GPCRDB: Swiss-Prot entry
ID PRIO_ATEPA STANDARD; PRT; 252 AA.
AC P51446;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, 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 Ateles paniscus (Black spider monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Platyrrhini; Cebidae; Atelinae; Ateles.
OX NCBI_TaxID=9510;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain;
RX MEDLINE=95083661; PubMed=7991600 [NCBI, ExPASy, EBI, Israel, Japan];
RA Cervenakova L., Brown P., Goldfarb L.G., Nagle J., Pettrone K.,
RA Rubenstein R., Dubnick M., Gibbs C.J., Gajdusek D.C.;
RT "Infectious amyloid precursor gene sequences in primates used for
RT experimental transmission of human spongiform encephalopathy.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12159-12162(1994).
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; U15164; AAA68634.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P23907; 1G04. [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; P51446.
DR ProtoNet; P51446.
DR ProtoMap; P51446.
DR PRESAGE; P51446.
DR DIP; P51446.
DR ModBase; P51446.
DR SMR; P51446.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Glycoprotein; GPI-anchor; Lipoprotein; Prion; Repeat; Signal.
FT SIGNAL 1 22 By similarity.
FT CHAIN 23 229 Major prion protein.
FT PROPEP 230 252 Removed in mature form (By similarity).
FT LIPID 229 229 GPI-anchor amidated serine (By
FT similarity).
FT DISULFID 178 213 By similarity.
FT CARBOHYD 180 180 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 196 196 N-linked (GlcNAc...) (Potential).
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.
SQ SEQUENCE 252 AA; 27718 MW; 20EA38A42DCC56D1 CRC64;
MANLGYWMLV LFVATWSDLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGWGQPH
GGGWGQPHGG GWGQPHGGGW GQPHGGGWGQ AGGTHNQWNK PSKPKTNMKH MAGAAAAGAV
VGGLGGYMLG SAMSRPLIHF GNDYEDRYYR ENMYRYPNQV YYRPVDQYNN QNNFVHDCVN
ITIKQHTVTT TTKGENLTET DVKMMERVVE QMCITQYERE SQAYYQRGSS MVLFSSPPVI
LLISFLIFLI VG
//