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   24-JAN-2024, entry version 69.
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}.
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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; 9913-ENSBTAP00000019477; -.
DR   Ensembl; ENSBTAT00000019477.5; ENSBTAP00000019477.4; ENSBTAG00000014628.6.
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; KQCERKM; -.
DR   OrthoDB; 4638494at2759; -.
DR   TreeFam; TF329749; -.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000014628; Expressed in neutrophil and 88 other cell types or 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:0009615; P:response to virus; TAS:UniProtKB.
DR   GO; GO:0060337; P:type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR   CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 2.
DR   Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
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:SF3; 2'-5'-OLIGOADENYLATE SYNTHASE 2; 1.
DR   PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF10421; OAS1_C; 2.
DR   Pfam; PF18144; SMODS; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 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
//