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Database: UniProt
Entry: A6N7Y9
LinkDB: A6N7Y9
Original site: A6N7Y9 
ID   PIWL1_CHICK             Reviewed;         867 AA.
AC   A6N7Y9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   16-OCT-2019, entry version 74.
DE   RecName: Full=Piwi-like protein 1;
DE            EC=3.1.26.- {ECO:0000250|UniProtKB:Q9JMB7};
GN   Name=PIWIL1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Wang Y., Li J., Wang C.Y., Leung F.C.;
RT   "Characterization of Piwi-like homolog 1 (Piwi) expression in the
RT   developing ovary and testis of chicken (Gallus gallus).";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease that plays a central role in postnatal
CC       germ cells by repressing transposable elements and preventing
CC       their mobilization, which is essential for the germline integrity.
CC       Acts via the piRNA metabolic process, which mediates the
CC       repression of transposable elements during meiosis by forming
CC       complexes composed of piRNAs and Piwi proteins and govern the
CC       methylation and subsequent repression of transposons. Directly
CC       binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that
CC       are generated by a Dicer-independent mechanism and are primarily
CC       derived from transposons and other repeated sequence elements.
CC       Strongly prefers a uridine in the first position of their guide
CC       (g1U preference, also named 1U-bias). Besides their function in
CC       transposable elements repression, piRNAs are probably involved in
CC       other processes during meiosis such as translation regulation. Not
CC       involved in the piRNA amplification loop, also named ping-pong
CC       amplification cycle. Acts as an endoribonuclease that cleaves
CC       transposon messenger RNAs (By similarity).
CC       {ECO:0000250|UniProtKB:Q9JMB7}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9JMB7};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JMB7}.
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:0000250|UniProtKB:Q9JMB7}.
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   -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC       {ECO:0000305}.
DR   EMBL; EF619343; ABR09543.1; -; mRNA.
DR   RefSeq; NP_001092322.1; NM_001098852.1.
DR   RefSeq; XP_015130744.1; XM_015275258.1.
DR   RefSeq; XP_015130745.1; XM_015275259.1.
DR   RefSeq; XP_015130746.1; XM_015275260.1.
DR   RefSeq; XP_015130747.1; XM_015275261.1.
DR   RefSeq; XP_015130748.1; XM_015275262.1.
DR   RefSeq; XP_015130749.1; XM_015275263.1.
DR   SMR; A6N7Y9; -.
DR   STRING; 9031.ENSGALP00000004162; -.
DR   PaxDb; A6N7Y9; -.
DR   Ensembl; ENSGALT00000004171; ENSGALP00000004162; ENSGALG00000002645.
DR   GeneID; 416804; -.
DR   KEGG; gga:416804; -.
DR   CTD; 9271; -.
DR   eggNOG; KOG1042; Eukaryota.
DR   eggNOG; ENOG410XNRH; LUCA.
DR   GeneTree; ENSGT00950000183200; -.
DR   HOGENOM; HOG000254789; -.
DR   InParanoid; A6N7Y9; -.
DR   KO; K02156; -.
DR   OMA; CVAPTHY; -.
DR   OrthoDB; 220258at2759; -.
DR   PhylomeDB; A6N7Y9; -.
DR   PRO; PR:A6N7Y9; -.
DR   Proteomes; UP000000539; Chromosome 15.
DR   Bgee; ENSGALG00000002645; Expressed in 5 organ(s), highest expression level in testis.
DR   GO; GO:0033391; C:chromatoid body; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0097433; C:dense body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR   GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0140262; F:mRNA cap binding complex binding; IEA:Ensembl.
DR   GO; GO:0034584; F:piRNA binding; ISS:UniProtKB.
DR   GO; GO:1905538; F:polysome binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
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: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; ISS: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; 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   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Developmental protein; Differentiation;
KW   Endonuclease; Hydrolase; Magnesium; Meiosis; Metal-binding;
KW   Methylation; Nuclease; Reference proteome; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation.
FT   CHAIN         1    867       Piwi-like protein 1.
FT                                /FTId=PRO_0000367286.
FT   DOMAIN      285    397       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      561    853       Piwi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00150}.
FT   REGION      324    326       Required for binding 2'-O-methylated 3'-
FT                                end of piRNAs.
FT                                {ECO:0000250|UniProtKB:Q9JMB7}.
FT   REGION      485    621       MID region.
FT                                {ECO:0000250|UniProtKB:Q9JMB7}.
FT   ACT_SITE    638    638       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE    676    676       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE    708    708       {ECO:0000250|UniProtKB:A8D8P8}.
FT   ACT_SITE    842    842       {ECO:0000250|UniProtKB:A8D8P8}.
SQ   SEQUENCE   867 AA;  99286 MW;  A8BAF115A1588475 CRC64;
     MTGRARARAR GRPPGQEAAI PPVGAASAQK TLPSHPSEQR QSLQPCHPPP LTEEPGGRGR
     QRGPQDAPKT LGLQISAGFQ ELSLADRGGR RRDFHDLGVN TRQAIEHVRE SKTGSSGAMI
     KLIANFFRLT SRPQWALYQY HVDYNPEMEA RRLRSGLLFQ HEDLIGKTHA FDGSILFLPK
     RLPNKVTEVY SKTRNGEDVR ITITLTNELP PTSPTCLQFY NIIFRRLLKM MNFQQIGRNY
     YNPKDPVSIP NHRLMVWPGF TSSILQYEES IMLCADVSHK ILRSETVLDF MYSLYEQVEE
     RRFRDACAKE LIGVIVLTKY NNRTYRVDDI DWDANPQCTF RRADGSEISY IDYYKRQYNQ
     DISDLNQPVL ISQYRRKRGN VTVGPVVLIP ELCYLTGLTE KMRNDFNMMK DLAVHTRLSP
     EQRQREIGKL VDCMKKDECV QKELRDWGLS FDSSLLSFTG RVVQAEKILQ AGNVFDYNPQ
     FADWSRETRV APLIHAKPLD NWLLIYTRRN YDAANMLLQN LFKVTPSMGI RMNKATMIEV
     DDRTEAYLRV LQQSITPDTN IVVCILSSTR KDKYDAIKKY LCTDCPIPSQ CVVARTLSKP
     QTALAIVTKI ALQMNCKMGG ELWSVEIPLK QLMIVGIDCY HDTLSGKQSI AGFVASLNEK
     MTRWFSRCVV QSRGQEIVDG LKACLQTALR EWFKWNKYLP SRIIVYRDGV GDGQLNTLVN
     YEVPQFLDCL KTVGKDYNPR LTVIVVKKRV STRFFAQAGG GLKNPPPGTV VDIEVTRPEW
     YDFFIVSQAV RNGCVAPTHY NVVYDTSKLK PDHVQRLTYK LCHMYYNWSG VIRVPAPCQY
     AHKLAFLVGQ SIHREPNLLL SDRLYYL
//
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