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Q8VI94 (OASL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2'-5'-oligoadenylate synthase-like protein 1
Alternative name(s):
2',5'-oligoadenylate synthetase-like 9
Gene names
Name:Oasl1
Synonyms:oasl9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity via an alternative antiviral pathway independent of RNase L. Ref.3 Ref.8

Subunit structure

Specifically interacts with the ligand binding domain of the thyroid receptor (TR). TRIP14 does not require the presence of thyroid hormone for its interaction. Binds MBD1 By similarity.

Subcellular location

Nucleusnucleolus By similarity. Cytoplasm By similarity.

Induction

By type I interferon (IFN) and viruses. Ref.8

Sequence similarities

Belongs to the 2-5A synthase family.

Contains 2 ubiquitin-like domains.

Sequence caution

The sequence BAE29916.1 differs from that shown. Reason: Frameshift at position 509.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5115112'-5'-oligoadenylate synthase-like protein 1
PRO_0000418632

Regions

Domain350 – 42980Ubiquitin-like 1
Domain430 – 50677Ubiquitin-like 2

Experimental info

Sequence conflict2981I → V in AAN31518. Ref.1
Sequence conflict2981I → V in AAH32152. Ref.7
Sequence conflict3391V → I in AAN31518. Ref.1
Sequence conflict3391V → I in AAH32152. Ref.7
Sequence conflict3521V → L in AAM08092. Ref.2
Sequence conflict3561E → D in AAM08092. Ref.2
Sequence conflict3561E → Q in AAN31518. Ref.1
Sequence conflict3561E → Q in AAH32152. Ref.7
Sequence conflict3601S → P in AAN31518. Ref.1
Sequence conflict3601S → P in AAH32152. Ref.7
Sequence conflict3821S → T in AAM08092. Ref.2
Sequence conflict3831Q → R in AAN31518. Ref.1
Sequence conflict3831Q → R in AAH32152. Ref.7
Sequence conflict3961P → L in AAN31518. Ref.1
Sequence conflict3961P → L in AAH32152. Ref.7
Sequence conflict4851F → L in AAN31518. Ref.1
Sequence conflict4851F → L in AAH32152. Ref.7
Sequence conflict5011T → M in AAN31518. Ref.1
Sequence conflict5011T → M in AAH32152. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q8VI94 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 8E679549424535C1

FASTA51159,088
        10         20         30         40         50         60 
MAVAQELYGF PASKLDSFVA QWLQPTREWK EEVLETVQTV EQFLRQENFR EDRGPARDVR 

        70         80         90        100        110        120 
VLKVLKVGCF GNGTVLRSTT DVELVVFLSC FHSFQEEAKH HQAVLRLIQK RMYYCQELMD 

       130        140        150        160        170        180 
LGLSNLSVTN RVPSSLIFTI QTRETWETIT VTVVPAYRAL GPSCPSSEVY ANLIKANGYP 

       190        200        210        220        230        240 
GNFSPSFSEL QRNFVKHRPT KLKSLLRLVK HWYQQYVRDK CPRANLPPLY ALELLTVYAW 

       250        260        270        280        290        300 
EAGTREDANF RLDEGLATVM ELLQDHELLC IYWTKHYTLQ HPVIEACVRR QLRGQRPIIL 

       310        320        330        340        350        360 
DPADPTNNVA EGYRWDIVAQ RANQCLKQDC CYDNRDSPVP SWRVKRAPDI QVTVQEWGHS 

       370        380        390        400        410        420 
DLTFWVNPYE PIKKLKEKIQ LSQGYLGLQR LSFQEPGGER QLIRSHCTLA YYGIFCDTHI 

       430        440        450        460        470        480 
CLLDTISPEI QVFVKNPDGR SHAYAIHPLD YVLNLKQQIE DRQGLRCQEQ RLEFQGHILE 

       490        500        510 
DWFDFKSYGI QDSVTVILSK TTEGAAPFVP S 

« Hide

References

« Hide 'large scale' references
[1]"Glucocorticoid-attenuated response genes induced in the lung during endotoxemia."
Smith J.B., Nguyen T.T., Hughes H.J., Herschman H.R., Widney D.P., Bui K.C., Rovai L.E.
Am. J. Physiol. 283:L636-L647(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Czech II.
[2]"Gene structure of the murine 2'-5'-oligoadenylate synthetase family."
Eskildsen S., Hartmann R., Kjeldgaard N.O., Justesen J.
Cell. Mol. Life Sci. 59:1212-1222(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FVB/N.
Tissue: Intestine.
[3]"Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene family."
Kakuta S., Shibata S., Iwakura Y.
J. Interferon Cytokine Res. 22:981-993(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: C57BL/6J.
Tissue: Colon.
[4]"Positional cloning of the murine flavivirus resistance gene."
Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y., Brinton M.A.
Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/He.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow, Eye and Kidney.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary tumor.
[8]"Characterization of the 2'-5'-oligoadenylate synthetase ubiquitin-like family."
Eskildsen S., Justesen J., Schierup M.H., Hartmann R.
Nucleic Acids Res. 31:3166-3173(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[9]"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: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF426289 mRNA. Translation: AAN31518.1.
AY089728 mRNA. Translation: AAM08092.1.
AY057107 mRNA. Translation: AAL12828.1.
AB067533 mRNA. Translation: BAB84133.1.
AK078690 mRNA. Translation: BAC37360.1.
AK149824 mRNA. Translation: BAE29106.1.
AK150863 mRNA. Translation: BAE29916.1. Frameshift.
AK165578 mRNA. Translation: BAE38269.1.
AC116500 Genomic DNA. No translation available.
BC032152 mRNA. Translation: AAH32152.1.
CCDSCCDS19575.1.
RefSeqNP_660210.1. NM_145209.3.
XP_006530357.1. XM_006530294.1.
UniGeneMm.95479.

3D structure databases

ProteinModelPortalQ8VI94.
SMRQ8VI94. Positions 350-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000031540.

Proteomic databases

MaxQBQ8VI94.
PRIDEQ8VI94.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031540; ENSMUSP00000031540; ENSMUSG00000041827.
ENSMUST00000112143; ENSMUSP00000107771; ENSMUSG00000041827.
GeneID231655.
KEGGmmu:231655.
UCSCuc008zcv.1. mouse.

Organism-specific databases

CTD231655.
MGIMGI:2180849. Oasl1.

Phylogenomic databases

eggNOGNOG309765.
GeneTreeENSGT00510000046406.
HOGENOMHOG000022614.
HOVERGENHBG000994.
InParanoidQ8VI94.
KOK14608.
OMACFHSFQE.
OrthoDBEOG7WDN1R.
PhylomeDBQ8VI94.
TreeFamTF329749.

Gene expression databases

BgeeQ8VI94.
GenevestigatorQ8VI94.

Family and domain databases

Gene3D1.10.1410.20. 1 hit.
InterProIPR006117. 2-5-oligoadenylate_synth_CS.
IPR006116. 2-5-oligoadenylate_synth_N.
IPR018952. 2-5-oligoAdlate_synth_1_dom2/C.
IPR026774. 2-5A_synthase.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR11258. PTHR11258. 1 hit.
PfamPF10421. OAS1_C. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 2 hits.
[Graphical view]
SUPFAMSSF54236. SSF54236. 2 hits.
PROSITEPS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio380687.
PROQ8VI94.
SOURCESearch...

Entry information

Entry nameOASL1_MOUSE
AccessionPrimary (citable) accession number: Q8VI94
Secondary accession number(s): Q3UBP8, Q8K2A2, Q8QZV5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot