F1N3B8 (OAS2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2'-5'-oligoadenylate synthase 2
Short name=(2-5')oligo(A) synthase 2
Short name=2-5A synthase 2
EC=2.7.7.84

Gene names

Name:

OAS2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	714 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate.
Cofactor	Magnesium Potential.
Enzyme regulation	Produced as a latent enzyme which is activated by dsRNA generated during the course of viral infection. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. ssRNA or dsDNA do not act as activators By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Mitochondrion By similarity. Nucleus By similarity. Microsome By similarity. Endoplasmic reticulum By similarity. Note: Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions By similarity.
Post-translational modification	Myristoylation is not essential for its activity By similarity. Glycosylated. Glycosylation is essential for its activity By similarity.
Sequence similarities	Belongs to the 2-5A synthase family.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm Endoplasmic reticulum Microsome Mitochondrion Nucleus
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding RNA-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Glycoprotein Lipoprotein Myristate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA catabolic process Inferred from electronic annotation. Source: Compara defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW protein glycosylation Inferred from sequence or structural similarity. Source: UniProtKB protein myristoylation Inferred from sequence or structural similarity. Source: UniProtKB purine nucleotide biosynthetic process Inferred from electronic annotation. Source: Compara response to virus Traceable author statement Ref.1. Source: UniProtKB
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	2'-5'-oligoadenylate synthetase activity Inferred from sequence or structural similarity. Source: UniProtKB ATP binding Inferred from sequence or structural similarity. Source: UniProtKB double-stranded RNA binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 714	714	2'-5'-oligoadenylate synthase 2		PRO_0000418627
Regions
	Region	11 – 336	326	OAS domain 1
	Region	344 – 683	340	OAS domain 2
Sites
	Metal binding	409	1	Magnesium; catalytic Potential
	Metal binding	480	1	Magnesium; catalytic Potential
	Binding site	544	1	ATP By similarity
	Binding site	544	1	Substrate By similarity
Amino acid modifications
	Lipidation	2	1	N-myristoyl glycine By similarity
Experimental info
	Sequence conflict	161	1	S → T in AAT44896. Ref.1
	Sequence conflict	219	1	S → P in AAT44896. Ref.1
	Sequence conflict	277	1	I → T in AAT44896. Ref.1
	Sequence conflict	522	1	A → V in AAT44896. Ref.1
	Sequence conflict	551	1	C → K in AAT44896. Ref.1
	Sequence conflict	573	1	S → T in AAT44896. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	F1N3B8 [UniParc]. Last modified May 3, 2011. Version 1. Checksum: 6962A98CC6D437BA	FASTA	714	81,967
	10 20 30 40 50 60 MGSRESHLYE KPSEKLEEFI QNHLRPSEDC QKDIDQSVDT ICEVLQEPCP SLTVTGVAKG 70 80 90 100 110 120 GSYGRRTVLR GNSDGILVVF FGDLEQFQDQ EKRQYELLSK IWAQMKHCES TWKLAAKMEL 130 140 150 160 170 180 QNTNRSSRVT IQLSTKQQSI TFNVLPAFNA LGLSEKSSLW SYRELKRSLD MVKARPGEFS 190 200 210 220 230 240 VCFTELQEKF FSNYPSKLKD LILLVKHWFQ KCQEKLINSS LLPPYALELL TVYAWEQGCG 250 260 270 280 290 300 AEDFDMAEGV RTVLRLIEKQ EQLCVYWTVN YNFGDEIVRN ILLSQLQAPR PVILDPTDPT 310 320 330 340 350 360 NNVSMDNTCW LQLKHEAQNW LRSLRQNESP GPSWNVLPAS LYITPGHLLD KFVKDFLQPN 370 380 390 400 410 420 QTFQDQIKKA LKIICSFLEE NCFRHSTTKI QVIQGGSTVK GTALKTGSDA SLVVFANSLK 430 440 450 460 470 480 SYTSPKNERY NIIKEIHEQL EACRQEKDFE VKFEISKWKP PWVLSFTLKS KVLNESVDFD 490 500 510 520 530 540 VLPAFNALGE LKSGSTPSPR TYTELIHLYK PSDVFLEGEF SACFTKLQRN FVRSLPLKLK 550 560 570 580 590 600 DLIRLLKHWY CGCEKKLKQK GSLPPKYALE LLSIYAWEKG SGAQDFDMAE GFRTVLELVI 610 620 630 640 650 660 QYQHLCVFWT VNYSFDDEIL RNFLLGQIRR TRPVILDPAD PTGDVGGGHR WCWHLLAKEA 670 680 690 700 710 TEWLSSLCFK DKSGCPIQPW NVPKKRVQTP GSCGAGIYSM VNEMHLLRSH RFLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for concerted evolution of paralogous Oas1 genes in Rodentia and Artiodactyla." Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A. J. Mol. Evol. 63:562-576(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of taurine cattle: a window to ruminant biology and evolution." The bovine genome sequencing and analysis consortium Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hereford.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY599197 mRNA. Translation: AAT44896.1. DAAA02045423 Genomic DNA. No translation available. DAAA02045424 Genomic DNA. No translation available. DAAA02045425 Genomic DNA. No translation available.
IPI	IPI00904754.
RefSeq	NP_001019728.1. NM_001024557.1.
UniGene	Bt.41610.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000019477; ENSBTAP00000019477; ENSBTAG00000014628.
GeneID	529660.
KEGG	bta:529660.
Organism-specific databases
CTD	4939.
Phylogenomic databases
GeneTree	ENSGT00510000046406.
HOVERGEN	HBG007855.
KO	K14216.
OMA	YRELKRS.
Family and domain databases
Gene3D	1.10.1410.20. 2 hits.
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. [Graphical view]
PANTHER	PTHR11258. PTHR11258. 1 hit.
Pfam	PF10421. OAS1_C. 2 hits. [Graphical view]
PROSITE	PS00832. 25A_SYNTH_1. False negative. PS00833. 25A_SYNTH_2. 2 hits. PS50152. 25A_SYNTH_3. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	20875078.

Entry information

Entry name

OAS2_BOVIN

Accession

Primary (citable) accession number: F1N3B8
Secondary accession number(s): Q53AV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2012
Last sequence update:	May 3, 2011
Last modified:	May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program