ID H0V2I1_CAVPO Unreviewed; 1104 AA.
AC H0V2I1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=2'-5' oligoadenylate synthase {ECO:0000256|ARBA:ARBA00012577};
DE EC=2.7.7.84 {ECO:0000256|ARBA:ARBA00012577};
GN Name=OAS3 {ECO:0000313|Ensembl:ENSCPOP00000003747.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000003747.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000003747.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003747.3};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001112};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family.
CC {ECO:0000256|ARBA:ARBA00009526}.
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DR EMBL; AAKN02052364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02052365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0V2I1; -.
DR STRING; 10141.ENSCPOP00000003747; -.
DR Ensembl; ENSCPOT00000004198.3; ENSCPOP00000003747.3; ENSCPOG00000004153.4.
DR VEuPathDB; HostDB:ENSCPOG00000004153; -.
DR eggNOG; ENOG502S649; Eukaryota.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_287245_0_0_1; -.
DR InParanoid; H0V2I1; -.
DR OMA; WQDPVPG; -.
DR TreeFam; TF329749; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000004153; Expressed in uterine cervix and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039530; P:MDA-5 signaling pathway; IEA:Ensembl.
DR GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; IEA:Ensembl.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
DR GO; GO:0035395; P:negative regulation of chemokine (C-X-C motif) ligand 9 production; IEA:Ensembl.
DR GO; GO:0071659; P:negative regulation of IP-10 production; IEA:Ensembl.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0039529; P:RIG-I signaling pathway; IEA:Ensembl.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 2.
DR Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 3.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 3.
DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
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:SF4; 2'-5'-OLIGOADENYLATE SYNTHASE 3; 1.
DR PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 3.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 3.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 3.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 2.
DR PROSITE; PS50152; 25A_SYNTH_3; 3.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT DOMAIN 158..335
FT /note="2'-5'-oligoadenylate synthetase 1"
FT /evidence="ECO:0000259|Pfam:PF10421"
FT DOMAIN 554..731
FT /note="2'-5'-oligoadenylate synthetase 1"
FT /evidence="ECO:0000259|Pfam:PF10421"
FT DOMAIN 767..835
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 891..1071
FT /note="2'-5'-oligoadenylate synthetase 1"
FT /evidence="ECO:0000259|Pfam:PF10421"
FT REGION 350..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 122539 MW; 8D4305F8A0E65F3F CRC64;
MDLYRTAALA LDALVARDLQ PQPEFVGAAR RALGTLDAAL RERRGRQGPK VLKTARGGSF
GRGTALRGGC DSESVVFLDC FESFQDLRAR RAGVLEDTRP LLEAWQQDPG PGLSVQLPAQ
CSPGVLQFRL VSEDLENWMD VTLVPAFDVL GQLNSGAKPK PQVYRTLLSS GCQGGEHAAC
FAELRRSFVN TRPAKLKSLI LLVKHWYRQV RLPSALPPVY ALELLTIFAW EQGCRNPNFS
LAQGLRTVLG LIEQYQQLCV FWTDNYSLED PVIGKSLRQQ LERPRPVILD PADPTWDVGS
GAAWRWDVLA REAASCYDNP CFTQATGDPV QPWDGLVSGG LPRTLGFAQQ AHRAVSHPNH
GDLPQEIPEH SRRHNTKPPR AKNKQPPPAS ASPWVPGTAP DLSRVSPKEL DRFIQDHLKP
SREFQEQVKR GVDGILSCLR ERCTHKVSRI CKGGSFGRGT DLRGDCDAEL VIFFNDLTGF
RGQGPRCVEI LDDMRAQLKS QWQDPVPGLS LKFPEQKVPG ALRCQLVSAA LGSPVDVSLL
PTYDAVGQLT SGAKPKPQVY LALLSSGCQG GEHAACFAEL RRSFVNTRPA KLKSLILLVK
HWYRQVGNTG ASLPPAYALE LLTIFAWEQG CGKDSFSMAQ GLRTVLGLVQ QHGQLCVYWT
LNYGIEEPAL RMHLLDQLRK TRPLVLDPAD PTWNVGQGSW QLLAREATAL EKQICHMSGA
GTAVEPWDVM PALLHQTPAR DLDRFISDFL QPNRQFLAQV NKAVDTICSF LRENCFRDSP
IRVLKVVKGG SSAKGTALRG RSDADIVVFL SCFRHFTEQG IKRAEVISEI RTQLEACQRK
QQFEVKFEIC KWDNPRVLSF TLTSHTLLDQ SVDFDVLPAF DALGHLVSGS RPESRIYADL
IRSYSVPGEF STCFTELQRD FIVSRPTKLK SLIRLVKHWY QESKKMPKGR GSLPPQHGLE
LLTVYAWEQG GRDPQFSMAQ GFRTVLELVT QYRQLCVYWT VNYSAEDKIV GEFLERQLQK
PRPIILDPAD PTGNLGLNAR WDLLAQEAAA CAKALCCMGI DGAPIQPWPV RVRIWGALGR
GPTVTLCLSF PACHVGSAPT GRLG
//