GenomeNet

Database: UniProt
Entry: F7FHW2_RAT
LinkDB: F7FHW2_RAT
Original site: F7FHW2_RAT 
ID   F7FHW2_RAT              Unreviewed;       378 AA.
AC   F7FHW2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 2.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Inactive 2'-5'-oligoadenylate synthase 1B {ECO:0000313|Ensembl:ENSRNOP00000042591};
GN   Name=Oas1k {ECO:0000313|RGD:1359279};
GN   Synonyms=Oas1b {ECO:0000313|Ensembl:ENSRNOP00000042591};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000042591, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000042591, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000042591,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000042591}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000042591};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the 2-5A synthase family.
CC       {ECO:0000256|ARBA:ARBA00009526}.
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DR   EMBL; AABR07036378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07036379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07036380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07072299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC098508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F7FHW2; -.
DR   SMR; F7FHW2; -.
DR   Ensembl; ENSRNOT00000048782; ENSRNOP00000042591; ENSRNOG00000033220.
DR   RGD; 708393; Oas1b.
DR   RGD; 1359279; Oas1k.
DR   VEuPathDB; HostDB:ENSRNOG00000033220; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000033220; Expressed in lung and 19 other cell types or tissues.
DR   ExpressionAtlas; F7FHW2; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; 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; PS50152; 25A_SYNTH_3; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        356..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..118
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          163..347
FT                   /note="2'-5'-oligoadenylate synthetase 1"
FT                   /evidence="ECO:0000259|Pfam:PF10421"
SQ   SEQUENCE   378 AA;  43705 MW;  57A57282E7023914 CRC64;
     MEKDLKSTPA SELDKFIQDH LLPDTTFRDE VRADIDFICT FLKEKCFHGA ALKVSKVVKG
     GSSGKGTTLQ GKSDADLVVF LNNLTSFEDQ LKRRGEVIEK IRKHLCQLQQ EKQFKLKFEF
     QTPEQANSRS LSFKLSSPQL QHVVKFDVLP AYDVLGHVNI NSKPNAQIYA SLIRKCTDLN
     KEGAFSTCFT ELQRNFLKRR PTKLKSLIRL VKHWYQLCKE KLGDPLPPQY ALELLTIYAW
     ERGGRLTKFN TAQGFRTVLE LITKYKQLLI YWTVCYDFQH PEVSKYLRRQ LKKPRPVILD
     PANPTGNIAG SNPKGWRRLA GEAAAWLRYP CFKYKDGFPV CPWDVPTEVD IPSQNYFFHI
     ICLIFWLLLR LIFGKHSV
//
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