GPCRDB: Swiss-Prot entry

ID   PRIO_CRIMI     STANDARD;      PRT;   254 AA.
AC   Q60468;
DT   15-JUL-1998 (Rel. 36, Created)
DT   15-JUL-1998 (Rel. 36, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Major prion protein precursor (PrP) (PrP27-30) (PrP33-35C).
GN   Name=PRNP;
OS   Cricetulus migratorius (Armenian hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Cricetinae; 
OC   Cricetulus. 
OX   NCBI_TaxID=10032;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=90158578; PubMed=2406562 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Lowenstein D.H., Butler D.A., Westaway D., McKinley M.P.,
RA   DeArmond S.J., Prusiner S.B.;
RT   "Three hamster species with different scrapie incubation times and
RT   neuropathological features encode distinct prion proteins.";
RL   Mol. Cell. Biol. 10:1153-1163(1990).
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: PrP is found in high quantity in the brain of humans and
CC       animals infected with the degenerative neurological diseases 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.
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 as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M33959; AAA37014.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P04925; 1AG2. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   InterPro; IPR000817; Prion.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00377; Prion; 1.
DR   Pfam; PF03991; Prion_octapep; 6.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00341; PRION.
DR   PROSITE; PS00291; PRION_1; 1.
DR   PROSITE; PS00706; PRION_2; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q60468.
DR   ProtoNet; Q60468.
DR   ProtoMap; Q60468.
DR   PRESAGE; Q60468.
DR   DIP; Q60468.
DR   ModBase; Q60468.
DR   SMR; Q60468.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Glycoprotein; GPI-anchor; Lipoprotein; Prion; Repeat; Signal.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    231       Major prion protein.
FT   PROPEP      232    254       Removed in mature form.
FT   LIPID       231    231       GPI-anchor amidated serine.
FT   DOMAIN       90    231       PrP27-30 (protease resistant core).
FT   CARBOHYD    181    181       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD    197    197       N-linked (GlcNAc...) (By similarity).
FT   DISULFID    179    214       By similarity.
FT   DOMAIN       51     91       5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
FT                                Q.
FT   REPEAT       51     59       1.
FT   REPEAT       60     67       2.
FT   REPEAT       68     75       3.
FT   REPEAT       76     83       4.
FT   REPEAT       84     91       5.
SQ   SEQUENCE   254 AA;  27855 MW;  7B963FC6F77F9D0F CRC64;
     MANLSYWLLA LFVATWTDVG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGTWGQP
     HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHNQWN KPNKPKTSMK HMAGAAAAGA
     VVGGLGGYML GSAMSRPMLH FGNDWEDRYY RENMNRYPNQ VYYRPVDQYN NQNNFVHDCV
     NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCVTQYQK ESQAYYDGRR SSAVLFSSPP
     VILLISFLIF LIVG
//