ID   OASL1_RAT               Reviewed;         512 AA.
AC   G3V645; Q5MYW3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=2'-5'-oligoadenylate synthase-like protein 1;
GN   Name=Oasl;
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=Ovary;
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].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-
CC       stranded RNA. Displays antiviral activity via an alternative antiviral
CC       pathway independent of RNase L (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Specifically interacts with the ligand binding domain of the
CC       thyroid receptor (TR). TRIP14 does not require the presence of thyroid
CC       hormone for its interaction. Binds MBD1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR   EMBL; AY227756; AAP55510.1; -; mRNA.
DR   EMBL; CH473973; EDM13919.1; -; Genomic_DNA.
DR   RefSeq; NP_001009681.1; NM_001009681.1.
DR   AlphaFoldDB; G3V645; -.
DR   SMR; G3V645; -.
DR   STRING; 10116.ENSRNOP00000001570; -.
DR   iPTMnet; G3V645; -.
DR   PhosphoSitePlus; G3V645; -.
DR   PaxDb; G3V645; -.
DR   PRIDE; G3V645; -.
DR   Ensembl; ENSRNOT00000001570; ENSRNOP00000001570; ENSRNOG00000001187.
DR   GeneID; 304545; -.
DR   KEGG; rno:304545; -.
DR   UCSC; RGD:1308586; rat.
DR   CTD; 8638; -.
DR   RGD; 1308586; Oasl.
DR   eggNOG; KOG0001; Eukaryota.
DR   GeneTree; ENSGT00510000046406; -.
DR   HOGENOM; CLU_040930_1_0_1; -.
DR   InParanoid; G3V645; -.
DR   OMA; VICIYWT; -.
DR   OrthoDB; 611234at2759; -.
DR   PhylomeDB; G3V645; -.
DR   TreeFam; TF329749; -.
DR   PRO; PR:G3V645; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Proteomes; UP000234681; Chromosome 12.
DR   Bgee; ENSRNOG00000001187; Expressed in stomach and 16 other tissues.
DR   Genevisible; G3V645; RN.
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:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
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:0070106; P:interleukin-27-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; ISO:RGD.
DR   GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISO:RGD.
DR   GO; GO:0060700; P:regulation of ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0009615; P:response to virus; ISS:UniProtKB.
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; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11258; PTHR11258; 1.
DR   Pfam; PF10421; OAS1_C; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 2.
DR   SUPFAM; SSF54236; SSF54236; 2.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   PROSITE; PS00833; 25A_SYNTH_2; 1.
DR   PROSITE; PS50152; 25A_SYNTH_3; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Antiviral defense; Cytoplasm; Immunity; Innate immunity; Nucleus;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..512
FT                   /note="2'-5'-oligoadenylate synthase-like protein 1"
FT                   /id="PRO_0000418633"
FT   DOMAIN          351..430
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          431..507
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CONFLICT        350
FT                   /note="D -> Y (in Ref. 1; AAP55510)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  58968 MW;  0A57272139AB0BFE CRC64;
     MAVAQELYSF PASKLDSFVA QWLQPTREWK EEVLETVQTV EQFLRQENFR GERGPAQDVR
     VLKVLKVGCF GNGTVLRSTT DVELVVFLSC FHSFQEEAKH HQAVLRLIQK RMSYCRDLLD
     LGLSNLSVIE EVPSSLIFTI QTRETWEPIT VTIVPAFRAL GPSCPNSAEV YVNLIKANGY
     PGNFSPSFSE LQRSFVKHRP TKLKSLLRLV KHWYQQYVRD KCPRANLPPL YALELLTVYA
     WEAGTQEDSN FRLDEGLATV MELLQDHELL CIYWTKYYTL QHPVIERFVR RQLKGERPII
     LDPADPTHNV AQGYRWDIVA QRASQCLKQD CCYDDRDAPV PSWTVKRAPD IQVTVQQWGH
     PDLILWVNPY EPIKKLKEKI RLSRGYSGLQ RLSFQEPGGQ RQLIRSQCSL AYYGIFCDTQ
     ICLLDTISPE IQVFVKNPDG GSHAYAIHPL DFVLSLKQQI EDRQGLQSQE QQLEFQGRVL
     EDWFDFKSYG IQDSITIILS RKREGKAPSA PS