DI3L2_XENTR
ID DI3L2_XENTR Reviewed; 834 AA.
AC Q0V9R3; F6YSH4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=DIS3-like exonuclease 2 {ECO:0000255|HAMAP-Rule:MF_03045};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_03045};
GN Name=dis3l2 {ECO:0000255|HAMAP-Rule:MF_03045};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs
CC polyuridylated at their 3' end and mediates their degradation.
CC Component of an exosome-independent RNA degradation pathway that
CC mediates degradation of both mRNAs and miRNAs that have been
CC polyuridylated by a terminal uridylyltransferase. Essential for correct
CC mitosis, and negatively regulates cell proliferation.
CC {ECO:0000255|HAMAP-Rule:MF_03045}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03045}.
CC Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03045}.
CC -!- DOMAIN: Specifically recognizes and binds polyuridylated RNAs via 3
CC RNA-binding regions (named U-zone 1, U-zone 2 and U-zone 3) that form
CC an open funnel on one face of the catalytic domain, allowing RNA to
CC navigate a path to the active site. {ECO:0000255|HAMAP-Rule:MF_03045}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03045}.
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DR EMBL; AAMC01069446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01069469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC121425; AAI21426.1; -; mRNA.
DR RefSeq; NP_001072804.1; NM_001079336.1.
DR AlphaFoldDB; Q0V9R3; -.
DR SMR; Q0V9R3; -.
DR STRING; 8364.ENSXETP00000062939; -.
DR PaxDb; Q0V9R3; -.
DR PRIDE; Q0V9R3; -.
DR DNASU; 780265; -.
DR GeneID; 780265; -.
DR KEGG; xtr:780265; -.
DR CTD; 129563; -.
DR Xenbase; XB-GENE-5958094; dis3l2.
DR eggNOG; KOG2102; Eukaryota.
DR InParanoid; Q0V9R3; -.
DR OrthoDB; 1104619at2759; -.
DR TreeFam; TF315191; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IEA:InterPro.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_03045; DIS3L2; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR028591; DIS3L2.
DR InterPro; IPR041093; Dis3l2_C.
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 Pfam; PF17877; Dis3l2_C_term; 1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Exonuclease; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Mitosis; Nuclease; Reference proteome;
KW RNA-binding; Tumor suppressor.
FT CHAIN 1..834
FT /note="DIS3-like exonuclease 2"
FT /id="PRO_0000314819"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT SITE 362
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT CONFLICT 606
FT /note="S -> T (in Ref. 2; AAI21426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 94135 MW; 185106D191678C8E CRC64;
MHNSEFLSPV QSGTQRGTNR SILNNKKSGK GKKKSVFEAY MTKEEVSAGL KRGELIQGPL
RINPKKFHEA YLPSPDGVRD LFIDGVVPRN RALNGDVVVV KLLPQEQWKV LKNDVCEDDD
TPGHSTGNKQ HALSPHLMKS SAKNPDLIIE AKVDSSAEDG HESALIGCLQ KEIKDQDKLG
AIEEKTSKQG DPKTFSDDCF QKTAKVVYIL EKKHSRAATG FIKPLSDKSS DLARKRALFS
PVDHRLPRIY VPLGDCPHDF AIHPETYANT LFICSITAWR DDSNFAEGKL MKSLGQAGEI
EPETEGILVE YGVDFSDFPD KVLQCLPQDL PWTIPQEEFQ KRKDLRNECI FTIDPATARD
LDDALSCKPL PDGNFEVGVH IADVSYFVAE GSALDIMASE RATSVYLVQK VIPMLPRLLC
EELCSLNPMT DRLTFSVIWK ITPQGEILDE WFGRSVICSC VKLSYDHAQN MINHPDKKIE
QHELPPVSPQ HTINEIHQAV LNLHLIAQNL RKQRFDDGAL RLDQLKLTFT LDKESGLPQG
CYIYQYRDSN KLVEEFMLLA NMAVAHHIYR RFPEEALLRR HPPPQTKMLN DLIEFCDQMG
LQLDFSSSGT LHKSLNDQFE TDEYSAARKE VLTNMCSRPM QMAVYFCTGA LKDETLFHHY
ALNVPLYTHF TSPIRRFADV IVHRLLAASL GCGPPLKMPK EVIQKQADHC NDRKTASKRV
QELSAELFFS VFVKECGPLE SEAMVMGVLN EAFDVIVLRF GVQKRIYCNS LPLVNSHFQQ
VGKRPELTLL WEPEKKGEEP VRQVISIFTL VEVVLKSDNV PLKYTAVLKS PEAQ
