OAS1D_MOUSE
ID OAS1D_MOUSE Reviewed; 361 AA.
AC Q8VI95; Q3UWZ6; Q7TPY2;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Inactive 2'-5'-oligoadenylate synthase 1D {ECO:0000305};
GN Name=Oas1d {ECO:0000312|MGI:MGI:2140770};
GN Synonyms=Oasl8 {ECO:0000303|PubMed:12396720};
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:BAC35788.1};
RN [1] {ECO:0000312|EMBL:BAB84132.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB84132.1};
RC TISSUE=Ovary {ECO:0000312|EMBL:BAB84132.1};
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 [2] {ECO:0000312|EMBL:AAL12825.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/RV {ECO:0000312|EMBL:AAL12825.1};
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:BAC35788.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC35788.1};
RC TISSUE=Ovary {ECO:0000312|EMBL:BAC35788.1};
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:EDL19742.1}
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:AAH52835.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52835.1};
RC TISSUE=Egg {ECO:0000312|EMBL:AAH52835.1};
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, INTERACTION WITH OAS1A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15899864; DOI=10.1128/mcb.25.11.4615-4624.2005;
RA Yan W., Ma L., Stein P., Pangas S.A., Burns K.H., Bai Y., Schultz R.M.,
RA Matzuk M.M.;
RT "Mice deficient in oocyte-specific oligoadenylate synthetase-like protein
RT OAS1D display reduced fertility.";
RL Mol. Cell. Biol. 25:4615-4624(2005).
RN [8] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17567914; DOI=10.1186/1471-213x-7-67;
RA Joshi S., Davies H., Sims L.P., Levy S.E., Dean J.;
RT "Ovarian gene expression in the absence of FIGLA, an oocyte-specific
RT transcription factor.";
RL BMC Dev. Biol. 7:67-67(2007).
RN [9] {ECO:0000305}
RP 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'-olygoadenylate synthetase activity, but
CC can bind double-stranded RNA (PubMed:15899864, PubMed:12396720). May
CC play a role in the control of female fertility, possibly by binding to
CC and inhibiting OAS1A (PubMed:15899864). {ECO:0000269|PubMed:12396720,
CC ECO:0000269|PubMed:15899864}.
CC -!- SUBUNIT: Interacts with OAS1A, the interaction inhibits OAS1A catalytic
CC activity. {ECO:0000269|PubMed:15899864}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899864}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in oocytes (at protein
CC level) (PubMed:15899864). Expressed at highest level in ovary with
CC lesser amounts in intestine, brain, thymus lung, kidney, liver and
CC uterus (PubMed:17567914, PubMed:27663720).
CC {ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:17567914,
CC ECO:0000269|PubMed:27663720}.
CC -!- DEVELOPMENTAL STAGE: Detected in fully grown, germinal vesicle (GV)-
CC intact oocytes and in oocytes at the metaphase II stage, with levels
CC decreasing thereafter (at protein level) (PubMed:15899864). Detected 1
CC week after birth in developing ovary (PubMed:27663720). Detected at
CC 17.5 dpc, with levels increasing thereafter (PubMed:17567914).
CC {ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:17567914,
CC ECO:0000269|PubMed:27663720}.
CC -!- INDUCTION: Unlike other OAS1 proteins, not induced by
CC polyinosinic:polycytidylic acid (poly I:C).
CC {ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:27663720}.
CC -!- DISRUPTION PHENOTYPE: Newborn mice are viable. Female mice display
CC reduced fertility due to deficiencies in ovarian follicle development,
CC reduced efficiency of ovulation, and the arrest of fertilized eggs at
CC one-cell stage. {ECO:0000269|PubMed:15899864}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
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DR EMBL; AB067532; BAB84132.1; -; mRNA.
DR EMBL; AY055829; AAL12825.1; -; mRNA.
DR EMBL; AK054465; BAC35788.1; -; mRNA.
DR EMBL; AK136001; BAE22768.1; -; mRNA.
DR EMBL; AC015535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL19742.1; -; Genomic_DNA.
DR EMBL; BC052835; AAH52835.1; -; mRNA.
DR CCDS; CCDS19631.1; -.
DR RefSeq; NP_598654.1; NM_133893.3.
DR AlphaFoldDB; Q8VI95; -.
DR SMR; Q8VI95; -.
DR STRING; 10090.ENSMUSP00000048054; -.
DR MaxQB; Q8VI95; -.
DR PaxDb; Q8VI95; -.
DR PRIDE; Q8VI95; -.
DR DNASU; 100535; -.
DR Ensembl; ENSMUST00000044224; ENSMUSP00000048054; ENSMUSG00000032623.
DR GeneID; 100535; -.
DR KEGG; mmu:100535; -.
DR UCSC; uc008zik.2; mouse.
DR CTD; 100535; -.
DR MGI; MGI:2140770; Oas1d.
DR VEuPathDB; HostDB:ENSMUSG00000032623; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_040930_0_0_1; -.
DR InParanoid; Q8VI95; -.
DR OMA; RIYWTWC; -.
DR OrthoDB; 611234at2759; -.
DR PhylomeDB; Q8VI95; -.
DR TreeFam; TF329749; -.
DR BRENDA; 2.7.7.84; 3474.
DR BioGRID-ORCS; 100535; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8VI95; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VI95; protein.
DR Bgee; ENSMUSG00000032623; Expressed in secondary oocyte and 10 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA: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:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:MGI.
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:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IMP: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 Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR InterPro; IPR026774; 2-5A_synthase.
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 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..361
FT /note="Inactive 2'-5'-oligoadenylate synthase 1D"
FT /id="PRO_0000440962"
FT CONFLICT 60
FT /note="V -> A (in Ref. 6; AAH52835)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="G -> W (in Ref. 1; BAE22768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 42831 MW; 7060C551B0601A6B CRC64;
MARELFRTPI WRLDKFIEDQ LLPDTTFLTE LRADIDSISA FLMERCFQGA AHPVRVSRVV
MGGCYNEYTV LKGRSEANMV VFLINLTSFE DQFNGQVVFI EEIWRHLLQL QQEKLCKLKF
EVQSPKEPNS RFLSFKLSCP ERQHELEFDV QPAYDALYEV RHFKPFDSSN YNKVYAQLTH
ECTTLEKEGE FSICFTDLHQ SFLRYRAPKL WNLIRLVKHW YQLCKEKLRG PLPPQYALEL
LTVYVWEYGI HENPGLHTAQ CFRTVLELVT KYKRLRIYWT WCYDFQHEIS DYLQGQIKKA
RPLILDPADP TRNVAGSDLQ AWDLLAKEAQ IWIDSTFFTN HDMSIVEAWE VMPERQECVF
L
