OAS3_RAT
ID OAS3_RAT Reviewed; 1137 AA.
AC Q5MYT7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=2'-5'-oligoadenylate synthase 3;
DE Short=(2-5')oligo(A) synthase 3;
DE Short=2-5A synthase 3;
DE EC=2.7.7.84;
GN Name=Oas3;
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=Large intestine;
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. In
CC addition, it may also play a role in other cellular processes such as
CC apoptosis, cell growth, differentiation and gene regulation.
CC Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from
CC ATP which then bind to the inactive monomeric form of ribonuclease L
CC (RNase L) leading to its dimerization and subsequent activation.
CC Activation of RNase L leads to degradation of cellular as well as viral
CC RNA, 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 (By similarity). {ECO:0000250}.
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 -!- 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. Strongly
CC activated by long dsRNAs at least 50 nucleotides in length. ssRNA does
CC not activate the enzyme. {ECO:0000250|UniProtKB:Q9Y6K5}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y6K5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: OAS domain 3 is catalytically active. OAS domain 1 has no
CC catalytic activity but is essential for recognition of long dsRNAs.
CC {ECO:0000250|UniProtKB:Q9Y6K5}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; AY250706; AAP76224.1; -; mRNA.
DR RefSeq; NP_001009493.1; NM_001009493.1.
DR AlphaFoldDB; Q5MYT7; -.
DR SMR; Q5MYT7; -.
DR PaxDb; Q5MYT7; -.
DR PRIDE; Q5MYT7; -.
DR GeneID; 494202; -.
DR KEGG; rno:494202; -.
DR CTD; 4940; -.
DR RGD; 1359319; Oas3.
DR eggNOG; ENOG502S649; Eukaryota.
DR InParanoid; Q5MYT7; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; Q5MYT7; -.
DR PRO; PR:Q5MYT7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; 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; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039530; P:MDA-5 signaling pathway; ISO:RGD.
DR GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; ISO:RGD.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; ISO:RGD.
DR GO; GO:0035395; P:negative regulation of chemokine (C-X-C motif) ligand 9 production; ISO:RGD.
DR GO; GO:0071659; P:negative regulation of IP-10 production; ISO:RGD.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISO:RGD.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:RGD.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:RGD.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0060700; P:regulation of ribonuclease activity; ISO:RGD.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR GO; GO:0039529; P:RIG-I signaling pathway; ISO:RGD.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 3.
DR Gene3D; 3.30.460.10; -; 3.
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; 2.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 3.
DR SUPFAM; SSF81301; SSF81301; 3.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 2.
DR PROSITE; PS50152; 25A_SYNTH_3; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Antiviral defense; ATP-binding; Cytoplasm; Immunity;
KW Innate immunity; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; RNA-binding;
KW Transferase.
FT CHAIN 1..1137
FT /note="2'-5'-oligoadenylate synthase 3"
FT /id="PRO_0000418631"
FT REGION 6..341
FT /note="OAS domain 1"
FT /evidence="ECO:0000305"
FT REGION 12..56
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT REGION 185..199
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT REGION 342..461
FT /note="Linker"
FT /evidence="ECO:0000305"
FT REGION 434..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..792
FT /note="OAS domain 2"
FT /evidence="ECO:0000305"
FT REGION 800..1134
FT /note="OAS domain 3"
FT /evidence="ECO:0000305"
FT COMPBIAS 434..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 854
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 866
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 868
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 938
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 997
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT BINDING 1000
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 1019
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT SITE 154
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT SITE 242
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K5"
SQ SEQUENCE 1137 AA; 126205 MW; B46A310B613485DF CRC64;
MDLYHTPAGA LDKLVAHSLH PAPEFTAAVR RALGSLDNVL RKNGAGGLQR PRVIRIIKGG
AHARGTALRG GTDVELVIFL DCLRSFGDQK TCHTEILGAI QALLESWGCN PGPGLTFEFS
GPKASGILQF RLASVDQENW IDVSLVPAFD ALGQLHSEVK PTPNVYSSLL SSHCQAGEHS
ACFTELRKNF VNIRPVKLKN LILLVKHWYR QVQTQVVRAT LPPSYALELL TIFAWEQGCR
KDAFSLAQGL RTVLALIQRN KHLCIFWTEN YGFEDPAVGE FLRRQLKRPR PVILDPADPT
WDLGNGTAWC WDVLAKEAEY SFNQQCFKEA SGALVQPWEG PGLPCAGILD LGHPIQQGAK
HALEDNNGHL AVQPMKESLQ PSNPARGLPE TATKISAMPD PTVTETHKSL KKSVHPKTVS
ETVVNPSSHV WITQSTASSN TPPGHSSMST AGSQMGPDLS QIPSKELDSF IQDHLRPSSQ
FQQQVRQAID TILCCLREKC VDKVLRVSKG GSFGRGTDLR GKCDVELVIF YKTLGDFKGQ
NSHQTEILCD MQAQLQRWCQ NPAPGLSLQF IEQKSNALHL QLVPTNLSNR VDLSVLPAFD
AVGPLKSGAK PLPETYSSLL SSGCQAGEHA ACFAELRRNF INTRPAKLRS LMLLVKHWYR
QVAARFEGGE TAGAALPPAY ALELLTVFAW EQGCGEQKFS MAEGLRTVLR LVQQHQSLCI
YWTVNYSVQD PAIRAHLLRQ LRKARPLILD PADPTWNMDQ GNWKLLAQEA AALESQVCLQ
SRDGNLVPPW DVMPALLHQT PAQNLDKFIC EFLQPDRHFL TQVKRAVDTI CSFLKENCFR
NSTIKVLKVV KGGSSAKGTA LQGRSDADLV VFLSCFRQFS EQGSHRAEII AEIQAQLEAC
QQKQRFDVKF EISKRKNPRV LSFTLTSKTL LGQSVDFDVL PAFDALGQLK SGSRPDPRVY
TDLIQSYSNA GEFSTCFTEL QRDFISSRPT KLKSLIRLVK HWYQQCNKTV KGKGSLPPQH
GLELLTVYAW ERGSQNPQFN MAEGFRTVLE LIGQYRQLCV YWTINYGAED ETIGDFLKMQ
LQKPRPVILD PADPTGNLGH NARWDLLAKE AAAYTSALCC MDKDGNPIKP WPVKAAV
