XRN1_MOUSE
ID XRN1_MOUSE Reviewed; 1719 AA.
AC P97789; O35651; P97790; Q3TE44; Q3TRE9; Q3UQL5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=5'-3' exoribonuclease 1;
DE Short=mXRN1;
DE EC=3.1.13.-;
DE AltName: Full=Protein Dhm2;
DE AltName: Full=Strand-exchange protein 1 homolog;
GN Name=Xrn1 {ECO:0000312|MGI:MGI:891964};
GN Synonyms=Dhm2 {ECO:0000312|MGI:MGI:891964}, Exo,
GN Sep1 {ECO:0000250|UniProtKB:Q8IZH2};
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 [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=9218715; DOI=10.1016/s0378-1119(97)00053-x;
RA Shobuike T., Sugano S., Yamashita T., Ikeda H.;
RT "Cloning and characterization of mouse Dhm2 cDNA, a functional homolog of
RT budding yeast SEP1.";
RL Gene 191:161-166(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN RNA DECAY,
RP DNA-BINDING, RNA-BINDING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=9049243; DOI=10.1083/jcb.136.4.761;
RA Bashkirov V.I., Scherthan H., Solinger J.A., Buerstedde J.-M., Heyer W.-D.;
RT "A mouse cytoplasmic exoribonuclease (mXRN1) with preference for G4
RT tetraplex substrates.";
RL J. Cell Biol. 136:761-773(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-778, AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1261-1719 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, Hypothalamus, and Thymus;
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 [4]
RP ASSOCIATION WITH ALPHA AND BETA TUBULINS, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=14580940; DOI=10.1016/s0306-4522(03)00487-1;
RA Shimoyama Y., Morikawa Y., Ichihara M., Kodama Y., Fukuda N., Hayashi H.,
RA Morinaga T., Iwashita T., Murakumo Y., Takahashi M.;
RT "Identification of human SEP1 as a glial cell line-derived neurotrophic
RT factor-inducible protein and its expression in the nervous system.";
RL Neuroscience 121:899-906(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1382, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, and 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).
RN [7]
RP INTERACTION WITH YTHDC2.
RX PubMed=29033321; DOI=10.1016/j.molcel.2017.09.021;
RA Wojtas M.N., Pandey R.R., Mendel M., Homolka D., Sachidanandam R.,
RA Pillai R.S.;
RT "Regulation of m6A transcripts by the 3'-5' RNA helicase YTHDC2 is
RT essential for a successful meiotic program in the mammalian germline.";
RL Mol. Cell 68:374-387(2017).
CC -!- FUNCTION: Major 5'-3' exoribonuclease involved in mRNA decay. Required
CC for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA
CC substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex
CC than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and
CC DNA. Plays a role in replication-dependent histone mRNA degradation (By
CC similarity). {ECO:0000250|UniProtKB:Q8IZH2,
CC ECO:0000269|PubMed:9049243}.
CC -!- SUBUNIT: Found in a mRNP complex with UPF1, UPF2, UPF3B and XRN1 (By
CC similarity). Associates with alpha and beta tubulins (PubMed:14580940).
CC Interacts with DIS3L2 (By similarity). Interacts with ZC3HAV1 in an
CC RNA-dependent manner (By similarity). Interacts with ZFP36L1 (By
CC similarity). Interacts with TRIM71 (via NHL repeats) in an RNA-
CC dependent manner (By similarity). Interacts with YTHDC2 (via ANK
CC repeats) (PubMed:29033321). Interacts with DHX34; the interaction is
CC RNA-independent (By similarity). {ECO:0000250|UniProtKB:Q8IZH2,
CC ECO:0000269|PubMed:14580940, ECO:0000269|PubMed:29033321}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9049243}.
CC Note=Discrete foci at the inner surface of the cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P97789-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97789-2; Sequence=VSP_016697;
CC Name=3;
CC IsoId=P97789-3; Sequence=VSP_016696, VSP_016698;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain (spinal cord, dorsal root
CC and superior cervical ganglia, neurons of the cerebrum and brain stem),
CC peripheral nerve fibers in the skin and intestine, spleen, lung, liver,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:14580940,
CC ECO:0000269|PubMed:9049243, ECO:0000269|PubMed:9218715}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo between 7 and 17 dpc.
CC {ECO:0000269|PubMed:14580940}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. {ECO:0000305}.
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DR EMBL; D88026; BAA21563.1; -; mRNA.
DR EMBL; X91617; CAA62819.1; -; mRNA.
DR EMBL; X91617; CAA62820.1; -; mRNA.
DR EMBL; AK142311; BAE25024.1; -; mRNA.
DR EMBL; AK162848; BAE37081.1; -; mRNA.
DR EMBL; AK169840; BAE41404.1; -; mRNA.
DR CCDS; CCDS81053.1; -. [P97789-1]
DR PIR; T30174; T30174.
DR PIR; T30175; T30175.
DR PIR; T30244; T30244.
DR AlphaFoldDB; P97789; -.
DR SMR; P97789; -.
DR BioGRID; 204909; 3.
DR IntAct; P97789; 2.
DR STRING; 10090.ENSMUSP00000034981; -.
DR iPTMnet; P97789; -.
DR PhosphoSitePlus; P97789; -.
DR SwissPalm; P97789; -.
DR EPD; P97789; -.
DR MaxQB; P97789; -.
DR PaxDb; P97789; -.
DR PeptideAtlas; P97789; -.
DR PRIDE; P97789; -.
DR ProteomicsDB; 299783; -. [P97789-1]
DR ProteomicsDB; 299784; -. [P97789-2]
DR ProteomicsDB; 299785; -. [P97789-3]
DR MGI; MGI:891964; Xrn1.
DR eggNOG; KOG2045; Eukaryota.
DR InParanoid; P97789; -.
DR PhylomeDB; P97789; -.
DR Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-MMU-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR ChiTaRS; Xrn1; mouse.
DR PRO; PR:P97789; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97789; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:BHF-UCL.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:BHF-UCL.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; NAS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0071028; P:nuclear mRNA surveillance; ISO:MGI.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISO:MGI.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:BHF-UCL.
DR GO; GO:0006396; P:RNA processing; TAS:UniProtKB.
DR GO; GO:0016075; P:rRNA catabolic process; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; NAS:UniProtKB.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR004859; Put_53exo.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR041412; Xrn1_helical.
DR PANTHER; PTHR12341; PTHR12341; 1.
DR PANTHER; PTHR12341:SF7; PTHR12341:SF7; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF18332; XRN1_D1; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF006743; Exonuclease_Xnr1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Exonuclease; Hydrolase;
KW Nuclease; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..1719
FT /note="5'-3' exoribonuclease 1"
FT /id="PRO_0000071393"
FT REGION 1268..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 1436
FT /note="P -> PSKKL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9218715"
FT /id="VSP_016696"
FT VAR_SEQ 1568..1580
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9049243"
FT /id="VSP_016697"
FT VAR_SEQ 1661..1719
FT /note="PQESPPASSSSSQAAQPVSSHVETASQGHVGSQPRSAPSSSKRKSRKLAVNF
FT SVSKPSE -> EFPGWVHLPVTSLTYGLWWRLPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9218715"
FT /id="VSP_016698"
FT CONFLICT 99
FT /note="G -> A (in Ref. 1; BAA21563)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="E -> D (in Ref. 3; BAE25024)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="D -> G (in Ref. 3; BAE25024)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="M -> L (in Ref. 1; BAA21563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1243
FT /note="T -> I (in Ref. 1; BAA21563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1261
FT /note="I -> L (in Ref. 3; BAE41404)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1719 AA; 194307 MW; 4FE6C888E3FE2459 CRC64;
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD VHFRISDDKI
FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKAIEKGE
TLPTEARFDS NCITPGTEFM ARLHEHLKYF VNMKISTDKS WQGVTIYFSG HETPGEGEHK
IMEFIRSEKA KPDHDPNTRH CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA
PEETTFHLLH LSLMREYIDY EFSALKEKIT FKYDIEKIID DWILMGFLVG NDFIPHLPHL
HINHDALPLL YGTYIAILPE LGGYINESGH LNLPRFERYL VKLSDFDREH FSEVFVDLKW
FESKVGNKYL NEAAGAAAEE AKNCKEKRKP KGQENSLSWA ALDKSEGEGV ASRDNFEDET
EDDDLFETEF RQYKRTYYMT KMGVDVVSDE FLANQAACYV QAIQWILHYY YHGVQSWSWY
YPYHYAPFLS DIRSISTLKI HFELGKPFKP FEQLLAVLPS ASKNLLPTCY QHLMTSEDSP
IIEYYPPDFK TDLNGKQQEW EAVVLIPFID ETRLLEAMET CNHSLKKEER KRNQHSECLM
CWYDRDTEFT YSSPWPEKFP AIERCCTRYK MISLDAWRVD INKNKITRVD QKALYFCGFP
TLKHIKHKFF LKKSGVQVFQ QSSRGENLML EISVNAEPDE LRIENIASAV LGKAVFVNWP
HLEEARVVAV SDGETKFYIE EPPGTQKVYL GKTAPPSKVI QLTDKEQSNW TKEIQGISEQ
YLRRKGIIIN ETSAVVYAQL LTGRKYQISQ NGEVRLEKQW SKQILPFVYQ TIVKDIRAFD
SRFSNIKTLD DLFPPRTMVF MLGTPYYGCT GEVQDSGDLI TEGRIRVVFS IPCEPNLDAL
IQNQHKYSIK YNPGYVLAGR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK ANVGLNLKFN
KKNEEVPGYT KKVGNEWMYS SAAEQLLAEY IERAPELFSY IAKNSQEDVF YEDDIWPGEN
ENGAEKVQEI ITWLKGHPVS TLSRSSCDLH ILDAAIVEKI EEEVEKCKQR KSNKKVRVTV
KPHLMYRPLE QQHGVIPDRD AEFRLFDRVV NVRESFSVPV GLRGTVIGIK GASREADVLF
EVLFDEEFPG GLTIRCSPGR GYRLPTSALV NLSHGSRCET GNQKLTAIVK PQPSVSHCSA
APSGHLGGLN HSPQSPFLPT QVPTKGDDEF CNIWQSLQGA GKTQHLQPTV QEKGAVLPQE
ISQVTEGHKS GFTDHSVRHQ QRKHDSQRKF KEEYKSPKAE CQSQKLSSKQ TSGGSARCSI
KLLKRNESPG TSEAQKVVTS YPNAVHKPPS GIENFLASLN LSKENEAQLP HHGEPPDEAD
LSPQSFAMKG TRMLKEILKI DSPDTRDSKN DMKKSDNEAT VSSRRDERGV SAHPKPTCHM
NKPHGTNEFQ NVASVDSVCW PGQMPPVSTP VTELSRICSL VGMPQPDFSF LRTTQTMTVC
QVKLSNGLLV HGPQCHSESE AKERAALFAL QQLGSLGVSF PLPPPIFTNY PPAVPPGAVP
PVFTQPTANI MPSSSHLFGS VSWRPPVPVA GNAFHYPSYP GTMPLAGGVP GGVHSQFIPL
QVTKKRVANR KNFENKEAQS SQATPLQTNK PGSSEATKMT PQESPPASSS SSQAAQPVSS
HVETASQGHV GSQPRSAPSS SKRKSRKLAV NFSVSKPSE
