OASL_HUMAN
ID OASL_HUMAN Reviewed; 514 AA.
AC Q15646; B2RAZ2; I1YDD2; O75686; Q17R95; Q9Y6K6; Q9Y6K7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=2'-5'-oligoadenylate synthase-like protein;
DE AltName: Full=2'-5'-OAS-related protein;
DE Short=2'-5'-OAS-RP;
DE AltName: Full=59 kDa 2'-5'-oligoadenylate synthase-like protein;
DE AltName: Full=Thyroid receptor-interacting protein 14;
DE Short=TR-interacting protein 14;
DE Short=TRIP-14;
DE AltName: Full=p59 OASL;
DE Short=p59OASL;
GN Name=OASL; Synonyms=TRIP14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P56).
RX PubMed=9722630; DOI=10.1093/nar/26.18.4121;
RA Hartmann R., Olsen H.S., Widder S., Joergensen R., Justesen J.;
RT "p59OASL, a 2'-5' oligoadenylate synthetase like protein: a novel human
RT gene related to the 2'-5' oligoadenylate synthetase family.";
RL Nucleic Acids Res. 26:4121-4127(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P56 AND P30), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Monocyte;
RX PubMed=9826176; DOI=10.1046/j.1432-1327.1998.2570319.x;
RA Rebouillat D., Marie I., Hovanessian A.G.;
RT "Molecular cloning and characterization of two related and interferon-
RT induced 56-kDa and 30-kDa proteins highly similar to 2'-5' oligoadenylate
RT synthetase.";
RL Eur. J. Biochem. 257:319-330(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=22531715; DOI=10.1016/j.biocel.2012.04.001;
RA Guo X., Li X., Xu Y., Sun T., Yang G., Wu Z., Li E.;
RT "Identification of OASL d, a splice variant of human OASL, with antiviral
RT activity.";
RL Int. J. Biochem. Cell Biol. 44:1133-1138(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P56).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P56).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 260-416 (ISOFORM P56).
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [8]
RP INTERACTION WITH MBD1.
RC TISSUE=Leukocyte;
RX PubMed=14728690; DOI=10.1046/j.1432-1033.2003.03966.x;
RA Andersen J.B., Strandbygaard D.J., Hartmann R., Justesen J.;
RT "Interaction between the 2'-5' oligoadenylate synthetase-like protein p59
RT OASL and the transcriptional repressor methyl CpG-binding protein 1.";
RL Eur. J. Biochem. 271:628-636(2004).
RN [9]
RP REVIEW ON FUNCTION.
RX PubMed=17408844; DOI=10.1016/j.biochi.2007.02.003;
RA Hovanessian A.G., Justesen J.;
RT "The human 2'-5'oligoadenylate synthetase family: unique interferon-
RT inducible enzymes catalyzing 2'-5' instead of 3'-5' phosphodiester bond
RT formation.";
RL Biochimie 89:779-788(2007).
RN [10]
RP FUNCTION.
RX PubMed=18931074; DOI=10.1099/vir.0.2008/003558-0;
RA Marques J., Anwar J., Eskildsen-Larsen S., Rebouillat D., Paludan S.R.,
RA Sen G., Williams B.R., Hartmann R.;
RT "The p59 oligoadenylate synthetase-like protein possesses antiviral
RT activity that requires the C-terminal ubiquitin-like domain.";
RL J. Gen. Virol. 89:2767-2772(2008).
RN [11]
RP INDUCTION.
RX PubMed=19203244; DOI=10.1089/jir.2008.0050;
RA Melchjorsen J., Kristiansen H., Christiansen R., Rintahaka J.,
RA Matikainen S., Paludan S.R., Hartmann R.;
RT "Differential regulation of the OASL and OAS1 genes in response to viral
RT infections.";
RL J. Interferon Cytokine Res. 29:199-207(2009).
RN [12]
RP REVIEW.
RX PubMed=19904482; DOI=10.1007/s00239-009-9299-1;
RA Kjaer K.H., Poulsen J.B., Reintamm T., Saby E., Martensen P.M., Kelve M.,
RA Justesen J.;
RT "Evolution of the 2'-5'-oligoadenylate synthetase family in eukaryotes and
RT bacteria.";
RL J. Mol. Evol. 69:612-624(2009).
RN [13]
RP FUNCTION, AND INDUCTION.
RX PubMed=20074559; DOI=10.1016/j.bbrc.2010.01.034;
RA Ishibashi M., Wakita T., Esumi M.;
RT "2',5'-Oligoadenylate synthetase-like gene highly induced by hepatitis C
RT virus infection in human liver is inhibitory to viral replication in
RT vitro.";
RL Biochem. Biophys. Res. Commun. 392:397-402(2010).
RN [14]
RP REVIEW ON FUNCTION.
RX PubMed=21142819; DOI=10.1089/jir.2010.0107;
RA Kristiansen H., Gad H.H., Eskildsen-Larsen S., Despres P., Hartmann R.;
RT "The oligoadenylate synthetase family: an ancient protein family with
RT multiple antiviral activities.";
RL J. Interferon Cytokine Res. 31:41-47(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP STRUCTURE BY NMR OF 432-507.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of C-terminal ubiquitin-like domain of human 2'-5'-
RT oligoadenylate synthetase-like protein (p59 OASL).";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-
CC stranded RNA. Displays antiviral activity against encephalomyocarditis
CC virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral
CC pathway independent of RNase L. {ECO:0000269|PubMed:18931074,
CC ECO:0000269|PubMed:20074559, ECO:0000269|PubMed:9826176}.
CC -!- SUBUNIT: Specifically interacts with the ligand binding domain of the
CC thyroid receptor (TR). TRIP14 does not require the presence of thyroid
CC hormone for its interaction. Binds MBD1. {ECO:0000269|PubMed:14728690}.
CC -!- INTERACTION:
CC Q15646; Q4G0J3: LARP7; NbExp=2; IntAct=EBI-3918068, EBI-2371923;
CC -!- SUBCELLULAR LOCATION: [Isoform p56]: Nucleus, nucleolus. Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform p30]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=p56; Synonyms=OASL a;
CC IsoId=Q15646-1; Sequence=Displayed;
CC Name=p30;
CC IsoId=Q15646-2; Sequence=VSP_003743, VSP_003744;
CC Name=3; Synonyms=OASL d;
CC IsoId=Q15646-3; Sequence=VSP_046572;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, with the highest levels
CC in primary blood Leukocytes and other hematopoietic system tissues,
CC colon, stomach and to some extent in testis.
CC -!- INDUCTION: By type I interferon (IFN) and viruses.
CC {ECO:0000269|PubMed:19203244, ECO:0000269|PubMed:20074559}.
CC -!- DOMAIN: The ubiquitin-like domains are essential for its antiviral
CC activity.
CC -!- MISCELLANEOUS: [Isoform 3]: Has antiviral activity against RNA viruses.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
CC -!- CAUTION: This is the ortholog of mouse OASL1. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC41733.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ225089; CAA12396.1; -; mRNA.
DR EMBL; AF063611; AAD28541.1; -; mRNA.
DR EMBL; AF063612; AAD28542.1; -; mRNA.
DR EMBL; JQ792168; AFJ00074.1; -; mRNA.
DR EMBL; AK314419; BAG37039.1; -; mRNA.
DR EMBL; AC079602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z93097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117408; AAI17409.1; -; mRNA.
DR EMBL; BC117410; AAI17411.1; -; mRNA.
DR EMBL; L40387; AAC41733.1; ALT_FRAME; Genomic_DNA.
DR CCDS; CCDS73536.1; -. [Q15646-3]
DR CCDS; CCDS9211.1; -. [Q15646-1]
DR CCDS; CCDS9212.1; -. [Q15646-2]
DR RefSeq; NP_001248754.1; NM_001261825.1. [Q15646-3]
DR RefSeq; NP_003724.1; NM_003733.3. [Q15646-1]
DR RefSeq; NP_937856.1; NM_198213.2. [Q15646-2]
DR RefSeq; XP_016875630.1; XM_017020141.1. [Q15646-2]
DR PDB; 1WH3; NMR; -; A=434-507.
DR PDB; 4XQ7; X-ray; 1.60 A; A=1-350.
DR PDBsum; 1WH3; -.
DR PDBsum; 4XQ7; -.
DR AlphaFoldDB; Q15646; -.
DR SMR; Q15646; -.
DR BioGRID; 114191; 269.
DR IntAct; Q15646; 119.
DR MINT; Q15646; -.
DR STRING; 9606.ENSP00000257570; -.
DR iPTMnet; Q15646; -.
DR PhosphoSitePlus; Q15646; -.
DR BioMuta; OASL; -.
DR DMDM; 6226835; -.
DR EPD; Q15646; -.
DR jPOST; Q15646; -.
DR MassIVE; Q15646; -.
DR MaxQB; Q15646; -.
DR PaxDb; Q15646; -.
DR PeptideAtlas; Q15646; -.
DR PRIDE; Q15646; -.
DR ProteomicsDB; 60683; -. [Q15646-1]
DR ProteomicsDB; 60684; -. [Q15646-2]
DR Antibodypedia; 808; 179 antibodies from 26 providers.
DR DNASU; 8638; -.
DR Ensembl; ENST00000257570.9; ENSP00000257570.4; ENSG00000135114.13. [Q15646-1]
DR Ensembl; ENST00000339275.10; ENSP00000341125.5; ENSG00000135114.13. [Q15646-2]
DR Ensembl; ENST00000543677.2; ENSP00000444127.2; ENSG00000135114.13. [Q15646-2]
DR Ensembl; ENST00000620239.5; ENSP00000479512.1; ENSG00000135114.13. [Q15646-3]
DR GeneID; 8638; -.
DR KEGG; hsa:8638; -.
DR MANE-Select; ENST00000257570.10; ENSP00000257570.4; NM_003733.4; NP_003724.1.
DR UCSC; uc001tzj.3; human. [Q15646-1]
DR CTD; 8638; -.
DR DisGeNET; 8638; -.
DR GeneCards; OASL; -.
DR HGNC; HGNC:8090; OASL.
DR HPA; ENSG00000135114; Tissue enhanced (bone marrow, stomach).
DR MIM; 603281; gene.
DR neXtProt; NX_Q15646; -.
DR OpenTargets; ENSG00000135114; -.
DR PharmGKB; PA31879; -.
DR VEuPathDB; HostDB:ENSG00000135114; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_040930_1_0_1; -.
DR OMA; VICIYWT; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; Q15646; -.
DR TreeFam; TF329749; -.
DR BRENDA; 2.7.7.84; 2681.
DR PathwayCommons; Q15646; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR Reactome; R-HSA-8983711; OAS antiviral response.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; Q15646; -.
DR BioGRID-ORCS; 8638; 6 hits in 1069 CRISPR screens.
DR ChiTaRS; OASL; human.
DR EvolutionaryTrace; Q15646; -.
DR GeneWiki; OASL; -.
DR GenomeRNAi; 8638; -.
DR Pharos; Q15646; Tbio.
DR PRO; PR:Q15646; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15646; protein.
DR Bgee; ENSG00000135114; Expressed in granulocyte and 117 other tissues.
DR ExpressionAtlas; Q15646; baseline and differential.
DR Genevisible; Q15646; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; TAS:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0060700; P:regulation of ribonuclease activity; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IDA: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; 2.
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 3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW Cytoplasm; Immunity; Innate immunity; Nucleus; Reference proteome; Repeat;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..514
FT /note="2'-5'-oligoadenylate synthase-like protein"
FT /id="PRO_0000160266"
FT DOMAIN 354..433
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 434..509
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 220..349
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:22531715"
FT /id="VSP_046572"
FT VAR_SEQ 220..255
FT /note="YVKARSPRANLPPLYALELLTIYAWEMGTEEDENFM -> AHHPGSGRPHPQ
FT RGRRVQMGHRCSEGLPVPETGLLL (in isoform p30)"
FT /evidence="ECO:0000303|PubMed:9826176"
FT /id="VSP_003743"
FT VAR_SEQ 256..514
FT /note="Missing (in isoform p30)"
FT /evidence="ECO:0000303|PubMed:9826176"
FT /id="VSP_003744"
FT VARIANT 341
FT /note="N -> I (in dbSNP:rs35249920)"
FT /id="VAR_053544"
FT CONFLICT 26..38
FT /note="HREWKEEVLDAVR -> TGVEGRGARRCA (in Ref. 2; AAD28541/
FT AAD28542)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> T (in Ref. 2; AAD28542)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..113
FT /note="QEAAKHHKDVLRLIWKTMW -> PGGSQASQRCSEADMENHV (in Ref.
FT 2; AAD28541/AAD28542)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="A -> S (in Ref. 2; AAD28541)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="Y -> I (in Ref. 2; AAD28541)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="I -> T (in Ref. 2; AAD28541)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="Q -> L (in Ref. 2; AAD28541)"
FT /evidence="ECO:0000305"
FT CONFLICT 341..342
FT /note="NP -> KG (in Ref. 7; AAC41733)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="L -> F (in Ref. 4; BAG37039)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="S -> T (in Ref. 2; AAD28541)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 27..46
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 94..112
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4XQ7"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:4XQ7"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 204..220
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4XQ7"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:4XQ7"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4XQ7"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:1WH3"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:1WH3"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:1WH3"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:1WH3"
FT HELIX 456..466
FT /evidence="ECO:0007829|PDB:1WH3"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:1WH3"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:1WH3"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:1WH3"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:1WH3"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:1WH3"
SQ SEQUENCE 514 AA; 59226 MW; 4D8BB655D9EA003E CRC64;
MALMQELYST PASRLDSFVA QWLQPHREWK EEVLDAVRTV EEFLRQEHFQ GKRGLDQDVR
VLKVVKVGSF GNGTVLRSTR EVELVAFLSC FHSFQEAAKH HKDVLRLIWK TMWQSQDLLD
LGLEDLRMEQ RVPDALVFTI QTRGTAEPIT VTIVPAYRAL GPSLPNSQPP PEVYVSLIKA
CGGPGNFCPS FSELQRNFVK HRPTKLKSLL RLVKHWYQQY VKARSPRANL PPLYALELLT
IYAWEMGTEE DENFMLDEGF TTVMDLLLEY EVICIYWTKY YTLHNAIIED CVRKQLKKER
PIILDPADPT LNVAEGYRWD IVAQRASQCL KQDCCYDNRE NPISSWNVKR ARDIHLTVEQ
RGYPDFNLIV NPYEPIRKVK EKIRRTRGYS GLQRLSFQVP GSERQLLSSR CSLAKYGIFS
HTHIYLLETI PSEIQVFVKN PDGGSYAYAI NPNSFILGLK QQIEDQQGLP KKQQQLEFQG
QVLQDWLGLG IYGIQDSDTL ILSKKKGEAL FPAS
