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Protein

3'-5' exoribonuclease 1

Gene

Eri1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Binds with high affinity to the 3' side of the stem-loop structure and to the downstream cleavage product (DCP) of histone pre-mRNAs. Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA.By similarity1 Publication

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Enzyme regulationi

Although it can bind simultaneously with SLBP to the 3'-end of histone mRNA, the presence of SLBP prevents the exonuclease activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Magnesium 1By similarity
Metal bindingi130 – 1301Magnesium 2By similarity
Active sitei132 – 1321Proton acceptorSequence analysis
Metal bindingi132 – 1321Magnesium 1By similarity
Binding sitei132 – 1321AMPBy similarity
Binding sitei133 – 1331AMP; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi230 – 2301Magnesium 2By similarity
Active sitei289 – 2891Proton acceptorSequence analysis
Binding sitei289 – 2891AMPBy similarity
Metal bindingi294 – 2941Magnesium 1By similarity

GO - Molecular functioni

  • 3'-5' exonuclease activity Source: UniProtKB
  • histone pre-mRNA stem-loop binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • ribosome binding Source: UniProtKB
  • rRNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

RNA-mediated gene silencing, rRNA processing

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
3'-5' exoribonuclease 1 (EC:3.1.-.-)
Alternative name(s):
3'-5' exonuclease ERI1
Eri-1 homolog
Histone mRNA 3'-exonuclease 1
Gene namesi
Name:Eri1
Synonyms:3'exo, Thex1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1914526. Eri1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • histone pre-mRNA 3'end processing complex Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

High neonatal mortality rate. Reduced body size in surviving mice which is observed as early as embryonic day 15.5 and remains significant in adults.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071K → A: Impairs binding to and processing of 5.8S rRNA; when associated with A-108. 1 Publication
Mutagenesisi108 – 1081K → A: Impairs binding to and processing of 5.8S rRNA; when associated with A-107. 1 Publication
Mutagenesisi130 – 1301D → G: No effect on binding to 5.8S rRNA; when associated with G-132. 1 Publication
Mutagenesisi132 – 1321E → G: No effect on binding to 5.8S rRNA; when associated with G-130. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3453453'-5' exoribonuclease 1PRO_0000187008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7TMF2.
MaxQBiQ7TMF2.
PaxDbiQ7TMF2.
PRIDEiQ7TMF2.

PTM databases

iPTMnetiQ7TMF2.
PhosphoSiteiQ7TMF2.

Expressioni

Tissue specificityi

Widely expressed with high levels in spleen, thymus and testis (at protein level).1 Publication

Gene expression databases

BgeeiQ7TMF2.
CleanExiMM_THEX1.

Interactioni

Subunit structurei

Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Binds to 40S and 60S ribosomal subunits and to 80S assembled ribosomes. Interacts in a cooperative manner with SLBP to the mature 3'-end of histone mRNAs. Found in a ternary complex with SLBP and the stem-loop structure of the 3'-end of histone mRNAs (By similarity).By similarity

Protein-protein interaction databases

BioGridi212065. 1 interaction.
DIPiDIP-60112N.
MINTiMINT-1861762.
STRINGi10090.ENSMUSP00000033927.

Structurei

3D structure databases

ProteinModelPortaliQ7TMF2.
SMRiQ7TMF2. Positions 56-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 10635SAPPROSITE-ProRule annotationAdd
BLAST
Domaini126 – 302177ExonucleaseAdd
BLAST

Domaini

The SAP domain is necessary for binding to the stem-loop structure of histone mRNAs and to form the ternary complex with SLBP, but not for 3'-end histone mRNA exonuclease activity.By similarity

Sequence similaritiesi

Contains 1 exonuclease domain.Curated
Contains 1 SAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0542. Eukaryota.
COG5018. LUCA.
HOGENOMiHOG000006635.
HOVERGENiHBG048925.
InParanoidiQ7TMF2.
KOiK18416.
OrthoDBiEOG7BGHM2.
PhylomeDBiQ7TMF2.
TreeFamiTF313449.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TMF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDERGRERG GDAAQQKTPR PECEESRPLS VEKKQRCRLD GKETDGSKFI
60 70 80 90 100
SSNGSDFSDP VYKEIAMTNG CINRMSKEEL RAKLSEFKLE TRGVKDVLKK
110 120 130 140 150
RLKNYYKKQK LMLKESSAGD SYYDYICIID FEATCEEGNP AEFLHEIIEF
160 170 180 190 200
PVVLLNTHTL EIEDTFQQYV RPEVNAQLSE FCIGLTGITQ DQVDRADAFP
210 220 230 240 250
QVLKKVIEWM KSKELGTKYK YCILTDGSWD MSKFLSIQCR LSRLKHPAFA
260 270 280 290 300
KKWINIRKSY GNFYKVPRSQ TKLTIMLEKL GMDYDGRPHS GLDDSKNIAR
310 320 330 340
IAVRMLQDGC ELRINEKILG GQLMSVSSSL PVEGAPAPQM PHSRK
Length:345
Mass (Da):39,493
Last modified:March 15, 2004 - v2
Checksum:i96BDFD215D950AEF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 162QQ → HE in BAB29127 (PubMed:16141072).Curated
Sequence conflicti176 – 1761A → D in BAB29127 (PubMed:16141072).Curated
Sequence conflicti176 – 1761A → D in BAB29333 (PubMed:16141072).Curated
Sequence conflicti176 – 1761A → D in BAE38007 (PubMed:16141072).Curated
Sequence conflicti303 – 3031V → I in BAB29127 (PubMed:16141072).Curated
Sequence conflicti303 – 3031V → I in BAB29333 (PubMed:16141072).Curated
Sequence conflicti303 – 3031V → I in BAC34136 (PubMed:16141072).Curated
Sequence conflicti303 – 3031V → I in BAE38007 (PubMed:16141072).Curated
Sequence conflicti344 – 3441R → K in BAC34136 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014041 mRNA. Translation: BAB29127.2.
AK014410 mRNA. Translation: BAB29333.2.
AK050230 mRNA. Translation: BAC34136.1.
AK165026 mRNA. Translation: BAE38007.1.
AK172005 mRNA. Translation: BAE42771.1.
BC046412 mRNA. Translation: AAH46412.1.
CCDSiCCDS22244.1.
RefSeqiNP_080343.4. NM_026067.3.
UniGeneiMm.207534.

Genome annotation databases

GeneIDi67276.
KEGGimmu:67276.
UCSCiuc009lky.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014041 mRNA. Translation: BAB29127.2.
AK014410 mRNA. Translation: BAB29333.2.
AK050230 mRNA. Translation: BAC34136.1.
AK165026 mRNA. Translation: BAE38007.1.
AK172005 mRNA. Translation: BAE42771.1.
BC046412 mRNA. Translation: AAH46412.1.
CCDSiCCDS22244.1.
RefSeqiNP_080343.4. NM_026067.3.
UniGeneiMm.207534.

3D structure databases

ProteinModelPortaliQ7TMF2.
SMRiQ7TMF2. Positions 56-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212065. 1 interaction.
DIPiDIP-60112N.
MINTiMINT-1861762.
STRINGi10090.ENSMUSP00000033927.

PTM databases

iPTMnetiQ7TMF2.
PhosphoSiteiQ7TMF2.

Proteomic databases

EPDiQ7TMF2.
MaxQBiQ7TMF2.
PaxDbiQ7TMF2.
PRIDEiQ7TMF2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi67276.
KEGGimmu:67276.
UCSCiuc009lky.2. mouse.

Organism-specific databases

CTDi90459.
MGIiMGI:1914526. Eri1.

Phylogenomic databases

eggNOGiKOG0542. Eukaryota.
COG5018. LUCA.
HOGENOMiHOG000006635.
HOVERGENiHBG048925.
InParanoidiQ7TMF2.
KOiK18416.
OrthoDBiEOG7BGHM2.
PhylomeDBiQ7TMF2.
TreeFamiTF313449.

Miscellaneous databases

NextBioi324080.
PROiQ7TMF2.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TMF2.
CleanExiMM_THEX1.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Eye, Head, Liver and Spleen.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-107; LYS-108; ASP-130 AND GLU-132.
  4. "Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA."
    Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.
    Mol. Cell. Biol. 29:4045-4056(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, RNA-BINDING.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiERI1_MOUSE
AccessioniPrimary (citable) accession number: Q7TMF2
Secondary accession number(s): Q3TA98
, Q3TNT0, Q80UN4, Q8BWR6, Q9CQ63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: May 11, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.