ERI1_MOUSE
ID ERI1_MOUSE Reviewed; 345 AA.
AC Q7TMF2; Q3TA98; Q3TNT0; Q80UN4; Q8BWR6; Q9CQ63;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=3'-5' exoribonuclease 1;
DE EC=3.1.-.-;
DE AltName: Full=3'-5' exonuclease ERI1;
DE AltName: Full=Eri-1 homolog;
DE AltName: Full=Histone mRNA 3'-exonuclease 1;
GN Name=Eri1; Synonyms=3'exo, Thex1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Eye, Head, Liver, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-107; LYS-108; ASP-130 AND GLU-132.
RX PubMed=18438418; DOI=10.1038/nsmb.1417;
RA Ansel K.M., Pastor W.A., Rath N., Lapan A.D., Glasmacher E., Wolf C.,
RA Smith L.C., Papadopoulou N., Lamperti E.D., Tahiliani M., Ellwart J.W.,
RA Shi Y., Kremmer E., Rao A., Heissmeyer V.;
RT "Mouse Eri1 interacts with the ribosome and catalyzes 5.8S rRNA
RT processing.";
RL Nat. Struct. Mol. Biol. 15:523-530(2008).
RN [4]
RP IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, AND RNA-BINDING.
RX PubMed=19470752; DOI=10.1128/mcb.00296-09;
RA Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT "Three proteins of the U7-specific Sm ring function as the molecular ruler
RT to determine the site of 3'-end processing in mammalian histone pre-mRNA.";
RL Mol. Cell. Biol. 29:4045-4056(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
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 (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds
CC to 5.8s ribosomal RNA. {ECO:0000250, ECO:0000269|PubMed:18438418}.
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 -!- INTERACTION:
CC Q7TMF2; Q8VC85: Lsm1; NbExp=3; IntAct=EBI-16026214, EBI-16026183;
CC Q7TMF2; Q9EPU0: Upf1; NbExp=2; IntAct=EBI-16026214, EBI-6876715;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18438418}. Nucleus
CC {ECO:0000269|PubMed:18438418}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:18438418}.
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in spleen, thymus
CC and testis (at protein level). {ECO:0000269|PubMed:18438418}.
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 -!- DISRUPTION PHENOTYPE: High neonatal mortality rate. Reduced body size
CC in surviving mice which is observed as early as embryonic day 15.5 and
CC remains significant in adults. {ECO:0000269|PubMed:18438418}.
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DR EMBL; AK014041; BAB29127.2; -; mRNA.
DR EMBL; AK014410; BAB29333.2; -; mRNA.
DR EMBL; AK050230; BAC34136.1; -; mRNA.
DR EMBL; AK165026; BAE38007.1; -; mRNA.
DR EMBL; AK172005; BAE42771.1; -; mRNA.
DR EMBL; BC046412; AAH46412.1; -; mRNA.
DR CCDS; CCDS22244.1; -.
DR RefSeq; NP_080343.4; NM_026067.3.
DR AlphaFoldDB; Q7TMF2; -.
DR SMR; Q7TMF2; -.
DR BioGRID; 212065; 1.
DR DIP; DIP-60112N; -.
DR IntAct; Q7TMF2; 3.
DR STRING; 10090.ENSMUSP00000033927; -.
DR iPTMnet; Q7TMF2; -.
DR PhosphoSitePlus; Q7TMF2; -.
DR EPD; Q7TMF2; -.
DR MaxQB; Q7TMF2; -.
DR PaxDb; Q7TMF2; -.
DR PeptideAtlas; Q7TMF2; -.
DR PRIDE; Q7TMF2; -.
DR ProteomicsDB; 275779; -.
DR DNASU; 67276; -.
DR GeneID; 67276; -.
DR KEGG; mmu:67276; -.
DR UCSC; uc009lky.2; mouse.
DR CTD; 90459; -.
DR MGI; MGI:1914526; Eri1.
DR eggNOG; KOG0542; Eukaryota.
DR InParanoid; Q7TMF2; -.
DR OrthoDB; 809000at2759; -.
DR PhylomeDB; Q7TMF2; -.
DR TreeFam; TF313449; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 67276; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Eri1; mouse.
DR PRO; PR:Q7TMF2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q7TMF2; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IDA: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; IDA: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 1: Evidence at protein 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_0000187008"
FT DOMAIN 72..106
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 126..302
FT /note="Exonuclease"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Basic and acidic residues"
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"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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"
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"
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"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV48"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV48"
FT MUTAGEN 107
FT /note="K->A: Impairs binding to and processing of 5.8S
FT rRNA; when associated with A-108."
FT /evidence="ECO:0000269|PubMed:18438418"
FT MUTAGEN 108
FT /note="K->A: Impairs binding to and processing of 5.8S
FT rRNA; when associated with A-107."
FT /evidence="ECO:0000269|PubMed:18438418"
FT MUTAGEN 130
FT /note="D->G: No effect on binding to 5.8S rRNA; when
FT associated with G-132."
FT /evidence="ECO:0000269|PubMed:18438418"
FT MUTAGEN 132
FT /note="E->G: No effect on binding to 5.8S rRNA; when
FT associated with G-130."
FT /evidence="ECO:0000269|PubMed:18438418"
FT CONFLICT 15..16
FT /note="QQ -> HE (in Ref. 1; BAB29127)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="A -> D (in Ref. 1; BAB29127/BAB29333/BAE38007)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="V -> I (in Ref. 1; BAB29127/BAB29333/BAC34136/
FT BAE38007)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="R -> K (in Ref. 1; BAC34136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 39493 MW; 96BDFD215D950AEF CRC64;
MEDERGRERG GDAAQQKTPR PECEESRPLS VEKKQRCRLD GKETDGSKFI SSNGSDFSDP
VYKEIAMTNG CINRMSKEEL RAKLSEFKLE TRGVKDVLKK RLKNYYKKQK LMLKESSAGD
SYYDYICIID FEATCEEGNP AEFLHEIIEF PVVLLNTHTL EIEDTFQQYV RPEVNAQLSE
FCIGLTGITQ DQVDRADAFP QVLKKVIEWM KSKELGTKYK YCILTDGSWD MSKFLSIQCR
LSRLKHPAFA KKWINIRKSY GNFYKVPRSQ TKLTIMLEKL GMDYDGRPHS GLDDSKNIAR
IAVRMLQDGC ELRINEKILG GQLMSVSSSL PVEGAPAPQM PHSRK
