USB1_SCHPO
ID USB1_SCHPO Reviewed; 265 AA.
AC O13915;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=U6 snRNA phosphodiesterase 1 {ECO:0000305};
DE AltName: Full=3'-5' RNA exonuclease USB1 {ECO:0000305|PubMed:26213367};
DE EC=4.6.1.- {ECO:0000269|PubMed:26213367};
DE AltName: Full=Mutated in Poikiloderma with Neutropenia protein 1 {ECO:0000303|PubMed:23022480};
GN Name=usb1 {ECO:0000255|HAMAP-Rule:MF_03040};
GN Synonyms=mnp1 {ECO:0000303|PubMed:23022480}; ORFNames=SPAC23C11.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, MUTAGENESIS OF HIS-109 AND HIS-199, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23022480; DOI=10.1016/j.celrep.2012.08.031;
RA Shchepachev V., Wischnewski H., Missiaglia E., Soneson C., Azzalin C.M.;
RT "Mpn1, mutated in poikiloderma with neutropenia protein 1, is a conserved
RT 3'-to-5' RNA exonuclease processing U6 small nuclear RNA.";
RL Cell Rep. 2:855-865(2012).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26213367; DOI=10.1016/j.febslet.2015.06.046;
RA Shchepachev V., Wischnewski H., Soneson C., Arnold A.W., Azzalin C.M.;
RT "Human Mpn1 promotes post-transcriptional processing and stability of
RT U6atac.";
RL FEBS Lett. 589:2417-2423(2015).
CC -!- FUNCTION: 3'-5' RNA exonuclease that trims the 3' end of oligo(U)
CC tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the
CC formation of a U6 snRNA 3' end-terminated with a 2',3'-cyclic
CC phosphate.d (PubMed:26213367). Participates in the U6 snRNA 3' end
CC processing that prevents U6 snRNA degradation (PubMed:26213367,
CC PubMed:23022480). {ECO:0000269|PubMed:23022480,
CC ECO:0000269|PubMed:26213367}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end uridylyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-
CC uridine-RNA + uridine; Xref=Rhea:RHEA:46052, Rhea:RHEA-COMP:17384,
CC Rhea:RHEA-COMP:17385, ChEBI:CHEBI:16704, ChEBI:CHEBI:85643,
CC ChEBI:CHEBI:85644; Evidence={ECO:0000269|PubMed:26213367};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46053;
CC Evidence={ECO:0000305|PubMed:26213367};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03040,
CC ECO:0000269|PubMed:23022480}.
CC -!- DISRUPTION PHENOTYPE: Deletion of mpn1 decreases cell population growth
CC at low temperature and leads to a generalized pre-mRNA splicing defect,
CC decrease of mature U6 snRNA levels, abnormal U6 snRNA 3'-end
CC processing, decrease levels of U4/U6 di-snRNPs.
CC {ECO:0000269|PubMed:23022480}.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. USB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03040}.
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DR EMBL; CU329670; CAB11163.2; -; Genomic_DNA.
DR PIR; T38248; T38248.
DR RefSeq; NP_593641.2; NM_001019072.1.
DR AlphaFoldDB; O13915; -.
DR SMR; O13915; -.
DR BioGRID; 278539; 3.
DR STRING; 4896.SPAC23C11.10.1; -.
DR PaxDb; O13915; -.
DR EnsemblFungi; SPAC23C11.10.1; SPAC23C11.10.1:pep; SPAC23C11.10.
DR GeneID; 2542061; -.
DR KEGG; spo:SPAC23C11.10; -.
DR PomBase; SPAC23C11.10; -.
DR VEuPathDB; FungiDB:SPAC23C11.10; -.
DR eggNOG; KOG3102; Eukaryota.
DR HOGENOM; CLU_1050353_0_0_1; -.
DR InParanoid; O13915; -.
DR OMA; WAVQIYL; -.
DR PhylomeDB; O13915; -.
DR PRO; PR:O13915; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:1990838; F:poly(U)-specific exoribonuclease activity, producing 3' uridine cyclic phosphate ends; IGI:PomBase.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; IMP:PomBase.
DR HAMAP; MF_03040; USB1; 1.
DR InterPro; IPR027521; Usb1.
DR PANTHER; PTHR13522; PTHR13522; 1.
DR Pfam; PF09749; HVSL; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lyase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..265
FT /note="U6 snRNA phosphodiesterase 1"
FT /id="PRO_0000116673"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT BINDING 109..111
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 195..201
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 197..201
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT MUTAGEN 109
FT /note="H->A: Does not affect expression; when associated
FT with A-199. Does not affect interaction with U6 RNA; when
FT associated with A-199. Does not restore U6 processing when
FT overexpressed in usb1 knockout cell; when associated with
FT A-199. Impairs pre-mRNA splicing when overexpressed in usb1
FT knockout cell; when associated with A-199. Impairs cell
FT growth when overexpressed in usb1 knockout cell; when
FT associated with A-199."
FT /evidence="ECO:0000269|PubMed:23022480"
FT MUTAGEN 199
FT /note="H->A: Does not affect expression; when associated
FT with A-109. Does not affect interaction with U6 RNA; when
FT associated with A-109. Does not restore U6 processing when
FT overexpressed in usb1 knockout cell; when associated with
FT A-199. Impairs pre-mRNA splicing when overexpressed in usb1
FT knockout cell; when associated with A-199. Impairs cell
FT growth when overexpressed in usb1 knockout cell; when
FT associated with A-199."
FT /evidence="ECO:0000269|PubMed:23022480"
SQ SEQUENCE 265 AA; 31600 MW; AFEDB135995A3FFA CRC64;
MSLVCYESSS SGEDDDETIS DNPRMLKVPK LQESFHELYK KKPKTFDSPE FHEGRIRGQK
HIEGLWFVQT YLEVDLSKKV KKGIREFLNS QSRFQSLLCS EHNVPRRLHL SISENYRINY
STKNQLVHKW EQYTNNLNYR TLKFRLGKMC LLFNDEKTRM FLAFECKFSD ENYKDLISHA
SDCMKEFTNR NLREDFLLHI SFASSLTNED EYQNWVSQDR ESHFFKTMNE IINTKIQKDQ
FSESFIVDSL KLSIGHLIFT FPFCK
