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Database: UniProt
Entry: B6RC85_PANTR
LinkDB: B6RC85_PANTR
Original site: B6RC85_PANTR 
ID   B6RC85_PANTR            Unreviewed;       719 AA.
AC   B6RC85; A0A2J8MYF2;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=2'-5' oligoadenylate synthase {ECO:0000256|ARBA:ARBA00012577};
DE            EC=2.7.7.84 {ECO:0000256|ARBA:ARBA00012577};
GN   Name=OAS2 {ECO:0000313|EMBL:ACJ13122.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000049895.3, ECO:0000313|VGNC:VGNC:5517};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:ACJ13122.1};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000049895.3, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:ACJ13122.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Coriell NG06939 {ECO:0000313|EMBL:ACJ13122.1};
RC   TISSUE=Skin {ECO:0000313|EMBL:ACJ13122.1};
RA   Magness C.L., Steiger K.V., Scherer C.A., Fellin P.C., Olson A.N.,
RA   Guillaudeux T., Miner D.G., Rosenberg G., Berthier A.M., Carithers R.L.,
RA   Green P., Growe G.H., Hagan H., Hough E., Justesen J., Katze M.G.,
RA   Mathisen T.L., Myers R.M., Shuhart M.C., Iadonato S.P.;
RT   "Human immune diversity and evidence of balancing natural selection in
RT   oligoadenylate synthetases.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000049895.3}
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; AACZ04070338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; EF364089; ACJ13122.1; -; Genomic_DNA.
DR   RefSeq; XP_001151534.1; XM_001151534.4.
DR   STRING; 9598.ENSPTRP00000049895; -.
DR   PaxDb; 9598-ENSPTRP00000049895; -.
DR   Ensembl; ENSPTRT00000010057.6; ENSPTRP00000049895.3; ENSPTRG00000005479.6.
DR   GeneID; 739230; -.
DR   KEGG; ptr:739230; -.
DR   CTD; 4939; -.
DR   VGNC; VGNC:5517; OAS2.
DR   eggNOG; KOG0001; Eukaryota.
DR   GeneTree; ENSGT00510000046406; -.
DR   HOGENOM; CLU_026275_0_0_1; -.
DR   OMA; KQCERKM; -.
DR   OrthoDB; 4638494at2759; -.
DR   TreeFam; TF329749; -.
DR   Proteomes; UP000002277; Chromosome 12.
DR   Bgee; ENSPTRG00000005479; Expressed in liver and 19 other cell types or tissues.
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; IEA:Ensembl.
DR   GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR   GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
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; IEA:Ensembl.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:Ensembl.
DR   GO; GO:0060337; P:type I interferon-mediated signaling pathway; IEA:Ensembl.
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; 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: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   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 2.
DR   PROSITE; PS00832; 25A_SYNTH_1; 2.
DR   PROSITE; PS00833; 25A_SYNTH_2; 2.
DR   PROSITE; PS50152; 25A_SYNTH_3; 2.
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:UP000002277}.
FT   DOMAIN          154..337
FT                   /note="2'-5'-oligoadenylate synthetase 1"
FT                   /evidence="ECO:0000259|Pfam:PF10421"
FT   DOMAIN          373..438
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          497..684
FT                   /note="2'-5'-oligoadenylate synthetase 1"
FT                   /evidence="ECO:0000259|Pfam:PF10421"
SQ   SEQUENCE   719 AA;  82381 MW;  9670EEFC0BC3D946 CRC64;
     MGNGESQLSS VPAQKLGWFI QEYLKPYEEC QTLIDEMVNT ICDVLQEPEQ FPLVQGVAIG
     GSYGRKTVLR GNSDGTLVLF FSDLKQFQDQ KRSQRDILDK TGDKLKFCLF TKWMENNFEI
     QKSLDGFTIQ VFTKNQRISF EVLAAFNALS LNDNPSPWIY RELKRSLDKT NASPGEFAVC
     FTELQQKFFD NRPGKLKDLI LLIKHWHQQC QKKIKNLPSL SPYALELLTV YAWEQGCRKD
     NFDIAEGVRT VLKLIKCQEQ LCVYWMVNYN FEDETIRNIL LHQLQSARPV ILDPVDPTNN
     VSGDKICWQW LKKEAQTWLT SPNLDNELPA PSWNVLPAPL FTTPGHLLDK FIKEFLQPNK
     CFLEQIDSAV NIICTFLKEN CFRQSTAKIQ IVRGGSTAKG TALKTGSDAD LVVFHNSLKS
     YTSQKNERHK IVKEIHEQLK AFWREKEEEL EVSFEPPKWK APRVLSFSLK SKVLNESVSF
     DVLPAFNALG QLSSGSTPSP EVYAGLIDLY KSSDLPGGEF STCFTVLQRN FIRSRPTKLK
     DLIRLVKHWY KECERKLKPK GSLPPKYALE LLTIYAWEQG SGVPDFDTAE GFRTVLELVT
     QYQQLCIFWK VNYNFEDETV RKFLLSQLQK TRPVILDPAE PTGDVGGGDR WCWHLLAKEA
     KEWLSSPCFK DGTGNPIPPW KVPTMQTPGS CGARIHPIVN EMFSSRSHRI LNNNSKRNF
//
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