DI3L1_RAT
ID DI3L1_RAT Reviewed; 1054 AA.
AC Q5U2P0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DIS3-like exonuclease 1;
DE EC=3.1.13.-;
GN Name=Dis3l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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=AAH85932.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC085932; AAH85932.1; ALT_INIT; mRNA.
DR RefSeq; NP_001008381.1; NM_001008380.1.
DR RefSeq; XP_006243323.1; XM_006243261.2.
DR RefSeq; XP_006243324.1; XM_006243262.3.
DR RefSeq; XP_006243325.1; XM_006243263.3.
DR AlphaFoldDB; Q5U2P0; -.
DR SMR; Q5U2P0; -.
DR STRING; 10116.ENSRNOP00000014071; -.
DR jPOST; Q5U2P0; -.
DR PaxDb; Q5U2P0; -.
DR PRIDE; Q5U2P0; -.
DR Ensembl; ENSRNOT00000014071; ENSRNOP00000014071; ENSRNOG00000010537.
DR GeneID; 363077; -.
DR KEGG; rno:363077; -.
DR UCSC; RGD:1308959; rat.
DR CTD; 115752; -.
DR RGD; 1308959; Dis3l.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_5_0_1; -.
DR InParanoid; Q5U2P0; -.
DR OMA; WKVNPEE; -.
DR OrthoDB; 1104619at2759; -.
DR PhylomeDB; Q5U2P0; -.
DR TreeFam; TF105755; -.
DR PRO; PR:Q5U2P0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010537; Expressed in testis and 20 other tissues.
DR Genevisible; Q5U2P0; RN.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; ISO:RGD.
DR GO; GO:0006396; P:RNA processing; ISO:RGD.
DR GO; GO:0016075; P:rRNA catabolic process; ISO:RGD.
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_0000314813"
FT REGION 313..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF46"
SQ SEQUENCE 1054 AA; 120759 MW; F1294C8EAF98C396 CRC64;
MLQKREKVLL LRTFQGRTLR IVREHYLRPS VPCNSPLCPQ PATCRNDGKL LSAEVTHYVI
PDWKVVQDYL EVLEFPELKG IIFMQTACQA VQHQRGRRQY NKLRNLLKDA RHDCVLFANE
FQQHCYLPRE KGEAMEKWQT RSIYNSAVWY YHHCEDRMPI VMVTEDEEAI QQYGSETEGV
FVISFKNYLD NFWPDLKAAH ELCDSIIQSR RERESESQET HGKEYPEHLP LEVLEAGIKS
GRYIQGILNV NKHRAQIEAF VRLQGASSKD SGLVSDILIH GSKARNRSIH GDVVVVELLP
KSEWKGRTAA LCENDSEDKA SGESPSEPMP TGRVVGILQK NWRDYVVTFP SKEEVQSQGK
NAQKILVTPW DYRIPKIRIS TQQAEALQDF RVVVRIDSWE TTSVYPNGHF VRVLGRIGDL
EGEIATILVE NSINVVPFSE AQMCEMPVNT AENPWKVSPK EEQERRDLRS THLVFSIDPK
GCEDVDDALS VRTLNNGNLE LGVHIADVTH FVAPNSYIDV EARTRATTYY LADRRYDMLP
SILSADLCSL LGGVDRYAVS VMWELDKTSY EIKKVWYGRT IIRSAYKLFY EAAQELLDGN
FSIVDDIPEF KTLEEQNRQA KLEELVWAIG KLTDIARHIR AKRDRCGALE LEGVEVRVQL
DDKKNIHDLI PKQPLEVHET VAECMILANH WVAKKIWESF PHQALLRQHP PPHQEFFSEL
RECAKAKGFF IDTRSNKTLA DSLDSANDPS DPLVNKLLRS MATQAMSNAL YFSTGSCAEE
EFHHYGLALD KYTHFTSPIR RYSDIVVHRL LMAAISKDKK VEIKENLFSN KNLEELCRHI
NNRNRAAQRS QKQSTELFQC MYFKDRDPET EERCVVDGII YSIRTNGVLV FIPRFGIKGA
AYLKNKDGLV ISCGPEGSSE WKPGSLQRSQ NKIISTTAGG QSVTFHLFDH VTVRISVQPS
RCHSDMIRLE IVSNKPYMMP NTELCHQSSL LLKSELVKEV TRSVEEAQLA QEVKGKVIEE
EHQEYRQTKG RSLYTLLEEI RDLALLDVSD SYAM