ID EXOSX_MOUSE Reviewed; 887 AA.
AC P56960; B1ARY9; Q9QYS8; Q9R0B1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Exosome complex component 10;
DE EC=3.1.13.- {ECO:0000250|UniProtKB:Q01780};
DE AltName: Full=Autoantigen PM/Scl 2 homolog;
DE AltName: Full=Polymyositis/scleroderma autoantigen 2 homolog;
GN Name=Exosc10; Synonyms=Pmscl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and BALB/cJ;
RX PubMed=10708524; DOI=10.1006/geno.2000.6118;
RA Bliskovski V., Liddell R., Ramsay E.S., Miller M.J., Mock B.A.;
RT "Structure and localization of mouse Pmscl1 and Pmscl2 genes.";
RL Genomics 64:106-110(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PROTEIN SEQUENCE OF 395-400, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=26857222; DOI=10.1261/rna.054411.115;
RA Knight J.R., Bastide A., Peretti D., Roobol A., Roobol J., Mallucci G.R.,
RA Smales C.M., Willis A.E.;
RT "Cooling-induced SUMOylation of EXOSC10 down-regulates ribosome
RT biogenesis.";
RL RNA 22:623-635(2016).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29118343; DOI=10.1038/s41598-017-14643-y;
RA Jamin S.P., Petit F.G., Kervarrec C., Smagulova F., Illner D.,
RA Scherthan H., Primig M.;
RT "EXOSC10/Rrp6 is post-translationally regulated in male germ cells and
RT controls the onset of spermatogenesis.";
RL Sci. Rep. 7:15065-15065(2017).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-313 AND GLU-315.
RX PubMed=32313933; DOI=10.1093/nar/gkaa249;
RA Wu D., Dean J.;
RT "EXOSC10 sculpts the transcriptome during the growth-to-maturation
RT transition in mouse oocytes.";
RL Nucleic Acids Res. 48:5349-5365(2020).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=34965385; DOI=10.1016/j.ydbio.2021.12.010;
RA Petit F.G., Jamin S.P., Kernanec P.Y., Becker E., Halet G., Primig M.;
RT "EXOSC10/Rrp6 is essential for the eight-cell embryo/morula transition.";
RL Dev. Biol. 483:58-65(2022).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=36923944; DOI=10.7150/ijbs.72889;
RA Demini L., Kervarrec C., Guillot L., Com E., Lavigne R., Kernanec P.Y.,
RA Primig M., Pineau C., Petit F.G., Jamin S.P.;
RT "Inactivation of Exosc10 in the oocyte impairs oocyte development and
RT maturation, leading to a depletion of the ovarian reserve in mice.";
RL Int. J. Biol. Sci. 19:1080-1093(2023).
CC -!- FUNCTION: Catalytic component of the RNA exosome complex which has
CC 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing and degradation events. In the nucleus, the RNA
CC exosome complex is involved in proper maturation of stable RNA species
CC such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC by-products and non-coding 'pervasive' transcripts, such as antisense
CC RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs
CC with processing defects, thereby limiting or excluding their export to
CC the cytoplasm. Part of the small subunit (SSU) processome, first
CC precursor of the small eukaryotic ribosomal subunit. During the
CC assembly of the SSU processome in the nucleolus, many ribosome
CC biogenesis factors, an RNA chaperone and ribosomal proteins associate
CC with the nascent pre-rRNA and work in concert to generate RNA folding,
CC modifications, rearrangements and cleavage as well as targeted
CC degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome
CC may be involved in Ig class switch recombination (CSR) and/or Ig
CC variable region somatic hypermutation (SHM) by targeting AICDA
CC deamination activity to transcribed dsDNA substrates. In the cytoplasm,
CC the RNA exosome complex is involved in general mRNA turnover and
CC specifically degrades inherently unstable mRNAs containing AU-rich
CC elements (AREs) within their 3' untranslated regions, and in RNA
CC surveillance pathways, preventing translation of aberrant mRNAs. It
CC seems to be involved in degradation of histone mRNA. EXOSC10 is
CC required for nucleolar localization of C1D and probably mediates the
CC association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in
CC the maturation of 5.8S rRNA (By similarity). Plays a role in the
CC recruitment of replication protein A complex (RPA) and RAD51 to DNA
CC double-strand breaks caused by irradiation, contributing to DNA repair
CC by homologous recombination (By similarity). Regulates levels of
CC damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA
CC double-strand breaks and limit DNA end resection after damage (By
CC similarity). Plays a role in oocyte development, maturation and
CC survival (PubMed:36923944, PubMed:32313933). Required for normal testis
CC development and mitotic division of spermatogonia (PubMed:29118343).
CC Plays a role in proper embryo development (PubMed:36923944,
CC PubMed:34965385, PubMed:32313933). Required for global protein
CC translation (By similarity). Required for cell proliferation (By
CC similarity). {ECO:0000250|UniProtKB:Q01780,
CC ECO:0000269|PubMed:29118343, ECO:0000269|PubMed:32313933,
CC ECO:0000269|PubMed:34965385, ECO:0000269|PubMed:36923944}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q01780};
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. Interacts with C1D and
CC MPHOSPH6 (By similarity). Interacts with ALYREF/THOC4 (By similarity).
CC Interacts with MTREX; the interaction mediates the association of MTREX
CC with nuclear RNA exosomes (By similarity). Interacts with DHX36; this
CC interaction occurs in a RNase-insensitive manner (By similarity).
CC Interacts with NRDE2 (By similarity). Interacts (via C-terminus) with
CC USP36 (via C-terminus); the interaction is facilitated by the
CC association with RNA and promotes sumoylation of EXOSC10 (By
CC similarity). {ECO:0000250|UniProtKB:Q01780}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29118343,
CC ECO:0000269|PubMed:34965385}. Nucleus {ECO:0000269|PubMed:29118343,
CC ECO:0000269|PubMed:32313933, ECO:0000269|PubMed:34965385,
CC ECO:0000269|PubMed:36923944}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:29118343, ECO:0000269|PubMed:34965385}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:34965385}. Note=Strongly enriched in
CC the nucleolus and a small amount has been found in cytoplasm supporting
CC the existence of a nucleolar RNA exosome complex form (By similarity).
CC In oocytes, the protein is diffusely distributed in the cytoplasm, in
CC zygotes it is found in both the cytoplasm and pronuclei and from the
CC two-cell stage onward the protein accumulates in the nucleus,
CC especially at the nucleolus precursor body periphery (PubMed:34965385).
CC In metaphase blastomeres that lack structured nuclei, the protein
CC localizes diffusely in the cytoplasm (PubMed:34965385). In
CC spermatocytes, the protein accumulates in the nucleolus during
CC zygotene, late pachytene and diplotene sub-stages and in the cytoplasm
CC during metaphase I (PubMed:29118343). {ECO:0000250|UniProtKB:Q01780,
CC ECO:0000269|PubMed:29118343, ECO:0000269|PubMed:34965385}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary (at protein level)
CC (PubMed:36923944). Expressed in testis (at protein level)
CC (PubMed:29118343). Expressed in lung (at protein level)
CC (PubMed:26857222). {ECO:0000269|PubMed:26857222,
CC ECO:0000269|PubMed:29118343, ECO:0000269|PubMed:36923944}.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes and during all the stages of
CC early embryogenesis (at protein level). {ECO:0000269|PubMed:34965385}.
CC -!- INDUCTION: Down-regulated by mild hypothermia (at protein level).
CC {ECO:0000269|PubMed:26857222}.
CC -!- PTM: Sumoylated by USP36; sumoylation does not significantly affect
CC EXOSC10 nucleolar localization and association with core exosome and
CC USP36, but regulates the nucleolar RNA exosome activity in rRNA
CC processing by promoting binding of EXOSC10 to pre-rRNAs. Effects of
CC sumoylation on EXOSC10 levels vary between different studies.
CC Sumoylation of EXOSC10 is required for the modulation of EXOSC10
CC effects on cellular protein translation and cell proliferation.
CC Sumoylation is promoted by mild hypothermia.
CC {ECO:0000250|UniProtKB:Q01780}.
CC -!- DISRUPTION PHENOTYPE: Prenatal lethality (PubMed:34965385,
CC PubMed:32313933, PubMed:29118343). Developmental arrest at the two-cell
CC to eight-cell embryo/morula transition stages (PubMed:34965385,
CC PubMed:32313933). Oocyte-specific knockdown does not affect the onset
CC of puberty but results in the loss of sexual receptivity and cyclicity
CC and leads to subfertility/infertility in female mice (PubMed:36923944,
CC PubMed:32313933). Rapid depletion of oocytes in ovaries and
CC disorganization of the ovarian tissue (PubMed:36923944). Dysregulation
CC of the pathways involved in meiotic cell cycle progression, oocyte
CC maturation, ribosome biogenesis, DNA replication and repair,
CC mitochondria activity, transcriptional control, RNA metabolism,
CC endomembrane and nucleocytoplasmic transport (PubMed:36923944,
CC PubMed:32313933). Aberrant formation of the endomembrane system in the
CC oocytes (PubMed:32313933). Defects in pre-rRNA processing in the
CC oocytes (PubMed:32313933). Testis-specific knockdown leads to
CC subfertility in male mice (PubMed:29118343). Abnormal testicular
CC development and defects in spermatogenesis (PubMed:29118343).
CC {ECO:0000269|PubMed:29118343, ECO:0000269|PubMed:32313933,
CC ECO:0000269|PubMed:34965385, ECO:0000269|PubMed:36923944}.
CC -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
CC {ECO:0000305}.
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DR EMBL; AF091392; AAF01779.1; -; mRNA.
DR EMBL; AF091505; AAF01781.1; -; Genomic_DNA.
DR EMBL; AF091506; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092074; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092075; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092076; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092077; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092078; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092079; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092080; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092081; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092082; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AF092083; AAF01781.1; JOINED; Genomic_DNA.
DR EMBL; AL606969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18939.1; -.
DR RefSeq; NP_057908.2; NM_016699.2.
DR AlphaFoldDB; P56960; -.
DR SMR; P56960; -.
DR BioGRID; 206151; 3.
DR ComplexPortal; CPX-594; Nuclear exosome complex, Dis3-Exosc10 variant.
DR ComplexPortal; CPX-595; Nucleolar exosome complex, Exosc10 variant.
DR ComplexPortal; CPX-601; Cytoplasmic exosome complex, Dis3l-Exosc10 variant.
DR CORUM; P56960; -.
DR IntAct; P56960; 2.
DR MINT; P56960; -.
DR STRING; 10090.ENSMUSP00000017408; -.
DR iPTMnet; P56960; -.
DR PhosphoSitePlus; P56960; -.
DR SwissPalm; P56960; -.
DR EPD; P56960; -.
DR MaxQB; P56960; -.
DR PaxDb; 10090-ENSMUSP00000017408; -.
DR PeptideAtlas; P56960; -.
DR ProteomicsDB; 275706; -.
DR Pumba; P56960; -.
DR Antibodypedia; 13683; 228 antibodies from 30 providers.
DR DNASU; 50912; -.
DR Ensembl; ENSMUST00000017408.14; ENSMUSP00000017408.8; ENSMUSG00000017264.17.
DR GeneID; 50912; -.
DR KEGG; mmu:50912; -.
DR UCSC; uc008vut.2; mouse.
DR AGR; MGI:1355322; -.
DR CTD; 5394; -.
DR MGI; MGI:1355322; Exosc10.
DR VEuPathDB; HostDB:ENSMUSG00000017264; -.
DR eggNOG; KOG2206; Eukaryota.
DR GeneTree; ENSGT00390000015408; -.
DR HOGENOM; CLU_010129_1_1_1; -.
DR InParanoid; P56960; -.
DR OMA; NIMRPQM; -.
DR OrthoDB; 2880475at2759; -.
DR PhylomeDB; P56960; -.
DR TreeFam; TF105991; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 50912; 21 hits in 112 CRISPR screens.
DR ChiTaRS; Exosc10; mouse.
DR PRO; PR:P56960; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P56960; Protein.
DR Bgee; ENSMUSG00000017264; Expressed in undifferentiated genital tubercle and 257 other cell types or tissues.
DR ExpressionAtlas; P56960; baseline and differential.
DR Genevisible; P56960; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); NAS:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0101019; C:nucleolar exosome (RNase complex); NAS:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004532; F:RNA exonuclease activity; ISO:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0071034; P:CUT catabolic process; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; ISO:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0071028; P:nuclear mRNA surveillance; ISO:MGI.
DR GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IBA:GO_Central.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IBA:GO_Central.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; ISO:MGI.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISO:MGI.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1905746; P:positive regulation of mRNA cis splicing, via spliceosome; IMP:MGI.
DR GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; ISO:MGI.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; ISO:MGI.
DR CDD; cd06147; Rrp6p_like_exo; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR045092; Rrp6-like.
DR InterPro; IPR049559; Rrp6p-like_exo.
DR PANTHER; PTHR12124:SF47; EXOSOME COMPONENT 10; 1.
DR PANTHER; PTHR12124; POLYMYOSITIS/SCLERODERMA AUTOANTIGEN-RELATED; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF08066; PMC2NT; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00341; HRDC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Exonuclease;
KW Exosome; Hydrolase; Isopeptide bond; Magnesium; Metal-binding;
KW Nonsense-mediated mRNA decay; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..887
FT /note="Exosome complex component 10"
FT /id="PRO_0000087134"
FT DOMAIN 289..455
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 503..583
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT BINDING 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT SITE 583
FT /note="Not ubiquitinated"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 710
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 835
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 861
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT CROSSLNK 875
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01780"
FT MUTAGEN 313
FT /note="D->N: Reduces exoribonuclease activity towards
FT poly(A) RNA substrates; when associated with Q-315."
FT /evidence="ECO:0000269|PubMed:32313933"
FT MUTAGEN 315
FT /note="E->Q: Reduces exoribonuclease activity towards
FT poly(A) RNA substrates; when associated with N-313."
FT /evidence="ECO:0000269|PubMed:32313933"
FT CONFLICT 792
FT /note="I -> V (in Ref. 1; AAF01779/AAF01781)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="C -> F (in Ref. 1; AAF01779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 887 AA; 100942 MW; 173164944163620C CRC64;
MAPPSPREHQ SAPATSATKP DAEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY
DFYRSFPAFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDTNDVI
LERVGMLLDE ASGVNKHQQP VLPAGLQVPK TIVSSWNRKA GEYGKKAKSE TFRLLHAKNI
VRPQLRFREK IDNSNTPFLP KIFVKPNARK PLPLALSKER RERPQDRPED LDVPPALADF
IHQQRTQQVE QDMFAHPYQY ELDHFTPPQS VLQRPKPQLY RAVGETPCHL VSSLDELVEL
NEKLLGCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFIV DTLELRSDMY ILNESLTDPA
IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLAR HSLDHLLRLY CGVESNKQYQ
LADWRIRPLP EEMLSYARDD THYLLYIYDR MRLELWERGN HQPVQLQVVW QRSRDICLKK
FVKPIFTDES YLELYRKQKK HLNSQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI
AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSENAAGV RKSGPLPSAE
RLENDLFGPH DCSHAPPDNY QNTSTDGTLP LQKQPSLFTE GKEETSVDAG CLLATAVITL
FSEPNTEEGG KTPLTVAQKK AQNIMQSFEN PFRMFLPSLE HKAHISQAAK FDPSSKIYEI
SNRWKLASQV QVQKEPKEAT KKKVAEQTAA REEAKEEAAA GVLEQAIPVR QQAALENATK
KRERATSDLR TIEQKQEKKR LKSSKKAKDP DPPGKDFSPY DYSQSDFRAF AGDSKSKPSS
QFDPNKLAPS GKKGVGAKKC KQSVGNKSMS FAVGKSDRGF RHNWPKR
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