USB1_RAT
ID USB1_RAT Reviewed; 267 AA.
AC Q5I0I5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=U6 snRNA phosphodiesterase 1 {ECO:0000305};
DE AltName: Full=3'-5' RNA exonuclease USB1 {ECO:0000250|UniProtKB:Q9BQ65};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:Q9BQ65};
GN Name=Usb1 {ECO:0000255|HAMAP-Rule:MF_03040, ECO:0000312|RGD:1305215};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: 3'-5' RNA exonuclease that trims the 3' end of oligo(U) and
CC oligo(A) tracts of the pre-U6 small nuclear RNA (snRNA) molecule,
CC leading to the formation of a mature U6 snRNA 3' end-terminated with a
CC 2',3'-cyclic phosphate. Participates in the U6 snRNA 3' end processing
CC that prevents U6 snRNA degradation. In addition also removes uridines
CC from the 3' end of U6atac snRNA and possibly the vault RNA VTRNA1-1.
CC {ECO:0000250|UniProtKB:Q9BQ65}.
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:0000250|UniProtKB:Q9BQ65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46053;
CC Evidence={ECO:0000250|UniProtKB:Q9BQ65};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end uridylyl-adenosine-RNA = a 3'-end 2',3'-cyclophospho-
CC uridine-RNA + adenosine; Xref=Rhea:RHEA:67896, Rhea:RHEA-COMP:17385,
CC Rhea:RHEA-COMP:17386, ChEBI:CHEBI:16335, ChEBI:CHEBI:85644,
CC ChEBI:CHEBI:176518; Evidence={ECO:0000250|UniProtKB:Q9BQ65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67897;
CC Evidence={ECO:0000250|UniProtKB:Q9BQ65};
CC -!- SUBUNIT: Interacts with PLRG1, CDC5L AND PRPF19.
CC {ECO:0000250|UniProtKB:Q9BQ65}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03040}.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. USB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03040}.
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DR EMBL; BC088280; AAH88280.1; -; mRNA.
DR RefSeq; NP_001014035.1; NM_001014013.1.
DR AlphaFoldDB; Q5I0I5; -.
DR SMR; Q5I0I5; -.
DR STRING; 10116.ENSRNOP00000017960; -.
DR PaxDb; Q5I0I5; -.
DR Ensembl; ENSRNOT00000017960; ENSRNOP00000017960; ENSRNOG00000013216.
DR GeneID; 307643; -.
DR KEGG; rno:307643; -.
DR UCSC; RGD:1305215; rat.
DR CTD; 79650; -.
DR RGD; 1305215; Usb1.
DR eggNOG; KOG3102; Eukaryota.
DR GeneTree; ENSGT00390000004596; -.
DR HOGENOM; CLU_057212_2_0_1; -.
DR InParanoid; Q5I0I5; -.
DR OMA; KTVVLQY; -.
DR OrthoDB; 1507496at2759; -.
DR PhylomeDB; Q5I0I5; -.
DR TreeFam; TF324364; -.
DR PRO; PR:Q5I0I5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000013216; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5I0I5; RN.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR GO; GO:0034472; P:snRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; ISS:UniProtKB.
DR HAMAP; MF_03040; USB1; 1.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR027521; Usb1.
DR PANTHER; PTHR13522; PTHR13522; 1.
DR Pfam; PF09749; HVSL; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lyase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..267
FT /note="U6 snRNA phosphodiesterase 1"
FT /id="PRO_0000274393"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT BINDING 122..124
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 166
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 204
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 204
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 206..212
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 208..212
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
SQ SEQUENCE 267 AA; 30475 MW; B678B7E0F6AD3B50 CRC64;
MNAAPLVGYS SSGSEDEAEA VAAGRSKPGS GLHRCGQNPL PSQRFPVPDS VLNMFPSTEE
GPEDDSARHG GRIRTFPHER GNWATHIYIP YEANEEFQDL LDVLLPRAQM FAPRLVQMEE
FHLSLSQSVV LRHHWILPFV QVLKDRMASF QRFFFTANRV KIYTNQEKTR TFIGLEVSSG
HAQFLDMVSE VDRVMKEFDL TTFYQDPSFH VSLAWCVGDA RLQLEGQCQQ ELQEIVDEFE
DSEMLLRVLA EQVRCKSGNK FFSMPLK
