Q8VI94 (OASL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2'-5'-oligoadenylate synthase-like protein 1

Alternative name(s):
2',5'-oligoadenylate synthetase-like 9

Gene names

Name:	Oasl1
Synonyms:	oasl9

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus 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.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	RNA-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of viral genome replication Inferred from electronic annotation. Source: Compara response to virus Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro DNA binding Inferred from sequence or structural similarity. Source: UniProtKB double-stranded RNA binding Inferred from direct assay Ref.3. Source: MGI transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 511	511	2'-5'-oligoadenylate synthase-like protein 1		PRO_0000418632
Regions
	Domain	350 – 429	80	Ubiquitin-like 1
	Domain	430 – 506	77	Ubiquitin-like 2
Experimental info
	Sequence conflict	298	1	I → V in AAN31518. Ref.1
	Sequence conflict	298	1	I → V in AAH32152. Ref.7
	Sequence conflict	339	1	V → I in AAN31518. Ref.1
	Sequence conflict	339	1	V → I in AAH32152. Ref.7
	Sequence conflict	352	1	V → L in AAM08092. Ref.2
	Sequence conflict	356	1	E → D in AAM08092. Ref.2
	Sequence conflict	356	1	E → Q in AAN31518. Ref.1
	Sequence conflict	356	1	E → Q in AAH32152. Ref.7
	Sequence conflict	360	1	S → P in AAN31518. Ref.1
	Sequence conflict	360	1	S → P in AAH32152. Ref.7
	Sequence conflict	382	1	S → T in AAM08092. Ref.2
	Sequence conflict	383	1	Q → R in AAN31518. Ref.1
	Sequence conflict	383	1	Q → R in AAH32152. Ref.7
	Sequence conflict	396	1	P → L in AAN31518. Ref.1
	Sequence conflict	396	1	P → L in AAH32152. Ref.7
	Sequence conflict	485	1	F → L in AAN31518. Ref.1
	Sequence conflict	485	1	F → L in AAH32152. Ref.7
	Sequence conflict	501	1	T → M in AAN31518. Ref.1
	Sequence conflict	501	1	T → M in AAH32152. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q8VI94 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 8E679549424535C1	FASTA	511	59,088
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00128953. IPI00991040.
RefSeq	NP_660210.1. NM_145209.3.
UniGene	Mm.95479.
3D structure databases
HSSP	HSSP built from PDB template 1PX5 based on UniProtKB Q29599.
ProteinModelPortal	Q8VI94.
SMR	Q8VI94. Positions 350-507.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000031540.
Proteomic databases
PRIDE	Q8VI94.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031540; ENSMUSP00000031540; ENSMUSG00000041827. ENSMUST00000112143; ENSMUSP00000107771; ENSMUSG00000041827.
GeneID	231655.
KEGG	mmu:231655.
UCSC	uc008zcv.1. mouse.
Organism-specific databases
CTD	231655.
MGI	MGI:2180849. Oasl1.
Phylogenomic databases
eggNOG	NOG309765.
GeneTree	ENSGT00510000046406.
HOGENOM	HOG000022614.
HOVERGEN	HBG000994.
InParanoid	Q8VI94.
KO	K14608.
OMA	IQVFVKN.
OrthoDB	EOG4M0F1G.
Gene expression databases
Bgee	Q8VI94.
Genevestigator	Q8VI94.
Family and domain databases
Gene3D	1.10.1410.20. 1 hit.
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. IPR000626. Ubiquitin. IPR019955. Ubiquitin_supergroup. [Graphical view]
PANTHER	PTHR11258. PTHR11258. 1 hit.
Pfam	PF10421. OAS1_C. 1 hit. PF00240. ubiquitin. 1 hit. [Graphical view]
SMART	SM00213. UBQ. 2 hits. [Graphical view]
PROSITE	PS00832. 25A_SYNTH_1. False negative. PS00833. 25A_SYNTH_2. 1 hit. PS50152. 25A_SYNTH_3. 1 hit. PS00299. UBIQUITIN_1. False negative. PS50053. UBIQUITIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	380687.
SOURCE	Search...

Entry information

Entry name

OASL1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program