Full text data of REXO2
REXO2
(SFN, SMFN)
[Confidence: low (only semi-automatic identification from reviews)]
Oligoribonuclease, mitochondrial; 3.1.-.- (RNA exonuclease 2 homolog; Small fragment nuclease; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Oligoribonuclease, mitochondrial; 3.1.-.- (RNA exonuclease 2 homolog; Small fragment nuclease; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y3B8
ID ORN_HUMAN Reviewed; 237 AA.
AC Q9Y3B8; Q32Q18; Q53FT1; Q6FIC6; Q9UFY7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Oligoribonuclease, mitochondrial;
DE EC=3.1.-.-;
DE AltName: Full=RNA exonuclease 2 homolog;
DE AltName: Full=Small fragment nuclease;
DE Flags: Precursor;
GN Name=REXO2; Synonyms=SFN, SMFN; ORFNames=CGI-114;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10851236; DOI=10.1074/jbc.M002672200;
RA Nguyen L.H., Erzberger J.P., Root J., Wilson D.M. III;
RT "The human homolog of Escherichia coli Orn degrades small single-
RT stranded RNA and DNA oligomers.";
RL J. Biol. Chem. 275:25900-25906(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP ENZYME REGULATION.
RX PubMed=16682444; DOI=10.1093/nar/gkl247;
RA Mechold U., Ogryzko V., Ngo S., Danchin A.;
RT "Oligoribonuclease is a common downstream target of lithium-induced
RT pAp accumulation in Escherichia coli and human cells.";
RL Nucleic Acids Res. 34:2364-2373(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: 3'-to-5' exoribonuclease specific for small
CC oligoribonucleotides. Active on small (primarily CC in length) single-stranded RNA and DNA oligomers. May have a role
CC in cellular nucleotide recycling.
CC -!- COFACTOR: Manganese.
CC -!- ENZYME REGULATION: Inhibited by adenosine 3',5'-bisphosphate.
CC -!- SUBUNIT: Homotetramer (Probable).
CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Sfn-alpha;
CC IsoId=Q9Y3B8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3B8-2; Sequence=VSP_003775;
CC -!- SIMILARITY: Belongs to the oligoribonuclease family.
CC -!- SIMILARITY: Contains 1 exonuclease domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF151872; AAD34109.1; -; mRNA.
DR EMBL; AL110239; CAB53690.1; -; mRNA.
DR EMBL; CR533500; CAG38531.1; -; mRNA.
DR EMBL; AK223200; BAD96920.1; -; mRNA.
DR EMBL; BC105024; AAI05025.1; -; mRNA.
DR EMBL; BC105026; AAI05027.1; -; mRNA.
DR EMBL; BC107887; AAI07888.1; -; mRNA.
DR PIR; T14770; T14770.
DR RefSeq; NP_056338.2; NM_015523.3.
DR UniGene; Hs.677190; -.
DR UniGene; Hs.714231; -.
DR ProteinModelPortal; Q9Y3B8; -.
DR SMR; Q9Y3B8; 41-216.
DR MINT; MINT-3085757; -.
DR STRING; 9606.ENSP00000265881; -.
DR PhosphoSite; Q9Y3B8; -.
DR DMDM; 116242694; -.
DR PaxDb; Q9Y3B8; -.
DR PRIDE; Q9Y3B8; -.
DR DNASU; 25996; -.
DR Ensembl; ENST00000265881; ENSP00000265881; ENSG00000076043.
DR GeneID; 25996; -.
DR KEGG; hsa:25996; -.
DR UCSC; uc001poy.3; human.
DR CTD; 25996; -.
DR GeneCards; GC11P114311; -.
DR H-InvDB; HIX0010145; -.
DR HGNC; HGNC:17851; REXO2.
DR HPA; HPA038450; -.
DR HPA; HPA038451; -.
DR MIM; 607149; gene.
DR neXtProt; NX_Q9Y3B8; -.
DR PharmGKB; PA142671085; -.
DR eggNOG; COG1949; -.
DR HOGENOM; HOG000246596; -.
DR HOVERGEN; HBG002323; -.
DR InParanoid; Q9Y3B8; -.
DR KO; K13288; -.
DR OMA; AFFHYRN; -.
DR OrthoDB; EOG7J4483; -.
DR PhylomeDB; Q9Y3B8; -.
DR ChiTaRS; REXO2; human.
DR GeneWiki; REXO2; -.
DR GenomeRNAi; 25996; -.
DR NextBio; 47710; -.
DR PRO; PR:Q9Y3B8; -.
DR ArrayExpress; Q9Y3B8; -.
DR Bgee; Q9Y3B8; -.
DR CleanEx; HS_REXO2; -.
DR CleanEx; HS_SFN; -.
DR Genevestigator; Q9Y3B8; -.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009117; P:nucleotide metabolic process; TAS:ProtInc.
DR InterPro; IPR006055; Exonuclease.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR012337; RNaseH-like_dom.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Exonuclease;
KW Hydrolase; Manganese; Mitochondrion; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1 25 Mitochondrion (Potential).
FT CHAIN 26 237 Oligoribonuclease, mitochondrial.
FT /FTId=PRO_0000020273.
FT DOMAIN 43 207 Exonuclease.
FT ACT_SITE 164 164 Potential.
FT MOD_RES 122 122 Phosphotyrosine.
FT MOD_RES 173 173 N6-acetyllysine (By similarity).
FT VAR_SEQ 1 38 Missing (in isoform 2).
FT /FTId=VSP_003775.
FT MUTAGEN 168 168 D->A: Abolishes activity.
FT CONFLICT 103 103 K -> R (in Ref. 2; CAB53690 and 3;
FT CAG38531).
SQ SEQUENCE 237 AA; 26833 MW; A0343A8918B11B82 CRC64;
MLGGSLGSRL LRGVGGSHGR FGARGVREGG AAMAAGESMA QRMVWVDLEM TGLDIEKDQI
IEMACLITDS DLNILAEGPN LIIKQPDELL DSMSDWCKEH HGKSGLTKAV KESTITLQQA
EYEFLSFVRQ QTPPGLCPLA GNSVHEDKKF LDKYMPQFMK HLHYRIIDVS TVKELCRRWY
PEEYEFAPKK AASHRALDDI SESIKELQFY RNNIFKKKID EKKRKIIENG ENEKTVS
//
ID ORN_HUMAN Reviewed; 237 AA.
AC Q9Y3B8; Q32Q18; Q53FT1; Q6FIC6; Q9UFY7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Oligoribonuclease, mitochondrial;
DE EC=3.1.-.-;
DE AltName: Full=RNA exonuclease 2 homolog;
DE AltName: Full=Small fragment nuclease;
DE Flags: Precursor;
GN Name=REXO2; Synonyms=SFN, SMFN; ORFNames=CGI-114;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10851236; DOI=10.1074/jbc.M002672200;
RA Nguyen L.H., Erzberger J.P., Root J., Wilson D.M. III;
RT "The human homolog of Escherichia coli Orn degrades small single-
RT stranded RNA and DNA oligomers.";
RL J. Biol. Chem. 275:25900-25906(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP ENZYME REGULATION.
RX PubMed=16682444; DOI=10.1093/nar/gkl247;
RA Mechold U., Ogryzko V., Ngo S., Danchin A.;
RT "Oligoribonuclease is a common downstream target of lithium-induced
RT pAp accumulation in Escherichia coli and human cells.";
RL Nucleic Acids Res. 34:2364-2373(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: 3'-to-5' exoribonuclease specific for small
CC oligoribonucleotides. Active on small (primarily CC in length) single-stranded RNA and DNA oligomers. May have a role
CC in cellular nucleotide recycling.
CC -!- COFACTOR: Manganese.
CC -!- ENZYME REGULATION: Inhibited by adenosine 3',5'-bisphosphate.
CC -!- SUBUNIT: Homotetramer (Probable).
CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Sfn-alpha;
CC IsoId=Q9Y3B8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3B8-2; Sequence=VSP_003775;
CC -!- SIMILARITY: Belongs to the oligoribonuclease family.
CC -!- SIMILARITY: Contains 1 exonuclease domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF151872; AAD34109.1; -; mRNA.
DR EMBL; AL110239; CAB53690.1; -; mRNA.
DR EMBL; CR533500; CAG38531.1; -; mRNA.
DR EMBL; AK223200; BAD96920.1; -; mRNA.
DR EMBL; BC105024; AAI05025.1; -; mRNA.
DR EMBL; BC105026; AAI05027.1; -; mRNA.
DR EMBL; BC107887; AAI07888.1; -; mRNA.
DR PIR; T14770; T14770.
DR RefSeq; NP_056338.2; NM_015523.3.
DR UniGene; Hs.677190; -.
DR UniGene; Hs.714231; -.
DR ProteinModelPortal; Q9Y3B8; -.
DR SMR; Q9Y3B8; 41-216.
DR MINT; MINT-3085757; -.
DR STRING; 9606.ENSP00000265881; -.
DR PhosphoSite; Q9Y3B8; -.
DR DMDM; 116242694; -.
DR PaxDb; Q9Y3B8; -.
DR PRIDE; Q9Y3B8; -.
DR DNASU; 25996; -.
DR Ensembl; ENST00000265881; ENSP00000265881; ENSG00000076043.
DR GeneID; 25996; -.
DR KEGG; hsa:25996; -.
DR UCSC; uc001poy.3; human.
DR CTD; 25996; -.
DR GeneCards; GC11P114311; -.
DR H-InvDB; HIX0010145; -.
DR HGNC; HGNC:17851; REXO2.
DR HPA; HPA038450; -.
DR HPA; HPA038451; -.
DR MIM; 607149; gene.
DR neXtProt; NX_Q9Y3B8; -.
DR PharmGKB; PA142671085; -.
DR eggNOG; COG1949; -.
DR HOGENOM; HOG000246596; -.
DR HOVERGEN; HBG002323; -.
DR InParanoid; Q9Y3B8; -.
DR KO; K13288; -.
DR OMA; AFFHYRN; -.
DR OrthoDB; EOG7J4483; -.
DR PhylomeDB; Q9Y3B8; -.
DR ChiTaRS; REXO2; human.
DR GeneWiki; REXO2; -.
DR GenomeRNAi; 25996; -.
DR NextBio; 47710; -.
DR PRO; PR:Q9Y3B8; -.
DR ArrayExpress; Q9Y3B8; -.
DR Bgee; Q9Y3B8; -.
DR CleanEx; HS_REXO2; -.
DR CleanEx; HS_SFN; -.
DR Genevestigator; Q9Y3B8; -.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009117; P:nucleotide metabolic process; TAS:ProtInc.
DR InterPro; IPR006055; Exonuclease.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR012337; RNaseH-like_dom.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Exonuclease;
KW Hydrolase; Manganese; Mitochondrion; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1 25 Mitochondrion (Potential).
FT CHAIN 26 237 Oligoribonuclease, mitochondrial.
FT /FTId=PRO_0000020273.
FT DOMAIN 43 207 Exonuclease.
FT ACT_SITE 164 164 Potential.
FT MOD_RES 122 122 Phosphotyrosine.
FT MOD_RES 173 173 N6-acetyllysine (By similarity).
FT VAR_SEQ 1 38 Missing (in isoform 2).
FT /FTId=VSP_003775.
FT MUTAGEN 168 168 D->A: Abolishes activity.
FT CONFLICT 103 103 K -> R (in Ref. 2; CAB53690 and 3;
FT CAG38531).
SQ SEQUENCE 237 AA; 26833 MW; A0343A8918B11B82 CRC64;
MLGGSLGSRL LRGVGGSHGR FGARGVREGG AAMAAGESMA QRMVWVDLEM TGLDIEKDQI
IEMACLITDS DLNILAEGPN LIIKQPDELL DSMSDWCKEH HGKSGLTKAV KESTITLQQA
EYEFLSFVRQ QTPPGLCPLA GNSVHEDKKF LDKYMPQFMK HLHYRIIDVS TVKELCRRWY
PEEYEFAPKK AASHRALDDI SESIKELQFY RNNIFKKKID EKKRKIIENG ENEKTVS
//
MIM
607149
*RECORD*
*FIELD* NO
607149
*FIELD* TI
*607149 RNA EXONUCLEASE 2, S. CEREVISIAE, HOMOLOG OF; REXO2
;;REX2, S. CEREVISIAE, HOMOLOG OF; REX2;;
read moreSMALL FRAGMENT NUCLEASE; SFN
*FIELD* TX
DESCRIPTION
Nucleases are components of DNA and RNA metabolism that carry out
functions in DNA repair, replication, and recombination and in RNA
processing and degradation. SFN is a homolog of Orn, a
3-prime-to-5-prime exoribonuclease of E. coli that attacks the free
3-prime hydroxyl group on single-stranded RNA, releasing 5-prime
mononucleotides in a sequential manner.
CLONING
Using the E. coli Orn sequence as query, Nguyen et al. (2000) identified
the REXO2 gene, which they called SFN, in an EST database and analyzed
the clone. The deduced 205-amino acid protein has a calculated molecular
mass of about 23.8 kD. The sequence shares about 50% identity with the
E. coli Orn protein and contains 3 characteristic motifs, termed Exo I,
II, and III, of the 3-prime-to-5-prime exonuclease superfamily. Four
conserved negatively charged residues within the 3 Exo motifs are
involved in positioning of the 2 divalent cations required for catalysis
and phosphodiester bond cleavage. Nguyen et al. (2000) identified a
splice variant, which they called SFN-alpha, that has an N-terminal
extension with a putative consensus cleavage site motif for
mitochondrial processing proteases. This variant appears to be a homolog
of yeast Ynt20, which shows both RNAse and DNAse activity. Both SFN and
SFN-alpha contain a consensus nuclear localization signal. Northern blot
analysis revealed a 1-kb transcript expressed in all fetal and adult
tissues tested, with highest levels in heart and relatively low levels
in adult lymph nodes, brain, lung, liver, spleen, and thymus. Since the
splice variants differ by only 2 nucleotides, Northern blot analysis
could not distinguish between the transcripts. EST analysis suggested
that the ratio of SFN to SFN-alpha is roughly 4 to 1. Gel filtration
chromatography revealed that recombinant SFN expressed in bacterial
cultures migrates as a 90-kD tetramer.
GENE FUNCTION
By in vitro analysis, Nguyen et al. (2000) confirmed 3-prime-to-5-prime
exonuclease activity in SFN for small (primarily 5 nucleotides or less
in length) single-stranded RNA and DNA oligomers. SFN shows a broad
substrate range, prefers Mn(2+) as a metal cofactor, and displays
nuclease activity up to 50 degrees Celsius. Kinetic analysis indicated
that SFN exhibits a similar affinity for small RNAs and DNAs, but
degrades small RNAs about 4-fold more efficiently than DNA. Mutation of
a conserved aspartate (asp136) to alanine abolished both nuclease
activities.
MAPPING
By genomic sequence analysis, Nguyen et al. (2000) mapped the REXO2 gene
to chromosome 11q23.1-q23.2.
*FIELD* RF
1. Nguyen, L. H.; Erzberger, J. P.; Root, J.; Wilson, D. M., III:
The human homolog of Escherichia coli Orn degrades small single-stranded
RNA and DNA oligomers. J. Biol. Chem. 275: 25900-25906, 2000.
*FIELD* CD
Patricia A. Hartz: 8/15/2002
*FIELD* ED
wwang: 09/28/2005
mgross: 8/15/2002
*RECORD*
*FIELD* NO
607149
*FIELD* TI
*607149 RNA EXONUCLEASE 2, S. CEREVISIAE, HOMOLOG OF; REXO2
;;REX2, S. CEREVISIAE, HOMOLOG OF; REX2;;
read moreSMALL FRAGMENT NUCLEASE; SFN
*FIELD* TX
DESCRIPTION
Nucleases are components of DNA and RNA metabolism that carry out
functions in DNA repair, replication, and recombination and in RNA
processing and degradation. SFN is a homolog of Orn, a
3-prime-to-5-prime exoribonuclease of E. coli that attacks the free
3-prime hydroxyl group on single-stranded RNA, releasing 5-prime
mononucleotides in a sequential manner.
CLONING
Using the E. coli Orn sequence as query, Nguyen et al. (2000) identified
the REXO2 gene, which they called SFN, in an EST database and analyzed
the clone. The deduced 205-amino acid protein has a calculated molecular
mass of about 23.8 kD. The sequence shares about 50% identity with the
E. coli Orn protein and contains 3 characteristic motifs, termed Exo I,
II, and III, of the 3-prime-to-5-prime exonuclease superfamily. Four
conserved negatively charged residues within the 3 Exo motifs are
involved in positioning of the 2 divalent cations required for catalysis
and phosphodiester bond cleavage. Nguyen et al. (2000) identified a
splice variant, which they called SFN-alpha, that has an N-terminal
extension with a putative consensus cleavage site motif for
mitochondrial processing proteases. This variant appears to be a homolog
of yeast Ynt20, which shows both RNAse and DNAse activity. Both SFN and
SFN-alpha contain a consensus nuclear localization signal. Northern blot
analysis revealed a 1-kb transcript expressed in all fetal and adult
tissues tested, with highest levels in heart and relatively low levels
in adult lymph nodes, brain, lung, liver, spleen, and thymus. Since the
splice variants differ by only 2 nucleotides, Northern blot analysis
could not distinguish between the transcripts. EST analysis suggested
that the ratio of SFN to SFN-alpha is roughly 4 to 1. Gel filtration
chromatography revealed that recombinant SFN expressed in bacterial
cultures migrates as a 90-kD tetramer.
GENE FUNCTION
By in vitro analysis, Nguyen et al. (2000) confirmed 3-prime-to-5-prime
exonuclease activity in SFN for small (primarily 5 nucleotides or less
in length) single-stranded RNA and DNA oligomers. SFN shows a broad
substrate range, prefers Mn(2+) as a metal cofactor, and displays
nuclease activity up to 50 degrees Celsius. Kinetic analysis indicated
that SFN exhibits a similar affinity for small RNAs and DNAs, but
degrades small RNAs about 4-fold more efficiently than DNA. Mutation of
a conserved aspartate (asp136) to alanine abolished both nuclease
activities.
MAPPING
By genomic sequence analysis, Nguyen et al. (2000) mapped the REXO2 gene
to chromosome 11q23.1-q23.2.
*FIELD* RF
1. Nguyen, L. H.; Erzberger, J. P.; Root, J.; Wilson, D. M., III:
The human homolog of Escherichia coli Orn degrades small single-stranded
RNA and DNA oligomers. J. Biol. Chem. 275: 25900-25906, 2000.
*FIELD* CD
Patricia A. Hartz: 8/15/2002
*FIELD* ED
wwang: 09/28/2005
mgross: 8/15/2002