OAS2_HUMAN
ID OAS2_HUMAN Reviewed; 719 AA.
AC P29728; A8K9T1; Q6PJ33; Q86XX8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=2'-5'-oligoadenylate synthase 2;
DE Short=(2-5')oligo(A) synthase 2;
DE Short=2-5A synthase 2;
DE EC=2.7.7.84 {ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:11986302, ECO:0000269|PubMed:9880569};
DE AltName: Full=p69 OAS / p71 OAS {ECO:0000303|PubMed:1577824};
DE Short=p69OAS / p71OAS {ECO:0000303|PubMed:1577824};
GN Name=OAS2 {ECO:0000312|HGNC:HGNC:8087};
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] (ISOFORMS P69 AND P71), AND INDUCTION.
RX PubMed=1577824; DOI=10.1016/s0021-9258(19)50182-x;
RA Marie I., Hovanessian A.G.;
RT "The 69-kDa 2-5A synthetase is composed of two homologous and adjacent
RT functional domains.";
RL J. Biol. Chem. 267:9933-9939(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P69).
RC TISSUE=Trachea;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P69 AND 3).
RC TISSUE=Blood, and Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 420-425 AND 539-547, IDENTIFICATION BY MASS
RP SPECTROMETRY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-421; ARG-544 AND LYS-547.
RX PubMed=11986302; DOI=10.1074/jbc.m110202200;
RA Sarkar S.N., Miyagi M., Crabb J.W., Sen G.C.;
RT "Identification of the substrate-binding sites of 2'-5'-oligoadenylate
RT synthetase.";
RL J. Biol. Chem. 277:24321-24330(2002).
RN [7]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=2211721; DOI=10.1016/s0021-9258(17)44794-6;
RA Marie I., Svab J., Robert N., Galabru J., Hovanessian A.G.;
RT "Differential expression and distinct structure of 69- and 100-kDa forms of
RT 2-5A synthetase in human cells treated with interferon.";
RL J. Biol. Chem. 265:18601-18607(1990).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBUNIT,
RP ACTIVITY REGULATION, GLYCOSYLATION, MYRISTOYLATION, AND MUTAGENESIS OF
RP GLY-2.
RX PubMed=9880569; DOI=10.1074/jbc.274.3.1848;
RA Sarkar S.N., Bandyopadhyay S., Ghosh A., Sen G.C.;
RT "Enzymatic characteristics of recombinant medium isozyme of 2'-5'
RT oligoadenylate synthetase.";
RL J. Biol. Chem. 274:1848-1855(1999).
RN [9]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASP-408; ASP-410; ASP-481; CYS-668; PHE-669 AND LYS-670.
RX PubMed=10464285; DOI=10.1074/jbc.274.36.25535;
RA Sarkar S.N., Ghosh A., Wang H.W., Sung S.S., Sen G.C.;
RT "The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases.";
RL J. Biol. Chem. 274:25535-25542(1999).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=11682059; DOI=10.1016/s0014-5793(01)02918-0;
RA Hartmann R., Walko G., Justesen J.;
RT "Inhibition of 2'-5' oligoadenylate synthetase by divalent metal ions.";
RL FEBS Lett. 507:54-58(2001).
RN [11]
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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19923450; DOI=10.4049/jimmunol.0902728;
RA Lin R.J., Yu H.P., Chang B.L., Tang W.C., Liao C.L., Lin Y.L.;
RT "Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family
RT members against dengue virus infection.";
RL J. Immunol. 183:8035-8043(2009).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which
CC plays a critical role in cellular innate antiviral response
CC (PubMed:10464285, PubMed:9880569). Activated by detection of double
CC stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-
CC oligoadenylates (2-5A) from ATP which then bind to the inactive
CC monomeric form of ribonuclease L (RNASEL) leading to its dimerization
CC and subsequent activation (PubMed:10464285, PubMed:9880569,
CC PubMed:11682059). Activation of RNASEL leads to degradation of cellular
CC as well as viral RNA, resulting in the inhibition of protein synthesis,
CC thus terminating viral replication (PubMed:10464285, PubMed:9880569).
CC Can mediate the antiviral effect via the classical RNASEL-dependent
CC pathway or an alternative antiviral pathway independent of RNASEL
CC (PubMed:21142819). In addition, it may also play a role in other
CC cellular processes such as apoptosis, cell growth, differentiation and
CC gene regulation (PubMed:21142819). May act as a negative regulator of
CC lactation, stopping lactation in virally infected mammary gland
CC lobules, thereby preventing transmission of viruses to neonates (By
CC similarity). Non-infected lobules would not be affected, allowing
CC efficient pup feeding during infection (By similarity).
CC {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000269|PubMed:10464285,
CC ECO:0000269|PubMed:11682059, ECO:0000269|PubMed:19923450,
CC ECO:0000269|PubMed:9880569, ECO:0000303|PubMed:21142819}.
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:10464285, ECO:0000269|PubMed:11682059,
CC ECO:0000269|PubMed:11986302, ECO:0000269|PubMed:9880569};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11682059};
CC -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by
CC double stranded RNA (dsRNA) generated during the course of viral
CC infection(PubMed:9880569). The dsRNA activator must be at least 15
CC nucleotides long, and no modification of the 2'-hydroxyl group is
CC tolerated (PubMed:9880569). ssRNA or dsDNA do not act as activators
CC (PubMed:9880569). Strongly inhibited by copper, iron and zinc ions
CC (PubMed:11682059). Partially inhibited by cobalt and nickel ions
CC (PubMed:11682059). {ECO:0000269|PubMed:11682059,
CC ECO:0000269|PubMed:9880569}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 mM for ATP {ECO:0000269|PubMed:10464285,
CC ECO:0000269|PubMed:11986302, ECO:0000269|PubMed:9880569};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10464285,
CC ECO:0000269|PubMed:9880569}.
CC -!- INTERACTION:
CC P29728; P49761: CLK3; NbExp=4; IntAct=EBI-10211452, EBI-745579;
CC P29728-2; P49761: CLK3; NbExp=5; IntAct=EBI-12270678, EBI-745579;
CC P29728-2; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-12270678, EBI-2510157;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19923450}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:19923450}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=p71 {ECO:0000303|PubMed:1577824}; Synonyms=71 kDa
CC {ECO:0000303|PubMed:1577824};
CC IsoId=P29728-1; Sequence=Displayed;
CC Name=p69 {ECO:0000303|PubMed:1577824, ECO:0000303|PubMed:2211721};
CC Synonyms=69 kDa {ECO:0000303|PubMed:1577824,
CC ECO:0000303|PubMed:2211721};
CC IsoId=P29728-2; Sequence=VSP_003741, VSP_003742;
CC Name=3;
CC IsoId=P29728-3; Sequence=VSP_043354, VSP_043355;
CC -!- INDUCTION: By type I interferon (IFN) and viruses.
CC {ECO:0000269|PubMed:1577824}.
CC -!- PTM: Myristoylation is not essential for its activity.
CC {ECO:0000269|PubMed:2211721, ECO:0000269|PubMed:9880569}.
CC -!- PTM: Glycosylated. Glycosylation is essential for its activity.
CC {ECO:0000269|PubMed:9880569}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; M87434; AAA60607.1; -; mRNA.
DR EMBL; M87284; AAA60606.1; -; mRNA.
DR EMBL; AK292796; BAF85485.1; -; mRNA.
DR EMBL; AC004551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98027.1; -; Genomic_DNA.
DR EMBL; BC023637; AAH23637.1; -; mRNA.
DR EMBL; BC049215; AAH49215.1; -; mRNA.
DR CCDS; CCDS31906.1; -. [P29728-1]
DR CCDS; CCDS41839.1; -. [P29728-2]
DR CCDS; CCDS44982.1; -. [P29728-3]
DR PIR; B42665; B42665.
DR RefSeq; NP_001027903.1; NM_001032731.1. [P29728-3]
DR RefSeq; NP_002526.2; NM_002535.2. [P29728-2]
DR RefSeq; NP_058197.2; NM_016817.2. [P29728-1]
DR AlphaFoldDB; P29728; -.
DR SMR; P29728; -.
DR BioGRID; 110993; 17.
DR IntAct; P29728; 5.
DR STRING; 9606.ENSP00000342278; -.
DR iPTMnet; P29728; -.
DR PhosphoSitePlus; P29728; -.
DR BioMuta; OAS2; -.
DR DMDM; 116242687; -.
DR EPD; P29728; -.
DR jPOST; P29728; -.
DR MassIVE; P29728; -.
DR MaxQB; P29728; -.
DR PaxDb; P29728; -.
DR PeptideAtlas; P29728; -.
DR PRIDE; P29728; -.
DR ProteomicsDB; 54606; -. [P29728-1]
DR ProteomicsDB; 54607; -. [P29728-2]
DR ProteomicsDB; 54608; -. [P29728-3]
DR Antibodypedia; 31214; 441 antibodies from 31 providers.
DR DNASU; 4939; -.
DR Ensembl; ENST00000342315.8; ENSP00000342278.4; ENSG00000111335.14. [P29728-1]
DR Ensembl; ENST00000392583.7; ENSP00000376362.3; ENSG00000111335.14. [P29728-2]
DR Ensembl; ENST00000449768.2; ENSP00000411763.2; ENSG00000111335.14. [P29728-3]
DR GeneID; 4939; -.
DR KEGG; hsa:4939; -.
DR MANE-Select; ENST00000392583.7; ENSP00000376362.3; NM_002535.3; NP_002526.2. [P29728-2]
DR UCSC; uc001tuh.4; human. [P29728-1]
DR CTD; 4939; -.
DR DisGeNET; 4939; -.
DR GeneCards; OAS2; -.
DR HGNC; HGNC:8087; OAS2.
DR HPA; ENSG00000111335; Tissue enhanced (salivary).
DR MIM; 603350; gene.
DR neXtProt; NX_P29728; -.
DR OpenTargets; ENSG00000111335; -.
DR PharmGKB; PA31876; -.
DR VEuPathDB; HostDB:ENSG00000111335; -.
DR eggNOG; ENOG502S649; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_026275_0_0_1; -.
DR OMA; WMKDSFE; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; P29728; -.
DR TreeFam; TF329749; -.
DR BioCyc; MetaCyc:ENSG00000111335-MON; -.
DR BRENDA; 2.7.7.84; 2681.
DR PathwayCommons; P29728; -.
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 SABIO-RK; P29728; -.
DR SignaLink; P29728; -.
DR BioGRID-ORCS; 4939; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; OAS2; human.
DR GeneWiki; OAS2; -.
DR GenomeRNAi; 4939; -.
DR Pharos; P29728; Tbio.
DR PRO; PR:P29728; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P29728; protein.
DR Bgee; ENSG00000111335; Expressed in monocyte and 145 other tissues.
DR ExpressionAtlas; P29728; baseline and differential.
DR Genevisible; P29728; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
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:0042742; P:defense response to bacterium; IMP:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IBA:GO_Central.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:ARUK-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:ARUK-UCL.
DR GO; GO:1903487; P:regulation of lactation; ISS:UniProtKB.
DR GO; GO:0060700; P:regulation of ribonuclease activity; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; TAS:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IEA:Ensembl.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISS:UniProtKB.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 2.
DR Gene3D; 3.30.460.10; -; 2.
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; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR11258; PTHR11258; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 2.
DR SUPFAM; SSF81301; SSF81301; 2.
DR PROSITE; PS00832; 25A_SYNTH_1; 2.
DR PROSITE; PS00833; 25A_SYNTH_2; 2.
DR PROSITE; PS50152; 25A_SYNTH_3; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Antiviral defense; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Glycoprotein; Immunity;
KW Innate immunity; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Repeat;
KW RNA-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2211721"
FT CHAIN 2..719
FT /note="2'-5'-oligoadenylate synthase 2"
FT /id="PRO_0000160264"
FT REGION 11..335
FT /note="OAS domain 1"
FT REGION 343..683
FT /note="OAS domain 2"
FT BINDING 396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00973"
FT BINDING 408
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 410
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:11986302"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:11986302"
FT MOD_RES 378
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:2211721"
FT VAR_SEQ 151..172
FT /note="LNDNPSPWIYRELKRSLDKTNA -> KHCWVSGEKSQRSGCQTALCNL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043354"
FT VAR_SEQ 173..719
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043355"
FT VAR_SEQ 684..687
FT /note="TMQT -> VKVI (in isoform p69)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1577824"
FT /id="VSP_003741"
FT VAR_SEQ 688..719
FT /note="Missing (in isoform p69)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1577824"
FT /id="VSP_003742"
FT MUTAGEN 2
FT /note="G->A,D: No loss of activity."
FT /evidence="ECO:0000269|PubMed:9880569"
FT MUTAGEN 408
FT /note="D->A: Loss of activity; when associated with A-410."
FT /evidence="ECO:0000269|PubMed:10464285"
FT MUTAGEN 410
FT /note="D->A: Loss of activity; when associated with A-408."
FT /evidence="ECO:0000269|PubMed:10464285"
FT MUTAGEN 421
FT /note="Y->P,A: Significant loss of activity."
FT /evidence="ECO:0000269|PubMed:11986302"
FT MUTAGEN 481
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10464285"
FT MUTAGEN 544
FT /note="R->A,Y: Significant loss of activity."
FT /evidence="ECO:0000269|PubMed:11986302"
FT MUTAGEN 547
FT /note="K->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:11986302"
FT MUTAGEN 668
FT /note="C->A: Loss of activity; when associated with A-669
FT and A-670."
FT /evidence="ECO:0000269|PubMed:10464285"
FT MUTAGEN 669
FT /note="F->A: Loss of activity; when associated with A-668
FT and A-670."
FT /evidence="ECO:0000269|PubMed:10464285"
FT MUTAGEN 670
FT /note="K->A: Loss of activity; when associated with A-668
FT and A-669."
FT /evidence="ECO:0000269|PubMed:10464285"
FT CONFLICT 45..47
FT /note="LQE -> CRN (in Ref. 1; AAA60607/AAA60606)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="F -> S (in Ref. 1; AAA60607/AAA60606)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="C -> G (in Ref. 1; AAA60607/AAA60606)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="A -> G (in Ref. 1; AAA60607/AAA60606)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="A -> D (in Ref. 1; AAA60607/AAA60606)"
FT /evidence="ECO:0000305"
FT CONFLICT 662..663
FT /note="EW -> VR (in Ref. 1; AAA60607/AAA60606)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="F -> FWRSSGNRF (in Ref. 1; AAA60607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 719 AA; 82431 MW; 1B680D397D5EDB78 CRC64;
MGNGESQLSS VPAQKLGWFI QEYLKPYEEC QTLIDEMVNT ICDVLQEPEQ FPLVQGVAIG
GSYGRKTVLR GNSDGTLVLF FSDLKQFQDQ KRSQRDILDK TGDKLKFCLF TKWLKNNFEI
QKSLDGFTIQ VFTKNQRISF EVLAAFNALS LNDNPSPWIY RELKRSLDKT NASPGEFAVC
FTELQQKFFD NRPGKLKDLI LLIKHWHQQC QKKIKDLPSL SPYALELLTV YAWEQGCRKD
NFDIAEGVRT VLELIKCQEK LCIYWMVNYN FEDETIRNIL LHQLQSARPV ILDPVDPTNN
VSGDKICWQW LKKEAQTWLT SPNLDNELPA PSWNVLPAPL FTTPGHLLDK FIKEFLQPNK
CFLEQIDSAV NIIRTFLKEN CFRQSTAKIQ IVRGGSTAKG TALKTGSDAD LVVFHNSLKS
YTSQKNERHK IVKEIHEQLK AFWREKEEEL EVSFEPPKWK APRVLSFSLK SKVLNESVSF
DVLPAFNALG QLSSGSTPSP EVYAGLIDLY KSSDLPGGEF STCFTVLQRN FIRSRPTKLK
DLIRLVKHWY KECERKLKPK GSLPPKYALE LLTIYAWEQG SGVPDFDTAE GFRTVLELVT
QYQQLCIFWK VNYNFEDETV RKFLLSQLQK TRPVILDPAE PTGDVGGGDR WCWHLLAKEA
KEWLSSPCFK DGTGNPIPPW KVPTMQTPGS CGARIHPIVN EMFSSRSHRI LNNNSKRNF
