ID 25A2_HUMAN STANDARD; PRT; 726 AA. AC P29728; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE (2'-5')OLIGOADENYLATE SYNTHETASE 2 (EC 2.7.7.-) ((2-5')OLIGO(A) DE SYNTHETASE 2) (2-5A SYNTHETASE 2) (P69/P71) (P69OAS/P71OAS). GN OAS2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92250658; PubMed=1577824; RA Marie I., Hovanessian A.G.; RT "The 69-kDa 2-5A synthetase is composed of two homologous and adjacent RT functional domains."; RL J. Biol. Chem. 267:9933-9939(1992). CC -!- CATALYTIC ACTIVITY: BINDS DOUBLE-STRANDED RNA AND POLYMERIZES ATP CC INTO PPP(A2'P5'A)N OLIGOMERS, WHICH ACTIVATE THE LATENT RNASE L CC THAT, WHEN ACTIVATED, CLEAVES SINGLE-STRANDED RNAS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: ASSOCIATED WITH DIFFERENT SUBCELLULAR CC FRACTIONS SUCH AS MITOCHONDRIAL, NUCLEAR, AND ROUGH/SMOOTH CC MICROSOMAL FRACTIONS. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; 71 KDA/P71 (SHOWN HERE) AND 69 CC KDA/P69; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- INDUCTION: BY INTERFERONS. CC -!- SIMILARITY: BELONGS TO THE 2-5A SYNTHETASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M87434; AAA60607.1; -. DR EMBL; M87284; AAA60606.1; -. DR MIM; 603350; -. DR INTERPRO; IPR001797; -. DR INTERPRO; IPR002934; -. DR PFAM; PF01909; NTP_transf_2; 1. DR PROSITE; PS00832; 25A_SYNTH_1; 2. DR PROSITE; PS00833; 25A_SYNTH_2; 2. KW RNA-binding; Transferase; Nucleotidyltransferase; Duplication; KW Interferon induction; Alternative splicing; Myristate. FT INIT_MET 0 0 PROBABLE. FT LIPID 1 1 MYRISTATE (PROBABLE). FT DOMAIN 10 334 OAS DOMAIN 1. FT DOMAIN 325 345 PRO-RICH (LINKER). FT DOMAIN 342 682 OAS DOMAIN 2. FT VARSPLIC 683 686 TMQT -> VKVI (IN ISOFORM P69). FT VARSPLIC 687 726 MISSING (IN ISOFORM P69). SQ SEQUENCE 726 AA; 83157 MW; B69393195C6CA190 CRC64; GNGESQLSSV PAQKLGWFIQ EYLKPYEECQ TLIDEMVNTI CDVCRNPEQF PLVQGVAIGG SYGRKTVLRG NSDGTLVLFF SDLKQFQDQK RSQRDILDKT GDKLKFCLFT KWLKNNFEIQ KSLDGSTIQV FTKNQRISFE VLAAFNALSL NDNPSPWIYR ELKRSLDKTN ASPGEFAVCF TELQQKFFDN RPGKLKDLIL LIKHWHQQCQ KKIKDLPSLS PYALELLTVY AWEQGCRKDN FDIAEGVRTV LELIKCQEKL CIYWMVNYNF EDETIRNILL HQLQSARPVI LDPVDPTNNV SGDKICWQWL KKEAQTWLTS PNLDNELPAP SWNVLPAPLF TTPGHLLDKF IKEFLQPNKC FLEQIDSAVN IIRTFLKENC FRQSTAKIQI VRGGSTAKGT ALKTGSDADL VVFHNSLKSY TSQKNERHKI VKEIHEQLKA FWREKEEELE VSFEPPKWKA PRVLSFSLKS KVLNESVSFD VLPAFNALGQ LSSGSTPSPE VYAGLIDLYK SSDLPGGEFS TCFTVLQRNF IRSRPTKLKD LIRLVKHWYK ECERKLKPKG SLPPKYALEL LTIYAWEQGS GVPDFDTAEG FRTVLELVTQ YQQLGIFWKV NYNFEDETVR KFLLSQLQKT RPVILDPGEP TGDVGGGDRW CWHLLDKEAK VRLSSPCFKD GTGNPIPPWK VPTMQTPGSC GARIHPIVNE MFSSRSHRIL NNNSKRNFWR SSGNRF //