ID OASL2_MOUSE Reviewed; 508 AA.
AC Q9Z2F2; Q9D6S2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 24-JAN-2024, entry version 149.
DE RecName: Full=2'-5'-oligoadenylate synthase-like protein 2;
DE EC=2.7.7.84 {ECO:0000269|PubMed:12799444};
DE AltName: Full=54 kDa 2'-5'-oligoadenylate synthase-like protein;
DE Short=p54 OASL;
DE AltName: Full=M1204;
GN Name=Oasl2;
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].
RC TISSUE=Spleen;
RX PubMed=10395668;
RA Tiefenthaler M., Marksteiner R., Neyer S., Koch F., Hofer S., Schuler G.,
RA Nussenzweig M., Schneider R., Heufler C.;
RT "M1204, a novel 2',5' oligoadenylate synthetase with a ubiquitin-like
RT extension, is induced during maturation of murine dendritic cells.";
RL J. Immunol. 163:760-765(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=12396720; DOI=10.1089/10799900260286696;
RA Kakuta S., Shibata S., Iwakura Y.;
RT "Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene
RT family.";
RL J. Interferon Cytokine Res. 22:981-993(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Tongue;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=12799444; DOI=10.1093/nar/gkg427;
RA Eskildsen S., Justesen J., Schierup M.H., Hartmann R.;
RT "Characterization of the 2'-5'-oligoadenylate synthetase ubiquitin-like
RT family.";
RL Nucleic Acids Res. 31:3166-3173(2003).
RN [6]
RP REVIEW.
RX PubMed=17024523; DOI=10.1007/s00239-006-0073-3;
RA Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.;
RT "The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for
RT concerted evolution of paralogous Oas1 genes in Rodentia and
RT Artiodactyla.";
RL J. Mol. Evol. 63:562-576(2006).
CC -!- FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which
CC plays a critical role in cellular innate antiviral response.
CC Synthesizes oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which
CC then bind to the inactive monomeric form of ribonuclease L (RNase L)
CC leading to its dimerization and subsequent activation. Activation of
CC RNase L leads to degradation of cellular as well as viral RNA,
CC resulting in the inhibition of protein synthesis, thus terminating
CC viral replication. Can mediate the antiviral effect via the classical
CC RNase L-dependent pathway or an alternative antiviral pathway
CC independent of RNase L. {ECO:0000269|PubMed:12396720,
CC ECO:0000269|PubMed:12799444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-
CC adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84;
CC Evidence={ECO:0000269|PubMed:12799444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34408;
CC Evidence={ECO:0000269|PubMed:12799444};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by
CC dsRNA generated during the course of viral infection. The dsRNA
CC activator must be at least 15 nucleotides long, and no modification of
CC the 2'-hydroxyl group is tolerated. ssRNA or dsDNA do not act as
CC activators. {ECO:0000269|PubMed:12799444}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.66 mM for ATP {ECO:0000269|PubMed:12799444};
CC Note=kcat is 0.39 sec(-1) with ATP as substrate.
CC {ECO:0000269|PubMed:12799444};
CC -!- TISSUE SPECIFICITY: Strongly expressed in spleen dendritic cells,
CC whereas, in bone marrow-derived dendritic cells, the amount increases
CC during the maturation process. Expressed in many organs, the highest
CC levels being in thymus, lung, and bone marrow.
CC {ECO:0000269|PubMed:12396720}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; AF068835; AAD02818.1; -; mRNA.
DR EMBL; AK010034; BAB26655.1; -; mRNA.
DR EMBL; AK150492; BAE29608.1; -; mRNA.
DR EMBL; AC116500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39226.1; -.
DR RefSeq; NP_035984.2; NM_011854.2.
DR RefSeq; XP_006530377.1; XM_006530314.3.
DR RefSeq; XP_006530378.1; XM_006530315.3.
DR AlphaFoldDB; Q9Z2F2; -.
DR SMR; Q9Z2F2; -.
DR MINT; Q9Z2F2; -.
DR STRING; 10090.ENSMUSP00000031542; -.
DR iPTMnet; Q9Z2F2; -.
DR PhosphoSitePlus; Q9Z2F2; -.
DR MaxQB; Q9Z2F2; -.
DR PaxDb; 10090-ENSMUSP00000031542; -.
DR ProteomicsDB; 291934; -.
DR DNASU; 23962; -.
DR Ensembl; ENSMUST00000031542.13; ENSMUSP00000031542.10; ENSMUSG00000029561.18.
DR GeneID; 23962; -.
DR KEGG; mmu:23962; -.
DR UCSC; uc008zcu.1; mouse.
DR AGR; MGI:1344390; -.
DR CTD; 23962; -.
DR MGI; MGI:1344390; Oasl2.
DR VEuPathDB; HostDB:ENSMUSG00000029561; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_040930_1_0_1; -.
DR InParanoid; Q9Z2F2; -.
DR OMA; AWEMGTD; -.
DR OrthoDB; 4638494at2759; -.
DR PhylomeDB; Q9Z2F2; -.
DR TreeFam; TF329749; -.
DR SABIO-RK; Q9Z2F2; -.
DR BioGRID-ORCS; 23962; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Oasl2; mouse.
DR PRO; PR:Q9Z2F2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z2F2; Protein.
DR Bgee; ENSMUSG00000029561; Expressed in small intestine Peyer's patch and 145 other cell types or tissues.
DR ExpressionAtlas; Q9Z2F2; baseline and differential.
DR Genevisible; Q9Z2F2; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IEP:ARUK-UCL.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IBA:GO_Central.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; TAS:UniProtKB.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR CDD; cd01811; Ubl1_OASL; 1.
DR Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR InterPro; IPR006117; 2-5OAS_C_CS.
DR InterPro; IPR043518; 2-5OAS_N_CS.
DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11258:SF7; 2'-5'-OLIGOADENYLATE SYNTHASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1.
DR Pfam; PF10421; OAS1_C; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Immunity; Innate immunity; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..508
FT /note="2'-5'-oligoadenylate synthase-like protein 2"
FT /id="PRO_0000160267"
FT DOMAIN 435..473
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT CONFLICT 469..473
FT /note="GPCAE -> AGGLT (in Ref. 1; AAD02818)"
FT /evidence="ECO:0000305"
FT CONFLICT 474..508
FT /note="Missing (in Ref. 1; AAD02818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 58767 MW; 9552B4540CC801A0 CRC64;
MDPFPDLYAT PGDSLDHFLE HSLQPQRDWK EEGQDAWERI ERFFREQCFR DELLLDQEVR
VIKVVKGGSS GKGTTLNHRS DQDMILFLSC FSSFEEQARN REVVISFIKK RLIHCSRSLA
YNIIVLTHRE GKRAPRSLTL KVQSRKTDDI IWMDILPAYD ALGPISRDSK PAPAIYETLI
RSKGYPGDFS PSFTELQRHF VKTRPVKLKN LLRLVKFWYL QCLRRKYGRG AVLPSKYALE
LLTIYAWEMG TESSDSFNLD EGFVAVMELL VNYRDICIYW TKYYNFQNEV VRNFLKKQLK
GDRPIILDPA DPTNNLGRRK GWEQVAAEAA FCLLQVCCTT VGPSERWNVQ RARDVQVRVK
QTGTVDWTLW TNPYSPIRKM KAEIRREKNF GGELRISFQE PGGERQLLSS RKTLADYGIF
SKVNIQVLET FPPEILVFVK YPGGQSKPFT IDPDDTILDL KEKIEDAGGP CAEDQVLLLD
DEELEDDESL KELEIKDCDT IILIRVID
//
