OAS1A_RAT
ID OAS1A_RAT Reviewed; 358 AA.
AC Q05961;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=2'-5'-oligoadenylate synthase 1A;
DE Short=(2-5')oligo(A) synthase 1A;
DE Short=2-5A synthase 1A;
DE EC=2.7.7.84 {ECO:0000250|UniProtKB:P11928};
GN Name=Oas1a; Synonyms=Oas1;
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].
RX PubMed=7764002; DOI=10.1038/nbt0993-1048;
RA Truve E., Aaspollu A., Honkanen J., Puska R., Mehto M., Hassi A.,
RA Teeri T.H., Kelve M., Seppanen P., Saarma M.;
RT "Transgenic potato plants expressing mammalian 2'-5' oligoadenylate
RT synthetase are protected from potato virus X infection under field
RT conditions.";
RL Biotechnology (N.Y.) 11:1048-1052(1993).
RN [2]
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. 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 higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP
CC which then bind to the inactive monomeric form of ribonuclease L (RNase
CC L) 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:0000250|UniProtKB:P00973}.
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:P11928};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00973};
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:0000250|UniProtKB:P00973}.
CC -!- SUBUNIT: Monomer. Homotetramer. Interacts with OAS1D.
CC {ECO:0000250|UniProtKB:P00973, ECO:0000250|UniProtKB:P11928,
CC ECO:0000303|PubMed:17024523}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11928}.
CC Mitochondrion {ECO:0000250|UniProtKB:P00973}. Nucleus
CC {ECO:0000250|UniProtKB:P00973}. Microsome
CC {ECO:0000250|UniProtKB:P00973}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P00973}. Note=Associated with different
CC subcellular fractions such as mitochondrial, nuclear, and rough/smooth
CC microsomal fractions. {ECO:0000250|UniProtKB:P00973}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; Z18877; CAA79317.1; -; mRNA.
DR PIR; S31407; S31407.
DR RefSeq; NP_620268.1; NM_138913.1.
DR AlphaFoldDB; Q05961; -.
DR SMR; Q05961; -.
DR STRING; 10116.ENSRNOP00000036734; -.
DR iPTMnet; Q05961; -.
DR PhosphoSitePlus; Q05961; -.
DR PaxDb; Q05961; -.
DR GeneID; 192281; -.
DR KEGG; rno:192281; -.
DR UCSC; RGD:621760; rat.
DR CTD; 246730; -.
DR RGD; 621760; Oas1a.
DR eggNOG; KOG0001; Eukaryota.
DR InParanoid; Q05961; -.
DR BRENDA; 2.7.7.84; 5301.
DR PRO; PR:Q05961; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140374; P:antiviral innate immune response; ISO:RGD.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:RGD.
DR GO; GO:0098586; P:cellular response to virus; ISO:RGD.
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:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:RGD.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 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; ISO:RGD.
DR GO; GO:0043129; P:surfactant homeostasis; ISO:RGD.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:RGD.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:RGD.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
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; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; ATP-binding; Cytoplasm; Endoplasmic reticulum; Immunity;
KW Innate immunity; Magnesium; Metal-binding; Microsome; Mitochondrion;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW RNA-binding; Transferase.
FT CHAIN 1..358
FT /note="2'-5'-oligoadenylate synthase 1A"
FT /id="PRO_0000160263"
FT REGION 14..61
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT REGION 201..211
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
SQ SEQUENCE 358 AA; 41666 MW; AE0F24E6A5D45BEA CRC64;
MEQELRSTPS WKLDKFIEVY LLPNTSFRDD VKSAINVLCD FLKERCFRDT VHPVRVSKVV
KGGSSGKGTT LKGKSDADLV VFLNNFTSFE DQLNRRGEFI KEIKKQLYEV QREKHFRVKF
EVQSSWWPNP RALSFKLSAP HLQQEVEFDV LPAYDVLGHV SLYSNPDPKI YTILISECIS
LGKDGEFSTC FTELQRNFLK QRPTKLKSLI RLVKHWYQLC KEKLGKPLPP QYALELLTVY
AWERGNGITE FNTAQGFRTI LELVTKYQQL RIYWTKYYDF QHPDVSKYLH RQLRKSRPVI
LDPADPTGNV AGGNQEGWRR LASEARLWLQ YPCFMNRGGS PVSSWEVPVD EAWSCILL
