| Tag | Content |
|---|
| CPLM ID | CPLM-024144 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 2'-5'-oligoadenylate synthase-like protein 2 |
Protein Synonyms/Alias | 54 kDa 2'-5'-oligoadenylate synthase-like protein; p54 OASL; M1204 |
Gene Name | Oasl2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 183 | YETLIRSKGYPGDFS | 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. Synthesizes oligomers 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 | DOMAIN 435 473 Ubiquitin-like.
METAL 81 81 Magnesium; catalytic (Potential).
METAL 83 83 Magnesium; catalytic (Potential).
METAL 154 154 Magnesium; catalytic (Potential).
BINDING 213 213 ATP (By similarity).
BINDING 213 213 Substrate (By similarity). |
Keyword | Antiviral defense; ATP-binding; Complete proteome; Immunity; Innate immunity; Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 508 AA |
Protein Sequence | MDPFPDLYAT PGDSLDHFLE HSLQPQRDWK EEGQDAWERI ERFFREQCFR DELLLDQEVR 60
VIKVVKGGSS GKGTTLNHRS DQDMILFLSC FSSFEEQARN REVVISFIKK RLIHCSRSLA 120
YNIIVLTHRE GKRAPRSLTL KVQSRKTDDI IWMDILPAYD ALGPISRDSK PAPAIYETLI 180
RSKGYPGDFS PSFTELQRHF VKTRPVKLKN LLRLVKFWYL QCLRRKYGRG AVLPSKYALE 240
LLTIYAWEMG TESSDSFNLD EGFVAVMELL VNYRDICIYW TKYYNFQNEV VRNFLKKQLK 300
GDRPIILDPA DPTNNLGRRK GWEQVAAEAA FCLLQVCCTT VGPSERWNVQ RARDVQVRVK 360
QTGTVDWTLW TNPYSPIRKM KAEIRREKNF GGELRISFQE PGGERQLLSS RKTLADYGIF 420
SKVNIQVLET FPPEILVFVK YPGGQSKPFT IDPDDTILDL KEKIEDAGGP CAEDQVLLLD 480
DEELEDDESL KELEIKDCDT IILIRVID 508 |
Gene Ontology | GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB. 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:0006164; P:purine nucleotide biosynthetic process; IDA:UniProtKB. GO:0009615; P:response to virus; TAS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |