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Protein

2'-5'-oligoadenylate synthase-like protein 1

Gene

Oasl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. DNA binding Source: UniProtKB
  3. double-stranded RNA binding Source: MGI
  4. poly(A) RNA binding Source: MGI
  5. transferase activity Source: InterPro

GO - Biological processi

  1. defense response to virus Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB-KW
  3. negative regulation of viral genome replication Source: MGI
  4. response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_198660. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase-like protein 1
Alternative name(s):
2',5'-oligoadenylate synthetase-like 9
Gene namesi
Name:Oasl1
Synonyms:oasl9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2180849. Oasl1.

Subcellular locationi

Nucleusnucleolus By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: MGI
  3. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5115112'-5'-oligoadenylate synthase-like protein 1PRO_0000418632Add
BLAST

Proteomic databases

MaxQBiQ8VI94.
PRIDEiQ8VI94.

Expressioni

Inductioni

By type I interferon (IFN) and viruses.1 Publication

Gene expression databases

BgeeiQ8VI94.
GenevestigatoriQ8VI94.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031540.

Structurei

3D structure databases

ProteinModelPortaliQ8VI94.
SMRiQ8VI94. Positions 350-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini350 – 42980Ubiquitin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini430 – 50677Ubiquitin-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-5A synthase family.Curated
Contains 2 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG309765.
GeneTreeiENSGT00510000046406.
HOGENOMiHOG000022614.
HOVERGENiHBG000994.
InParanoidiQ8VI94.
KOiK14608.
OMAiCFHSFQE.
OrthoDBiEOG7WDN1R.
PhylomeDBiQ8VI94.
TreeFamiTF329749.

Family and domain databases

Gene3Di1.10.1410.20. 1 hit.
InterProiIPR006117. 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]
PANTHERiPTHR11258. PTHR11258. 1 hit.
PfamiPF10421. OAS1_C. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 2 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 2 hits.
PROSITEiPS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VI94-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVAQELYGF PASKLDSFVA QWLQPTREWK EEVLETVQTV EQFLRQENFR
60 70 80 90 100
EDRGPARDVR VLKVLKVGCF GNGTVLRSTT DVELVVFLSC FHSFQEEAKH
110 120 130 140 150
HQAVLRLIQK RMYYCQELMD LGLSNLSVTN RVPSSLIFTI QTRETWETIT
160 170 180 190 200
VTVVPAYRAL GPSCPSSEVY ANLIKANGYP GNFSPSFSEL QRNFVKHRPT
210 220 230 240 250
KLKSLLRLVK HWYQQYVRDK CPRANLPPLY ALELLTVYAW EAGTREDANF
260 270 280 290 300
RLDEGLATVM ELLQDHELLC IYWTKHYTLQ HPVIEACVRR QLRGQRPIIL
310 320 330 340 350
DPADPTNNVA EGYRWDIVAQ RANQCLKQDC CYDNRDSPVP SWRVKRAPDI
360 370 380 390 400
QVTVQEWGHS DLTFWVNPYE PIKKLKEKIQ LSQGYLGLQR LSFQEPGGER
410 420 430 440 450
QLIRSHCTLA YYGIFCDTHI CLLDTISPEI QVFVKNPDGR SHAYAIHPLD
460 470 480 490 500
YVLNLKQQIE DRQGLRCQEQ RLEFQGHILE DWFDFKSYGI QDSVTVILSK
510
TTEGAAPFVP S
Length:511
Mass (Da):59,088
Last modified:March 1, 2002 - v1
Checksum:i8E679549424535C1
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti298 – 2981I → V in AAN31518. (PubMed:12169584)Curated
Sequence conflicti298 – 2981I → V in AAH32152. (PubMed:15489334)Curated
Sequence conflicti339 – 3391V → I in AAN31518. (PubMed:12169584)Curated
Sequence conflicti339 – 3391V → I in AAH32152. (PubMed:15489334)Curated
Sequence conflicti352 – 3521V → L in AAM08092. (PubMed:12222967)Curated
Sequence conflicti356 – 3561E → D in AAM08092. (PubMed:12222967)Curated
Sequence conflicti356 – 3561E → Q in AAN31518. (PubMed:12169584)Curated
Sequence conflicti356 – 3561E → Q in AAH32152. (PubMed:15489334)Curated
Sequence conflicti360 – 3601S → P in AAN31518. (PubMed:12169584)Curated
Sequence conflicti360 – 3601S → P in AAH32152. (PubMed:15489334)Curated
Sequence conflicti382 – 3821S → T in AAM08092. (PubMed:12222967)Curated
Sequence conflicti383 – 3831Q → R in AAN31518. (PubMed:12169584)Curated
Sequence conflicti383 – 3831Q → R in AAH32152. (PubMed:15489334)Curated
Sequence conflicti396 – 3961P → L in AAN31518. (PubMed:12169584)Curated
Sequence conflicti396 – 3961P → L in AAH32152. (PubMed:15489334)Curated
Sequence conflicti485 – 4851F → L in AAN31518. (PubMed:12169584)Curated
Sequence conflicti485 – 4851F → L in AAH32152. (PubMed:15489334)Curated
Sequence conflicti501 – 5011T → M in AAN31518. (PubMed:12169584)Curated
Sequence conflicti501 – 5011T → M in AAH32152. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19575.1.
RefSeqiNP_660210.1. NM_145209.3.
XP_006530357.1. XM_006530294.1.
UniGeneiMm.95479.

Genome annotation databases

EnsembliENSMUST00000031540; ENSMUSP00000031540; ENSMUSG00000041827.
ENSMUST00000112143; ENSMUSP00000107771; ENSMUSG00000041827.
GeneIDi231655.
KEGGimmu:231655.
UCSCiuc008zcv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19575.1.
RefSeqiNP_660210.1. NM_145209.3.
XP_006530357.1. XM_006530294.1.
UniGeneiMm.95479.

3D structure databases

ProteinModelPortaliQ8VI94.
SMRiQ8VI94. Positions 350-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031540.

Proteomic databases

MaxQBiQ8VI94.
PRIDEiQ8VI94.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031540; ENSMUSP00000031540; ENSMUSG00000041827.
ENSMUST00000112143; ENSMUSP00000107771; ENSMUSG00000041827.
GeneIDi231655.
KEGGimmu:231655.
UCSCiuc008zcv.1. mouse.

Organism-specific databases

CTDi231655.
MGIiMGI:2180849. Oasl1.

Phylogenomic databases

eggNOGiNOG309765.
GeneTreeiENSGT00510000046406.
HOGENOMiHOG000022614.
HOVERGENiHBG000994.
InParanoidiQ8VI94.
KOiK14608.
OMAiCFHSFQE.
OrthoDBiEOG7WDN1R.
PhylomeDBiQ8VI94.
TreeFamiTF329749.

Enzyme and pathway databases

ReactomeiREACT_198660. Interferon gamma signaling.

Miscellaneous databases

NextBioi380687.
PROiQ8VI94.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VI94.
GenevestigatoriQ8VI94.

Family and domain databases

Gene3Di1.10.1410.20. 1 hit.
InterProiIPR006117. 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]
PANTHERiPTHR11258. PTHR11258. 1 hit.
PfamiPF10421. OAS1_C. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 2 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 2 hits.
PROSITEiPS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiOASL1_MOUSE
AccessioniPrimary (citable) accession number: Q8VI94
Secondary accession number(s): Q3UBP8, Q8K2A2, Q8QZV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: March 1, 2002
Last modified: February 4, 2015
This is version 100 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.