OAS2_RAT
ID OAS2_RAT Reviewed; 733 AA.
AC Q5MYU0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=2'-5'-oligoadenylate synthase 2;
DE Short=(2-5')oligo(A) synthase 2;
DE Short=2-5A synthase 2;
DE EC=2.7.7.84;
GN Name=Oas2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
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. Activated
CC by detection of double stranded RNA (dsRNA): polymerizes higher
CC oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to
CC the inactive monomeric form of ribonuclease L (RNASEL) leading to its
CC dimerization and subsequent activation. Activation of RNASEL leads to
CC degradation of cellular as well as viral RNA, resulting in the
CC inhibition of protein synthesis, thus terminating viral replication.
CC Can mediate the antiviral effect via the classical RNASEL-dependent
CC pathway or an alternative antiviral pathway independent of RNASEL. In
CC addition, it may also play a role in other cellular processes such as
CC apoptosis, cell growth, differentiation and gene regulation (By
CC similarity). May act as a negative regulator of lactation, stopping
CC lactation in virally infected mammary gland lobules, thereby preventing
CC transmission of viruses to neonates (By similarity). Non-infected
CC lobules would not be affected, allowing efficient pup feeding during
CC infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9,
CC ECO:0000250|UniProtKB:P29728}.
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:0000250|UniProtKB:P29728};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29728};
CC -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by
CC double stranded RNA (dsRNA) generated during the course of viral
CC infection. The dsRNA activator must be at least 15 nucleotides long,
CC and no modification of the 2'-hydroxyl group is tolerated. ssRNA or
CC dsDNA do not act as activators. Strongly inhibited by copper, iron and
CC zinc ions. Partially inhibited by cobalt and nickel ions.
CC {ECO:0000250|UniProtKB:P29728}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29728}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29728}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}.
CC -!- PTM: Myristoylation is not essential for its activity.
CC {ECO:0000250|UniProtKB:P29728}.
CC -!- PTM: Glycosylated. Glycosylation is essential for its activity.
CC {ECO:0000250|UniProtKB:P29728}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; AY230746; AAP57396.1; -; mRNA.
DR RefSeq; NP_001009715.1; NM_001009715.1.
DR AlphaFoldDB; Q5MYU0; -.
DR SMR; Q5MYU0; -.
DR STRING; 10116.ENSRNOP00000066845; -.
DR iPTMnet; Q5MYU0; -.
DR PhosphoSitePlus; Q5MYU0; -.
DR PaxDb; Q5MYU0; -.
DR GeneID; 363938; -.
DR KEGG; rno:363938; -.
DR CTD; 4939; -.
DR RGD; 1359697; Oas2.
DR eggNOG; ENOG502S649; Eukaryota.
DR InParanoid; Q5MYU0; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; Q5MYU0; -.
DR PRO; PR:Q5MYU0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:RGD.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IBA:GO_Central.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:1903487; P:regulation of lactation; ISS:UniProtKB.
DR GO; GO:0060700; P:regulation of ribonuclease activity; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0009615; P:response to virus; TAS:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; ISO:RGD.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISS:UniProtKB.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 2.
DR Gene3D; 3.30.460.10; -; 2.
DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR InterPro; IPR026774; 2-5A_synthase.
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; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR11258; PTHR11258; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 2.
DR SUPFAM; SSF81301; SSF81301; 2.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 2.
DR PROSITE; PS50152; 25A_SYNTH_3; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Antiviral defense; ATP-binding; Cytoplasm; Glycoprotein;
KW Immunity; Innate immunity; Lipoprotein; Magnesium; Metal-binding;
KW Myristate; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Repeat; RNA-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT CHAIN 2..733
FT /note="2'-5'-oligoadenylate synthase 2"
FT /id="PRO_0000418629"
FT REGION 47..365
FT /note="OAS domain 1"
FT REGION 373..713
FT /note="OAS domain 2"
FT BINDING 427
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT MOD_RES 408
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P29728"
SQ SEQUENCE 733 AA; 84066 MW; 136B28AAE998544D CRC64;
MGNWMPGWSS SGSLGVPPMP VQKLEKSVQV NLEPDEKCLS QTEVSSVPSQ KLEEYIQANL
KPDEESLKQI DQAVDAISDL LCSEVMIDVL KVVKGGSYGR KTVLRDCSDG TLVLFTGLFK
QFQDQKKYQD KLLDLIEQRL KSHEKYKKSV KRKLSLLEVQ VSIPGQSILL QLLPTFNPLC
ISENPSAQVY QNLKRSMDQV KASPGEFSDC FTTLQQRFFE KYPGRLKDLI LLVKHWYKQL
QDKWIIPSPP PLLYALELLT VYAWEQGCQT KDFDITQGIR TVLQLISQPT NLCVYWLDNY
NFEDETVRNN LLHQLNSPRP VILDPTDPTN NVGKDDRFWQ LLAEEAQEWL NSLRLNKPHK
PCWDVLPMPF FITPSHCLDK FIKDFLQPDK VFLNQIKRAV DIICSFLKET CFQNSDIKVL
KIIKGGSTAK GTALQQRSDA DIIVFLSSLD SYDSLETERS QYVQEIRKQL EACQKAFNLG
VKFDISKWMA PRVLSFTLES KSLKQSVEFD VLPAYDALGQ LRSDYTSRLK AYKKLIELYA
SQDSLKGGEF SVCFTELQRD FIETRPTKLK GLIRLIKHWY KQCERKMKPK ASLPPKYALE
LLTVYAWEHG SGTDGFDTAE GFRTVLDLVI RYRQLCVFWT VNYNFEEDHM RKFLLTQIQK
KRPVILDPAD PTGDVGGGDR WCWHLLAKEA KEWLSSSCFQ VEPKSPVQPW KVPVVQTPGS
CGAQIYPVVG GVY
