| Tag | Content |
|---|
| CPLM ID | CPLM-018225 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 2'-5'-oligoadenylate synthase 3 |
Protein Synonyms/Alias | (2-5')oligo(A) synthase 3; 2-5A synthase 3; 2',5'-oligoadenylate synthetase-like 10 |
Gene Name | Oas3 |
Gene Synonyms/Alias | oasl10 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1079 | KTIGDFLKMQLRKPR | ubiquitination | [1] | | 1084 | FLKMQLRKPRPVILD | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'- oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. |
Sequence Annotation | REGION 6 341 OAS domain 1.
REGION 342 462 Linker.
REGION 463 793 OAS domain 2.
REGION 801 1135 OAS domain 3.
METAL 867 867 Magnesium; catalytic (Potential).
METAL 869 869 Magnesium; catalytic (Potential).
METAL 939 939 Magnesium; catalytic (Potential).
BINDING 998 998 ATP (By similarity).
BINDING 998 998 Substrate (By similarity).
MOD_RES 1 1 N-acetylmethionine (By similarity). |
Keyword | Acetylation; Antiviral defense; ATP-binding; Complete proteome; Cytoplasm; Immunity; Innate immunity; Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; RNA-binding; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1138 AA |
Protein Sequence | MDLFHTPAGA LDKLVAHNLH PAPEFTAAVR GALGSLNITL QQHRARGSQR PRVIRIAKGG 60
AYARGTALRG GTDVELVIFL DCFQSFGDQK TCHSETLGAM RMLLESWGGH PGPGLTFEFS 120
QSKASRILQF RLASADGEHW IDVSLVPAFD VLGQPRSGVK PTPNVYSSLL SSHCQAGEYS 180
ACFTEPRKNF VNTRPAKLKN LILLVKHWYH QVQTRAVRAT LPPSYALELL TIFAWEQGCG 240
KDSFSLAQGL RTVLALIQHS KYLCIFWTEN YGFEDPAVGE FLRRQLKRPR PVILDPADPT 300
WDVGNGTAWR WDVLAQEAES SFSQQCFKQA SGVLVQPWEG PGLPRAGILD LGHPIYQGPN 360
QALEDNKGHL AVQSKERSQK PSNSAPGFPE AATKIPAMPN PSANKTRKIR KKAAHPKTVQ 420
EAALDSISSH VRITQSTASS HMPPDRSSIS TAGSRMSPDL SQIPSKDLDC FIQDHLRPSP 480
QFQQQVKQAI DAILCCLREK SVYKVLRVSK GGSFGRGTDL RGSCDVELVI FYKTLGDFKG 540
QKPHQAEILR DMQAQLRHWC QNPVPGLSLQ FIEQKPNALQ LQLASTDLSN RVDLSVLPAF 600
DAVGPLKSGT KPQPQVYSSL LSSGCQAGEH AACFAELRRN FINTCPPKLK SLMLLVKHWY 660
RQVVTRYKGG EAAGDAPPPA YALELLTIFA WEQGCGEQKF SLAEGLRTIL RLIQQHQSLC 720
IYWTVNYSVQ DPAIRAHLLC QLRKARPLVL DPADPTWNVG QGDWKLLAQE AAALGSQVCL 780
QSGDGTLVPP WDVTPALLHQ TLAEDLDKFI SEFLQPNRHF LTQVKRAVDT ICSFLKENCF 840
RNSTIKVLKV VKGGSSAKGT ALQGRSDADL VVFLSCFRQF SEQGSHRAEI ISEIQAHLEA 900
CQQMHSFDVK FEVSKRKNPR VLSFTLTSQT LLDQSVDFDV LPAFDALGQL RSGSRPDPRV 960
YTDLIHSCSN AGEFSTCFTE LQRDFITSRP TKLKSLIRLV KYWYQQCNKT IKGKGSLPPQ 1020
HGLELLTVYA WEQGGQNPQF NMAEGFRTVL ELIVQYRQLC VYWTINYSAE DKTIGDFLKM 1080
QLRKPRPVIL DPADPTGNLG HNARWDLLAK EATVYASALC CVDRDGNPIK PWPVKAAV 1138 |
Gene Ontology | GO:0005737; C:cytoplasm; ISS:UniProtKB. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:MGI. GO:0005524; F:ATP binding; ISS:UniProtKB. GO:0003725; F:double-stranded RNA binding; IDA:MGI. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. GO:0045087; P:innate immune response; IEA:UniProtKB-KW. GO:0045071; P:negative regulation of viral genome replication; IEA:Compara. GO:0060700; P:regulation of ribonuclease activity; IEA:Compara. GO:0009615; P:response to virus; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |