ID   PNDC1_PONAB             Reviewed;         520 AA.
AC   Q5R6R6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Poly(A)-specific ribonuclease PNLDC1 {ECO:0000250|UniProtKB:Q8NA58};
DE            EC=3.1.13.4 {ECO:0000250|UniProtKB:B2RXZ1, ECO:0000250|UniProtKB:Q8NA58};
DE   AltName: Full=PARN-like domain-containing protein 1 {ECO:0000250|UniProtKB:Q8NA58};
DE   AltName: Full=Poly(A)-specific ribonuclease domain-containing protein 1 {ECO:0000250|UniProtKB:Q8NA58};
GN   Name=PNLDC1 {ECO:0000250|UniProtKB:Q8NA58};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of
CC       mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic
CC       degradation of the poly(A) tail is often the first step in the decay of
CC       eukaryotic mRNAs and is also used to silence certain maternal mRNAs
CC       translationally during oocyte maturation and early embryonic
CC       development (By similarity). May act as a regulator of multipotency in
CC       embryonic stem cells (By similarity). Is a critical factor for proper
CC       spermatogenesis, involved in pre-piRNAs processing to generate mature
CC       piRNAs (By similarity). {ECO:0000250|UniProtKB:B2RXZ1,
CC       ECO:0000250|UniProtKB:Q8NA58}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC         Evidence={ECO:0000250|UniProtKB:Q8NA58};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8NA58};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8NA58}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8NA58}. Note=Localizes mainly in the
CC       endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8NA58}.
CC   -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR   EMBL; CR860419; CAH92544.1; -; mRNA.
DR   RefSeq; NP_001126488.1; NM_001133016.1.
DR   AlphaFoldDB; Q5R6R6; -.
DR   SMR; Q5R6R6; -.
DR   STRING; 9601.ENSPPYP00000019204; -.
DR   GeneID; 100173475; -.
DR   KEGG; pon:100173475; -.
DR   CTD; 154197; -.
DR   eggNOG; KOG1990; Eukaryota.
DR   InParanoid; Q5R6R6; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; ISS: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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Exonuclease; Hydrolase; Magnesium; Membrane;
KW   Metal-binding; Nonsense-mediated mRNA decay; Nuclease; Reference proteome;
KW   RNA-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..520
FT                   /note="Poly(A)-specific ribonuclease PNLDC1"
FT                   /id="PRO_0000311366"
FT   TRANSMEM        497..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O95453"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O95453"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O95453"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O95453"
SQ   SEQUENCE   520 AA;  59867 MW;  9971408E8AFCB93C CRC64;
     MFCTRGLVFF AFPAGLDIEF TGLRSNLSGP QQISLFDLPS EWYLKTRQSV QQFTICQIGL
     SVFSAIEGEA NKYTAHSCNF YLFPTTFGIL DSEFSFQASS VQFLNQYGFN YNKFLKNGIP
     YMNEEQEKKI RHDILTGNWR VRSSPDKDQI KVVIDEVTRW LDLAKEGDWM TLPGITGFQA
     FEVQLVLRQA LPNIWTVLKD EGVVVKKVSK QHRWYLQNTS CDRESCWKEN ILLSARGFSA
     FFQMLVKAQK PLVGHNMMMD LLHLHEKFFR PLPESYDQFK QNIHSLFPVL IDTKSVTKDI
     WKEMNFPRVS NLSKVYEVLN SDLNPTKNSG PEIVHASRCE KYVETKCPHE AAYDAFLCGS
     VLLKVAHLLL QKVHRIDPVP ESSFPQYLDV LAPYVNQVNL IRAGVPKINF SGPDYPGIRP
     PILILSVKRW PGVSEQQVCH KFQNLCKFDV RRLTRSQFLL LTNKFKDARN ILKEYRGHPT
     LCISLYRYWR HSPNVNCLLQ VCGIVTAWAL LAFTLGRSGP