GPCRDB: Swiss-Prot entry

ID   PRIO_CALMO     STANDARD;      PRT;   241 AA.
AC   P40248;
DT   01-FEB-1995 (Rel. 31, Created)
DT   01-FEB-1995 (Rel. 31, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Major prion protein precursor (PrP) (PrP27-30) (PrP33-35C) (Fragment).
GN   Name=PRNP;
OS   Callicebus moloch (Dusky titi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Primates; Platyrrhini; Cebidae; Callicebinae; 
OC   Callicebus. 
OX   NCBI_TaxID=9523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=95139066; PubMed=7837269 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Schatzl H.M., Dacosta M., Taylor L., Cohen F.E., Prusiner S.B.;
RT   "Prion protein gene variation among primates.";
RL   J. Mol. Biol. 245:362-374(1995).
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; U08312; AAC50100.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; S71048; S71048.
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   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P40248.
DR   ProtoNet; P40248.
DR   ProtoMap; P40248.
DR   PRESAGE; P40248.
DR   DIP; P40248.
DR   ModBase; P40248.
DR   SMR; P40248.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Prion; Repeat;
KW   Signal.
FT   NON_TER       1      1
FT   SIGNAL       <1     15       By similarity.
FT   CHAIN        16    223       Major prion protein.
FT   PROPEP      224   >241       Removed in mature form (By similarity).
FT   DISULFID    172    207       By similarity.
FT   LIPID       223    223       GPI-anchor amidated serine (By
FT                                similarity).
FT   CARBOHYD    174    174       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    190    190       N-linked (GlcNAc...) (Potential).
FT   DOMAIN       44     84       5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
FT                                Q.
FT   REPEAT       44     52       1.
FT   REPEAT       53     60       2.
FT   REPEAT       61     68       3.
FT   REPEAT       69     76       4.
FT   REPEAT       77     84       5.
FT   NON_TER     241    241
SQ   SEQUENCE   241 AA;  26373 MW;  C6D2013EE7CAEC93 CRC64;
     MLVLFVATWS DLGLCKKRPK PGGWNTGGSR YPGQGSPGGN RYPPQGGGSW GQPHGGGWGQ
     PHGGGWGQPH GGGWGQPHGG GWGQGGGTHN QWNKPSKPKT NMKHVAGAAA AGAVVGGLGG
     YMLGSAMSRP LIHFGNDYED RYYRENMYRY PNQVYYRPVD QYSNQNNFVH DCVNITIKQH
     TVTTTTKGEN FTETDVKMME RVVEQMCITQ YEKESQAYYQ RGSSMVLFSS PPVILLISFL
     I
//