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F1N3B8

- OAS2_BOVIN

UniProt

F1N3B8 - OAS2_BOVIN

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Protein

2'-5'-oligoadenylate synthase 2

Gene

OAS2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate.

Cofactori

Magnesium.Curated

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi409 – 4091Magnesium; catalyticSequence Analysis
Metal bindingi480 – 4801Magnesium; catalyticSequence Analysis
Binding sitei544 – 5441ATPBy similarity
Binding sitei544 – 5441SubstrateBy similarity

GO - Molecular functioni

  1. 2'-5'-oligoadenylate synthetase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. double-stranded RNA binding Source: UniProtKB
  4. zinc ion binding Source: Ensembl

GO - Biological processi

  1. defense response to virus Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB-KW
  3. protein glycosylation Source: UniProtKB
  4. protein myristoylation Source: UniProtKB
  5. purine nucleotide biosynthetic process Source: Ensembl
  6. response to virus Source: UniProtKB
  7. RNA catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase 2 (EC:2.7.7.84)
Short name:
(2-5')oligo(A) synthase 2
Short name:
2-5A synthase 2
Gene namesi
Name:OAS2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 17

Subcellular locationi

Cytoplasm By similarity. Cytoplasmperinuclear 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

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. mitochondrion Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
  4. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 7147132'-5'-oligoadenylate synthase 2PRO_0000418627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity

Post-translational modificationi

Myristoylation is not essential for its activity.By similarity
Glycosylated. Glycosylation is essential for its activity (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Myristate

Interactioni

Subunit structurei

Homodimer.By similarity

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 336326OAS domain 1Add
BLAST
Regioni344 – 683340OAS domain 2Add
BLAST

Sequence similaritiesi

Belongs to the 2-5A synthase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00510000046406.
HOVERGENiHBG007855.
InParanoidiF1N3B8.
KOiK14216.
OMAiKSYTSQK.
OrthoDBiEOG7WDN1R.
TreeFamiTF329749.

Family and domain databases

Gene3Di1.10.1410.20. 2 hits.
InterProiIPR006117. 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]
PANTHERiPTHR11258. PTHR11258. 1 hit.
PfamiPF10421. OAS1_C. 2 hits.
[Graphical view]
PROSITEiPS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

F1N3B8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSRESHLYE KPSEKLEEFI QNHLRPSEDC QKDIDQSVDT ICEVLQEPCP
60 70 80 90 100
SLTVTGVAKG GSYGRRTVLR GNSDGILVVF FGDLEQFQDQ EKRQYELLSK
110 120 130 140 150
IWAQMKHCES TWKLAAKMEL QNTNRSSRVT IQLSTKQQSI TFNVLPAFNA
160 170 180 190 200
LGLSEKSSLW SYRELKRSLD MVKARPGEFS VCFTELQEKF FSNYPSKLKD
210 220 230 240 250
LILLVKHWFQ KCQEKLINSS LLPPYALELL TVYAWEQGCG AEDFDMAEGV
260 270 280 290 300
RTVLRLIEKQ EQLCVYWTVN YNFGDEIVRN ILLSQLQAPR PVILDPTDPT
310 320 330 340 350
NNVSMDNTCW LQLKHEAQNW LRSLRQNESP GPSWNVLPAS LYITPGHLLD
360 370 380 390 400
KFVKDFLQPN QTFQDQIKKA LKIICSFLEE NCFRHSTTKI QVIQGGSTVK
410 420 430 440 450
GTALKTGSDA SLVVFANSLK SYTSPKNERY NIIKEIHEQL EACRQEKDFE
460 470 480 490 500
VKFEISKWKP PWVLSFTLKS KVLNESVDFD VLPAFNALGE LKSGSTPSPR
510 520 530 540 550
TYTELIHLYK PSDVFLEGEF SACFTKLQRN FVRSLPLKLK DLIRLLKHWY
560 570 580 590 600
CGCEKKLKQK GSLPPKYALE LLSIYAWEKG SGAQDFDMAE GFRTVLELVI
610 620 630 640 650
QYQHLCVFWT VNYSFDDEIL RNFLLGQIRR TRPVILDPAD PTGDVGGGHR
660 670 680 690 700
WCWHLLAKEA TEWLSSLCFK DKSGCPIQPW NVPKKRVQTP GSCGAGIYSM
710
VNEMHLLRSH RFLD
Length:714
Mass (Da):81,967
Last modified:May 3, 2011 - v1
Checksum:i6962A98CC6D437BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611S → T in AAT44896. (PubMed:17024523)Curated
Sequence conflicti219 – 2191S → P in AAT44896. (PubMed:17024523)Curated
Sequence conflicti277 – 2771I → T in AAT44896. (PubMed:17024523)Curated
Sequence conflicti522 – 5221A → V in AAT44896. (PubMed:17024523)Curated
Sequence conflicti551 – 5511C → K in AAT44896. (PubMed:17024523)Curated
Sequence conflicti573 – 5731S → T in AAT44896. (PubMed:17024523)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY599197 mRNA. Translation: AAT44896.1.
DAAA02045423 Genomic DNA. No translation available.
DAAA02045424 Genomic DNA. No translation available.
DAAA02045425 Genomic DNA. No translation available.
RefSeqiNP_001019728.1. NM_001024557.1.
UniGeneiBt.41610.

Genome annotation databases

EnsembliENSBTAT00000019477; ENSBTAP00000019477; ENSBTAG00000014628.
GeneIDi529660.
KEGGibta:529660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY599197 mRNA. Translation: AAT44896.1 .
DAAA02045423 Genomic DNA. No translation available.
DAAA02045424 Genomic DNA. No translation available.
DAAA02045425 Genomic DNA. No translation available.
RefSeqi NP_001019728.1. NM_001024557.1.
UniGenei Bt.41610.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000019477 ; ENSBTAP00000019477 ; ENSBTAG00000014628 .
GeneIDi 529660.
KEGGi bta:529660.

Organism-specific databases

CTDi 4939.

Phylogenomic databases

GeneTreei ENSGT00510000046406.
HOVERGENi HBG007855.
InParanoidi F1N3B8.
KOi K14216.
OMAi KSYTSQK.
OrthoDBi EOG7WDN1R.
TreeFami TF329749.

Miscellaneous databases

NextBioi 20875078.

Family and domain databases

Gene3Di 1.10.1410.20. 2 hits.
InterProi 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 ]
PANTHERi PTHR11258. PTHR11258. 1 hit.
Pfami PF10421. OAS1_C. 2 hits.
[Graphical view ]
PROSITEi PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.

Entry informationi

Entry nameiOAS2_BOVIN
AccessioniPrimary (citable) accession number: F1N3B8
Secondary accession number(s): Q53AV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: May 3, 2011
Last modified: October 29, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3