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Database: UniProt
Entry: F7EI55_MACMU
LinkDB: F7EI55_MACMU
Original site: F7EI55_MACMU 
ID   F7EI55_MACMU            Unreviewed;       413 AA.
AC   F7EI55;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   24-JAN-2024, entry version 50.
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|VGNC:VGNC:75570};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000016794.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000016794.4, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000016794.4,
RC   ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000016794.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000016794.4};
RG   Ensembl;
RL   Submitted (JUL-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   AlphaFoldDB; F7EI55; -.
DR   Ensembl; ENSMMUT00000017933.4; ENSMMUP00000016794.4; ENSMMUG00000012782.4.
DR   VEuPathDB; HostDB:ENSMMUG00000012782; -.
DR   VGNC; VGNC:75570; OAS1.
DR   eggNOG; ENOG502RH25; Eukaryota.
DR   GeneTree; ENSGT00510000046406; -.
DR   OMA; VHIISTF; -.
DR   Proteomes; UP000006718; Chromosome 11.
DR   Bgee; ENSMMUG00000012782; Expressed in colon and 21 other cell types or tissues.
DR   ExpressionAtlas; F7EI55; baseline.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; ISS:UniProtKB.
DR   GO; GO:0035457; P:cellular response to interferon-alpha; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
DR   GO; GO:0060700; P:regulation of ribonuclease activity; ISS:UniProtKB.
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:UP000006718}.
FT   DOMAIN          38..111
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          164..345
FT                   /note="2'-5'-oligoadenylate synthetase 1"
FT                   /evidence="ECO:0000259|Pfam:PF10421"
SQ   SEQUENCE   413 AA;  47268 MW;  FE1DCB3C2F6CA845 CRC64;
     MMDLRKTPAK SLDKFIEDYL LPDTHFRMQI NHAIDIICGF LKERCFRGSS YPVRVSKVVK
     GGSSGKGTSL RGRSDADLVV FLSPLTTFQD QLNRRGEFIR EIRKQLEACQ RERAFSVKFE
     VQAPRWDNPR ALSFVLSSPQ LGEGVEFDVL PAFDALGQLT GGYKPDPQIY VELIEECVSL
     QKEGEFSTCF TELQRNFLKQ RPTKLKSLIR LVKHWYQNCK KQLGKLPPQY ALELLTVYAW
     EQGSTETDFN TAQGFRTVLE LVINYQQLCV YWTKYYDFQN PIIGKYLSRQ LRKPRPVILD
     PADPTGNLGG GDTKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLPQHT PGSIHSAGRR
     ELDMHHPLNA SASAKGLQCY LDQPLHFQVG RLIQRGQRSS VSWCIIQDRT QVS
//
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