OAS1C_MOUSE
ID OAS1C_MOUSE Reviewed; 362 AA.
AC Q924S2;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Inactive 2'-5' oligoadenylate synthetase 1C {ECO:0000305};
DE AltName: Full=2',5'-oligoadenylate synthetase-like 5 {ECO:0000303|PubMed:11418248};
GN Name=Oas1c {ECO:0000312|MGI:MGI:2149633};
GN Synonyms=Oasl5 {ECO:0000303|PubMed:11418248, ECO:0000312|MGI:MGI:2149633};
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 {ECO:0000312|EMBL:BAC26225.1};
RN [1] {ECO:0000312|EMBL:BAB62296.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:BAB62296.1};
RX PubMed=11418248; DOI=10.1016/s0378-1119(01)00508-x;
RA Shibata S., Kakuta S., Hamada K., Sokawa Y., Iwakura Y.;
RT "Cloning of a novel 2',5'-oligoadenylate synthetase-like molecule, Oasl5 in
RT mice.";
RL Gene 271:261-271(2001).
RN [2] {ECO:0000312|EMBL:AAM47560.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/RV {ECO:0000312|EMBL:AAM47560.1};
RX PubMed=12080145; DOI=10.1073/pnas.142287799;
RA Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
RA Brinton M.A.;
RT "Positional cloning of the murine flavivirus resistance gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
RN [3] {ECO:0000312|EMBL:BAC26225.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26225.1};
RC TISSUE=Cecum {ECO:0000312|EMBL:BAC37475.1},
RC Egg {ECO:0000312|EMBL:BAE37260.1}, and Skin {ECO:0000312|EMBL:BAC26225.1};
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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] {ECO:0000312|EMBL:EDL19749.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000312|EMBL:AAI08956.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=27663720; DOI=10.1016/j.meegid.2016.09.018;
RA Elkhateeb E., Tag-El-Din-Hassan H.T., Sasaki N., Torigoe D., Morimatsu M.,
RA Agui T.;
RT "The role of mouse 2',5'-oligoadenylate synthetase 1 paralogs.";
RL Infect. Genet. Evol. 45:393-401(2016).
CC -!- FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-
CC stranded RNA. {ECO:0000269|PubMed:11418248,
CC ECO:0000269|PubMed:27663720}.
CC -!- TISSUE SPECIFICITY: Expressed at highest level in brain with lesser
CC amounts in spleen, kidney, stomach, liver, intestine, ovary, skin and
CC testis. Not detected in lung, thymus, heart and uterus.
CC {ECO:0000269|PubMed:11418248, ECO:0000269|PubMed:27663720}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem cells and embryonic
CC fibroblasts (PubMed:11418248). Detected 1 week after birth in
CC developing ovary (PubMed:27663720). {ECO:0000269|PubMed:11418248,
CC ECO:0000269|PubMed:27663720}.
CC -!- INDUCTION: By interferon (IFN) and polyinosinic:polycytidylic acid
CC (poly I:C). {ECO:0000269|PubMed:11418248, ECO:0000269|PubMed:27663720}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; AB067528; BAB62296.1; -; mRNA.
DR EMBL; AF459815; AAM47560.1; -; mRNA.
DR EMBL; AK028986; BAC26225.1; -; mRNA.
DR EMBL; AK078952; BAC37475.1; -; mRNA.
DR EMBL; AK163253; BAE37260.1; -; mRNA.
DR EMBL; AC115937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL19749.1; -; Genomic_DNA.
DR EMBL; BC108955; AAI08956.1; -; mRNA.
DR EMBL; BC126877; AAI26878.1; -; mRNA.
DR CCDS; CCDS19626.1; -.
DR RefSeq; NP_291019.1; NM_033541.4.
DR AlphaFoldDB; Q924S2; -.
DR SMR; Q924S2; -.
DR STRING; 10090.ENSMUSP00000112584; -.
DR MaxQB; Q924S2; -.
DR PaxDb; Q924S2; -.
DR PRIDE; Q924S2; -.
DR ProteomicsDB; 289955; -.
DR DNASU; 114643; -.
DR Ensembl; ENSMUST00000117193; ENSMUSP00000112584; ENSMUSG00000001166.
DR GeneID; 114643; -.
DR KEGG; mmu:114643; -.
DR UCSC; uc008zid.1; mouse.
DR CTD; 114643; -.
DR MGI; MGI:2149633; Oas1c.
DR VEuPathDB; HostDB:ENSMUSG00000001166; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_040930_0_0_1; -.
DR InParanoid; Q924S2; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; Q924S2; -.
DR TreeFam; TF329749; -.
DR BRENDA; 2.7.7.84; 3474.
DR BioGRID-ORCS; 114643; 4 hits in 70 CRISPR screens.
DR PRO; PR:Q924S2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q924S2; protein.
DR Bgee; ENSMUSG00000001166; Expressed in animal zygote and 88 other tissues.
DR ExpressionAtlas; Q924S2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISO:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0006006; P:glucose metabolic process; ISO:MGI.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
DR GO; GO:0071659; P:negative regulation of IP-10 production; ISO:MGI.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:1901857; P:positive regulation of cellular respiration; ISO:MGI.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR GO; GO:0060700; P:regulation of ribonuclease activity; ISO:MGI.
DR GO; GO:0009615; P:response to virus; ISO:MGI.
DR GO; GO:0043129; P:surfactant homeostasis; ISO:MGI.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:MGI.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:MGI.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISO:MGI.
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; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR11258; PTHR11258; 1.
DR Pfam; PF10421; OAS1_C; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; RNA-binding.
FT CHAIN 1..362
FT /note="Inactive 2'-5' oligoadenylate synthetase 1C"
FT /id="PRO_0000440068"
SQ SEQUENCE 362 AA; 42912 MW; 3AD6A796879EA75B CRC64;
MENGLCSIQA RELDEFICDY LFPDTTFLTE LRADIDSISA FLKERCFQGA AHPVRVSRVV
MGGSYDEHTA LKGKSEAKMV LFFNNLTSFE EQLKRRGEFV EEIQKHLCQL QQEKPFKVKF
EVQSSEEPNS RSLSFKLSSP ELQQEVEFDV QPAYDVLYEL RNNTYAEPQF YNKVYAQLIH
ECTTLEKEGD FSICFTDLHQ NFMRYRAPKL WNLIRLVKHW YQLCKEKLRE PLPPQYALEL
LTVYVWEHSN KNQEKVTTAK NFRTFLELVA YYKNLRIYWT WYYDFRHQEV CAYLCRQLKK
ARPLILDPAD PTRNVAGSDL QAWDLLAKEA QTWMQSSCFR NCDMSFVPTW DLSPERQECA
FQ
