ID H0V4X2_CAVPO Unreviewed; 877 AA.
AC H0V4X2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=DIS3-like exonuclease 2 {ECO:0000256|HAMAP-Rule:MF_03045};
DE EC=3.1.13.- {ECO:0000256|HAMAP-Rule:MF_03045};
GN Name=DIS3L2 {ECO:0000256|HAMAP-Rule:MF_03045,
GN ECO:0000313|Ensembl:ENSCPOP00000004679.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000004679.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000004679.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000004679.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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, such as ZCCHC11/TUT4.
CC Mediates degradation of cytoplasmic mRNAs that have been deadenylated
CC and subsequently uridylated at their 3'. Mediates degradation of
CC uridylated pre-let-7 miRNAs, contributing to the maintenance of
CC embryonic stem (ES) cells. Essential for correct mitosis, and
CC negatively regulates cell proliferation. {ECO:0000256|HAMAP-
CC Rule:MF_03045}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03045};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03045}.
CC Cytoplasm, P-body {ECO:0000256|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:0000256|HAMAP-Rule:MF_03045}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03045}.
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DR EMBL; AAKN02019321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02019322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02019323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02019324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013013049.1; XM_013157595.1.
DR AlphaFoldDB; H0V4X2; -.
DR STRING; 10141.ENSCPOP00000004679; -.
DR Ensembl; ENSCPOT00000005260.3; ENSCPOP00000004679.3; ENSCPOG00000005205.4.
DR GeneID; 100725226; -.
DR CTD; 129563; -.
DR VEuPathDB; HostDB:ENSCPOG00000005205; -.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_5_2_1; -.
DR InParanoid; H0V4X2; -.
DR OMA; EVAEHCN; -.
DR OrthoDB; 945235at2759; -.
DR TreeFam; TF315191; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000005205; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0008266; F:poly(U) RNA binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010587; P:miRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR Gene3D; 2.40.50.690; -; 1.
DR Gene3D; 2.40.50.700; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
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; Nucleic acid-binding proteins; 2.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_03045};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_03045};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03045};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_03045};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03045};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03045};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_03045};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03045}; Mitosis {ECO:0000256|HAMAP-Rule:MF_03045};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03045};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03045}.
FT DOMAIN 371..721
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 13..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT SITE 391
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
SQ SEQUENCE 877 AA; 98068 MW; BFAD1D8DFB3E62D3 CRC64;
MSHSEYKLNF RALGAPKGGG VSPMVGPHGA GASPSDKKSK NKSMRGKKKS IFETYMSKED
VSKGLKRGTL IQGVLRINPK KFHEAFIPSP DGDRDIFIDG VVARNRALNG DLVVVKLLPE
EQWKVIKPES NDKVAEAAYE SELPEELCGH HLPLQSLRGY NDSPDVIIEA QYDDSDSEDG
HGGTQNVLVD GVKKLSVCSH DKGKSDTQVT KDESSPMSPD ARGPSEKSPQ KSAKVVYILE
KKHSRAATGV LKLLAEKNSD LFRKYALFSP SDHRVPRIYV PLKDCPQDFM TRPKDYASTL
FICHIVDWKE DCNFALGKLA KSLGQAGEIE PETEGILTEY GVDFSDFSSE VLECLPRSLP
WTIPPEEVSK RRDLRKDCVF TIDPPTARDL DDALSCRPLA DGTFQVGVHI ADVSYFVPQG
SQLDKVAAER ATSVYLVQKV VPMLPRLLCE ELCSLNPMTD KLTFSVIWTL TSEGKILDEW
FGRTIIRSCT KLSYEHAQSM IERPAEKIPE RELPPISPEH SPEELHQAVL NLHRIAKQLR
RQRFANGALR LDQLKLAFTL DHETGLPQGC HIYEYHDSNK LVEEFMLLAN MAVAHKIHGA
FPEQALLRRH PPPQTKMLGD LVEFCDQMGL AVDVSSAGAL HKSLTKIFGD DKYSLARKEV
LTNMFSRPMQ MALYFCSGVL RDQAQFQHYA LNVPLYTHFT SPIRRFADVL VHRLLAAALG
CGQQLEVEPD ALQKQADHCN DRRMASKRVQ ELSTALFFGI LVKESGPLES EAMVMGVLNQ
AFDVLVLRFG VQKRVYCNAL ALRSYHFEKV GRKPELTLLW EPEDPEQEPV RQVITVFSLV
EVTLQAEAAA LKYRAILKRP SPEGCPSLEG QEPEPEP
//
