XRN1_SCHPO
ID XRN1_SCHPO Reviewed; 1328 AA.
AC P40383;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=5'-3' exoribonuclease 1;
DE EC=3.1.13.-;
DE AltName: Full=Exonuclease 2;
DE AltName: Full=Exonuclease II;
DE Short=Exo II;
DE AltName: Full=p140;
GN Name=exo2; ORFNames=SPAC17A5.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 47-71; 620-636
RP AND 666-674.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8781170; DOI=10.1007/s002940050134;
RA Szankasi P., Smith G.R.;
RT "Requirement of S. pombe exonuclease II, a homologue of S. cerevisiae Sep1,
RT for normal mitotic growth and viability.";
RL Curr. Genet. 30:284-293(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PROTEIN SEQUENCE OF 488-501, AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8188690; DOI=10.1016/s0021-9258(17)36759-5;
RA Kaeslin E., Heyer W.-D.;
RT "A multifunctional exonuclease from vegetative Schizosaccharomyces pombe
RT cells exhibiting in vitro strand exchange activity.";
RL J. Biol. Chem. 269:14094-14102(1994).
RN [4]
RP CHARACTERIZATION OF SINGLE-STRANDED DNA EXONUCLEASE ACTIVITY, FUNCTION, AND
RP COFACTOR.
RX PubMed=1637812; DOI=10.1021/bi00144a017;
RA Szankasi P., Smith G.R.;
RT "A single-stranded DNA exonuclease from Schizosaccharomyces pombe.";
RL Biochemistry 31:6769-6773(1992).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=8188691; DOI=10.1016/s0021-9258(17)36760-1;
RA Kaeslin E., Heyer W.-D.;
RT "Schizosaccharomyces pombe fatty acid synthase mediates DNA strand exchange
RT in vitro.";
RL J. Biol. Chem. 269:14103-14110(1994).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Multifunctional protein that exhibits several independent
CC functions at different levels of the cellular processes
CC (PubMed:8188690, PubMed:1637812). 5'-3' exonuclease component of the
CC nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA
CC degradation pathway, an RNA surveillance system whose role is to
CC identify and rid cells of mRNA with premature termination codons and
CC thus prevents accumulation of potentially harmful truncated proteins
CC (By similarity). Involved in the degradation of several hypomodified
CC mature tRNA species and participates in the 5'-processing or the
CC degradation of the snoRNA precursors and rRNA processing (By
CC similarity). {ECO:0000250|UniProtKB:P22147, ECO:0000269|PubMed:1637812,
CC ECO:0000269|PubMed:8188690}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1637812};
CC -!- ACTIVITY REGULATION: Strand exchange activity is enhanced by fatty acid
CC synthase (stimulatory factor P190/210). {ECO:0000269|PubMed:8188691}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. {ECO:0000305}.
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DR EMBL; L35232; AAB42181.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11514.1; -; Genomic_DNA.
DR PIR; S78457; S78457.
DR RefSeq; NP_593482.1; NM_001018915.2.
DR AlphaFoldDB; P40383; -.
DR SMR; P40383; -.
DR BioGRID; 278679; 19.
DR STRING; 4896.SPAC17A5.14.1; -.
DR iPTMnet; P40383; -.
DR MaxQB; P40383; -.
DR PaxDb; P40383; -.
DR PRIDE; P40383; -.
DR EnsemblFungi; SPAC17A5.14.1; SPAC17A5.14.1:pep; SPAC17A5.14.
DR GeneID; 2542204; -.
DR KEGG; spo:SPAC17A5.14; -.
DR PomBase; SPAC17A5.14; exo2.
DR VEuPathDB; FungiDB:SPAC17A5.14; -.
DR eggNOG; KOG2045; Eukaryota.
DR HOGENOM; CLU_001581_1_2_1; -.
DR InParanoid; P40383; -.
DR OMA; VASWPWF; -.
DR PhylomeDB; P40383; -.
DR PRO; PR:P40383; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:PomBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IDA:PomBase.
DR GO; GO:0004540; F:ribonuclease activity; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:PomBase.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR004859; Put_53exo.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR041106; XRN1_D2_D3.
DR InterPro; IPR040486; Xrn1_D3.
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; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF18194; Xrn1_D3; 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 Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase; Magnesium;
KW Nonsense-mediated mRNA decay; Nuclease; Reference proteome; RNA-binding;
KW rRNA processing.
FT CHAIN 1..1328
FT /note="5'-3' exoribonuclease 1"
FT /id="PRO_0000071394"
FT REGION 1211..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1328 AA; 152589 MW; 597D7E29726F56C9 CRC64;
MGIPKFFRWM SERYPLCSQL IENDRIPEFD NLYLDMNGIL HNCTHKNDDH SSPPLPEEEM
YIAIFNYIEH LFEKIKPKKL LYMAVDGCAP RAKMNQQRSR RFRTAKDAHD ARLKAERNGE
DFPEEQFDSN CITPGTTFME RVSRQLYYFI HKKVTNDSQW QNIEVIFSGH DCPGEGEHKI
MEYIRTQKAQ PSYNPNTRHC LYGLDADLIM LGLLSHDPHF CLLREEVTFG PASRNRSKEL
AHQKFYLLHL SLLREYLEFE FQECRSTFTF KYDLEKILDD FILLAFFVGN DFLPHLPGLH
INEGALALMF SIYKKVMPSA GGYINEKGVI NMARLELILL ELENFEKEIF KAEVSETKNN
GNSDKPSFDF LKYITESTND IKAMTGEQKN YFLQIKKFLS SREPFIDFSA NISSVDQRFL
RRLCNDLHLS FSKIIKVDGT HLLRITFRDL EFNDEDEDEI EQDEIERVLQ KYDNIPLLNE
EQALKEKNVE KDFIQWKDDY YRSKVGFSYY DEEALKAMAE RYVEGLQWVL FYYYRGCQSW
GWYYNYHFAP KISDVLKGLD VKIDFKMGTP FRPFEQLMAV LPARSQALVP PCFRDLMVNS
ESPIIDFYPE NFALDQNGKT ASWEAVVIIP FIDETRLIDA LASKDKFLTE EERKRNSFNA
PTVFSLAEDY TSFYPSSLPS LFPDLVTRCI QKPYSLPSME GKEYLVGLCP GVFLGAFGMV
GFPSFHTLKH KAELVYHGIN VFGNESRNPS VIVNVEDVKS ALTSEQIAMQ YVGKRIFVDW
PYLREAYVES AMDESYMYLA SNSTIEKRDL AEIEKSQWGR KCSHKIREYS KRFGVLFGDI
SLLLQVRPIK GLEYTREGAL VKIFNESVLE DYPAQLVVEK IAIDDPRFTE REAPPVEVEY
PPGTKAFHLG EYNYGRPAQI TGCKDNKLII WLSTAPGLDA QWGRVLVNDS KSKEKYYPSY
IVAKLLNIHP LLLSKITSSF LISNGTKREN IGLNLKFDAR NQKVLGFSRK STKGWEFSNK
TVALVKEYIN TFPQLFNILT THATKDNLTV KDCFPKDDTQ QLAAVKHWIK EKGINSLTRV
SLDEDALDSD IIKLIEEKAS TIDSTYQVPK KVFGVPRYAL LKPSQTRGIL HSQEFALGDR
VVYVQDSGKV PIAAYGTVVG IMLHHLDVVF DLPFMSGTTL DGRCSPYHGM QVEVSMVLNV
TNPQFVVNTR AGKNRKTNVS ANNVSQGTDS RLVTKPTSTF PSPPSPPSSS VWNKREHHPK
PFSLHQVPPP ESLIHKSKSK FSKGNHHSTN GTQSIRGRGG KRGKPLRSKE LNRKHDHIVQ
PMGKLQIN
