I20L2_MOUSE
ID I20L2_MOUSE Reviewed; 368 AA.
AC Q3U1G5; Q4KMV7; Q8BKA9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Interferon-stimulated 20 kDa exonuclease-like 2;
DE EC=3.1.-.-;
GN Name=Isg20l2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: 3'-> 5'-exoribonuclease involved in ribosome biogenesis in
CC the processing of the 12S pre-rRNA. Displays a strong specificity for a
CC 3'-end containing a free hydroxyl group. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH98326.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin.; Evidence={ECO:0000305};
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DR EMBL; AK053778; BAC35519.1; -; mRNA.
DR EMBL; AK155979; BAE33533.1; -; mRNA.
DR EMBL; BC098326; AAH98326.1; ALT_SEQ; mRNA.
DR CCDS; CCDS17459.1; -.
DR RefSeq; NP_808331.1; NM_177663.4.
DR AlphaFoldDB; Q3U1G5; -.
DR SMR; Q3U1G5; -.
DR BioGRID; 230851; 17.
DR STRING; 10090.ENSMUSP00000059783; -.
DR iPTMnet; Q3U1G5; -.
DR PhosphoSitePlus; Q3U1G5; -.
DR EPD; Q3U1G5; -.
DR MaxQB; Q3U1G5; -.
DR PaxDb; Q3U1G5; -.
DR PeptideAtlas; Q3U1G5; -.
DR PRIDE; Q3U1G5; -.
DR ProteomicsDB; 267031; -.
DR DNASU; 229504; -.
DR GeneID; 229504; -.
DR KEGG; mmu:229504; -.
DR UCSC; uc008ptj.1; mouse.
DR CTD; 81875; -.
DR MGI; MGI:2140076; Isg20l2.
DR eggNOG; KOG2249; Eukaryota.
DR InParanoid; Q3U1G5; -.
DR OrthoDB; 1562214at2759; -.
DR PhylomeDB; Q3U1G5; -.
DR TreeFam; TF354340; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 229504; 23 hits in 71 CRISPR screens.
DR ChiTaRS; Isg20l2; mouse.
DR PRO; PR:Q3U1G5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3U1G5; protein.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd06149; ISG20; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR037433; ISG20_DEDDh.
DR InterPro; IPR034933; ISG20L2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR12801:SF78; PTHR12801:SF78; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Exonuclease; Hydrolase; Nuclease; Nucleus; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..368
FT /note="Interferon-stimulated 20 kDa exonuclease-like 2"
FT /id="PRO_0000315280"
FT DOMAIN 194..368
FT /note="Exonuclease"
FT REGION 33..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 77
FT /note="K -> KK (in Ref. 1; BAE33533)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="Missing (in Ref. 1; BAC35519)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="R -> Q (in Ref. 1; BAC35519 and 2; AAH98326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41020 MW; 075F41D4629AEF21 CRC64;
MSTILLNLDF GQPSKKAFGG NAKHQRFVKK RRFLEQKGFL NKKNQPPNKV SKLNSEPPKK
GETSRVDGIL KILPCPKKKE AAASKRDSER SKDKKAPLSW LTPAPSKKTA SVVSKIDLLG
EFQSALPKTK STQKKGSKKK SLKKKIATEN STQAQSKDKG SKKKPLKKNA VPNSTQARSE
DKCPTVPQNL PGKMVAIDCE MVGTGPKGRV SSLARCSIVN YNGDVLYDEY VLPPCYIVNY
RTRWSGIRKC HMVNATPFKT ARSQILKILS GKVVIGHAIH NDYKALQYFH PKSLTRDTSR
IPLLNRKADC PENVTLSLKH LTKKLLSRDI QVGNTGHSSV EDAQATMELY KLVEVEWEQH
LAQNPPEN
