ID I3MYC8_ICTTR Unreviewed; 393 AA.
AC I3MYC8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=2'-5' oligoadenylate synthase {ECO:0000256|ARBA:ARBA00012577};
DE EC=2.7.7.84 {ECO:0000256|ARBA:ARBA00012577};
GN Name=OAS1 {ECO:0000313|Ensembl:ENSSTOP00000017124.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000017124.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000017124.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001112};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family.
CC {ECO:0000256|ARBA:ARBA00009526}.
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DR EMBL; AGTP01090594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01090595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005336891.1; XM_005336834.1.
DR AlphaFoldDB; I3MYC8; -.
DR STRING; 43179.ENSSTOP00000017124; -.
DR Ensembl; ENSSTOT00000024817.2; ENSSTOP00000017124.2; ENSSTOG00000024010.2.
DR eggNOG; ENOG502RH25; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_040930_0_0_1; -.
DR InParanoid; I3MYC8; -.
DR OrthoDB; 4638494at2759; -.
DR TreeFam; TF329749; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
DR GO; GO:0071659; P:negative regulation of IP-10 production; IEA:Ensembl.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IEA:Ensembl.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
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:SF13; 2'-5'-OLIGOADENYLATE SYNTHASE 1; 1.
DR PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 48..107
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 162..346
FT /note="2'-5'-oligoadenylate synthetase 1"
FT /evidence="ECO:0000259|Pfam:PF10421"
SQ SEQUENCE 393 AA; 45467 MW; 99C0C4D969F233BB CRC64;
MDLRSVWASD LDKYIEDHLL PDTRFRKEVK KAIHIICSFL KERCFQGASH RVRVSKVVKG
GSSGKGTTLR GRSDADLVVF LENLTSFEDQ LEHRGLFITE IKKQLEACPK EKFDVKFRIQ
NSRWSNPRVL SFVLSSSDLS EEVEFDVLPA FDALGHLTKG YRPSPQIYVK LIQECISWER
EGEFSTCFTE LQRAFLKQRP TKLKSLIRLV KHWFQLCKEK LGKPLPPQYA LELLTVYAWE
RGSGESEFKM AQGFKTVLRL VIDYRQLCIY WTKYYDFEEP IIGTYLTQQL EKPRPVILDP
ADPTGNVGGG NPTGWYRLAQ EAKAWLKLPC FRKRDGSPVG IWDVPHMADL GTVWPFQQRG
YIRTAEDADL WCQNEYQADP LPQEDGNWTC TIL
//
