PARN1_CAEEL
ID PARN1_CAEEL Reviewed; 566 AA.
AC Q21412;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=3'-5' exoribonuclease parn-1 {ECO:0000305};
DE AltName: Full=Poly(A)-specific ribonuclease homolog 1 {ECO:0000303|PubMed:23843623, ECO:0000312|WormBase:K10C8.1};
DE AltName: Full=RNase parn-1 {ECO:0000303|PubMed:26919432};
DE EC=3.1.13.- {ECO:0000269|PubMed:26919432};
GN Name=parn-1 {ECO:0000312|EMBL:CAA98954.2, ECO:0000312|WormBase:K10C8.1};
GN ORFNames=K10C8.1 {ECO:0000312|WormBase:K10C8.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CAA98954.2};
RN [1] {ECO:0000312|EMBL:CAA98954.2, ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA98954.2,
RC ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND PHYLOGENETIC ANALYSIS.
RX PubMed=23843623; DOI=10.1242/jcs.132936;
RA Nousch M., Techritz N., Hampel D., Millonigg S., Eckmann C.R.;
RT "The Ccr4-Not deadenylase complex constitutes the main poly(A) removal
RT activity in C. elegans.";
RL J. Cell Sci. 126:4274-4285(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-29.
RX PubMed=26919432; DOI=10.1016/j.cell.2016.02.008;
RA Tang W., Tu S., Lee H.C., Weng Z., Mello C.C.;
RT "The RNase PARN-1 trims piRNA 3' ends to promote transcriptome surveillance
RT in C. elegans.";
RL Cell 164:974-984(2016).
CC -!- FUNCTION: Involved in transcriptome surveillance. Required for piwi-
CC interacting RNAs (piRNAs) 3'-end trimming, which is important for both
CC fertility and piRNA-directed gene silencing. Has 3' to 5' exonuclease
CC activity in vitro. {ECO:0000269|PubMed:26919432}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:O95453};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 nM for 5' end-labeled 14-nucleotide RNA substrate
CC {ECO:0000269|PubMed:26919432};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26919432}. Note=Co-
CC localizes with prg-1 in germline nuage structures called P granules.
CC {ECO:0000269|PubMed:26919432}.
CC -!- TISSUE SPECIFICITY: Expressed in germline cells.
CC {ECO:0000269|PubMed:23843623, ECO:0000269|PubMed:26919432}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels at the L1 to L3 larval
CC stages, but begins to accumulate at the L4 stage and reaches its
CC highest expression level at the gravid adult stage.
CC {ECO:0000269|PubMed:26919432}.
CC -!- DISRUPTION PHENOTYPE: Slight changes of mRNA bulk poly(A) tail lengths
CC (PubMed:23843623). Animals display a reduced brood size at elevated
CC temperature of 25 degrees Celsius compared to wild-type
CC (PubMed:23843623, PubMed:26919432). Accumulation of untrimmed piRNAs
CC with 3' extensions, which are stable and able to co-localize with the
CC piwi protein prg-1. However, while the expression levels of piRNAs
CC remain unchanged, the piwi-dependent mRNA silencing is reduced, as is
CC the production of piwi-dependent secondary small interfering RNAs
CC (siRNAs), also called 22G-RNAs, on mRNA targets. 5'-end processing and
CC methylation of 3'-ends are unaffected. No changes in length
CC distribution of other small RNA species, such as microRNAs (miRNAs)
CC (PubMed:26919432). {ECO:0000269|PubMed:23843623,
CC ECO:0000269|PubMed:26919432}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284605; CAA98954.2; -; Genomic_DNA.
DR PIR; T23559; T23559.
DR RefSeq; NP_506169.2; NM_073768.2.
DR AlphaFoldDB; Q21412; -.
DR SMR; Q21412; -.
DR DIP; DIP-24647N; -.
DR STRING; 6239.K10C8.1; -.
DR PaxDb; Q21412; -.
DR EnsemblMetazoa; K10C8.1.1; K10C8.1.1; WBGene00010734.
DR GeneID; 187256; -.
DR KEGG; cel:CELE_K10C8.1; -.
DR UCSC; K10C8.1; c. elegans.
DR CTD; 187256; -.
DR WormBase; K10C8.1; CE39514; WBGene00010734; parn-1.
DR eggNOG; KOG1990; Eukaryota.
DR GeneTree; ENSGT00940000153167; -.
DR HOGENOM; CLU_018030_2_0_1; -.
DR InParanoid; Q21412; -.
DR OMA; HRWYLEH; -.
DR OrthoDB; 1402758at2759; -.
DR PhylomeDB; Q21412; -.
DR SABIO-RK; Q21412; -.
DR PRO; PR:Q21412; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010734; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0043169; F:cation binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:UniProtKB.
DR GO; GO:0071025; P:RNA surveillance; IMP:UniProtKB.
DR Gene3D; 3.30.420.10; -; 2.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF04857; CAF1; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..566
FT /note="3'-5' exoribonuclease parn-1"
FT /id="PRO_0000437545"
FT BINDING 29
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT BINDING 31
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT BINDING 283
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT BINDING 379
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT SITE 317
FT /note="Interaction with poly(A)"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MUTAGEN 29
FT /note="D->A: Greatly reduced nuclease activity in vitro."
FT /evidence="ECO:0000269|PubMed:26919432"
SQ SEQUENCE 566 AA; 65493 MW; 8688937ED4C2E196 CRC64;
MVIVTDSNFL DAAGTLRKGL LYCDFVAIDF EFLGLDVSAI SLHDTVESRY QILRDNVIKY
RPCQLGLTLF KQKSNRAYKA DTYSVPLFQR FGDNDTSISL PSMRFLVKNK FNLNQVFMDG
VEFCTRKEFK KFERALLAGT AASYLSREVK SQIELLKVMV HEKCYQSTSY HITHRTDEPM
QKIPLKMKPN SSVSLRMPRN LSSVEKYMII YELTKAFPQF LFTCDEKQQN LHVKNISDDY
LKEKDNLERA RARCSESVKG VSAILQVVHM TGKLVVGHNS LLDAMYMYHY FFSHLPANYQ
MFKDKFNALF PRIMDTKLLA QALRFELPGV GDSLENLGDY FGSDKSDKTV PPELRGFIEP
WMNPLEDESE NVYHNAGFDS YVTGEVFLKL AHIYINRRNN FKNEILDFDR IYQYLEAPIL
NRLPFQLMDV GCCYLTGDDS KGFRPDVITI VRRDRVAIEE DEFRYLEKAL GTLMATYQFD
IEWSKNKKEL FLATNSPGSY AFLCEKFSND SSLAPLDELD SGKKWTFEQR QTAWRSFKNR
GVGIGINAKR IRAQNQATKI QRAMEI
