位置:首页 > 蛋白库 > OASL2_MOUSE
OASL2_MOUSE
ID   OASL2_MOUSE             Reviewed;         508 AA.
AC   Q9Z2F2; Q9D6S2;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=2'-5'-oligoadenylate synthase-like protein 2;
DE            EC=2.7.7.84 {ECO:0000269|PubMed:12799444};
DE   AltName: Full=54 kDa 2'-5'-oligoadenylate synthase-like protein;
DE            Short=p54 OASL;
DE   AltName: Full=M1204;
GN   Name=Oasl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   PubMed=10395668;
RA   Tiefenthaler M., Marksteiner R., Neyer S., Koch F., Hofer S., Schuler G.,
RA   Nussenzweig M., Schneider R., Heufler C.;
RT   "M1204, a novel 2',5' oligoadenylate synthetase with a ubiquitin-like
RT   extension, is induced during maturation of murine dendritic cells.";
RL   J. Immunol. 163:760-765(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   PubMed=12396720; DOI=10.1089/10799900260286696;
RA   Kakuta S., Shibata S., Iwakura Y.;
RT   "Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene
RT   family.";
RL   J. Interferon Cytokine Res. 22:981-993(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=12799444; DOI=10.1093/nar/gkg427;
RA   Eskildsen S., Justesen J., Schierup M.H., Hartmann R.;
RT   "Characterization of the 2'-5'-oligoadenylate synthetase ubiquitin-like
RT   family.";
RL   Nucleic Acids Res. 31:3166-3173(2003).
RN   [6]
RP   REVIEW.
RX   PubMed=17024523; DOI=10.1007/s00239-006-0073-3;
RA   Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.;
RT   "The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for
RT   concerted evolution of paralogous Oas1 genes in Rodentia and
RT   Artiodactyla.";
RL   J. Mol. Evol. 63:562-576(2006).
CC   -!- FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which
CC       plays a critical role in cellular innate antiviral response.
CC       Synthesizes oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which
CC       then bind to the inactive monomeric form of ribonuclease L (RNase L)
CC       leading to its dimerization and subsequent activation. Activation of
CC       RNase L leads to degradation of cellular as well as viral RNA,
CC       resulting in the inhibition of protein synthesis, thus terminating
CC       viral replication. Can mediate the antiviral effect via the classical
CC       RNase L-dependent pathway or an alternative antiviral pathway
CC       independent of RNase L. {ECO:0000269|PubMed:12396720,
CC       ECO:0000269|PubMed:12799444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-
CC         adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84;
CC         Evidence={ECO:0000269|PubMed:12799444};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34408;
CC         Evidence={ECO:0000269|PubMed:12799444};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by
CC       dsRNA generated during the course of viral infection. The dsRNA
CC       activator must be at least 15 nucleotides long, and no modification of
CC       the 2'-hydroxyl group is tolerated. ssRNA or dsDNA do not act as
CC       activators. {ECO:0000269|PubMed:12799444}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.66 mM for ATP {ECO:0000269|PubMed:12799444};
CC         Note=kcat is 0.39 sec(-1) with ATP as substrate.
CC         {ECO:0000269|PubMed:12799444};
CC   -!- TISSUE SPECIFICITY: Strongly expressed in spleen dendritic cells,
CC       whereas, in bone marrow-derived dendritic cells, the amount increases
CC       during the maturation process. Expressed in many organs, the highest
CC       levels being in thymus, lung, and bone marrow.
CC       {ECO:0000269|PubMed:12396720}.
CC   -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF068835; AAD02818.1; -; mRNA.
DR   EMBL; AK010034; BAB26655.1; -; mRNA.
DR   EMBL; AK150492; BAE29608.1; -; mRNA.
DR   EMBL; AC116500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS39226.1; -.
DR   RefSeq; NP_035984.2; NM_011854.2.
DR   RefSeq; XP_006530377.1; XM_006530314.3.
DR   RefSeq; XP_006530378.1; XM_006530315.3.
DR   AlphaFoldDB; Q9Z2F2; -.
DR   SMR; Q9Z2F2; -.
DR   MINT; Q9Z2F2; -.
DR   STRING; 10090.ENSMUSP00000031542; -.
DR   iPTMnet; Q9Z2F2; -.
DR   PhosphoSitePlus; Q9Z2F2; -.
DR   MaxQB; Q9Z2F2; -.
DR   PaxDb; Q9Z2F2; -.
DR   PRIDE; Q9Z2F2; -.
DR   ProteomicsDB; 291934; -.
DR   DNASU; 23962; -.
DR   Ensembl; ENSMUST00000031542; ENSMUSP00000031542; ENSMUSG00000029561.
DR   GeneID; 23962; -.
DR   KEGG; mmu:23962; -.
DR   UCSC; uc008zcu.1; mouse.
DR   CTD; 23962; -.
DR   MGI; MGI:1344390; Oasl2.
DR   VEuPathDB; HostDB:ENSMUSG00000029561; -.
DR   eggNOG; KOG0001; Eukaryota.
DR   GeneTree; ENSGT00510000046406; -.
DR   HOGENOM; CLU_040930_1_0_1; -.
DR   InParanoid; Q9Z2F2; -.
DR   OMA; AWEMGTD; -.
DR   OrthoDB; 611234at2759; -.
DR   PhylomeDB; Q9Z2F2; -.
DR   TreeFam; TF329749; -.
DR   SABIO-RK; Q9Z2F2; -.
DR   BioGRID-ORCS; 23962; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Oasl2; mouse.
DR   PRO; PR:Q9Z2F2; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9Z2F2; protein.
DR   Bgee; ENSMUSG00000029561; Expressed in small intestine Peyer's patch and 142 other tissues.
DR   ExpressionAtlas; Q9Z2F2; baseline and differential.
DR   Genevisible; Q9Z2F2; MM.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IEP:ARUK-UCL.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IBA:GO_Central.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0060700; P:regulation of ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0009615; P:response to virus; TAS:UniProtKB.
DR   CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR   InterPro; IPR026774; 2-5A_synthase.
DR   InterPro; IPR006117; 2-5OAS_C_CS.
DR   InterPro; IPR043518; 2-5OAS_N_CS.
DR   InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11258; PTHR11258; 1.
DR   Pfam; PF10421; OAS1_C; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 2.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   PROSITE; PS00832; 25A_SYNTH_1; 1.
DR   PROSITE; PS00833; 25A_SYNTH_2; 1.
DR   PROSITE; PS50152; 25A_SYNTH_3; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; ATP-binding; Immunity; Innate immunity; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-binding; Transferase.
FT   CHAIN           1..508
FT                   /note="2'-5'-oligoadenylate synthase-like protein 2"
FT                   /id="PRO_0000160267"
FT   DOMAIN          435..473
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00973"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P29728"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00973"
FT   CONFLICT        469..473
FT                   /note="GPCAE -> AGGLT (in Ref. 1; AAD02818)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474..508
FT                   /note="Missing (in Ref. 1; AAD02818)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   508 AA;  58767 MW;  9552B4540CC801A0 CRC64;
     MDPFPDLYAT PGDSLDHFLE HSLQPQRDWK EEGQDAWERI ERFFREQCFR DELLLDQEVR
     VIKVVKGGSS GKGTTLNHRS DQDMILFLSC FSSFEEQARN REVVISFIKK RLIHCSRSLA
     YNIIVLTHRE GKRAPRSLTL KVQSRKTDDI IWMDILPAYD ALGPISRDSK PAPAIYETLI
     RSKGYPGDFS PSFTELQRHF VKTRPVKLKN LLRLVKFWYL QCLRRKYGRG AVLPSKYALE
     LLTIYAWEMG TESSDSFNLD EGFVAVMELL VNYRDICIYW TKYYNFQNEV VRNFLKKQLK
     GDRPIILDPA DPTNNLGRRK GWEQVAAEAA FCLLQVCCTT VGPSERWNVQ RARDVQVRVK
     QTGTVDWTLW TNPYSPIRKM KAEIRREKNF GGELRISFQE PGGERQLLSS RKTLADYGIF
     SKVNIQVLET FPPEILVFVK YPGGQSKPFT IDPDDTILDL KEKIEDAGGP CAEDQVLLLD
     DEELEDDESL KELEIKDCDT IILIRVID
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024