OAS2_BOVIN
ID OAS2_BOVIN Reviewed; 714 AA.
AC F1N3B8; Q53AV7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY599197; AAT44896.1; -; mRNA.
DR EMBL; DAAA02045423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02045424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02045425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001019728.1; NM_001024557.1.
DR AlphaFoldDB; F1N3B8; -.
DR SMR; F1N3B8; -.
DR STRING; 9913.ENSBTAP00000019477; -.
DR PaxDb; F1N3B8; -.
DR PRIDE; F1N3B8; -.
DR Ensembl; ENSBTAT00000019477; ENSBTAP00000019477; ENSBTAG00000014628.
DR GeneID; 529660; -.
DR KEGG; bta:529660; -.
DR CTD; 4939; -.
DR VEuPathDB; HostDB:ENSBTAG00000014628; -.
DR VGNC; VGNC:32391; OAS2.
DR eggNOG; ENOG502S649; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_026275_0_0_1; -.
DR InParanoid; F1N3B8; -.
DR OMA; WMKDSFE; -.
DR OrthoDB; 611234at2759; -.
DR TreeFam; TF329749; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000014628; Expressed in neutrophil and 88 other tissues.
DR ExpressionAtlas; F1N3B8; baseline and differential.
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; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
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:0009615; P:response to virus; TAS:UniProtKB.
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; 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; PS00833; 25A_SYNTH_2; 2.
DR PROSITE; PS50152; 25A_SYNTH_3; 2.
PE 2: Evidence at transcript level;
KW Antiviral defense; ATP-binding; Cytoplasm; Glycoprotein; Immunity;
KW Innate immunity; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Repeat;
KW RNA-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT CHAIN 2..714
FT /note="2'-5'-oligoadenylate synthase 2"
FT /id="PRO_0000418627"
FT REGION 11..336
FT /note="OAS domain 1"
FT REGION 344..683
FT /note="OAS domain 2"
FT BINDING 397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 409
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P29728"
FT CONFLICT 161
FT /note="S -> T (in Ref. 1; AAT44896)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="S -> P (in Ref. 1; AAT44896)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="I -> T (in Ref. 1; AAT44896)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="A -> V (in Ref. 1; AAT44896)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="C -> K (in Ref. 1; AAT44896)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="S -> T (in Ref. 1; AAT44896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 81967 MW; 6962A98CC6D437BA CRC64;
MGSRESHLYE KPSEKLEEFI QNHLRPSEDC QKDIDQSVDT ICEVLQEPCP SLTVTGVAKG
GSYGRRTVLR GNSDGILVVF FGDLEQFQDQ EKRQYELLSK IWAQMKHCES TWKLAAKMEL
QNTNRSSRVT IQLSTKQQSI TFNVLPAFNA LGLSEKSSLW SYRELKRSLD MVKARPGEFS
VCFTELQEKF FSNYPSKLKD LILLVKHWFQ KCQEKLINSS LLPPYALELL TVYAWEQGCG
AEDFDMAEGV RTVLRLIEKQ EQLCVYWTVN YNFGDEIVRN ILLSQLQAPR PVILDPTDPT
NNVSMDNTCW LQLKHEAQNW LRSLRQNESP GPSWNVLPAS LYITPGHLLD KFVKDFLQPN
QTFQDQIKKA LKIICSFLEE NCFRHSTTKI QVIQGGSTVK GTALKTGSDA SLVVFANSLK
SYTSPKNERY NIIKEIHEQL EACRQEKDFE VKFEISKWKP PWVLSFTLKS KVLNESVDFD
VLPAFNALGE LKSGSTPSPR TYTELIHLYK PSDVFLEGEF SACFTKLQRN FVRSLPLKLK
DLIRLLKHWY CGCEKKLKQK GSLPPKYALE LLSIYAWEKG SGAQDFDMAE GFRTVLELVI
QYQHLCVFWT VNYSFDDEIL RNFLLGQIRR TRPVILDPAD PTGDVGGGHR WCWHLLAKEA
TEWLSSLCFK DKSGCPIQPW NVPKKRVQTP GSCGAGIYSM VNEMHLLRSH RFLD
