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Major prion protein (PrP) (ASCR) (PrP27-30) (PrP33-35C) (CD antigen CD230)

 PRIO_HUMAN              Reviewed;         253 AA.
P04156; O60489; P78446; Q15216; Q15221; Q27H91; Q5QPB4; Q8TBG0;
Q96E70; Q9UP19;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1986, sequence version 1.
22-NOV-2017, entry version 229.
RecName: Full=Major prion protein;
Short=PrP;
AltName: Full=ASCR;
AltName: Full=PrP27-30;
AltName: Full=PrP33-35C;
AltName: CD_antigen=CD230;
Flags: Precursor;
Name=PRNP; Synonyms=ALTPRP, PRIP, PRP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3755672; DOI=10.1089/dna.1986.5.315;
Kretzschmar H.A., Stowring L.E., Westaway D., Stubblebine W.H.,
Prusiner S.B., Dearmond S.J.;
"Molecular cloning of a human prion protein cDNA.";
DNA 5:315-324(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT 56-GLY--GLY-63 DEL.
TISSUE=Brain;
PubMed=1678248;
Puckett C., Concannon P., Casey C., Hood L.E.;
"Genomic structure of the human prion protein gene.";
Am. J. Hum. Genet. 49:320-329(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9799790;
Lee I.Y., Westaway D., Smit A.F.A., Wang K., Seto J., Chen L.,
Acharya C., Ankener M., Baskin D., Cooper C., Yao H., Prusiner S.B.,
Hood L.E.;
"Complete genomic sequence and analysis of the prion protein gene
region from three mammalian species.";
Genome Res. 8:1022-1037(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GSD ARG-187.
TISSUE=Blood;
PubMed=10581485;
DOI=10.1002/(SICI)1096-8628(19991215)88:6<653::AID-AJMG14>3.0.CO;2-E;
Cervenakova L., Buetefisch C., Lee H.S., Taller I., Stone G.,
Gibbs C.J. Jr., Brown P., Hallett M., Goldfarb L.G.;
"Novel PRNP sequence variant associated with familial
encephalopathy.";
Am. J. Med. Genet. 88:653-656(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Prostate;
Hryb D.J., Reynolds T.A., Nakhla A.M., Kahn S.M., Khan S.M.,
Romas N.A., Rosner W.;
"Cloning of human prostate prion protein cDNA.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Zhang J., Liu Y., Chen H., Jiang H., Lu W., Zhu X., Xie Q., Cai X.,
Liu X.;
"Analysis and comparison of several mammalian prion protein genes
Prnp.";
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-253.
PubMed=3014653; DOI=10.1126/science.3014653;
Liao Y.-C.J., Lebo R.V., Clawson G.A., Smuckler E.A.;
"Human prion protein cDNA: molecular cloning, chromosomal mapping, and
biological implications.";
Science 233:364-367(1986).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-232, AND VARIANT 56-GLY--GLY-63
DEL.
TISSUE=Brain;
PubMed=1363802; DOI=10.1093/hmg/1.6.443;
Diedrich J.F., Knopman D.S., List J.F., Olson K., Frey W.H.,
Emory C.R., Sung J.H., Haase A.T.;
"Deletion in the prion protein gene in a demented patient.";
Hum. Mol. Genet. 1:443-444(1992).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-253, AND VARIANT
SCHIZOAFFECTIVE DISORDER SER-171.
PubMed=9384372; DOI=10.1038/36757;
Samaia H.B., Mari J.J., Vallada H.P., Moura R.P., Simpson A.J.G.,
Brentani R.R.;
"A prion-linked psychiatric disorder.";
Nature 390:241-241(1997).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-85, AND VARIANT 56-GLY--GLY-63
DEL.
PubMed=7485229; DOI=10.1002/ajmg.1320600104;
Perry R.T., Go R.C., Harrell L.E., Acton R.T.;
"SSCP analysis and sequencing of the human prion protein gene (PRNP)
detects two different 24 bp deletions in an atypical Alzheimer's
disease family.";
Am. J. Med. Genet. 60:12-18(1995).
[13]
PROTEIN SEQUENCE OF 58-85 AND 111-150.
PubMed=1672107;
Tagliavini F., Prelli F., Ghiso J., Bugiani O., Serban D.,
Prusiner S.B., Farlow M.R., Ghetti B., Frangione B.;
"Amyloid protein of Gerstmann-Straussler-Scheinker disease (Indiana
kindred) is an 11 kd fragment of prion protein with an N-terminal
glycine at codon 58.";
EMBO J. 10:513-519(1991).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-91.
PubMed=1683708; DOI=10.1073/pnas.88.23.10926;
Goldfarb L.G., Brown P., McCombie W.R., Goldgaber D., Swergold G.D.,
Wills P.R., Cervenakova L., Baron H., Gibbs C.J. Jr., Gajdusek D.C.;
"Transmissible familial Creutzfeldt-Jakob disease associated with
five, seven, and eight extra octapeptide coding repeats in the PRNP
gene.";
Proc. Natl. Acad. Sci. U.S.A. 88:10926-10930(1991).
[15]
INVOLVEMENT IN HDL1.
PubMed=9792871; DOI=10.1086/302093;
Xiang F., Almqvist E.W., Huq M., Lundin A., Hayden M.R., Edstroem L.,
Anvret M., Zhang Z.;
"A Huntington disease-like neurodegenerative disorder maps to
chromosome 20p.";
Am. J. Hum. Genet. 63:1431-1438(1998).
[16]
COPPER-BINDING, AND FUNCTION.
PubMed=12732622; DOI=10.1074/jbc.M300394200;
Mani K., Cheng F., Havsmark B., Jonsson M., Belting M., Fransson L.A.;
"Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support
S-nitroso-dependent autocleavage of glypican-1 heparan sulfate.";
J. Biol. Chem. 278:38956-38965(2003).
[17]
GLYCOSYLATION AT ASN-181, VARIANT SENF ALA-183, AND CHARACTERIZATION
OF VARIANT SENF ALA-183.
PubMed=12214108;
Capellari S., Zaidi S.I., Long A.C., Kwon E.E., Petersen R.B.;
"The Thr183Ala mutation, not the loss of the first glycosylation site,
alters the physical properties of the prion protein.";
J. Alzheimers Dis. 2:27-35(2000).
[18]
COPPER-BINDING.
PubMed=16144413; DOI=10.1021/ja053254z;
Chattopadhyay M., Walter E.D., Newell D.J., Jackson P.J.,
Aronoff-Spencer E., Peisach J., Gerfen G.J., Bennett B.,
Antholine W.E., Millhauser G.L.;
"The octarepeat domain of the prion protein binds Cu(II) with three
distinct coordination modes at pH 7.4.";
J. Am. Chem. Soc. 127:12647-12656(2005).
[19]
COPPER-BINDING, AND ZINC-BINDING.
PubMed=18034490; DOI=10.1021/ja077146j;
Walter E.D., Stevens D.J., Visconte M.P., Millhauser G.L.;
"The prion protein is a combined zinc and copper binding protein: Zn2+
alters the distribution of Cu2+ coordination modes.";
J. Am. Chem. Soc. 129:15440-15441(2007).
[20]
ALTERNATIVE INITIATION (ISOFORM 2), SUBCELLULAR LOCATION, AND
MUTAGENESIS OF MET-1 AND MET-8.
PubMed=19059915; DOI=10.1074/jbc.M804051200;
Juanes M.E., Elvira G., Garcia-Grande A., Calero M., Gasset M.;
"Biosynthesis of prion protein nucleocytoplasmic isoforms by
alternative initiation of translation.";
J. Biol. Chem. 284:2787-2794(2009).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND DISEASE ASSOCIATION.
PubMed=19936054; DOI=10.1371/journal.ppat.1000666;
Taylor D.R., Whitehouse I.J., Hooper N.M.;
"Glypican-1 mediates both prion protein lipid raft association and
disease isoform formation.";
PLoS Pathog. 5:E1000666-E1000666(2009).
[23]
COPPER-BINDING.
PubMed=19381258; DOI=10.1371/journal.ppat.1000390;
Stevens D.J., Walter E.D., Rodriguez A., Draper D., Davies P.,
Brown D.R., Millhauser G.L.;
"Early onset prion disease from octarepeat expansion correlates with
copper or zinc binding properties.";
PLoS Pathog. 5:E1000390-E1000390(2009).
[24]
SUBUNIT, AND DOMAIN.
PubMed=20375014; DOI=10.1074/jbc.M110.111815;
Adrover M., Pauwels K., Prigent S., de Chiara C., Xu Z., Chapuis C.,
Pastore A., Rezaei H.;
"Prion fibrillization is mediated by a native structural element that
comprises helices H2 and H3.";
J. Biol. Chem. 285:21004-21012(2010).
[25]
COPPER-BINDING, CIRCULAR DICHROISM, DOMAIN, FUNCTION, AND SUBUNIT.
PubMed=20564047; DOI=10.1002/jcb.22743;
Wu D., Zhang W., Luo Q., Luo K., Huang L., Wang W., Huang T., Chen R.,
Lin Y., Pang D., Xiao G.;
"Copper (II) promotes the formation of soluble neurotoxic PrP
oligomers in acidic environment.";
J. Cell. Biochem. 111:627-633(2010).
[26]
BICISTRONIC GENE.
PubMed=21478263; DOI=10.1096/fj.10-173815;
Vanderperre B., Staskevicius A.B., Tremblay G., McCoy M.,
O'Neill M.A., Cashman N.R., Roucou X.;
"An overlapping reading frame in the PRNP gene encodes a novel
polypeptide distinct from the prion protein.";
FASEB J. 25:2373-2386(2011).
[27]
INTERACTION WITH KIAA1191.
PubMed=21153684; DOI=10.1007/s11010-010-0690-4;
Mishra M., Inoue N., Heese K.;
"Characterizing the novel protein p33MONOX.";
Mol. Cell. Biochem. 350:127-134(2011).
[28]
STRUCTURE BY NMR OF 90-231 OF MUTANT LYS-200.
PubMed=10954699; DOI=10.1074/jbc.C000483200;
Zhang Y., Swietnicki W., Zagorski M.G., Surewicz W.K.,
Soennichsen F.D.;
"Solution structure of the E200K variant of human prion protein.
Implications for the mechanism of pathogenesis in familial prion
diseases.";
J. Biol. Chem. 275:33650-33654(2000).
[29]
STRUCTURE BY NMR OF 23-230.
PubMed=10618385; DOI=10.1073/pnas.97.1.145;
Zahn R., Liu A., Luhrs T., Riek R., von Schroetter C.,
Lopez Garcia F., Billeter M., Calzolai L., Wider G., Wuethrich K.;
"NMR solution structure of the human prion protein.";
Proc. Natl. Acad. Sci. U.S.A. 97:145-150(2000).
[30]
STRUCTURE BY NMR OF 118-221.
PubMed=10900000; DOI=10.1073/pnas.97.15.8340;
Calzolai L., Lysek D.A., Guntert P., von Schroetter C., Riek R.,
Zahn R., Wuethrich K.;
"NMR structures of three single-residue variants of the human prion
protein.";
Proc. Natl. Acad. Sci. U.S.A. 97:8340-8345(2000).
[31]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 119-226, DOMAIN, AND SUBUNIT.
PubMed=11524679; DOI=10.1038/nsb0901-770;
Knaus K.J., Morillas M., Swietnicki W., Malone M., Surewicz W.K.,
Yee V.C.;
"Crystal structure of the human prion protein reveals a mechanism for
oligomerization.";
Nat. Struct. Biol. 8:770-774(2001).
[32]
X-RAY CRYSTALLOGRAPHY (0.75 ANGSTROMS) OF 61-65 IN COMPLEX WITH COPPER
ION, DOMAIN, AND SUBUNIT.
PubMed=11900542; DOI=10.1021/bi011922x;
Burns C.S., Aronoff-Spencer E., Dunham C.M., Lario P., Avdievich N.I.,
Antholine W.E., Olmstead M.M., Vrielink A., Gerfen G.J., Peisach J.,
Scott W.G., Millhauser G.L.;
"Molecular features of the copper binding sites in the octarepeat
domain of the prion protein.";
Biochemistry 41:3991-4001(2002).
[33]
STRUCTURE BY NMR OF 61-68, DISULFIDE BOND, AND SUBUNIT.
PubMed=14623188; DOI=10.1016/j.jmb.2003.09.048;
Zahn R.;
"The octapeptide repeats in mammalian prion protein constitute a pH-
dependent folding and aggregation site.";
J. Mol. Biol. 334:477-488(2003).
[34]
REVIEW ON VARIANTS.
PubMed=8364585; DOI=10.1002/humu.1380020303;
Palmer M.S., Collinge J.;
"Mutations and polymorphisms in the prion protein gene.";
Hum. Mutat. 2:168-173(1993).
[35]
REVIEW ON VARIANTS, AND INVOLVEMENT IN PRION DISEASES.
PubMed=8105771; DOI=10.1001/archneur.1993.00540110011002;
Prusiner S.B.;
"Genetic and infectious prion diseases.";
Arch. Neurol. 50:1129-1153(1993).
[36]
X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS) OF 170-175, SUBUNIT, AND
DOMAIN.
PubMed=17468747; DOI=10.1038/nature05695;
Sawaya M.R., Sambashivan S., Nelson R., Ivanova M.I., Sievers S.A.,
Apostol M.I., Thompson M.J., Balbirnie M., Wiltzius J.J.,
McFarlane H.T., Madsen A.O., Riekel C., Eisenberg D.;
"Atomic structures of amyloid cross-beta spines reveal varied steric
zippers.";
Nature 447:453-457(2007).
[37]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 119-231 IN COMPLEX WITH FAB
FRAGMENT OF MONOCLONAL ANTIBODY ICSM 18, AND SUBUNIT.
PubMed=19204296; DOI=10.1073/pnas.0809170106;
Antonyuk S.V., Trevitt C.R., Strange R.W., Jackson G.S., Sangar D.,
Batchelor M., Cooper S., Fraser C., Jones S., Georgiou T.,
Khalili-Shirazi A., Clarke A.R., Hasnain S.S., Collinge J.;
"Crystal structure of human prion protein bound to a therapeutic
antibody.";
Proc. Natl. Acad. Sci. U.S.A. 106:2554-2558(2009).
[38]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 125-227 OF VARIANT VAL-129,
VARIANT VAL-129, VARIANT CJD ASN-178, VARIANT FFI ASN-178, VARIANT GSD
SER-198, SUBUNIT, AND DOMAIN.
PubMed=19927125; DOI=10.1038/emboj.2009.333;
Lee S., Antony L., Hartmann R., Knaus K.J., Surewicz K.,
Surewicz W.K., Yee V.C.;
"Conformational diversity in prion protein variants influences
intermolecular beta-sheet formation.";
EMBO J. 29:251-262(2010).
[39]
VARIANT GSD LEU-102.
PubMed=2564168; DOI=10.1038/338342a0;
Hsiao K., Baker H.F., Crow T.J., Poulter M., Owen F.,
Terwilliger J.D., Westaway D., Ott J., Pursiner S.B.;
"Linkage of a prion protein missense variant to Gerstmann-Straussler
syndrome.";
Nature 338:342-345(1989).
[40]
VARIANTS LEU-102; VAL-117 AND VAL-129.
PubMed=2783132; DOI=10.1016/0006-291X(89)92317-6;
Doh-Ura K., Tateishi J., Sasaki H., Kitamoto T., Sakaki Y.;
"Pro-->Leu change at position 102 of prion protein is the most common
but not the sole mutation related to Gerstmann-Straussler syndrome.";
Biochem. Biophys. Res. Commun. 163:974-979(1989).
[41]
VARIANT FFI ASN-178.
PubMed=1347910; DOI=10.1212/WNL.42.3.669;
Medori R., Montagna P., Tritschler H.J., Leblanc A., Cortelli P.,
Tinuper P., Lugaresi E., Gambetti P.;
"Fatal familial insomnia: a second kindred with mutation of prion
protein gene at codon 178.";
Neurology 42:669-670(1992).
[42]
VARIANT CJD ASN-178.
PubMed=1671440; DOI=10.1016/0140-6736(91)91198-4;
Goldfarb L.G., Haltia M., Brown P., Nieto A., Kovanen J.,
McCombie W.R., Trapp S., Gajdusek D.C.;
"New mutation in scrapie amyloid precursor gene (at codon 178) in
Finnish Creutzfeldt-Jakob kindred.";
Lancet 337:425-425(1991).
[43]
VARIANT CJD LYS-200.
PubMed=1975028; DOI=10.1016/0140-6736(90)92073-Q;
Goldfarb L., Mitrova E., Brown P., Toh B.K., Gajdusek D.C.;
"Mutation in codon 200 of scrapie amyloid protein gene in two clusters
of Creutzfeldt-Jakob disease in Slovakia.";
Lancet 336:514-515(1990).
[44]
VARIANT GSD ARG-217.
PubMed=1363810; DOI=10.1038/ng0492-68;
Hsiao K., Dlouhy S.R., Farlow M.R., Cass C., da Costa M.,
Conneally P.M., Hodes M.E., Ghetti B., Prusiner S.B.;
"Mutant prion proteins in Gerstmann-Straussler-Scheinker disease with
neurofibrillary tangles.";
Nat. Genet. 1:68-71(1992).
[45]
VARIANT VAL-129, VARIANT CJD ASN-178, VARIANT FFI ASN-178,
CHARACTERIZATION OF VARIANT VAL-129, CHARACTERIZATION OF VARIANT CJD
ASN-178, CHARACTERIZATION OF VARIANT FFI ASN-178, AND POLYMORPHISM.
PubMed=1439789; DOI=10.1126/science.1439789;
Goldfarb L.G., Petersen R.B., Tabaton M., Brown P., LeBlanc A.C.,
Montagna P., Cortelli P., Julien J., Vital C., Pendelbury W.W.;
"Fatal familial insomnia and familial Creutzfeldt-Jakob disease:
disease phenotype determined by a DNA polymorphism.";
Science 258:806-808(1992).
[46]
VARIANTS CJD ILE-180 AND ARG-232.
PubMed=8461023; DOI=10.1006/bbrc.1993.1275;
Kitamoto T., Ohta M., Doh-Ura K., Hitoshi S., Terao Y., Tateishi J.;
"Novel missense variants of prion protein in Creutzfeldt-Jakob disease
or Gerstmann-Straussler syndrome.";
Biochem. Biophys. Res. Commun. 191:709-714(1993).
[47]
VARIANT CJD ILE-210.
PubMed=7902693; DOI=10.1002/ana.410340608;
Pocchiari M., Salvatore M., Cutruzzola F., Genuardi M.,
Allcatelli C.T., Masullo C., Macchi G., Alema G., Galgani S., Xi Y.G.,
Petraroli R., Silvestrini M.C., Brunori M.;
"A new point mutation of the prion protein gene in Creutzfeldt-Jakob
disease.";
Ann. Neurol. 34:802-807(1993).
[48]
VARIANT GSD LEU-105.
PubMed=7902972; DOI=10.1212/WNL.43.12.2723-a;
Yamada M., Itoh Y., Fujigasaki H., Naruse S., Kaneko K., Kitamoto T.,
Tateishi J., Otomo E., Hayakawa M., Tanaka J., Matsushita M.,
Miyatake T.;
"A missense mutation at codon 105 with codon 129 polymorphism of the
prion protein gene in a new variant of Gerstmann-Straussler-Scheinker
disease.";
Neurology 43:2723-2724(1993).
[49]
VARIANT GSD LEU-105.
PubMed=7699395; DOI=10.1016/0022-510X(94)90138-4;
Itoh Y., Yamada M., Hayakawa M., Shozawa T., Tanaka J., Matsushita M.,
Kitamoto T., Tateishi J., Otomo E.;
"A variant of Gerstmann-Straussler-Scheinker disease carrying codon
105 mutation with codon 129 polymorphism of the prion protein gene: a
clinicopathological study.";
J. Neurol. Sci. 127:77-86(1994).
[50]
VARIANT CJD LYS-200.
PubMed=7906019; DOI=10.1212/WNL.44.2.299;
Inoue I., Kitamoto T., Doh-Ura K., Shii H., Goto I., Tateishi J.;
"Japanese family with Creutzfeldt-Jakob disease with codon 200 point
mutation of the prion protein gene.";
Neurology 44:299-301(1994).
[51]
VARIANT CJD LYS-200.
PubMed=7913755; DOI=10.1098/rstb.1994.0033;
Gabizon R., Rosenman H., Meiner Z., Kahana I., Kahana E., Shugart Y.,
Ott J., Prusiner S.B.;
"Mutation in codon 200 and polymorphism in codon 129 of the prion
protein gene in Libyan Jews with Creutzfeldt-Jakob disease.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 343:385-390(1994).
[52]
VARIANT GSD LEU-102.
PubMed=7783876; DOI=10.1212/WNL.45.6.1127;
Young K., Jones C.K., Piccardo P., Lazzarini A., Golbe L.I.,
Zimmerman T.R., Dickson D.W., McLachlan D.C., St George-Hyslop P.H.,
Lennox A.;
"Gerstmann-Straussler-Scheinker disease with mutation at codon 102 and
methionine at codon 129 of PRNP in previously unreported patients.";
Neurology 45:1127-1134(1995).
[53]
VARIANT GSD LEU-102, AND VARIANT LYS-219.
PubMed=8797472; DOI=10.1212/WNL.47.3.734;
Barbanti P., Fabbrini G., Salvatore M., Petraroli R., Cardone F.,
Maras B., Equestre M., Macchi G., Lenzi G.L., Pocchiari M.;
"Polymorphism at codon 129 or codon 219 of PRNP and clinical
heterogeneity in a previously unreported family with Gerstmann-
Straussler-Scheinker disease (PrP-P102L mutation).";
Neurology 47:734-741(1996).
[54]
VARIANT CJD HIS-208.
PubMed=8909447; DOI=10.1212/WNL.47.5.1305;
Mastrianni J.A., Iannicola C., Myers R.M., Dearmond S., Prusiner S.B.;
"Mutation of the prion protein gene at codon 208 in familial
Creutzfeldt-Jakob disease.";
Neurology 47:1305-1312(1996).
[55]
VARIANT SENF ALA-183.
PubMed=9266722; DOI=10.1002/ana.410420203;
Nitrini R., Rosemberg S., Passos-Bueno M.R., da Silva L.S.,
Iughetti P., Papadopoulos M., Carrilho P.M., Caramelli P.,
Albrecht S., Zatz M., Leblanc A.;
"Familial spongiform encephalopathy associated with a novel prion
protein gene mutation.";
Ann. Neurol. 42:138-146(1997).
[56]
VARIANTS GSD ASN-202 AND PRO-212.
PubMed=9786248; DOI=10.1097/00005072-199810000-00010;
Piccardo P., Dlouhy S.R., Lievens P.M., Young K., Bird T.D.,
Nochlin D., Dickson D.W., Vinters H.V., Zimmerman T.R.,
Mackenzie I.R., Kish S.J., Ang L.C., De Carli C., Pocchiari M.,
Brown P., Gibbs C.J. Jr., Gajdusek D.C., Bugiani O., Ironside J.,
Tagliavini F., Ghetti B.;
"Phenotypic variability of Gerstmann-Straussler-Scheinker disease is
associated with prion protein heterogeneity.";
J. Neuropathol. Exp. Neurol. 57:979-988(1998).
[57]
VARIANT LYS-219, CHARACTERIZATION OF VARIANT LYS-219, AND
POLYMORPHISM.
PubMed=9482303; DOI=10.1016/S0140-6736(05)78358-6;
Shibuya S., Higuchi J., Shin R.W., Tateishi J., Kitamoto T.;
"Protective prion protein polymorphisms against sporadic Creutzfeldt-
Jakob disease.";
Lancet 351:419-419(1998).
[58]
VARIANTS ARG-188 AND SER-238.
PubMed=10987652; DOI=10.1007/s004390051096;
Windl O., Giese A., Schulz-Schaeffer W., Zerr I., Skworc K.,
Arendt S., Oberdieck C., Bodemer M., Poser S., Kretzschmar H.A.;
"Molecular genetics of human prion diseases in Germany.";
Hum. Genet. 105:244-252(1999).
[59]
VARIANTS EARLY-ONSET DEMENTIA LEU-102; ALA-183 AND LYS-188.
PubMed=10631141; DOI=10.1086/302702;
Finckh U., Mueller-Thomsen T., Mann U., Eggers C., Marksteiner J.,
Meins W., Binetti G., Alberici A., Hock C., Nitsch R.M., Gal A.;
"High prevalence of pathogenic mutations in patients with early-onset
dementia detected by sequence analyses of four different genes.";
Am. J. Hum. Genet. 66:110-117(2000).
[60]
VARIANTS CJD LYS-196; ILE-203 AND GLN-211.
PubMed=10790216;
DOI=10.1002/(SICI)1098-1004(200005)15:5<482::AID-HUMU16>3.0.CO;2-1;
Peoc'h K., Manivet P., Beaudry P., Attane F., Besson G., Didier H.,
Delasnerie-Laupretre N., Laplanche J.-L.;
"Identification of three novel mutations (E196K, V203I, E211Q) in the
prion protein gene (PRNP) in inherited prion diseases with
Creutzfeldt-Jakob disease phenotype.";
Hum. Mutat. 15:482-482(2000).
[61]
VARIANT GSD VAL-131.
PubMed=11709001; DOI=10.1001/archneur.58.11.1899;
Panegyres P.K., Toufexis K., Kakulas B.A., Cernevakova L., Brown P.,
Ghetti B., Piccardo P., Dlouhy S.R.;
"A new PRNP mutation (G131V) associated with Gerstmann-Straussler-
Scheinker disease.";
Arch. Neurol. 58:1899-1902(2001).
[62]
VARIANT VAL-129, AND CHARACTERIZATION OF VARIANT VAL-129.
PubMed=12690204; DOI=10.1126/science.1083320;
Mead S., Stumpf M.P., Whitfield J., Beck J.A., Poulter M.,
Campbell T., Uphill J.B., Goldstein D., Alpers M., Fisher E.M.,
Collinge J.;
"Balancing selection at the prion protein gene consistent with
prehistoric kurulike epidemics.";
Science 300:640-643(2003).
[63]
VARIANT VAL-127, AND INVOLVEMENT IN KURU.
PubMed=19923577; DOI=10.1056/NEJMoa0809716;
Mead S., Whitfield J., Poulter M., Shah P., Uphill J., Campbell T.,
Al-Dujaily H., Hummerich H., Beck J., Mein C.A., Verzilli C.,
Whittaker J., Alpers M.P., Collinge J.;
"A novel protective prion protein variant that colocalizes with kuru
exposure.";
N. Engl. J. Med. 361:2056-2065(2009).
[64]
VARIANT VAL-127, CHARACTERIZATION OF VARIANT VAL-127, INVOLVEMENT IN
KURU, AND POLYMORPHISM.
PubMed=26061765; DOI=10.1038/nature14510;
Asante E.A., Smidak M., Grimshaw A., Houghton R., Tomlinson A.,
Jeelani A., Jakubcova T., Hamdan S., Richard-Londt A., Linehan J.M.,
Brandner S., Alpers M., Whitfield J., Mead S., Wadsworth J.D.,
Collinge J.;
"A naturally occurring variant of the human prion protein completely
prevents prion disease.";
Nature 522:478-481(2015).
-!- FUNCTION: Its primary physiological function is unclear. May play
a role in neuronal development and synaptic plasticity. May be
required for neuronal myelin sheath maintenance. May promote
myelin homeostasis through acting as a agonist for ADGRG6
receptor. May play a role in iron uptake and iron homeostasis.
Soluble oligomers are toxic to cultured neuroblastoma cells and
induce apoptosis (in vitro) (By similarity). Association with GPC1
(via its heparan sulfate chains) targets PRNP to lipid rafts. Also
provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1
deaminase degradation of its heparan sulfate side chains (By
similarity). {ECO:0000250|UniProtKB:P04156,
ECO:0000250|UniProtKB:P04925, ECO:0000269|PubMed:12732622,
ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:20564047,
ECO:0000305}.
-!- SUBUNIT: Monomer and homodimer. Has a tendency to aggregate into
amyloid fibrils containing a cross-beta spine, formed by a steric
zipper of superposed beta-strands. Soluble oligomers may represent
an intermediate stage on the path to fibril formation. Copper
binding may promote oligomerization (PubMed:11524679,
PubMed:11900542, PubMed:14623188, PubMed:17468747,
PubMed:19204296, PubMed:19927125, PubMed:20375014,
PubMed:20564047). Interacts with GRB2, APP, ERI3/PRNPIP and SYN1.
Mislocalized cytosolically exposed PrP interacts with MGRN1; this
interaction alters MGRN1 subcellular location and causes lysosomal
enlargement (By similarity). Interacts with KIAA1191
(PubMed:21153684). Interacts with ADGRG6 (By similarity).
{ECO:0000250|UniProtKB:P04925, ECO:0000269|PubMed:11524679,
ECO:0000269|PubMed:11900542, ECO:0000269|PubMed:14623188,
ECO:0000269|PubMed:17468747, ECO:0000269|PubMed:19204296,
ECO:0000269|PubMed:19927125, ECO:0000269|PubMed:20375014,
ECO:0000269|PubMed:20564047, ECO:0000269|PubMed:21153684}.
-!- INTERACTION:
Self; NbExp=28; IntAct=EBI-977302, EBI-977302;
Q9UL18:AGO1; NbExp=2; IntAct=EBI-977302, EBI-527363;
Q9UKV8:AGO2; NbExp=4; IntAct=EBI-977302, EBI-528269;
Q8CJG0:Ago2 (xeno); NbExp=2; IntAct=EBI-977302, EBI-528299;
P05067:APP; NbExp=3; IntAct=EBI-977302, EBI-77613;
P05067-4:APP; NbExp=2; IntAct=EBI-977302, EBI-302641;
P31424-2:Grm5 (xeno); NbExp=4; IntAct=EBI-8830282, EBI-8830305;
P49639:HOXA1; NbExp=4; IntAct=EBI-977302, EBI-740785;
P10636:MAPT; NbExp=2; IntAct=EBI-977302, EBI-366182;
P29372:MPG; NbExp=4; IntAct=EBI-977302, EBI-1043398;
Q9BSJ6:PIMREG; NbExp=5; IntAct=EBI-977302, EBI-2568609;
P52480:Pkm (xeno); NbExp=5; IntAct=EBI-8830282, EBI-647785;
Q9H4B4:PLK3; NbExp=4; IntAct=EBI-977302, EBI-751877;
P10279:PRNP (xeno); NbExp=5; IntAct=EBI-977302, EBI-7430632;
P23907:PRNP (xeno); NbExp=3; IntAct=EBI-977302, EBI-7670302;
P04925:Prnp (xeno); NbExp=3; IntAct=EBI-977302, EBI-768613;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:19936054}. Golgi apparatus
{ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via
association with the heparan sulfate chains of GPC1. Colocates, in
the presence of Cu(2+), to vesicles in para- and perinuclear
regions, where both proteins undergo internalization. Heparin
displaces PRNP from lipid rafts and promotes endocytosis.
{ECO:0000269|PubMed:19936054}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:19059915}. Nucleus
{ECO:0000269|PubMed:19059915}. Note=Accumulates outside the
secretory route in the cytoplasm, from where it relocates to the
nucleus. {ECO:0000269|PubMed:19059915}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=1; Synonyms=PrP;
IsoId=P04156-1; Sequence=Displayed;
Name=2; Synonyms=PrP(M8);
IsoId=P04156-2; Sequence=VSP_039045;
Name=3; Synonyms=AltPrP;
IsoId=F7VJQ1-1; Sequence=External;
-!- DOMAIN: The normal, monomeric form, PRPN(C), has a mainly alpha-
helical structure. Misfolding of this form produces a disease-
associated, protease-resistant form, PRPN (Sc), accompanied by a
large increase of the beta-sheet content and formation of amyloid
fibrils. These fibrils consist of a cross-beta spine, formed by a
steric zipper of superposed beta-strands. Disease mutations may
favor intermolecular contacts via short beta strands, and may
thereby trigger oligomerization. In addition, the heparan-sulfate
proteoglycan, GPC1, promotes the association of PRPN (C) to lipid
rafts and appears to facilitate the conversion to PRPN (Sc).
{ECO:0000269|PubMed:17468747, ECO:0000269|PubMed:19927125,
ECO:0000269|PubMed:20564047}.
-!- DOMAIN: Contains an N-terminal region composed of octamer repeats.
At low copper concentrations, the sidechains of His residues from
three or four repeats contribute to the binding of a single copper
ion. Alternatively, a copper ion can be bound by interaction with
the sidechain and backbone amide nitrogen of a single His residue.
The observed copper binding stoichiometry suggests that two repeat
regions cooperate to stabilize the binding of a single copper ion.
At higher copper concentrations, each octamer can bind one copper
ion by interactions with the His sidechain and Gly backbone atoms.
A mixture of binding types may occur, especially in the case of
octamer repeat expansion. Copper binding may stabilize the
conformation of this region and may promote oligomerization.
{ECO:0000269|PubMed:11524679, ECO:0000269|PubMed:11900542,
ECO:0000269|PubMed:20375014}.
-!- PTM: The glycosylation pattern (the amount of mono-, di- and non-
glycosylated forms or glycoforms) seems to differ in normal and
CJD prion. {ECO:0000269|PubMed:12214108}.
-!- PTM: Isoform 2 is sumoylated with SUMO1.
{ECO:0000250|UniProtKB:P04273}.
-!- POLYMORPHISM: The five tandem octapeptide repeats region is highly
unstable. Insertions or deletions of octapeptide repeat units are
associated to prion disease. {ECO:0000269|PubMed:1683708}.
-!- POLYMORPHISM: A number of polymorphisms confer resistance to prion
diseases (PubMed:1439789, PubMed:9482303, PubMed:19923577,
PubMed:26061765). Val-127 has been selected for in response to the
Kuru epidemic and confers resistance to prion disease by acting as
a 'dominant negative' inhibitor of prion conversion
(PubMed:26061765). Val-127 is not only itself resistant to
conformational conversion, but also inhibits conversion of wild-
type proteins. Confers protection against classical Creutzfeldt-
Jakob disease (CJD) and Kuru in the heterozygous state, but can be
infected with variant CJD prions, resulting from exposure to
bovine spongiform encephalopathy prions. Confers complete
resistance to all prion strains when homozygous (PubMed:26061765).
Always associated with M-129 variant (PubMed:26061765). Val-129
confers relative protection against acquired, sporadic and some
inherited prion diseases in the heterozygous state, possibly by
preventing homodimerization (PubMed:1439789). Lys-219 confers
relative protection against sporadic Creutzfeldt-Jakob disease
(CJD) in the heterozygous state (PubMed:9482303).
{ECO:0000269|PubMed:1439789, ECO:0000269|PubMed:26061765,
ECO:0000269|PubMed:9482303}.
-!- DISEASE: Note=PrP is found in high quantity in the brain of humans
and animals infected with neurodegenerative diseases known as
transmissible spongiform encephalopathies or prion diseases, like:
Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI),
Gerstmann-Straussler disease (GSD), Huntington disease-like type 1
(HDL1) and kuru in humans; scrapie in sheep and goat; bovine
spongiform encephalopathy (BSE) in cattle; transmissible mink
encephalopathy (TME); chronic wasting disease (CWD) of mule deer
and elk; feline spongiform encephalopathy (FSE) in cats and exotic
ungulate encephalopathy (EUE) in nyala and greater kudu. The prion
diseases illustrate three manifestations of CNS degeneration: (1)
infectious (2) sporadic and (3) dominantly inherited forms. TME,
CWD, BSE, FSE, EUE are all thought to occur after consumption of
prion-infected foodstuffs. {ECO:0000269|PubMed:8105771}.
-!- DISEASE: Creutzfeldt-Jakob disease (CJD) [MIM:123400]: Occurs
primarily as a sporadic disorder (1 per million), while 10-15% are
familial. Accidental transmission of CJD to humans appears to be
iatrogenic (contaminated human growth hormone (HGH), corneal
transplantation, electroencephalographic electrode implantation,
etc.). Epidemiologic studies have failed to implicate the
ingestion of infected animal meat in the pathogenesis of CJD in
human. The triad of microscopic features that characterize the
prion diseases consists of (1) spongiform degeneration of neurons,
(2) severe astrocytic gliosis that often appears to be out of
proportion to the degree of nerve cell loss, and (3) amyloid
plaque formation. CJD is characterized by progressive dementia and
myoclonic seizures, affecting adults in mid-life. Some patients
present sleep disorders, abnormalities of high cortical function,
cerebellar and corticospinal disturbances. The disease ends in
death after a 3-12 months illness. {ECO:0000269|PubMed:10790216,
ECO:0000269|PubMed:1439789, ECO:0000269|PubMed:1671440,
ECO:0000269|PubMed:1975028, ECO:0000269|PubMed:19927125,
ECO:0000269|PubMed:7902693, ECO:0000269|PubMed:7906019,
ECO:0000269|PubMed:7913755, ECO:0000269|PubMed:8461023,
ECO:0000269|PubMed:8909447}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Fatal familial insomnia (FFI) [MIM:600072]: Autosomal
dominant disorder and is characterized by neuronal degeneration
limited to selected thalamic nuclei and progressive insomnia.
{ECO:0000269|PubMed:1347910, ECO:0000269|PubMed:1439789,
ECO:0000269|PubMed:19927125}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Gerstmann-Straussler disease (GSD) [MIM:137440]: A rare
inherited prion disease characterized by adult onset of memory
loss, dementia, ataxia, and pathologic deposition of amyloid-like
plaques in the brain. GSD presents with progressive limb and
truncal ataxia, dysarthria, and cognitive decline in the thirties
and forties, and the average disease duration is 7 years.
{ECO:0000269|PubMed:10581485, ECO:0000269|PubMed:11709001,
ECO:0000269|PubMed:1363810, ECO:0000269|PubMed:1439789,
ECO:0000269|PubMed:19927125, ECO:0000269|PubMed:2564168,
ECO:0000269|PubMed:7699395, ECO:0000269|PubMed:7783876,
ECO:0000269|PubMed:7902972, ECO:0000269|PubMed:8797472,
ECO:0000269|PubMed:9786248}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Huntington disease-like 1 (HDL1) [MIM:603218]: Autosomal
dominant, early-onset neurodegenerative disorder with prominent
psychiatric features. {ECO:0000269|PubMed:9792871}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. {ECO:0000269|PubMed:9792871}.
-!- DISEASE: Kuru (KURU) [MIM:245300]: Kuru is transmitted during
ritualistic cannibalism, among natives of the New Guinea
highlands. Patients exhibit various movement disorders like
cerebellar abnormalities, rigidity of the limbs, and clonus.
Emotional lability is present, and dementia is conspicuously
absent. Death usually occurs from 3 to 12 month after onset.
{ECO:0000269|PubMed:19923577, ECO:0000269|PubMed:26061765}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Spongiform encephalopathy with neuropsychiatric features
(SENF) [MIM:606688]: Autosomal dominant presenile dementia with a
rapidly progressive and protracted clinical course. The dementia
was characterized clinically by frontotemporal features, including
early personality changes. Some patients had memory loss, several
showed aggressiveness, hyperorality and verbal stereotypy, others
had parkinsonian symptoms. {ECO:0000269|PubMed:12214108,
ECO:0000269|PubMed:9266722}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: This protein is produced by a bicistronic gene
which also produces the The alternative prion protein/AltPrP (AC
F7VJQ1) from an overlapping reading frame.
{ECO:0000305|PubMed:21478263}.
-!- MISCELLANEOUS: The alternative prion protein/AltPrP (AC F7VJQ1)
and PRNP have no apparent direct functional relation since a
mutation that removes the start codon of the AltPrP has no
apparent effect on the biology of PRNP. In mouse and hamster, the
alternative initiation AUG codon is absent and is replaced by a
GUG codon. {ECO:0000305}.
-!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
-!- WEB RESOURCE: Name=The Official Mad Cow Disease Home Page;
URL="http://www.mad-cow.org/";
-!- WEB RESOURCE: Name=Wikipedia; Note=PRNP entry;
URL="https://en.wikipedia.org/wiki/PRNP";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The shape of harm
- Issue 179 of May 2016;
URL="https://web.expasy.org/spotlight/back_issues/179/";
-----------------------------------------------------------------------
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EMBL; M13899; AAA60182.1; -; mRNA.
EMBL; X83416; CAA58442.1; -; Genomic_DNA.
EMBL; U29185; AAC78725.1; -; Genomic_DNA.
EMBL; AF076976; AAD46098.1; -; Genomic_DNA.
EMBL; AY008282; AAG21693.1; -; mRNA.
EMBL; DQ408531; ABD63004.1; -; Genomic_DNA.
EMBL; AL133396; CAB75503.1; -; Genomic_DNA.
EMBL; AL133396; CAI19053.1; -; Genomic_DNA.
EMBL; BC012844; AAH12844.1; -; mRNA.
EMBL; BC022532; AAH22532.1; -; mRNA.
EMBL; D00015; BAA00011.1; -; mRNA.
EMBL; M13667; AAA19664.1; -; mRNA.
EMBL; M81929; AAB59442.1; -; Genomic_DNA.
EMBL; M81930; AAB59443.1; -; Genomic_DNA.
EMBL; AF030575; AAC05365.1; -; Genomic_DNA.
EMBL; S80732; AAB50648.2; -; Genomic_DNA.
EMBL; S80743; AAB50649.2; -; Genomic_DNA.
EMBL; S71208; AAB20521.1; -; Genomic_DNA.
EMBL; S71210; AAB20522.1; -; Genomic_DNA.
EMBL; S71212; AAB20523.1; -; Genomic_DNA.
CCDS; CCDS13080.1; -. [P04156-1]
PIR; A24173; UJHU.
RefSeq; NP_000302.1; NM_000311.4. [P04156-1]
RefSeq; NP_001073590.1; NM_001080121.2. [P04156-1]
RefSeq; NP_001073591.1; NM_001080122.2. [P04156-1]
RefSeq; NP_001073592.1; NM_001080123.2. [P04156-1]
RefSeq; NP_001258490.1; NM_001271561.2.
RefSeq; NP_898902.1; NM_183079.3. [P04156-1]
UniGene; Hs.472010; -.
UniGene; Hs.610285; -.
UniGene; Hs.721670; -.
PDB; 1E1G; NMR; -; A=125-228.
PDB; 1E1J; NMR; -; A=125-228.
PDB; 1E1P; NMR; -; A=125-228.
PDB; 1E1S; NMR; -; A=125-228.
PDB; 1E1U; NMR; -; A=125-228.
PDB; 1E1W; NMR; -; A=125-228.
PDB; 1FKC; NMR; -; A=90-231.
PDB; 1FO7; NMR; -; A=90-231.
PDB; 1H0L; NMR; -; A=121-230.
PDB; 1HJM; NMR; -; A=125-228.
PDB; 1HJN; NMR; -; A=125-228.
PDB; 1I4M; X-ray; 2.00 A; A=119-226.
PDB; 1OEH; NMR; -; A=77-84.
PDB; 1OEI; NMR; -; A=61-84.
PDB; 1QLX; NMR; -; A=23-230.
PDB; 1QLZ; NMR; -; A=23-230.
PDB; 1QM0; NMR; -; A=90-230.
PDB; 1QM1; NMR; -; A=90-230.
PDB; 1QM2; NMR; -; A=121-230.
PDB; 1QM3; NMR; -; A=121-230.
PDB; 2IV4; NMR; -; A=180-195.
PDB; 2IV5; NMR; -; A=173-195.
PDB; 2IV6; NMR; -; A=173-195.
PDB; 2K1D; NMR; -; A=90-231.
PDB; 2KUN; NMR; -; A=90-231.
PDB; 2LBG; NMR; -; A=110-136.
PDB; 2LEJ; NMR; -; A=90-231.
PDB; 2LFT; NMR; -; A=90-231.
PDB; 2LSB; NMR; -; A=90-231.
PDB; 2LV1; NMR; -; A=90-231.
PDB; 2M8T; NMR; -; A=90-231.
PDB; 2OL9; X-ray; 0.85 A; A=170-175.
PDB; 2W9E; X-ray; 2.90 A; A=119-231.
PDB; 3HAF; X-ray; 2.26 A; A=90-231.
PDB; 3HAK; X-ray; 1.80 A; A=125-227.
PDB; 3HEQ; X-ray; 1.80 A; A/B=90-231.
PDB; 3HER; X-ray; 1.85 A; A/B=90-231.
PDB; 3HES; X-ray; 2.00 A; A/B=90-231.
PDB; 3HJ5; X-ray; 3.10 A; A/B=90-231.
PDB; 3HJX; X-ray; 2.00 A; A=126-231.
PDB; 3MD4; X-ray; 1.15 A; A/B=127-132.
PDB; 3MD5; X-ray; 1.40 A; A/B=127-132.
PDB; 3NHC; X-ray; 1.57 A; A/B=127-132.
PDB; 3NHD; X-ray; 1.92 A; A/B=127-132.
PDB; 3NVF; X-ray; 1.80 A; A=138-143.
PDB; 4DGI; X-ray; 2.40 A; A=120-230.
PDB; 4E1H; X-ray; 1.40 A; A/C/E/G/I/K=177-182, B/D/F/H/J/L=211-216.
PDB; 4E1I; X-ray; 2.03 A; A/C/E/G/I/K=177-182, B/D/F/H/J/L=211-216.
PDB; 4KML; X-ray; 1.50 A; A=24-231.
PDB; 4N9O; X-ray; 1.50 A; A=90-231.
PDB; 5L6R; NMR; -; A=90-226.
PDBsum; 1E1G; -.
PDBsum; 1E1J; -.
PDBsum; 1E1P; -.
PDBsum; 1E1S; -.
PDBsum; 1E1U; -.
PDBsum; 1E1W; -.
PDBsum; 1FKC; -.
PDBsum; 1FO7; -.
PDBsum; 1H0L; -.
PDBsum; 1HJM; -.
PDBsum; 1HJN; -.
PDBsum; 1I4M; -.
PDBsum; 1OEH; -.
PDBsum; 1OEI; -.
PDBsum; 1QLX; -.
PDBsum; 1QLZ; -.
PDBsum; 1QM0; -.
PDBsum; 1QM1; -.
PDBsum; 1QM2; -.
PDBsum; 1QM3; -.
PDBsum; 2IV4; -.
PDBsum; 2IV5; -.
PDBsum; 2IV6; -.
PDBsum; 2K1D; -.
PDBsum; 2KUN; -.
PDBsum; 2LBG; -.
PDBsum; 2LEJ; -.
PDBsum; 2LFT; -.
PDBsum; 2LSB; -.
PDBsum; 2LV1; -.
PDBsum; 2M8T; -.
PDBsum; 2OL9; -.
PDBsum; 2W9E; -.
PDBsum; 3HAF; -.
PDBsum; 3HAK; -.
PDBsum; 3HEQ; -.
PDBsum; 3HER; -.
PDBsum; 3HES; -.
PDBsum; 3HJ5; -.
PDBsum; 3HJX; -.
PDBsum; 3MD4; -.
PDBsum; 3MD5; -.
PDBsum; 3NHC; -.
PDBsum; 3NHD; -.
PDBsum; 3NVF; -.
PDBsum; 4DGI; -.
PDBsum; 4E1H; -.
PDBsum; 4E1I; -.
PDBsum; 4KML; -.
PDBsum; 4N9O; -.
PDBsum; 5L6R; -.
DisProt; DP00466; -.
ProteinModelPortal; P04156; -.
SMR; P04156; -.
BioGrid; 111606; 60.
CORUM; P04156; -.
DIP; DIP-29933N; -.
ELM; P04156; -.
IntAct; P04156; 94.
MINT; MINT-1420984; -.
STRING; 9606.ENSP00000368752; -.
BindingDB; P04156; -.
ChEMBL; CHEMBL4869; -.
DrugBank; DB00759; Tetracycline.
TCDB; 1.C.48.1.2; the prion peptide (prp) family.
iPTMnet; P04156; -.
PhosphoSitePlus; P04156; -.
SwissPalm; P04156; -.
BioMuta; PRNP; -.
DMDM; 130912; -.
EPD; P04156; -.
PaxDb; P04156; -.
PeptideAtlas; P04156; -.
PRIDE; P04156; -.
DNASU; 5621; -.
Ensembl; ENST00000379440; ENSP00000368752; ENSG00000171867. [P04156-1]
Ensembl; ENST00000430350; ENSP00000399376; ENSG00000171867. [P04156-1]
GeneID; 5621; -.
KEGG; hsa:5621; -.
CTD; 5621; -.
DisGeNET; 5621; -.
EuPathDB; HostDB:ENSG00000171867.16; -.
GeneCards; PRNP; -.
GeneReviews; PRNP; -.
HGNC; HGNC:9449; PRNP.
HPA; HPA042754; -.
HPA; HPA043398; -.
MalaCards; PRNP; -.
MIM; 123400; phenotype.
MIM; 137440; phenotype.
MIM; 176640; gene.
MIM; 245300; phenotype.
MIM; 600072; phenotype.
MIM; 603218; phenotype.
MIM; 606688; phenotype.
neXtProt; NX_P04156; -.
OpenTargets; ENSG00000171867; -.
Orphanet; 397606; Chronic diarrhea with hereditary sensory and autonomic neuropathy.
Orphanet; 280397; Familial Alzheimer-like prion disease.
Orphanet; 466; Fatal familial insomnia.
Orphanet; 356; Gerstmann-Straussler-Scheinker syndrome.
Orphanet; 157941; Huntington disease-like 1.
Orphanet; 282166; Inherited Creutzfeldt-Jakob disease.
PharmGKB; PA33796; -.
eggNOG; ENOG410IJMM; Eukaryota.
eggNOG; ENOG410YXUU; LUCA.
GeneTree; ENSGT00510000049083; -.
HOVERGEN; HBG008260; -.
InParanoid; P04156; -.
KO; K05634; -.
OMA; GYPHNPG; -.
OrthoDB; EOG091G0HMV; -.
PhylomeDB; P04156; -.
TreeFam; TF105188; -.
Reactome; R-HSA-419037; NCAM1 interactions.
ChiTaRS; PRNP; human.
EvolutionaryTrace; P04156; -.
GenomeRNAi; 5621; -.
PMAP-CutDB; P04156; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000171867; -.
ExpressionAtlas; P04156; baseline and differential.
Genevisible; P04156; HS.
GO; GO:0031362; C:anchored component of external side of plasma membrane; NAS:ARUK-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; TAS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0016234; C:inclusion body; IMP:CAFA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
GO; GO:0014069; C:postsynaptic density; TAS:ARUK-UCL.
GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
GO; GO:0043008; F:ATP-dependent protein binding; IEA:Ensembl.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:1903135; F:cupric ion binding; IEA:Ensembl.
GO; GO:1903136; F:cuprous ion binding; IMP:CAFA.
GO; GO:0005539; F:glycosaminoglycan binding; ISS:ARUK-UCL.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0005521; F:lamin binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; ISS:ARUK-UCL.
GO; GO:0032403; F:protein complex binding; IPI:ARUK-UCL.
GO; GO:0004872; F:receptor activity; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; IEA:Ensembl.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IPI:ARUK-UCL.
GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:ARUK-UCL.
GO; GO:0007050; P:cell cycle arrest; IEA:UniProtKB-KW.
GO; GO:0006878; P:cellular copper ion homeostasis; NAS:UniProtKB.
GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0071280; P:cellular response to copper ion; IDA:MGI.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
GO; GO:0007616; P:long-term memory; TAS:ARUK-UCL.
GO; GO:0008152; P:metabolic process; TAS:ProtInc.
GO; GO:0090647; P:modulation of age-related behavioral decline; ISS:ARUK-UCL.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISS:BHF-UCL.
GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; ISS:ARUK-UCL.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:ARUK-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:BHF-UCL.
GO; GO:0043086; P:negative regulation of catalytic activity; IEA:Ensembl.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IEA:Ensembl.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:BHF-UCL.
GO; GO:0032700; P:negative regulation of interleukin-17 production; ISS:BHF-UCL.
GO; GO:0032703; P:negative regulation of interleukin-2 production; ISS:BHF-UCL.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:BHF-UCL.
GO; GO:0010955; P:negative regulation of protein processing; TAS:ARUK-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; ISS:BHF-UCL.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:BHF-UCL.
GO; GO:1990535; P:neuron projection maintenance; ISS:ARUK-UCL.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:CAFA.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:ARUK-UCL.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IGI:ARUK-UCL.
GO; GO:0031648; P:protein destabilization; IMP:CAFA.
GO; GO:0051260; P:protein homooligomerization; IMP:CAFA.
GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; IEA:Ensembl.
GO; GO:1902938; P:regulation of intracellular calcium activated chloride channel activity; IGI:ARUK-UCL.
GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
Gene3D; 1.10.790.10; -; 1.
InterPro; IPR000817; Prion.
InterPro; IPR036924; Prion/Doppel_b-ribbon_dom_sf.
InterPro; IPR022416; Prion/Doppel_prot_b-ribbon_dom.
InterPro; IPR025860; Prion_N_dom.
PANTHER; PTHR10502:SF134; PTHR10502:SF134; 1.
Pfam; PF00377; Prion; 1.
Pfam; PF11587; Prion_bPrPp; 1.
PRINTS; PR00341; PRION.
SMART; SM00157; PRP; 1.
SUPFAM; SSF54098; SSF54098; 1.
PROSITE; PS00291; PRION_1; 1.
PROSITE; PS00706; PRION_2; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Amyloid; Amyloidosis;
Cell cycle; Cell membrane; Complete proteome; Copper; Cytoplasm;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Golgi apparatus; GPI-anchor; Growth arrest; Lipoprotein;
Membrane; Metal-binding; Nucleus; Polymorphism; Prion;
Reference proteome; Repeat; Signal; Ubl conjugation; Zinc.
SIGNAL 1 22 {ECO:0000250|UniProtKB:P04925}.
CHAIN 23 230 Major prion protein.
/FTId=PRO_0000025675.
PROPEP 231 253 Removed in mature form.
{ECO:0000250|UniProtKB:P04273}.
/FTId=PRO_0000025676.
REPEAT 51 59 1.
REPEAT 60 67 2.
REPEAT 68 75 3.
REPEAT 76 83 4.
REPEAT 84 91 5.
REGION 23 230 Interaction with GRB2, ERI3 and SYN1.
{ECO:0000250|UniProtKB:P04925}.
REGION 23 38 Interaction with ADGRG6.
{ECO:0000250|UniProtKB:P04925}.
REGION 51 91 5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
Q.
METAL 61 61 Copper or zinc 1.
{ECO:0000269|PubMed:11900542}.
METAL 62 62 Copper or zinc 1; via amide nitrogen.
{ECO:0000269|PubMed:11900542}.
METAL 63 63 Copper or zinc 1; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:11900542}.
METAL 69 69 Copper or zinc 2.
{ECO:0000305|PubMed:11900542}.
METAL 70 70 Copper or zinc 2; via amide nitrogen.
{ECO:0000305|PubMed:11900542}.
METAL 71 71 Copper or zinc 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000305|PubMed:11900542}.
METAL 77 77 Copper or zinc 3.
{ECO:0000305|PubMed:11900542}.
METAL 78 78 Copper or zinc 3; via amide nitrogen.
{ECO:0000305|PubMed:11900542}.
METAL 79 79 Copper or zinc 3; via amide nitrogen and
carbonyl oxygen.
{ECO:0000305|PubMed:11900542}.
METAL 85 85 Copper or zinc 4.
{ECO:0000305|PubMed:11900542}.
METAL 86 86 Copper or zinc 4; via amide nitrogen.
{ECO:0000305|PubMed:11900542}.
METAL 87 87 Copper or zinc 4; via amide nitrogen and
carbonyl oxygen.
{ECO:0000305|PubMed:11900542}.
LIPID 230 230 GPI-anchor amidated serine.
{ECO:0000250|UniProtKB:P04273}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12214108}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 179 214 {ECO:0000269|PubMed:14623188}.
VAR_SEQ 1 7 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_039045.
VARIANT 56 63 Missing. {ECO:0000269|PubMed:1363802,
ECO:0000269|PubMed:1678248,
ECO:0000269|PubMed:7485229}.
/FTId=VAR_013763.
VARIANT 102 102 P -> L (in GSD and early-onset dementia;
dbSNP:rs74315401).
{ECO:0000269|PubMed:10631141,
ECO:0000269|PubMed:2564168,
ECO:0000269|PubMed:2783132,
ECO:0000269|PubMed:7783876,
ECO:0000269|PubMed:8797472}.
/FTId=VAR_006464.
VARIANT 105 105 P -> L (in GSD; dbSNP:rs11538758).
{ECO:0000269|PubMed:7699395,
ECO:0000269|PubMed:7902972}.
/FTId=VAR_006465.
VARIANT 117 117 A -> V (linked to development of
dementing Gerstmann-Straussler disease;
dbSNP:rs74315402).
{ECO:0000269|PubMed:2783132}.
/FTId=VAR_006466.
VARIANT 127 127 G -> V (polymorphism; variant that has
been selected for in response to the Kuru
epidemic and confers resistance to prion
disease by acting as a 'dominant
negative' inhibitor of prion conversion;
is not only itself resistant to
conformational conversion, but also
inhibits conversion of wild-type
proteins; confers protection against
classical Creutzfeldt-Jakob disease (CJD)
and Kuru in the heterozygous state, but
can be infected with variant CJD prions,
resulting from exposure to bovine
spongiform encephalopathy prions; confers
complete resistance to all prion strains
when homozygous. Always associated with
M-129 variant; dbSNP:rs267606980).
{ECO:0000269|PubMed:19923577,
ECO:0000269|PubMed:26061765}.
/FTId=VAR_073722.
VARIANT 129 129 M -> V (polymorphism; confers relative
protection against acquired, sporadic and
some inherited prion diseases in the
heterozygous state, possibly by
preventing homodimerization; determines
the disease phenotype in patients who
have a PrP mutation at position 178;
patients with M-129 develop FFI, those
with V-129 develop CJD; dbSNP:rs1799990).
{ECO:0000269|PubMed:12690204,
ECO:0000269|PubMed:1439789,
ECO:0000269|PubMed:19927125,
ECO:0000269|PubMed:2783132}.
/FTId=VAR_006467.
VARIANT 131 131 G -> V (in GSD; dbSNP:rs74315410).
{ECO:0000269|PubMed:11709001}.
/FTId=VAR_014264.
VARIANT 171 171 N -> S (in schizoaffective disorder;
dbSNP:rs16990018).
{ECO:0000269|PubMed:9384372}.
/FTId=VAR_006468.
VARIANT 178 178 D -> N (in FFI and CJD;
dbSNP:rs74315403).
{ECO:0000269|PubMed:1347910,
ECO:0000269|PubMed:1439789,
ECO:0000269|PubMed:1671440,
ECO:0000269|PubMed:19927125}.
/FTId=VAR_006469.
VARIANT 180 180 V -> I (in CJD; dbSNP:rs74315408).
{ECO:0000269|PubMed:1439789,
ECO:0000269|PubMed:19927125,
ECO:0000269|PubMed:8461023}.
/FTId=VAR_006470.
VARIANT 183 183 T -> A (in SENF and early-onset dementia;
induces loss of glycosylation at N-181;
dbSNP:rs74315411).
{ECO:0000269|PubMed:10631141,
ECO:0000269|PubMed:12214108,
ECO:0000269|PubMed:9266722}.
/FTId=VAR_006471.
VARIANT 187 187 H -> R (in GSD; dbSNP:rs74315413).
{ECO:0000269|PubMed:10581485}.
/FTId=VAR_008746.
VARIANT 188 188 T -> K (in early-onset dementia; dementia
associated to prion diseases).
{ECO:0000269|PubMed:10631141}.
/FTId=VAR_008748.
VARIANT 188 188 T -> R (in dbSNP:rs372878791).
{ECO:0000269|PubMed:10987652}.
/FTId=VAR_008747.
VARIANT 196 196 E -> K (in CJD).
{ECO:0000269|PubMed:10790216}.
/FTId=VAR_008749.
VARIANT 198 198 F -> S (in GSD; atypical form with
neurofibrillary tangles;
dbSNP:rs74315405).
{ECO:0000269|PubMed:19927125}.
/FTId=VAR_006472.
VARIANT 200 200 E -> K (in CJD; dbSNP:rs28933385).
{ECO:0000269|PubMed:1975028,
ECO:0000269|PubMed:7906019,
ECO:0000269|PubMed:7913755}.
/FTId=VAR_006473.
VARIANT 202 202 D -> N (in GSD; dbSNP:rs761807915).
{ECO:0000269|PubMed:9786248}.
/FTId=VAR_008750.
VARIANT 203 203 V -> I (in CJD; unknown pathological
significance; dbSNP:rs776593792).
{ECO:0000269|PubMed:10790216}.
/FTId=VAR_008751.
VARIANT 208 208 R -> H (in CJD; dbSNP:rs74315412).
{ECO:0000269|PubMed:8909447}.
/FTId=VAR_006474.
VARIANT 210 210 V -> I (in CJD; dbSNP:rs74315407).
{ECO:0000269|PubMed:7902693}.
/FTId=VAR_006475.
VARIANT 211 211 E -> Q (in CJD; dbSNP:rs398122370).
{ECO:0000269|PubMed:10790216}.
/FTId=VAR_008752.
VARIANT 212 212 Q -> P (in GSD; dbSNP:rs751882709).
{ECO:0000269|PubMed:9786248}.
/FTId=VAR_008753.
VARIANT 217 217 Q -> R (in GSD; with neurofibrillary
tangles; dbSNP:rs74315406).
{ECO:0000269|PubMed:1363810}.
/FTId=VAR_006476.
VARIANT 219 219 E -> K (polymorphism; confers relative
protection against sporadic Creutzfeldt-
Jakob disease (CJD) in the heterozygous
state; dbSNP:rs1800014).
{ECO:0000269|PubMed:8797472,
ECO:0000269|PubMed:9482303}.
/FTId=VAR_006477.
VARIANT 232 232 M -> R (in CJD; dbSNP:rs74315409).
{ECO:0000269|PubMed:8461023}.
/FTId=VAR_006478.
VARIANT 238 238 P -> S. {ECO:0000269|PubMed:10987652}.
/FTId=VAR_008754.
MUTAGEN 1 1 M->S: Protein detected. No protein
detected; when associated with S-8.
{ECO:0000269|PubMed:19059915}.
MUTAGEN 8 8 M->S: No protein detected; when
associated with S-1.
{ECO:0000269|PubMed:19059915}.
CONFLICT 118 118 Missing (in Ref. 9; AAA19664/BAA00011).
{ECO:0000305}.
CONFLICT 169 169 Y -> H (in Ref. 6; ABD63004).
{ECO:0000305}.
CONFLICT 227 227 Q -> K (in Ref. 8; AAH22532).
{ECO:0000305}.
STRAND 63 67 {ECO:0000244|PDB:1OEI}.
STRAND 70 73 {ECO:0000244|PDB:1OEI}.
TURN 74 76 {ECO:0000244|PDB:1OEI}.
STRAND 79 82 {ECO:0000244|PDB:1OEH}.
STRAND 99 101 {ECO:0000244|PDB:5L6R}.
STRAND 118 122 {ECO:0000244|PDB:4KML}.
STRAND 125 127 {ECO:0000244|PDB:1H0L}.
STRAND 128 131 {ECO:0000244|PDB:3MD4}.
STRAND 141 143 {ECO:0000244|PDB:1E1S}.
HELIX 144 153 {ECO:0000244|PDB:4KML}.
HELIX 154 156 {ECO:0000244|PDB:4KML}.
STRAND 159 163 {ECO:0000244|PDB:1E1U}.
HELIX 166 168 {ECO:0000244|PDB:4KML}.
TURN 171 173 {ECO:0000244|PDB:1QM0}.
STRAND 178 181 {ECO:0000244|PDB:4E1H}.
HELIX 185 187 {ECO:0000244|PDB:1E1P}.
TURN 188 190 {ECO:0000244|PDB:1E1P}.
TURN 193 195 {ECO:0000244|PDB:3HAK}.
STRAND 212 215 {ECO:0000244|PDB:4E1H}.
TURN 223 225 {ECO:0000244|PDB:3HER}.
TURN 228 230 {ECO:0000244|PDB:2LFT}.
SEQUENCE 253 AA; 27661 MW; 43DB596BAAA66484 CRC64;
MANLGCWMLV LFVATWSDLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGGWGQP
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHSQWN KPSKPKTNMK HMAGAAAAGA
VVGGLGGYML GSAMSRPIIH FGSDYEDRYY RENMHRYPNQ VYYRPMDEYS NQNNFVHDCV
NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCITQYER ESQAYYQRGS SMVLFSSPPV
ILLISFLIFL IVG


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11-593-C100 CD230 _ Human Prion Protein (PrP) 0.1 mg
YSRTAHP498 CD230, Prion Protein, Goat anti_Human 0.1 ml.
YSRTAHP498T CD230, Prion Protein, Goat anti_Human 0.02 ml.
11-593-C025 Mouse Monoclonal to CD230 Human Prion Protein (PrP) 0.025 mg
bs-11788R Rabbit Anti-Prion protein PrP-CD230 Polyclonal Antibody 100ul


 

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