ID   DI3L1_PONAB             Reviewed;        1054 AA.
AC   Q5R5N8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=DIS3-like exonuclease 1;
DE            EC=3.1.13.-;
GN   Name=DIS3L;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative cytoplasm-specific catalytic component of the RNA
CC       exosome complex which has 3'->5' exoribonuclease activity and
CC       participates in a multitude of cellular RNA processing and degradation
CC       events. In the cytoplasm, the RNA exosome complex is involved in
CC       general mRNA turnover and specifically degrades inherently unstable
CC       mRNAs containing AU-rich elements (AREs) within their 3' untranslated
CC       regions, and in RNA surveillance pathways, preventing translation of
CC       aberrant mRNAs. It seems to be involved in degradation of histone mRNA.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Component of the RNA exosome complex. The catalytically
CC       inactive RNA exosome core (Exo-9) complex is believed to associate with
CC       catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and
CC       nuclear-specific RNA exosome complex forms (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR   EMBL; CR860819; CAH92928.1; -; mRNA.
DR   RefSeq; NP_001126723.1; NM_001133251.1.
DR   AlphaFoldDB; Q5R5N8; -.
DR   SMR; Q5R5N8; -.
DR   STRING; 9601.ENSPPYP00000007457; -.
DR   GeneID; 100173724; -.
DR   KEGG; pon:100173724; -.
DR   CTD; 115752; -.
DR   eggNOG; KOG2102; Eukaryota.
DR   InParanoid; Q5R5N8; -.
DR   OrthoDB; 1104619at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR041505; Dis3_CSD2.
DR   InterPro; IPR031192; DIS3L.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR033771; Rrp44_CSD1.
DR   InterPro; IPR033770; RRP44_S1.
DR   PANTHER; PTHR23355:SF30; PTHR23355:SF30; 1.
DR   Pfam; PF17849; OB_Dis3; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF17216; Rrp44_CSD1; 1.
DR   Pfam; PF17215; Rrp44_S1; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; SSF50249; 3.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Exonuclease; Exosome; Hydrolase; Magnesium; Nuclease;
KW   Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..1054
FT                   /note="DIS3-like exonuclease 1"
FT                   /id="PRO_0000314812"
FT   MOD_RES         989
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TF46"
SQ   SEQUENCE   1054 AA;  120769 MW;  9D5445EA619461DB CRC64;
     MLQKREKVLL LRTFQGRTLR IVREHYLRPC VPCHSPLCPQ PAACSHDGKL LSNDVTHYVI
     PDWKVVQDYL EILEFPELKG IIFMQTACQA VQHQRGRRQY NKLRNLLKDA RHDCILFANE
     FQQCCYLPRE RGESMEKWQT RSIYNAAVWY YHHCQDRMPI VMVTEDEEAI QQYGSETEGV
     FVISFKNYLD NFWPDLKAAH ELCDSILQSR RERENESQES HGKEYPEHLP LEVLEAGIKS
     GRYIQGILNV NKHRAQIEAF VRLQGASSKD SDLVSDILIH GMKARNRSIH GDVVVVELLP
     KNEWKGRTVA LCENDCDDKA SGESPSEPMP TGRVVGILQK NWRDYVVTFP SKEEVQSQGK
     NAQKILVTPW DYRIPKIRIS TQQAETLQDF RVVVRIDSWE STSVYPNGHF VRVLGRIGDL
     EGEIATILVE NSISVIPFSE AQMCEMPVNT PENPWKVSPE EEQKRKDLRK SHLVFSIDPK
     GCEDVDDTLS VRTLNNGNLE LGVHIADVTH FVAPNSYIDI EARTRATTYY LADRRYDMLP
     SVLSADLCSL LGGVDRYAVS IMWELDKASY EIKKVWYGRT IIRSAYKLFY EAAQELLDGN
     LSVVDDIPEF KDLDEKSRQA KLEELVWAIG KLTDIARHVR AKRDGCGALE LEGVEVRVQL
     DDKKNIHDLI PKQPLEVHET VAECMILANH WVAKKIWESF PHQALLRQHP PPHQEFFSEL
     RECAKAKGFF IDTRSNKTLA DSLDNANGPH DPIVNRLLRS MATQAMSNAL YFSTGSCAEE
     EFHHYGLALD KYTHFTSPIR RYSDIVVHRL LMAAISKDKK MEIKGNLFSN KDLEELCRHI
     NNRNRAAQHS QKQSTELFQC MYFKDKDPAT EERCISDGVI YSIRANGVLV FIPRFGIKGA
     AYLKNKDGLV ISCGPDSCSE WKPGSLQRFQ NKITSTTTDG ESVTFHLFDH VTVRISIQVS
     RCHSDTTRLE IISNKPYKIP NTELIHQSSP LLKSELVKEV TKSVEEAQLA QEVKVNIIQE
     EYQEYCQTKG RSLYTLLEEI RDLALLDVSN NYGI