PIWL1_CHICK
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 03-AUG-2022, entry version 84.
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; Phasianidae;
OC 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 germ
CC cells by repressing transposable elements and preventing their
CC mobilization, which is essential for the germline integrity. Acts via
CC the piRNA metabolic process, which mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and govern the methylation and subsequent
CC repression of transposons. Directly binds methylated piRNAs, a class of
CC 24 to 30 nucleotide RNAs that are generated by a Dicer-independent
CC mechanism and are primarily derived from transposons and other repeated
CC sequence elements. Strongly prefers a uridine in the first position of
CC their guide (g1U preference, also named 1U-bias). Besides their
CC function in transposable elements repression, piRNAs are probably
CC involved in other processes during meiosis such as translation
CC regulation. Not involved in the piRNA amplification loop, also named
CC ping-pong 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-cell-
CC specific organelle required to repress transposon activity during
CC 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 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 -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
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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 AlphaFoldDB; A6N7Y9; -.
DR SMR; A6N7Y9; -.
DR STRING; 9031.ENSGALP00000004162; -.
DR PaxDb; A6N7Y9; -.
DR PRIDE; A6N7Y9; -.
DR Ensembl; ENSGALT00000004171; ENSGALP00000004162; ENSGALG00000002645.
DR GeneID; 416804; -.
DR KEGG; gga:416804; -.
DR CTD; 9271; -.
DR VEuPathDB; HostDB:geneid_416804; -.
DR eggNOG; KOG1042; Eukaryota.
DR GeneTree; ENSGT00950000183200; -.
DR HOGENOM; CLU_008813_0_0_1; -.
DR InParanoid; A6N7Y9; -.
DR OMA; NPTMSRW; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; A6N7Y9; -.
DR PRO; PR:A6N7Y9; -.
DR Proteomes; UP000000539; Chromosome 15.
DR Bgee; ENSGALG00000002645; Expressed in spermatid and 6 other tissues.
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:0003723; F:RNA binding; IBA:GO_Central.
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: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; 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; 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 Cytoplasm; 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..867
FT /note="Piwi-like protein 1"
FT /id="PRO_0000367286"
FT DOMAIN 285..397
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 561..853
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..326
FT /note="Required for binding 2'-O-methylated 3'-end of
FT piRNAs"
FT /evidence="ECO:0000250|UniProtKB:Q9JMB7"
FT REGION 485..621
FT /note="MID region"
FT /evidence="ECO:0000250|UniProtKB:Q9JMB7"
FT COMPBIAS 30..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 638
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 676
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 708
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 842
FT /evidence="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
