GPCRDB: Swiss-Prot entry

ID   PRIO_FELCA     STANDARD;      PRT;   256 AA.
AC   O18754; O19016;
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).
GN   Name=PRNP; Synonyms=PRP;
OS   Felis silvestris catus (Cat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Carnivora; Fissipedia; Felidae; Felis. 
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood, and Brain;
RA   Rohwer R.G., Edelman D., Protzman J.L.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 112-235.
RA   Taylor M.S., Newton D.J., Flanagan B.F., Christmas S.E.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: Ref.1 sequence seems to be incorrect, it is too close in
CC       sequence to that of sheep to be taxonomically correct. We have
CC       used Ref.2 sequence in the region where it is available (112-235),
CC       but the rest of the sequence probably contains incorrect residues.
CC   -!- DATABASE: NAME=Cat PRP; NOTE=Web page on cat sequence problems;
CC       WWW="http://www.mad-cow.org/~tom/cat_prion.html".
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; AF003087; AAB70468.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; Y13698; CAA74032.1; -. [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; 5.
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; O18754.
DR   ProtoNet; O18754.
DR   ProtoMap; O18754.
DR   PRESAGE; O18754.
DR   DIP; O18754.
DR   ModBase; O18754.
DR   SMR; O18754.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Prion; Repeat;
KW   Signal.
FT   SIGNAL        1     24       By similarity.
FT   CHAIN        25    233       Major prion protein.
FT   PROPEP      234    256       Removed in mature form (Potential).
FT   LIPID       233    233       GPI-anchor amidated alanine (Potential).
FT   CARBOHYD    184    184       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    200    200       N-linked (GlcNAc...) (Potential).
FT   DISULFID    182    217       By similarity.
FT   DOMAIN       54     95       5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
FT                                Q.
FT   REPEAT       54     62       1.
FT   REPEAT       63     70       2.
FT   REPEAT       71     78       3.
FT   REPEAT       79     86       4.
FT   REPEAT       87     95       5.
FT   CONFLICT    162    162       D -> N (in Ref. 1).
FT   CONFLICT    180    180       R -> H (in Ref. 1).
FT   CONFLICT    190    190       R -> H (in Ref. 1).
FT   CONFLICT    206    206       M -> I (in Ref. 1).
FT   CONFLICT    218    218       V -> I (in Ref. 1).
FT   CONFLICT    223    223       K -> R (in Ref. 1).
FT   CONFLICT    232    232       R -> G (in Ref. 1).
FT   CONFLICT    235    235       A -> V (in Ref. 1).
SQ   SEQUENCE   256 AA;  27975 MW;  7C687C3BCE6BEBB9 CRC64;
     MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW
     GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GGWGQGGSHS QWNKPSKPKT NMKHVAGAAA
     AGAVVGGLGG YMLGSAMSRP LIHFGNDYED RYYRENMYRY PDQVYYRPVD QYSNQNNFVR
     DCVNITVKQR TVTTTTKGEN FTETDMKIME RVVEQMCVTQ YQKESEAYYQ RRASAILFSS
     PPVILLISFL IFLIVG
//