Swiss-Prot entry
ID PRIO_PAPHA STANDARD; PRT; 253 AA.
AC P67996; P40254;
DT 01-FEB-1995 (Rel. 31, Created)
DT 01-FEB-1995 (Rel. 31, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Major prion protein precursor (PrP) (PrP27-30) (PrP33-35C).
GN Name=PRNP; Synonyms=PRP;
OS Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=95139066; PubMed=7837269 [NCBI, ExPASy, EBI, Israel, Japan];
RA Schaetzl H.M., Da Costa M., Taylor L., Cohen F.E., Prusiner S.B.;
RT "Prion protein gene variation among primates.";
RL J. Mol. Biol. 245:362-374(1995).
RN [2]
RP ERRATUM.
RX PubMed=9020986 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1006/jmbi.1996.0791;
RA Schaetzl H.M., Da Costa M., Taylor L., Cohen F.E., Prusiner S.B.;
RL J. Mol. Biol. 265:257-257(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 (By
CC similarity).
CC -!- SUBUNIT: PrP has a tendency to aggregate yielding polymers called
CC "rods" (By similarity).
CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a GPI-anchor (By
CC similarity).
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; U08294; AAC50083.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P23907; 1G04. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P67996; 119-226.
DR InterPro; IPR000817; Prion.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00377; Prion; 1.
DR Pfam; PF03991; Prion_octapep; 5.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00341; PRION.
DR SMART; SM00157; PRP; 1.
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; P67996.
DR ProtoNet; P67996.
DR ProtoMap; P67996.
DR PRESAGE; P67996.
DR DIP; P67996.
DR ModBase; P67996.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Prion; Repeat;
KW Signal.
FT SIGNAL 1 22 By similarity.
FT CHAIN 23 230 Major prion protein.
FT PROPEP 231 253 Removed in mature form (By similarity).
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.
FT REGION 51 91 5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
FT Q.
FT LIPID 230 230 GPI-anchor amidated serine (By
FT similarity).
FT CARBOHYD 181 181 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 197 197 N-linked (GlcNAc...) (Potential).
FT DISULFID 179 214 By similarity.
SQ SEQUENCE 253 AA; 27676 MW; F01D5EA64AB68C31 CRC64;
MANLGCWMLV LFVATWSDLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGGWGQP
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHNQWH KPSKPKTSMK HMAGAAAAGA
VVGGLGGYML GSAMSRPLIH FGNDYEDRYY RENMYRYPNQ VYYRPVDQYS NQNNFVHDCV
NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCITQYEK ESQAYYQRGS SMVLFSSPPV
ILLISFLIFL IVG
//