ID H9GZX8_HORSE Unreviewed; 365 AA.
AC H9GZX8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=2'-5' oligoadenylate synthase {ECO:0000256|ARBA:ARBA00012577};
DE EC=2.7.7.84 {ECO:0000256|ARBA:ARBA00012577};
GN Name=OAS1 {ECO:0000313|Ensembl:ENSECAP00000011171.3,
GN ECO:0000313|VGNC:VGNC:20997};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000011171.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000011171.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000011171.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000011171.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000011171.3};
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 AlphaFoldDB; H9GZX8; -.
DR STRING; 9796.ENSECAP00000011171; -.
DR PaxDb; 9796-ENSECAP00000011171; -.
DR Ensembl; ENSECAT00000014019.3; ENSECAP00000011171.3; ENSECAG00000013435.4.
DR VGNC; VGNC:20997; OAS1.
DR GeneTree; ENSGT00510000046406; -.
DR HOGENOM; CLU_040930_0_0_1; -.
DR InParanoid; H9GZX8; -.
DR OMA; VHIISTF; -.
DR TreeFam; TF329749; -.
DR Proteomes; UP000002281; Chromosome 8.
DR Bgee; ENSECAG00000013435; Expressed in epithelium of bronchus and 21 other cell types or tissues.
DR ExpressionAtlas; H9GZX8; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IBA:GO_Central.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
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:SF13; 2'-5'-OLIGOADENYLATE SYNTHASE 1; 1.
DR PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
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:UP000002281}.
FT DOMAIN 27..71
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 130..314
FT /note="2'-5'-oligoadenylate synthetase 1"
FT /evidence="ECO:0000259|Pfam:PF10421"
SQ SEQUENCE 365 AA; 41546 MW; 65A7BAEE32BB9CCE CRC64;
VDGRILVGAG GVKTGNALGP GLALKNGGSS GKGTTLRGRS DADLVVFLDY LTSFREQFER
RAEFIEEIRR QLKACQREKR FDVEFEVQGQ QWARPRALSF VLTSPQLNEG VEFDVLPAFD
VLGQVTTSYR PDPDIYVLLI KECQSLGKEG EFSPCFTELQ RAFLRQRPTK LKSLIRLVKH
WYQKCKDKLG KPLPAQYALE LLTVYAWEQG SRQTEFNTAQ GFRTVLELVL NYQQLCIYWT
KYYNFDDPVI GQYLKRQLKK PRPVILDPAD PTGNVGGGDP RGWPRLAQEA RAWLSYPCFK
NWDGSPVGSW DVGPEEDSED DTLTWAERAY YQCDHGWRPE FPQTGSTPQR ASAPDAEENW
TCTIL
//