ID PRIO_MOUSE STANDARD; PRT; 254 AA. AC P04925; DT 13-AUG-1987 (REL. 05, CREATED) DT 01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE MAJOR PRION PROTEIN PRECURSOR (PRP) (PRP27-30) (PRP33-35C). GN PRNP OR PRN-P. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NZW, AND I/LNJ; RX MEDLINE; 88052869. RA WESTAWAY D., GOODMAN P.A., MIRENDA C.A., MCKINLEY M.P., CARLSON G.A., RA PRUSINER S.B.; RL CELL 51:651-662(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 86313583. RA LOCHT C., CHESEBRO B., RACE R., KEITH J.M.; RL PROC. NATL. ACAD. SCI. U.S.A. 83:6372-6376(1986). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE; 88166695. RA HOPE J., MULTHAUP G., REEKIE L.J.D., KIMBERLIN R.H., BEYREUTHER K.; RL EUR. J. BIOCHEM. 172:271-277(1988). RN [4] RP SEQUENCE OF 87-164 FROM N.A. RX MEDLINE; 85213844. RA CHESEBRO B., RACE R., WEHRLY K., NISHIO J., BLOOM M., LECHNER D., RA BERGSTROM S., ROBBINS K., MAYER L., KEITH J.M., GARON C., HAASE A.; RL NATURE 315:331-333(1985). RN [5] RP STRUCTURE BY NMR OF 120-230. RX MEDLINE; 96317593. RA RIEK R., HORNEMANN S., WIDER G., BILETER M., GLOCKSHUBER R., RA WUETHRICH K.; RL NATURE 382:180-182(1996). RN [6] RP STRUCTURE BY NMR OF 23-231. RX MEDLINE; 97424376. RA RIEK R., HORNEMANN S., WIDER G., GLOCKSHUBER R., WUETHRICH K.; RL FEBS LETT. 413:282-288(1997). CC -!- FUNCTION: THE FUNCTION OF PRP IS NOT KNOWN. PRP IS ENCODED IN THE CC HOST GENOME AND IS EXPRESSED BOTH IN NORMAL AND INFECTED CELLS. CC -!- SUBUNIT: PRP HAS A TENDENCY TO AGGREGATE YIELDING POLYMERS CALLED CC "RODS". CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR. CC -!- DISEASE: FOUND IN HIGH QUANTITY IN THE BRAIN OF HUMANS AND ANIMALS CC INFECTED WITH DEGENERATIVE NEUROLOGICAL DISEASES SUCH AS KURU, CC CREUTZFELDT-JAKOB DISEASE (CJD), GERSTMANN-STRAUSSLER SYNDROME CC (GSS), SCRAPIE, BOVINE SPONGIFORM ENCEPHALOPATHY (BSE), CC TRANSMISSIBLE MINK ENCEPHALOPATHY (TME), ETC. CC -!- SIMILARITY: BELONGS TO THE PRION FAMILY. DR EMBL; M18070; G200529; -. DR EMBL; M18071; G200531; -. DR EMBL; M13685; G200527; -. DR EMBL; M30384; E30957; -. DR PIR; A22315; A22315. DR PIR; A23544; A23544. DR PIR; A29669; A29669. DR PIR; S02521; S02521. DR PDB; 1AG2; 08-OCT-97. DR MGD; MGI:97769; PRN-P. DR PROSITE; PS00291; PRION_1; 1. DR PROSITE; PS00706; PRION_2; 1. KW PRION; BRAIN; GLYCOPROTEIN; GPI-ANCHOR; REPEAT; SIGNAL; KW DISEASE MUTATION; 3D-STRUCTURE. FT SIGNAL 1 22 FT CHAIN 23 230 MAJOR PRION PROTEIN. FT PROPEP 231 254 REMOVED IN MATURE FORM (BY SIMILARITY). #FT LIPID 230 230 GPI-ANCHOR (BY SIMILARITY). FT LIPID 231 231 GPI-ANCHOR (BY SIMILARITY). FT CARBOHYD 180 180 PROBABLE. FT CARBOHYD 196 196 PROBABLE. FT DISULFID 178 213 FT DOMAIN 51 90 5 X 8 AA TANDEM REPEATS OF P-H-G-G-G-W-G- FT Q. FT REPEAT 51 58 1. FT REPEAT 59 66 2. FT REPEAT 67 74 3. FT REPEAT 75 82 4. FT REPEAT 83 90 5. FT VARIANT 108 108 L -> F (LINKED TO LONG INCUBATION TIME). FT VARIANT 189 189 T -> V (LINKED TO LONG INCUBATION TIME). FT CONFLICT 133 133 M -> V (IN REF. 2 AND 4). SQ SEQUENCE 254 AA; 27977 MW; DC2236E3 CRC32; MANLGYWLLA LFVTMWTDVG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGTWGQPH GGGWGQPHGG SWGQPHGGSW GQPHGGGWGQ GGGTHNQWNK PSKPKTNLKH VAGAAAAGAV VGGLGGYMLG SAMSRPMIHF GNDWEDRYYR ENMYRYPNQV YYRPVDQYSN QNNFVHDCVN ITIKQHTVTT TTKGENFTET DVKMMERVVE QMCVTQYQKE SQAYYDGRRS SSTVLFSSPP VILLISFLIF LIVG //