EXD1_DANRE
ID EXD1_DANRE Reviewed; 378 AA.
AC Q0P3U3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=piRNA biogenesis protein EXD1 {ECO:0000305};
DE AltName: Full=Exonuclease 3'-5' domain-containing protein 1 {ECO:0000250|UniProtKB:Q8NHP7};
DE AltName: Full=Exonuclease 3'-5' domain-like-containing protein 1 {ECO:0000250|UniProtKB:Q8NHP7};
DE AltName: Full=Inactive exonuclease EXD1 {ECO:0000305};
GN Name=exd1; Synonyms=exdl1; ORFNames=zgc:154068;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding component of the PET complex, a multiprotein
CC complex required for the processing of piRNAs during spermatogenesis.
CC The piRNA metabolic process mediates the repression of transposable
CC elements during meiosis by forming complexes composed of piRNAs and
CC Piwi proteins and governs the methylation and subsequent repression of
CC transposable elements, preventing their mobilization, which is
CC essential for the germline integrity. The PET complex is required
CC during the secondary piRNAs metabolic process for the piwil2 slicing-
CC triggered loading of piwil4 piRNAs. In the PET complex, exd1 probably
CC acts as an RNA adapter. Exd1 is an inactive exonuclease.
CC {ECO:0000250|UniProtKB:H9IUR0, ECO:0000250|UniProtKB:Q8CDF7}.
CC -!- SUBUNIT: Homodimer (By similarity). Component of the PET complex (By
CC similarity). {ECO:0000250|UniProtKB:H9IUR0,
CC ECO:0000250|UniProtKB:Q8CDF7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:H9IUR0}.
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:H9IUR0}.
CC -!- DOMAIN: The 3'-5' exonuclease domain lacks the conserved Asp-Glu-Asp-
CC Asp (DEDD) residues that coordinates divalent ions essential for
CC exonuclease activity. {ECO:0000250|UniProtKB:Q8CDF7}.
CC -!- SIMILARITY: Belongs to the EXD1 family. {ECO:0000305}.
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DR EMBL; BC122448; AAI22449.1; -; mRNA.
DR RefSeq; NP_001038930.1; NM_001045465.2.
DR AlphaFoldDB; Q0P3U3; -.
DR SMR; Q0P3U3; -.
DR PRIDE; Q0P3U3; -.
DR GeneID; 751755; -.
DR KEGG; dre:751755; -.
DR CTD; 161829; -.
DR ZFIN; ZDB-GENE-060825-267; exd1.
DR InParanoid; Q0P3U3; -.
DR OrthoDB; 1535075at2759; -.
DR PhylomeDB; Q0P3U3; -.
DR PRO; PR:Q0P3U3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:1990923; C:PET complex; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
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:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Meiosis; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..378
FT /note="piRNA biogenesis protein EXD1"
FT /id="PRO_0000337246"
FT DOMAIN 112..304
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255"
SQ SEQUENCE 378 AA; 42794 MW; DCE27A8E1CBB2C28 CRC64;
MNNRLNTTSS SEESRFLEEM KRKRVNITLS DTEISGVIQK ITQKKTLILE DVSEVRSGRR
FPGAKLIFGK EIVKVEFPLS AGQASVFSNE KHKSEFQTFK KKMTLDGEED GVSYVLIDEL
HEKFGPAVMH IQEQDVIGIG ADVYGQSGQE RLCWLQVATK KVVYLFDILL LGGPAFKNGL
SMILENTHIL KVLHDCRCIT RCLRTEFRVQ LTNVFDTQVA ELLLFFNESG GFLPDRPASL
PELLQLHLRL TTAEIQPLCS KQQQSRECVQ LWYVRPCPPD LLSLMCSSVQ HLLSLRLLLL
DALLADYTVL VDSFMSSSHC PPLHFQQDEC AVPPELQELM CVRQQRMDWA SQCYSQTDSG
LLQRSSFKAS PHTPADAQ