ID   DI3L1_BOVIN             Reviewed;        1053 AA.
AC   A0JN80;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=DIS3-like exonuclease 1;
DE            EC=3.1.13.-;
GN   Name=DIS3L;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI26556.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC126555; AAI26556.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001071624.1; NM_001078156.1.
DR   AlphaFoldDB; A0JN80; -.
DR   SMR; A0JN80; -.
DR   STRING; 9913.ENSBTAP00000000481; -.
DR   PaxDb; A0JN80; -.
DR   PRIDE; A0JN80; -.
DR   GeneID; 777771; -.
DR   KEGG; bta:777771; -.
DR   CTD; 115752; -.
DR   eggNOG; KOG2102; Eukaryota.
DR   InParanoid; A0JN80; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR   GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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; IBA:GO_Central.
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..1053
FT                   /note="DIS3-like exonuclease 1"
FT                   /id="PRO_0000314809"
FT   REGION          307..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         989
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TF46"
SQ   SEQUENCE   1053 AA;  120594 MW;  67CA0ADF2886E052 CRC64;
     MLQKREKVLL LRTFHGRTLR IVREHYLRPS VPCNSPLCPQ PATCHNDGKL LSSDVTHYMV
     PDWKVVQDYL EILEFPELKG IVFMQTACQA VQHQRGRRQY NKLRNLLKDA RHDCVLFANE
     FQQSCYLPRE RGESMEKWQS RSIYNAAAWY YHHCQDRMPI VMVTEDEEAI QQYGSETGGV
     FVISFKNYLD NFWPDLKAAH ELCESILQSR RERENESQES HGKEYPEHVP LEVLEAGIKS
     GRYIQGTLNV NKHRAQIEAF VRLQGASSKD SDLVSDVLIH GMKARNRSIH GDVVVVELLP
     KSEWKGRTTA LGENDGDDKA LGESPSEPMP TGRVVGILQK NWRDYVVTFP SIEEVQSQGK
     NAQKILVTPW DYRIPKIRIS TQQAEALQDF RVVVRIDSWE STSMYPNGHF VRVLGRIGDL
     EGEIATILVE NSISVVPFSE AQMCEMPVNT PENPWKVSSQ EEREREDLRK THLVFSIDPS
     GCEDVDDTLS VRALDNGNLE LGVHIADVTH FVAPHSYIDI EARTRATTYY LADRRYDMLP
     AILSADVCSL LGGVDRYAVS VMWELDKTSY EIKKVWYGRT IIRSAYKLFY EAAQDLLDGN
     FSVVKDIPEF KDLDEKSRQA KLEELVWAIR KLTDIARHIR AKRDSCGALE LEGVEVRIQL
     DEKKNIHDLI PKQPLEVHET VAECMILANH WVAKKIWESF PHQALLRRHP PPHQEFFSEL
     RECAKAKGFF IDTRSNKALA DSLDNANDPN DPIVNKLLRS MATQAMSNAL YFSTGSCAEE
     EFHHYGLALD KYTHFTSPIR RYSDIIVHRL LMAAISKDKK MEIQENLFSN KDLEELCRHI
     NNRNRAAQHS QKQSTELFQC MYFKDKDPET EERCISDGVI YSIRTNGVLV FIPRFGIKGA
     AYLRNKDGLV VSCGPDGHSE WKPGSLQRFQ NKITCTTTGG ESVTFHLFDH VTVRISVQTS
     RCHSDTIRLE IISNKPHMTP DTELLQQCSL LLKSDLVKEV TRSVEEAQLA QEVAVNITED
     YQKYCQTKGR SLYTLLEEIR DLALLDVSNS YGI