| Tag |
Content |
| dbPAF ID |
dbPAF-0051002 |
| Uniprot Accession |
E9Q9A9; OAS2_MOUSE; Q8K4E5; Q8VI92;
|
| Genbank Protein ID |
NP_660262.2; XP_006530388.1;
|
| Genbank Nucleotide ID |
NM_145227.3; XM_006530325.2;
|
| Protein Name |
2'-5'-oligoadenylate synthase 2 |
| Protein Synonyms/Alias |
|
| Gene Name |
Oas2 |
| Gene Synonyms/Alias |
oasl11; |
| Organism |
Mus musculus(Mouse) |
| NCBI Taxa ID |
10090 |
Functional Description
(View all) |
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 higher 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.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 higher 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. |
Phosphorylation Sites
|
dbPAF PTMs: 2 |
Sequence
(Fasta) | MGNWLTGNWS SDRSSGYSSG WSPGGSSGVP SGPVHKLEKS IQANLTPNEN CLKQIAVSSV 60
PSQKLEGYIQ ENLKPNRESL KQIDQAVDAI WDLLRSQIPV KEVAKGGSYG RETALRGCSD 120
GTLVLFMDCF QQFQDQIKYQ DAYLDVIELW LKIHEKKSVK HEHALVVQVS VPGQRILLQL 180
LPVFNPLRSN ENPSSCVYVD LKKSMDQVRA SPGEFSDCFT TLQQRFFKKY PQRLKDLILL 240
VKHWYEQCQE KWKTPPPQPL LYALELLTVY AWEQGCQAED FDMAQGVRTV LRLIQRPTEL 300
CVYWTVNYNF EDETVRNILL HQLRSQRPVI LDPTDPTNNV GKDDGFWELL TEEAMAWLYS 360
PSLNTESPAP YWDVLPMPLF VTPSHLLNKF IKDFLQPNKL FLKQIKEAVD IICSFLKNVC 420
FLNSDTKVLK TVKGGSTAKG TALKRGSDAD IVVFLSSLES YDSLKTNRSQ FVQEIQKQLE 480
EFVQAQEWEV TFEISKWKAP RVLSFTLKSK TLNESVEFDV LPAYDALGQL RSDFTLRPEA 540
YKDLIELCAS QDIKEGEFSI CFTELQRNFI QTRPTKLKSL LRLIKHWYKQ YERKMKPKAS 600
LPPKYALELL TVYAWEQGSG TDDFDIAEGF RTVLDLVIKY RQLCIFWTVN YNFEEEYMRK 660
FLLTQIQKKR PVILDPADPT GDVGGGDRWC WHLLAEEAKE WLSSPCFQVE QKGLVQPWKV 720
PVMQTPGSCG GQIYPTVGGV TK
743Fasta Sequence
>E9Q9A9|Oas2|Mus musculus(Mouse)
MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILLHQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKLFLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLEEFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSICFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKYRQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKVPVMQTPGSCGGQIYPTVGGVTK
|
| Keyword |
KW-0007--Acetylation
KW-0025--Alternative splicing
KW-0051--Antiviral defense
KW-0067--ATP-binding
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0256--Endoplasmic reticulum
KW-0325--Glycoprotein
KW-0391--Immunity
KW-0399--Innate immunity
KW-0449--Lipoprotein
KW-0460--Magnesium
KW-0479--Metal-binding
KW-0492--Microsome
KW-0496--Mitochondrion
KW-0519--Myristate
KW-0547--Nucleotide-binding
KW-0548--Nucleotidyltransferase
KW-0539--Nucleus
KW-1185--Reference proteome
KW-0677--Repeat
KW-0694--RNA-binding
KW-0808--Transferase
|
| Interpro |
IPR006117--2-5-oligoadenylate_synth_CS
IPR006116--2-5-oligoadenylate_synth_N
IPR018952--2-5-oligoAdlate_synth_1_dom2/C
IPR026774--2-5A_synthase
IPR002934--Polymerase_NTP_transf_dom
|
| PROSITE |
PS00832--25A_SYNTH_1
PS00833--25A_SYNTH_2
PS50152--25A_SYNTH_3
|
| Pfam |
PF01909--NTP_transf_2
PF10421--OAS1_C
|
| Gene Ontology |
GO:0005737--C:cytoplasm
GO:0005783--C:endoplasmic reticulum
GO:0016020--C:membrane
GO:0005739--C:mitochondrion
GO:0005634--C:nucleus
GO:0048471--C:perinuclear region of cytoplasm
GO:0001730--F:2'-5'-oligoadenylate synthetase activity
GO:0005524--F:ATP binding
GO:0003725--F:double-stranded RNA binding
GO:0008270--F:zinc ion binding
GO:0051607--P:defense response to virus
GO:0045087--P:innate immune response
GO:0006486--P:protein glycosylation
GO:0018377--P:protein myristoylation
GO:0006164--P:purine nucleotide biosynthetic process
GO:0009615--P:response to virus
GO:0006401--P:RNA catabolic process
|
