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Protein

DIS3-like exonuclease 2

Gene

Dis3l2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of both mRNAs and miRNAs that have been polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. Mediates degradation of uridylated pre-let-7 miRNAs, contributing to the maintenance of embryonic stem (ES) cells. Essential for correct mitosis, and negatively regulates cell proliferation.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation1 Publication, Mn2+UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi381Magnesium1 Publication1
Sitei389Important for catalytic activity1 Publication1
Metal bindingi390Magnesium1 Publication1

GO - Molecular functioni

  • 3'-5'-exoribonuclease activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • poly(U) RNA binding Source: UniProtKB
  • ribonuclease activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DIS3-like exonuclease 2UniRule annotation (EC:3.1.13.-UniRule annotation)
Gene namesi
Name:Dis3l2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2442555. Dis3l2.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication
  • CytoplasmP-body UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi74R → A: Loss of enzyme activity and polyuridylated RNA-binding; when associated with A-612. 1 Publication1
Mutagenesisi389D → N: Loss of exoribonuclease activity. 1 Publication1
Mutagenesisi548 – 553RLDQLK → AAAAAA: 40% decreased enzyme activity. 1 Publication6
Mutagenesisi612Q → A: Loss of enzyme activity and polyuridylated RNA-binding; when associated with A-74. 1 Publication1
Mutagenesisi777N → A: 40% increased enzyme activity. 1 Publication1
Mutagenesisi778Q → A: Impaired enzyme activity and polyuridylated RNA-binding. 1 Publication1
Mutagenesisi796N → A: Does not affect enzyme activity. 1 Publication1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003148181 – 870DIS3-like exonuclease 2Add BLAST870

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31PhosphoserineBy similarity1
Modified residuei172PhosphoserineBy similarity1
Modified residuei250N6-acetyllysineBy similarity1
Modified residuei864PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CI75.
PaxDbiQ8CI75.
PeptideAtlasiQ8CI75.
PRIDEiQ8CI75.

PTM databases

iPTMnetiQ8CI75.
PhosphoSitePlusiQ8CI75.

Expressioni

Gene expression databases

BgeeiENSMUSG00000053333.
ExpressionAtlasiQ8CI75. baseline and differential.
GenevisibleiQ8CI75. MM.

Interactioni

Protein-protein interaction databases

DIPiDIP-60224N.
STRINGi10090.ENSMUSP00000132673.

Structurei

Secondary structure

1870
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi56 – 65Combined sources10
Beta strandi66 – 72Combined sources7
Beta strandi82 – 85Combined sources4
Beta strandi94 – 97Combined sources4
Turni98 – 104Combined sources7
Beta strandi110 – 115Combined sources6
Beta strandi231 – 238Combined sources8
Beta strandi243 – 250Combined sources8
Beta strandi262 – 270Combined sources9
Beta strandi276 – 279Combined sources4
Helixi280 – 282Combined sources3
Helixi285 – 289Combined sources5
Helixi291 – 294Combined sources4
Beta strandi297 – 305Combined sources9
Beta strandi311 – 323Combined sources13
Helixi327 – 337Combined sources11
Helixi347 – 350Combined sources4
Beta strandi356 – 358Combined sources3
Helixi363 – 368Combined sources6
Beta strandi369 – 371Combined sources3
Beta strandi378 – 381Combined sources4
Beta strandi390 – 396Combined sources7
Beta strandi402 – 409Combined sources8
Helixi411 – 414Combined sources4
Helixi420 – 428Combined sources9
Helixi444 – 447Combined sources4
Turni448 – 450Combined sources3
Beta strandi457 – 468Combined sources12
Beta strandi474 – 485Combined sources12
Beta strandi488 – 491Combined sources4
Helixi492 – 500Combined sources9
Helixi520 – 543Combined sources24
Beta strandi554 – 558Combined sources5
Turni560 – 562Combined sources3
Beta strandi565 – 570Combined sources6
Helixi575 – 598Combined sources24
Beta strandi604 – 608Combined sources5
Helixi613 – 624Combined sources12
Helixi625 – 627Combined sources3
Helixi635 – 641Combined sources7
Helixi650 – 662Combined sources13
Beta strandi671 – 674Combined sources4
Helixi675 – 677Combined sources3
Helixi681 – 684Combined sources4
Turni687 – 690Combined sources4
Beta strandi701 – 703Combined sources3
Helixi704 – 716Combined sources13
Helixi727 – 762Combined sources36
Beta strandi766 – 775Combined sources10
Beta strandi777 – 784Combined sources8
Turni785 – 787Combined sources3
Beta strandi790 – 794Combined sources5
Beta strandi800 – 806Combined sources7
Beta strandi809 – 811Combined sources3
Beta strandi813 – 818Combined sources6
Beta strandi821 – 825Combined sources5
Beta strandi829 – 833Combined sources5
Beta strandi837 – 844Combined sources8
Beta strandi851 – 854Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PMWX-ray2.95A/B37-856[»]
ProteinModelPortaliQ8CI75.
SMRiQ8CI75.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Specifically recognizes and binds polyuridylated RNAs via 3 RNA-binding regions (named U-zone 1, U-zone 2 and U-zone 3) that form an open funnel on one face of the catalytic domain, allowing RNA to navigate a path to the active site.1 Publication

Sequence similaritiesi

Belongs to the RNR ribonuclease family. DIS3L2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2102. Eukaryota.
COG0557. LUCA.
GeneTreeiENSGT00530000063106.
HOGENOMiHOG000017705.
HOVERGENiHBG107810.
InParanoidiQ8CI75.
KOiK18758.
OMAiIDDCDGK.
OrthoDBiEOG091G06EJ.
PhylomeDBiQ8CI75.
TreeFamiTF315191.

Family and domain databases

HAMAPiMF_03045. DIS3L2. 1 hit.
InterProiIPR028591. DIS3L2.
IPR012340. NA-bd_OB-fold.
IPR022966. RNase_II/R_CS.
IPR033771. Rrp44_CSD1.
[Graphical view]
PfamiPF17216. Rrp44_CSD1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 3 hits.
PROSITEiPS01175. RIBONUCLEASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CI75-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNHPDYKLNL RSPGTPRGVS SVVGPSAVGA SPGDKKSKNK SMRGKKKSIF
60 70 80 90 100
ETYMSKEDVS EGLKRGTLIQ GVLRINPKKF HEAFIPSPDG DRDIFIDGVV
110 120 130 140 150
ARNRALNGDL VVVKLLPEDQ WKAVKPESND KEIEATYEAD IPEEGCGHHP
160 170 180 190 200
LQQSRKGWSG PDVIIEAQFD DSDSEDRHGN TSGLVDGVKK LSISTPDRGK
210 220 230 240 250
EDSSTPVMKD ENTPIPQDTR GLSEKSLQKS AKVVYILEKK HSRAATGILK
260 270 280 290 300
LLADKNSDLF KKYALFSPSD HRVPRIYVPL KDCPQDFMTR PKDFANTLFI
310 320 330 340 350
CRIIDWKEDC NFALGQLAKS LGQAGEIEPE TEGILTEYGV DFSDFSSEVL
360 370 380 390 400
ECLPQSLPWT IPPDEVGKRR DLRKDCIFTI DPSTARDLDD ALACRRLTDG
410 420 430 440 450
TFEVGVHIAD VSYFVPEGSS LDKVAAERAT SVYLVQKVVP MLPRLLCEEL
460 470 480 490 500
CSLNPMTDKL TFSVIWKLTP EGKILEEWFG RTIIRSCTKL SYDHAQSMIE
510 520 530 540 550
NPTEKIPEEE LPPISPEHSV EEVHQAVLNL HSIAKQLRRQ RFVDGALRLD
560 570 580 590 600
QLKLAFTLDH ETGLPQGCHI YEYRDSNKLV EEFMLLANMA VAHKIFRTFP
610 620 630 640 650
EQALLRRHPP PQTKMLSDLV EFCDQMGLPM DVSSAGALNK SLTKTFGDDK
660 670 680 690 700
YSLARKEVLT NMYSRPMQMA LYFCSGMLQD QEQFRHYALN VPLYTHFTSP
710 720 730 740 750
IRRFADVIVH RLLAAALGYS EQPDVEPDTL QKQADHCNDR RMASKRVQEL
760 770 780 790 800
SIGLFFAVLV KESGPLESEA MVMGVLNQAF DVLVLRFGVQ KRIYCNALAL
810 820 830 840 850
RSYSFQKVGK KPELTLVWEP DDLEEEPTQQ VITIFSLVDV VLQAEATALK
860 870
YSAILKRPGL EKASDEEPED
Length:870
Mass (Da):97,775
Last modified:March 1, 2003 - v1
Checksum:iE54474450DCD363F
GO
Isoform 2 (identifier: Q8CI75-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-122: K → KPRITLSLPGVLGLQ

Note: No experimental confirmation available.
Show »
Length:884
Mass (Da):99,220
Checksum:iFDD0AEB9C4F05712
GO

Sequence cautioni

The sequence BAC27292 differs from that shown. Reason: Frameshift at position 53.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_030379122K → KPRITLSLPGVLGLQ in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031180 mRNA. Translation: BAC27292.1. Frameshift.
BC036177 mRNA. Translation: AAH36177.1.
CCDSiCCDS15124.1. [Q8CI75-1]
CCDS48304.1. [Q8CI75-2]
RefSeqiNP_001165628.1. NM_001172157.1. [Q8CI75-2]
NP_705758.1. NM_153530.2. [Q8CI75-1]
UniGeneiMm.389152.

Genome annotation databases

EnsembliENSMUST00000065694; ENSMUSP00000070506; ENSMUSG00000053333. [Q8CI75-1]
ENSMUST00000168237; ENSMUSP00000132673; ENSMUSG00000053333. [Q8CI75-2]
GeneIDi208718.
KEGGimmu:208718.
UCSCiuc007bvu.2. mouse. [Q8CI75-1]
uc007bvw.2. mouse. [Q8CI75-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031180 mRNA. Translation: BAC27292.1. Frameshift.
BC036177 mRNA. Translation: AAH36177.1.
CCDSiCCDS15124.1. [Q8CI75-1]
CCDS48304.1. [Q8CI75-2]
RefSeqiNP_001165628.1. NM_001172157.1. [Q8CI75-2]
NP_705758.1. NM_153530.2. [Q8CI75-1]
UniGeneiMm.389152.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PMWX-ray2.95A/B37-856[»]
ProteinModelPortaliQ8CI75.
SMRiQ8CI75.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60224N.
STRINGi10090.ENSMUSP00000132673.

PTM databases

iPTMnetiQ8CI75.
PhosphoSitePlusiQ8CI75.

Proteomic databases

EPDiQ8CI75.
PaxDbiQ8CI75.
PeptideAtlasiQ8CI75.
PRIDEiQ8CI75.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065694; ENSMUSP00000070506; ENSMUSG00000053333. [Q8CI75-1]
ENSMUST00000168237; ENSMUSP00000132673; ENSMUSG00000053333. [Q8CI75-2]
GeneIDi208718.
KEGGimmu:208718.
UCSCiuc007bvu.2. mouse. [Q8CI75-1]
uc007bvw.2. mouse. [Q8CI75-2]

Organism-specific databases

CTDi129563.
MGIiMGI:2442555. Dis3l2.

Phylogenomic databases

eggNOGiKOG2102. Eukaryota.
COG0557. LUCA.
GeneTreeiENSGT00530000063106.
HOGENOMiHOG000017705.
HOVERGENiHBG107810.
InParanoidiQ8CI75.
KOiK18758.
OMAiIDDCDGK.
OrthoDBiEOG091G06EJ.
PhylomeDBiQ8CI75.
TreeFamiTF315191.

Miscellaneous databases

PROiQ8CI75.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000053333.
ExpressionAtlasiQ8CI75. baseline and differential.
GenevisibleiQ8CI75. MM.

Family and domain databases

HAMAPiMF_03045. DIS3L2. 1 hit.
InterProiIPR028591. DIS3L2.
IPR012340. NA-bd_OB-fold.
IPR022966. RNase_II/R_CS.
IPR033771. Rrp44_CSD1.
[Graphical view]
PfamiPF17216. Rrp44_CSD1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 3 hits.
PROSITEiPS01175. RIBONUCLEASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDI3L2_MOUSE
AccessioniPrimary (citable) accession number: Q8CI75
Secondary accession number(s): Q8BMG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2003
Last modified: November 30, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.