ERI1_RAT
ID ERI1_RAT Reviewed; 345 AA.
AC Q5FVR4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=3'-5' exoribonuclease 1;
DE EC=3.1.-.-;
DE AltName: Full=Histone mRNA 3'-exonuclease 1;
GN Name=Eri1; Synonyms=Thex1;
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=Liver;
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: RNA exonuclease that binds to the 3'-end of histone mRNAs and
CC degrades them, suggesting that it plays an essential role in histone
CC mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last
CC nucleotide of the histone 3'-end is required for efficient degradation
CC of RNA substrates. Also able to degrade the 3'-overhangs of short
CC interfering RNAs (siRNAs) in vitro, suggesting a possible role as
CC regulator of RNA interference (RNAi). Binds with high affinity to the
CC 3' side of the stem-loop structure and to the downstream cleavage
CC product (DCP) of histone pre-mRNAs. Requires for binding the 5'-ACCCA-
CC 3' sequence present in stem-loop structure. Able to bind other mRNAs.
CC Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal
CC RNA (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Although it can bind simultaneously with SLBP to
CC the 3'-end of histone mRNA, the presence of SLBP prevents the
CC exonuclease activity. {ECO:0000250}.
CC -!- SUBUNIT: Identified in a histone pre-mRNA complex, at least composed of
CC ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Binds to 40S and 60S
CC ribosomal subunits and to 80S assembled ribosomes. Interacts in a
CC cooperative manner with SLBP to the mature 3'-end of histone mRNAs.
CC Found in a ternary complex with SLBP and the stem-loop structure of the
CC 3'-end of histone mRNAs (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The SAP domain is necessary for binding to the stem-loop
CC structure of histone mRNAs and to form the ternary complex with SLBP,
CC but not for 3'-end histone mRNA exonuclease activity. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC089828; AAH89828.1; -; mRNA.
DR RefSeq; NP_001014165.1; NM_001014143.1.
DR AlphaFoldDB; Q5FVR4; -.
DR SMR; Q5FVR4; -.
DR IntAct; Q5FVR4; 5.
DR STRING; 10116.ENSRNOP00000015239; -.
DR PaxDb; Q5FVR4; -.
DR PRIDE; Q5FVR4; -.
DR Ensembl; ENSRNOT00000015239; ENSRNOP00000015239; ENSRNOG00000011448.
DR GeneID; 361159; -.
DR KEGG; rno:361159; -.
DR UCSC; RGD:1308378; rat.
DR CTD; 90459; -.
DR RGD; 1308378; Eri1.
DR eggNOG; KOG0542; Eukaryota.
DR GeneTree; ENSGT00530000063205; -.
DR HOGENOM; CLU_037266_4_1_1; -.
DR InParanoid; Q5FVR4; -.
DR OMA; QLSEFCI; -.
DR OrthoDB; 809000at2759; -.
DR PhylomeDB; Q5FVR4; -.
DR TreeFam; TF313449; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q5FVR4; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000011448; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5FVR4; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0071207; F:histone pre-mRNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031125; P:rRNA 3'-end processing; ISS:UniProtKB.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; rRNA processing.
FT CHAIN 1..345
FT /note="3'-5' exoribonuclease 1"
FT /id="PRO_0000187009"
FT DOMAIN 72..106
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 126..302
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8IV48"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8IV48"
FT BINDING 132
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8IV48"
FT BINDING 133
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8IV48"
FT BINDING 289
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8IV48"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV48"
SQ SEQUENCE 345 AA; 39580 MW; 50DE97E5A8E60E43 CRC64;
MEDERGREHG GDAAQQKTPR PECEESRPLS VEKKQRCRLD GKDTDGSKFI TSNGGDFSDP
VYKEIAMTNG CINRMSKEEL RAKLSEFKLE TRGVKDVLKK RLKNYYKKQK LMLKESNAVD
SYYDYICIID FEATCEEGNP AEFLHEIIEF PVVLLNTHSL EIEDTFQQYV RPEVNSQLSE
FCIGLTGITQ DQVDRADAFP QVLKKVIEWM KSKELGTKYK YCILTDGSWD MSKFLNIQCQ
LSRLKYPSFA KKWINIRKSY GNFYKVPRSQ TKLTIMLEKL GMDYDGRPHS GLDDSKNIAR
IAVRMLQDGC ELRINEKLHG GQLMSVSSSL PVEGAPAPQM PHSRK
