derived from transposons and other repeated sequence
CC       elements (PubMed:14516689, PubMed:17418787, PubMed:18833190). Has
CC       a strong preference for piRNAs with a uridine nucleotide at their
CC       5'-end (g1U preference, also named 1U-bias) and binds piRNAs in an
CC       opposite direction compared to piwil2/zili (PubMed:14516689,
CC       PubMed:17418787, PubMed:18833190). Participates in a piRNA
CC       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
CC       as 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       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-
CC       cell-specific organelle required to repress transposon activity
CC       during 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         Note=No experimental confirmation available. {ECO:0000305};
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in the adult gonads;
CC       expression in the ovary weaker than in the testis (at protein
CC       level). During neurogenesis and organogenesis, expression is
CC       detected in CNS (midbrain and eye) and fin buds. Starting from 24
CC       hours post-fertilization, expression is found in the genital
CC       ridge. {ECO:0000269|PubMed:14516689, ECO:0000269|PubMed:17418787}.
CC   -!- DEVELOPMENTAL STAGE: Initially detected during embryonic
CC       segmentation 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
CC       recognition of uridine in the first position of piRNAs (g1U
CC       preference, also named 1U-bias). {ECO:0000250|UniProtKB:Q9JMB7}.
CC   -!- PTM: Methylated on arginine residues; required for the interaction
CC       with Tudor domain-containing protein and subsequent localization
CC       to the meiotic nuage, also named P granule.
CC       {ECO:0000250|UniProtKB:Q9JMB7}.
CC   -!- DISRUPTION PHENOTYPE: Progressive loss of germ cells due to
CC       apoptosis during larval development.
CC       {ECO:0000269|PubMed:17418787}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC       {ECO:0000305}.
DR   EMBL; AF336369; AAL57170.1; -; mRNA.
DR   EMBL; BC049495; AAH49495.1; -; mRNA.
DR   RefSeq; NP_899181.1; NM_183338.1. [Q8UVX0-1]
DR   SMR; Q8UVX0; -.
DR   IntAct; Q8UVX0; 2.
DR   MINT; Q8UVX0; -.
DR   STRING; 7955.ENSDARP00000121147; -.
DR   PaxDb; 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   eggNOG; ENOG410XNRH; LUCA.
DR   GeneTree; ENSGT00950000183200; -.
DR   HOGENOM; HOG000254789; -.
DR   InParanoid; Q8UVX0; -.
DR   KO; K02156; -.
DR   OMA; CVAPTHY; -.
DR   OrthoDB; 220258at2759; -.
DR   PhylomeDB; Q8UVX0; -.
DR   TreeFam; TF354206; -.
DR   PRO; PR:Q8UVX0; -.
DR   Proteomes; UP000000437; Chromosome 8.
DR   Bgee; ENSDARG00000041699; Expressed in 25 organ(s), highest expression level in testis.
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: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:0007275; P:multicellular organism development; 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; 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; 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; Complete proteome; Cytoplasm;
KW   Developmental protein; Differentiation; Endonuclease; Hydrolase;
KW   Magnesium; Meiosis; Metal-binding; Methylation; Nuclease;
KW   Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW   Translation regulation.
FT   CHAIN         1    858       Piwi-like protein 1.
FT                                /FTId=PRO_0000194066.
FT   DOMAIN      272    388       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      552    844       Piwi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00150}.
FT   REGION      314    316       Required for binding 2'-O-methylated 3'-
FT                                end of piRNAs.
FT                                {ECO:0000250|UniProtKB:Q9JMB7}.
FT   REGION      476    612       MID region.
FT                                {ECO:0000250|UniProtKB:Q9JMB7}.
FT   ACT_SITE    629    629       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE    667    667       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE    699    699       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE    833    833       {ECO:0000250|UniProtKB:A8D8P8}.
FT   SITE        378    378       Required for binding 2'-O-methylated 3'-
FT                                end of piRNAs.
FT                                {ECO:0000250|UniProtKB:Q9JMB7}.
FT   VAR_SEQ     350    373       DITDGNQVLLVSHVKRLGPSGRPP -> VIIRLLFFVIRCS
FT                                NLKFLYLEIVN (in isoform 2).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_050727.
FT   VAR_SEQ     374    858       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_050728.
FT   MUTAGEN     687    687       N->K: In hu2410; induces germ cells
FT                                apoptosis. {ECO:0000269|PubMed:17418787}.
FT   MUTAGEN     694    694       I->N: In fh222; induces germ cells
FT                                apoptosis. {ECO:0000269|PubMed:17418787}.
FT   CONFLICT    322    322       W -> R (in Ref. 2; AAH49495).
FT                                {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
//
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