P22147 (XRN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5'-3' exoribonuclease 1
EC=3.1.11.-

Alternative name(s):
DNA strand transfer protein beta
Short name=STP-beta
KAR(-)-enhancing mutation protein
Strand exchange protein 1
p175

Gene names

Name:	XRN1
Synonyms:	DST2, KEM1, RAR5, SEP1, SKI1
Ordered Locus Names:	YGL173C
ORF Names:	G1645

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1528 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. The NMD pathway has a second role regulating the decay of wild-type mRNAs, and especially mRNAs that are important for telomere functions. Participate in CTH2-mediated and VTS1-mediated mRNA turnover. Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing. Involved in defense against virus and suppresses viral RNA recombination by rapidly removing the 5'-truncated RNAs, the substrates of recombination, and thus reducing the chance for recombination to occur in the parental strain. Required for the assembly of the virus-like particles of the Ty3 retrotransposon and contributes to the efficient generation of narnavirus 20S RNA by playing a major role in the elimination of the non-viral upstream sequences from the primary transcripts. Degrades single-stranded DNA (ss-DNA) and can renature complementary ss-DNA as well as catalyzes the formation of heteroduplex DNA from circular ss-DNA and homologous linear ds-DNA in vitro. Acts as a microtubule-associated protein which interacts with cytoplasmic microtubules through beta-tubulin and promotes in vitro assembly of tubulin into microtubules. Associates with microtubule functions such as chromosome transmission, nuclear migration, and SPB duplication. Has also a role in G1 to S transition and is involved in nuclear fusion during karyogamy. Required for the expression of ROK1 at the post-transcriptional level and for the alpha-factor induction of the karyogamy genes KAR3 and KAR4. Plays a role in filamentous growth. Ref.1 Ref.11 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.44 Ref.45 Ref.46 Ref.47 Ref.49 Ref.53 Ref.54 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61
Cofactor	Magnesium. Both strand exchange and nuclease activities require magnesium, for the strand exchange activity, calcium can replace magnesium when the linear ds-DNA has been first resected with an exogenous endonuclease.
Enzyme regulation	3'-phosphoadenosine 5'-phosphate (pAp) is an inhibitor of KEM1. Sodium-induced GCN4 expression reduces pAp accumulation by activating HAL2 expression, and therefore maintains mRNA degradation capacity which is likely to be important for the accurate and rapid adaptation of gene expression to salt stress. Ref.43
Subcellular location	Cytoplasm. Cytoplasm › perinuclear region. Cytoplasm › P-body Ref.18 Ref.35 Ref.46 Ref.50 Ref.55 Ref.58.
Disruption phenotype	Mutations affect nuclear fusion, leed to reduced chromosome stability and defects in spindle pole body duplication and/or separation as well as loss of viability under conditions of nitrogen starvation. Homozygous diploids are unable to sporulate. Leads also to arrest in pachytene and deficiency in meiotic recombination and sensitivity to oleate. Ref.5 Ref.17 Ref.48
Miscellaneous	Present with 11700 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the 5'-3' exonuclease family.

Ontologies

Keywords
Biological process	Karyogamy Nonsense-mediated mRNA decay rRNA processing
Cellular component	Cytoplasm Microtubule
Ligand	Magnesium RNA-binding
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	karyogamy Inferred from electronic annotation. Source: UniProtKB-KW nonfunctional rRNA decay Inferred from mutant phenotype PubMed 19481524. Source: SGD nuclear-transcribed mRNA catabolic process Traceable author statement PubMed 10690410. Source: SGD nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW rRNA processing Traceable author statement PubMed 10690410. Source: SGD traversing start control point of mitotic cell cycle Inferred from mutant phenotype Ref.39. Source: SGD
Cellular_component	cytoplasmic mRNA processing body Inferred from direct assay Ref.35. Source: SGD cytosol Traceable author statement. Source: Reactome microtubule Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5'-3' exoribonuclease activity Inferred from direct assay PubMed 3545079. Source: SGD RNA binding Inferred from electronic annotation. Source: UniProtKB-KW deoxyribonuclease activity Traceable author statement PubMed 8970740. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1528	1528	5'-3' exoribonuclease 1		PRO_0000071395
Amino acid modifications
	Modified residue	454	1	Phosphoserine Ref.52
	Modified residue	1329	1	Phosphoserine Ref.42 Ref.51 Ref.59
	Modified residue	1330	1	Phosphoserine Ref.59
	Modified residue	1505	1	Phosphoserine Ref.52
	Modified residue	1510	1	Phosphoserine Ref.51 Ref.52 Ref.59
Experimental info
	Mutagenesis	37	1	N → D: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	41	1	H → R or D: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	86	1	D → G: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	87	1	G → D: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	93	1	K → M: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	97	1	Q → E or R: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	101	1	R → G: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	176	1	E → G: Reduces strongly exonuclease activity.
	Mutagenesis	178	1	E → D or G: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	201	1	C → Y or R: Reduces strongly exonuclease activity. Ref.23
	Mutagenesis	206	1	D → A: Abolishes exonuclease activity in vitro. Ref.25
	Mutagenesis	208	1	D → A: Abolishes exonuclease activity in vitro. Ref.25
	Mutagenesis	592	1	L → P: Reduces strongly exonuclease activity; when associated with Y-710. Ref.23
	Mutagenesis	710	1	Y → C: Reduces strongly exonuclease activity; when associated with P-592. Ref.23
	Mutagenesis	798	1	W → R: Reduces strongly exonuclease activity; when associated with D-1024; F-1043 and P-1197. Ref.23
	Mutagenesis	1024	1	E → D: Reduces strongly exonuclease activity; when associated with R-798; F-1043 and P-1197. Ref.23
	Mutagenesis	1043	1	Y → F: Reduces strongly exonuclease activity; when associated with R-798; D-1024 and P-1197. Ref.23
	Mutagenesis	1197	1	S → P: Reduces strongly exonuclease activity; when associated with R-798; D-1024 and F-1043. Ref.23

Sequences

	Sequence		Length	Mass (Da)
	P22147 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 49C2EDAF73D3EB92	FASTA	1,528	175,460
	10 20 30 40 50 60 MGIPKFFRYI SERWPMILQL IEGTQIPEFD NLYLDMNSIL HNCTHGNDDD VTKRLTEEEV 70 80 90 100 110 120 FAKICTYIDH LFQTIKPKKI FYMAIDGVAP RAKMNQQRAR RFRTAMDAEK ALKKAIENGD 130 140 150 160 170 180 EIPKGEPFDS NSITPGTEFM AKLTKNLQYF IHDKISNDSK WREVQIIFSG HEVPGEGEHK 190 200 210 220 230 240 IMNFIRHLKS QKDFNQNTRH CIYGLDADLI MLGLSTHGPH FALLREEVTF GRRNSEKKSL 250 260 270 280 290 300 EHQNFYLLHL SLLREYMELE FKEIADEMQF EYNFERILDD FILVMFVIGN DFLPNLPDLH 310 320 330 340 350 360 LNKGAFPVLL QTFKEALLHT DGYINEHGKI NLKRLGVWLN YLSQFELLNF EKDDIDVEWF 370 380 390 400 410 420 NKQLENISLE GERKRQRVGK KLLVKQQKKL IGSIKPWLME QLQEKLSPDL PDEEIPTLEL 430 440 450 460 470 480 PKDLDMKDHL EFLKEFAFDL GLFITHSKSK GSYSLKMDLD SINPDETEEE FQNRVNSIRK 490 500 510 520 530 540 TIKKYQNAII VEDKEELETE KTIYNERFER WKHEYYHDKL KFTTDSEEKV RDLAKDYVEG 550 560 570 580 590 600 LQWVLYYYYR GCPSWSWYYP HHYAPRISDL AKGLDQDIEF DLSKPFTPFQ QLMAVLPERS 610 620 630 640 650 660 KNLIPPAFRP LMYDEQSPIH DFYPAEVQLD KNGKTADWEA VVLISFVDEK RLIEAMQPYL 670 680 690 700 710 720 RKLSPEEKTR NQFGKDLIYS FNPQVDNLYK SPLGGIFSDI EHNHCVEKEY ITIPLDSSEI 730 740 750 760 770 780 RYGLLPNAKL GAEMLAGFPT LLSLPFTSSL EYNETMVFQQ PSKQQSMVLQ ITDIYKTNNV 790 800 810 820 830 840 TLEDFSKRHL NKVIYTRWPY LRESKLVSLT DGKTIYEYQE SNDKKKFGFI TKPAETQDKK 850 860 870 880 890 900 LFNSLKNSML RMYAKQKAVK IGPMEAIATV FPVTGLVRDS DGGYIKTFSP TPDYYPLQLV 910 920 930 940 950 960 VESVVNEDER YKERGPIPIE EEFPLNSKVI FLGDYAYGGE TTIDGYSSDR RLKITVEKKF 970 980 990 1000 1010 1020 LDSEPTIGKE RLQMDHQAVK YYPSYIVSKN MHLHPLFLSK ITSKFMITDA TGKHINVGIP 1030 1040 1050 1060 1070 1080 VKFEARHQKV LGYARRNPRG WEYSNLTLNL LKEYRQTFPD FFFRLSKVGN DIPVLEDLFP 1090 1100 1110 1120 1130 1140 DTSTKDAMNL LDGIKQWLKY VSSKFIAVSL ESDSLTKTSI AAVEDHIMKY AANIEGHERK 1150 1160 1170 1180 1190 1200 QLAKVPREAV LNPRSSFALL RSQKFDLGDR VVYIQDSGKV PIFSKGTVVG YTTLSSSLSI 1210 1220 1230 1240 1250 1260 QVLFDHEIVA GNNFGGRLRT NRGLGLDASF LLNITNRQFI YHSKASKKAL EKKKQSNNRN 1270 1280 1290 1300 1310 1320 NNTKTAHKTP SKQQSEEKLR KERAHDLLNF IKKDTNEKNS ESVDNKSMGS QKDSKPAKKV 1330 1340 1350 1360 1370 1380 LLKRPAQKSS ENVQVDLANF EKAPLDNPTV AGSIFNAVAN QYSDGIGSNL NIPTPPHPMN 1390 1400 1410 1420 1430 1440 VVGGPIPGAN DVADVGLPYN IPPGFMTHPN GLHPLHPHQM PYPNMNGMSI PPPAPHGFGQ 1450 1460 1470 1480 1490 1500 PISFPPPPPM TNVSDQGSRI VVNEKESQDL KKFINGKQHS NGSTIGGETK NSRKGEIKPS 1510 1520 SGTNSTECQS PKSQSNAADR DNKKDEST

References

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[1]	"kem mutations affect nuclear fusion in Saccharomyces cerevisiae." Kim J., Ljungdahl P.O., Fink G.R. Genetics 126:799-812(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Molecular and genetic analysis of the gene encoding the Saccharomyces cerevisiae strand exchange protein Sep1." Tishkoff D., Johnson A.W., Kolodner R.D. Mol. Cell. Biol. 11:2593-2608(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[3]	"Cloning and characterization of DST2, the gene for DNA strand transfer protein beta from Saccharomyces cerevisiae." Dykstra C.C., Kitada K., Clark A.B., Hamatake R.K., Sugino A. Mol. Cell. Biol. 11:2583-2592(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204626 / S288c / A364A.
[4]	"Disruption of the gene XRN1, coding for a 5'-->3' exoribonuclease, restricts yeast cell growth." Larimer F.W., Stevens A. Gene 95:85-90(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"rar mutations which increase artificial chromosome stability in Saccharomyces cerevisiae identify transcription and recombination proteins." Kipling D., Tambini C., Kearsey S.E. Nucleic Acids Res. 19:1385-1391(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
[6]	"The sequence of an 11.1 kb fragment on the left arm of Saccharomyces cerevisiae chromosome VII reveals six open reading frames including NSP49, KEM1 and four putative new genes." Bertani I., Coglievina M., Zaccaria P., Klima R., Bruschi C.V. Yeast 11:1187-1194(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[7]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[8]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[9]	"Strand exchange protein 1 from Saccharomyces cerevisiae. A novel multifunctional protein that contains DNA strand exchange and exonuclease activities." Johnson A.W., Kolodner R.D. J. Biol. Chem. 266:14046-14054(1991) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF EXONUCLEASE ACTIVITY.
[10]	"Characterization of the XRN1 gene encoding a 5'-->3' exoribonuclease: sequence data and analysis of disparate protein and mRNA levels of gene-disrupted yeast cells." Larimer F.W., Hsu C.L., Maupin M.K., Stevens A. Gene 120:51-57(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF EXORIBONUCLEASE ACTIVITY.
[11]	"The Sep1 strand exchange protein from Saccharomyces cerevisiae promotes a paranemic joint between homologous DNA molecules." Chen J., Kanaar R., Cozzarelli N.R. Genes Dev. 8:1356-1366(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"The activity of the Saccharomyces cerevisiae strand exchange protein 1 intrinsic exonuclease during joint molecule formation." Johnson A.W., Kolodner R.D. J. Biol. Chem. 269:3664-3672(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF EXONUCLEASE ACTIVITY DURING STRAND EXCHANGE.
[13]	"Characterization of the interaction of Saccharomyces cerevisiae strand exchange protein 1 with DNA." Johnson A.W., Kolodner R.D. J. Biol. Chem. 269:3673-3681(1994) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING PROPERTIES.
[14]	"A multifunctional exonuclease from vegetative Schizosaccharomyces pombe cells exhibiting in vitro strand exchange activity." Kaeslin E., Heyer W.-D. J. Biol. Chem. 269:14094-14102(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF EXONUCLEASE AND STRAND EXCHANGE ACTIVITIES.
[15]	"The yeast KEM1 gene encodes a nuclease specific for G4 tetraplex DNA: implication of in vivo functions for this novel DNA structure." Liu Z., Gilbert W. Cell 77:1083-1092(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF SPECIFICITY FOR G4 TETRAPLEX DNA.
[16]	"A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae." Interthal H., Bellocq C., Baehler J., Bashkirov V.I., Edelstein S.J., Heyer W.-D. EMBO J. 14:1057-1066(1995) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH MICROTUBULES.
[17]	"The sep1 mutant of Saccharomyces cerevisiae arrests in pachytene and is deficient in meiotic recombination." Tishkoff D.X., Rockmill B., Roeder G.S., Kolodner R.D. Genetics 139:495-509(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[18]	"Regulation and intracellular localization of Saccharomyces cerevisiae strand exchange protein 1 (Sep1/Xrn1/Kem1), a multifunctional exonuclease." Heyer W.-D., Johnson A.W., Reinhart U., Kolodner R.D. Mol. Cell. Biol. 15:2728-2736(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[19]	"Gene disruption of a G4-DNA-dependent nuclease in yeast leads to cellular senescence and telomere shortening." Liu Z., Lee A., Gilbert W. Proc. Natl. Acad. Sci. U.S.A. 92:6002-6006(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively." Johnson A.W. Mol. Cell. Biol. 17:6122-6130(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"Processing of the precursors to small nucleolar RNAs and rRNAs requires common components." Petfalski E., Dandekar T., Henry Y., Tollervey D. Mol. Cell. Biol. 18:1181-1189(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"Telomere length regulation and telomeric chromatin require the nonsense-mediated mRNA decay pathway." Lew J.E., Enomoto S., Berman J. Mol. Cell. Biol. 18:6121-6130(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Mutational analysis of exoribonuclease I from Saccharomyces cerevisiae." Page A.M., Davis K., Molineux C., Kolodner R.D., Johnson A.W. Nucleic Acids Res. 26:3707-3716(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASN-37; HIS-41; ASP-86; GLY-87; LYS-93; GLN-97; ARG-101; GLU-178; CYS-201; LEU-592; TYR-710; TRP-798; GLU-1024; TYR-1043 AND SER-1197.
[24]	"The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex." Anderson J.S.J., Parker R.P. EMBO J. 17:1497-1506(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[25]	"Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces cerevisiae reveal a specific role in meiosis." Solinger J.A., Pascolini D., Heyer W.-D. Mol. Cell. Biol. 19:5930-5942(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-206 AND ASP-208.
[26]	"The final step in the formation of 25S rRNA in Saccharomyces cerevisiae is performed by 5'->3' exonucleases." Geerlings T.H., Vos J.C., Raue H.A. RNA 6:1698-1703(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[27]	"Upf1p, Nmd2p, and Upf3p regulate the decapping and exonucleolytic degradation of both nonsense-containing mRNAs and wild-type mRNAs." He F., Jacobson A. Mol. Cell. Biol. 21:1515-1530(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[28]	"KEM1 is involved in filamentous growth of Saccharomyces cerevisiae." Kim J., Kim J. FEMS Microbiol. Lett. 216:33-38(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[29]	"An mRNA surveillance mechanism that eliminates transcripts lacking termination codons." Frischmeyer P.A., van Hoof A., O'Donnell K., Guerrerio A.L., Parker R., Dietz H.C. Science 295:2258-2261(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[30]	"Genome-wide analysis of mRNAs regulated by the nonsense-mediated and 5' to 3' mRNA decay pathways in yeast." He F., Li X., Spatrick P., Casillo R., Dong S., Jacobson A. Mol. Cell 12:1439-1452(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[31]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[32]	"The Upf-dependent decay of wild-type PPR1 mRNA depends on its 5'-UTR and first 92 ORF nucleotides." Kebaara B., Nazarenus T., Taylor R., Forch A., Atkin A.L. Nucleic Acids Res. 31:3157-3165(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[33]	"Initiation-mediated mRNA decay in yeast affects heat-shock mRNAs, and works through decapping and 5'-to-3' hydrolysis." Heikkinen H.L., Llewellyn S.A., Barnes C.A. Nucleic Acids Res. 31:4006-4016(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[34]	"The roles of endonucleolytic cleavage and exonucleolytic digestion in the 5'-end processing of S. cerevisiae box C/D snoRNAs." Lee C.Y., Lee A., Chanfreau G. RNA 9:1362-1370(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[35]	"Decapping and decay of messenger RNA occur in cytoplasmic processing bodies." Sheth U., Parker R. Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[36]	"Deletion of OSH3 gene confers resistance against ISP-1 in Saccharomyces cerevisiae." Yano T., Inukai M., Isono F. Biochem. Biophys. Res. Commun. 315:228-234(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[37]	"Posttranscriptional regulation of the karyogamy gene by Kem1p/Xrn1p exoribonuclease and Rok1p RNA helicase of Saccharomyces cerevisiae." Kim J., Jeon S., Yang Y.-S., Kim J. Biochem. Biophys. Res. Commun. 321:1032-1039(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[38]	"RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel method of mRNA degradation." Gill T., Cai T., Aulds J., Wierzbicki S., Schmitt M.E. Mol. Cell. Biol. 24:945-953(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[39]	"A role for KEM1 at the START of the cell cycle in Saccharomyces cerevisiae." Pathak R., Bogomolnaya L.M., Guo J., Polymenis M. Curr. Genet. 48:300-309(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[40]	"Regulation and surveillance of normal and 3'-extended forms of the yeast aci-reductone dioxygenase mRNA by RNase III cleavage and exonucleolytic degradation." Zer C., Chanfreau G. J. Biol. Chem. 280:28997-29003(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[41]	"Multiple RNA surveillance pathways limit aberrant expression of iron uptake mRNAs and prevent iron toxicity in S. cerevisiae." Lee A., Henras A.K., Chanfreau G. Mol. Cell 19:39-51(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[42]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1329, MASS SPECTROMETRY. Strain: YAL6B.
[43]	"Sodium-induced GCN4 expression controls the accumulation of the 5' to 3' RNA degradation inhibitor, 3'-phosphoadenosine 5'-phosphate." Todeschini A.-L., Condon C., Benard L. J. Biol. Chem. 281:3276-3282(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[44]	"Determinants of Rbp1p localization in specific cytoplasmic mRNA-processing foci, P-bodies." Jang L.-T., Buu L.-M., Lee F.-J.S. J. Biol. Chem. 281:29379-29390(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[45]	"Suppression of viral RNA recombination by a host exoribonuclease." Cheng C.-P., Serviene E., Nagy P.D. J. Virol. 80:2631-2640(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[46]	"Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components." Beliakova-Bethell N., Beckham C., Giddings T.H. Jr., Winey M., Parker R., Sandmeyer S. RNA 12:94-101(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[47]	"Yeast transcripts cleaved by an internal ribozyme provide new insight into the role of the cap and poly(A) tail in translation and mRNA decay." Meaux S., Van Hoof A. RNA 12:1323-1337(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[48]	"The sensitivity of yeast mutants to oleic acid implicates the peroxisome and other processes in membrane function." Lockshon D., Surface L.E., Kerr E.O., Kaeberlein M., Kennedy B.K. Genetics 175:77-91(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[49]	"Respiratory deficiency mediates the regulation of CHO1-encoded phosphatidylserine synthase by mRNA stability in Saccharomyces cerevisiae." Choi H.-S., Carman G.M. J. Biol. Chem. 282:31217-31227(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[50]	"Analysis of P-body assembly in Saccharomyces cerevisiae." Teixeira D., Parker R. Mol. Biol. Cell 18:2274-2287(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[51]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1329 AND SER-1510, MASS SPECTROMETRY.
[52]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454; SER-1505 AND SER-1510, MASS SPECTROMETRY.
[53]	"Degradation of several hypomodified mature tRNA species in Saccharomyces cerevisiae is mediated by Met22 and the 5'-3' exonucleases Rat1 and Xrn1." Chernyakov I., Whipple J.M., Kotelawala L., Grayhack E.J., Phizicky E.M. Genes Dev. 22:1369-1380(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[54]	"Transcription in the nucleus and mRNA decay in the cytoplasm are coupled processes." Goler-Baron V., Selitrennik M., Barkai O., Haimovich G., Lotan R., Choder M. Genes Dev. 22:2022-2027(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[55]	"Synthetic genetic array analysis in Saccharomyces cerevisiae provides evidence for an interaction between RAT8/DBP5 and genes encoding P-body components." Scarcelli J.J., Viggiano S., Hodge C.A., Heath C.V., Amberg D.C., Cole C.N. Genetics 179:1945-1955(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[56]	"20S RNA narnavirus defies the antiviral activity of SKI1/XRN1 in Saccharomyces cerevisiae." Esteban R., Vega L., Fujimura T. J. Biol. Chem. 283:25812-25820(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[57]	"The Cth2 ARE-binding protein recruits the Dhh1 helicase to promote the decay of succinate dehydrogenase SDH4 mRNA in response to iron deficiency." Pedro-Segura E., Vergara S.V., Rodriguez-Navarro S., Parker R., Thiele D.J., Puig S. J. Biol. Chem. 283:28527-28535(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[58]	"The DEAD-box RNA helicase Ded1p affects and accumulates in Saccharomyces cerevisiae P-bodies." Beckham C., Hilliker A., Cziko A.-M., Noueiry A., Ramaswami M., Parker R. Mol. Biol. Cell 19:984-993(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[59]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1329; SER-1330 AND SER-1510, MASS SPECTROMETRY.
[60]	"S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation and interacts with the Ccr4p-Pop2p-Not deadenylase complex." Rendl L.M., Bieman M.A., Smibert C.A. RNA 14:1328-1336(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[61]	"Cordycepin interferes with 3' end formation in yeast independently of its potential to terminate RNA chain elongation." Holbein S., Wengi A., Decourty L., Freimoser F.M., Jacquier A., Dichtl B. RNA 15:837-849(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M90097 Genomic DNA. Translation: AAA35219.1. X54717 Genomic DNA. Translation: CAA38520.1. M58367 Genomic DNA. Translation: AAA35036.1. M36725 Genomic DNA. Translation: AAA35125.1. X61181 Genomic DNA. Translation: CAA43487.1. X84705 Genomic DNA. Translation: CAA59180.1. Z72695 Genomic DNA. Translation: CAA96885.1. BK006941 Genomic DNA. Translation: DAA07940.1.
PIR	S13743.
RefSeq	NP_011342.1. NM_001181038.1.
3D structure databases
ProteinModelPortal	P22147.
SMR	P22147. Positions 1-366, 511-679.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-656N.
IntAct	P22147. 72 interactions.
MINT	MINT-414332.
STRING	4932.YGL173C.
Proteomic databases
PaxDb	P22147.
PeptideAtlas	P22147.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL173C; YGL173C; YGL173C.
GeneID	852702.
KEGG	sce:YGL173C.
Organism-specific databases
CYGD	YGL173c.
SGD	S000003141. XRN1.
Phylogenomic databases
eggNOG	COG5049.
GeneTree	ENSGT00670000098080.
HOGENOM	HOG000160331.
KO	K12618.
OMA	NIFAYIE.
OrthoDB	EOG4PP1R0.
Enzyme and pathway databases
Reactome	REACT_78815. Metabolism of RNA. REACT_83470. Gene Expression.
Gene expression databases
Genevestigator	P22147.
GermOnline	YGL173C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR027073. 5_3_exoribonuclease. IPR016494. 5_3_exoribonuclease_1. IPR004859. Put_53exo. [Graphical view]
PANTHER	PTHR12341. PTHR12341. 1 hit.
Pfam	PF03159. XRN_N. 1 hit. [Graphical view]
PIRSF	PIRSF006743. Exonuclease_Xnr1. 1 hit.
ProtoNet	Search...
Other
NextBio	972050.

Entry information

Entry name

XRN1_YEAST

Accession

Primary (citable) accession number: P22147
Secondary accession number(s): D6VTX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program