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Major prion protein (PrP) (CD antigen CD230)

 PRIO_SHEEP              Reviewed;         256 AA.
P23907; Q5ECG0; Q6V638; Q6V654; Q712W2; Q712W3; Q7JGT4;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
30-AUG-2017, entry version 138.
RecName: Full=Major prion protein;
Short=PrP;
AltName: CD_antigen=CD230;
Flags: Precursor;
Name=PRNP; Synonyms=PRP, SIP;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-171.
STRAIN=Suffolk; TISSUE=Spleen;
PubMed=1969635; DOI=10.1073/pnas.87.7.2476;
Goldmann W., Hunter N., Foster J.D., Salbaum J.M., Beyreuther K.,
Hope J.;
"Two alleles of a neural protein gene linked to scrapie in sheep.";
Proc. Natl. Acad. Sci. U.S.A. 87:2476-2480(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-171.
STRAIN=Suffolk; TISSUE=Brain;
PubMed=7926780; DOI=10.1101/gad.8.8.959;
Westaway D., Zuliani V., Cooper C.M., da Costa M., Neuman S.,
Jenny A.L., Detwiler L., Prusiner S.B.;
"Homozygosity for prion protein alleles encoding glutamine-171 renders
sheep susceptible to natural scrapie.";
Genes Dev. 8:959-969(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-171.
TISSUE=Brain;
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 GLN-171.
PubMed=10466827;
Goldmann W., O'Neill G., Cheung F., Charleson F., Ford P., Hunter N.;
"PrP (prion) gene expression in sheep may be modulated by alternative
polyadenylation of its messenger RNA.";
J. Gen. Virol. 80:2275-2283(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-171.
PubMed=14970684; DOI=10.1159/000075730;
Seabury C.M., Derr J.N.;
"Identification of a novel ovine PrP polymorphism and scrapie-
resistant genotypes for St. Croix White and a related composite
breed.";
Cytogenet. Genome Res. 102:85-88(2003).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-141 AND GLN-171.
PubMed=14769911; DOI=10.1099/vir.0.19520-0;
Billinis C., Psychas V., Leontides L., Spyrou V., Argyroudis S.,
Vlemmas I., Leontides S., Sklaviadis T., Papadopoulos O.;
"Prion protein gene polymorphisms in healthy and scrapie affected
sheep in Greece.";
J. Gen. Virol. 85:547-554(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
Inoue S., Watanabe A., Horiuchi M., Ishiguro N., Shinagawa M.;
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-141; GLN-171 AND
GLN-211.
Bossers A.;
"PrP allelic variants associated with natural scrapie.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-171.
Heaton M.P., Leymaster K.A., Clawson M.L., Laegreid W.W.;
"A set of genotyping controls for 15 haplotype combinations of ovine
PRNP codons 136, 154, and 171.";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[10]
IDENTIFICATION IN COMPLEX WITH CES5A; CLU; BPI; MANBA AND GLB1.
TISSUE=Epididymis;
PubMed=16029166; DOI=10.1042/BJ20050459;
Ecroyd H., Belghazi M., Dacheux J.-L., Gatti J.-L.;
"The epididymal soluble prion protein forms a high-molecular-mass
complex in association with hydrophobic proteins.";
Biochem. J. 392:211-219(2005).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 128-233.
PubMed=15037077; DOI=10.1016/j.jmb.2003.12.059;
Haire L.F., Whyte S.M., Vasisht N., Gill A.C., Verma C., Dodson E.J.,
Dodson G.G., Bayley P.M.;
"The crystal structure of the globular domain of sheep prion
protein.";
J. Mol. Biol. 336:1175-1183(2004).
[12]
X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 115-234 IN COMPLEX WITH
ANTIBODY.
PubMed=15240887; DOI=10.1073/pnas.0400014101;
Eghiaian F., Grosclaude J., Lesceu S., Debey P., Doublet B.,
Treguer E., Rezaei H., Knossow M.;
"Insight into the PrPC-->PrPSc conversion from the structures of
antibody-bound ovine prion scrapie-susceptibility variants.";
Proc. Natl. Acad. Sci. U.S.A. 101:10254-10259(2004).
[13]
STRUCTURE BY NMR OF 124-234.
PubMed=15647367; DOI=10.1073/pnas.0408937102;
Lysek D.A., Schorn C., Nivon L.G., Esteve-Moya V., Christen B.,
Calzolai L., von Schroetter C., Fiorito F., Herrmann T., Guentert P.,
Wuethrich K.;
"Prion protein NMR structures of cats, dogs, pigs, and sheep.";
Proc. Natl. Acad. Sci. U.S.A. 102:640-645(2005).
[14]
STRUCTURE BY NMR OF 167-234, 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).
[15]
VARIANTS SCRAPIE VAL-136; HIS-154 AND GLN-171, AND POLYMORPHISM.
PubMed=1681027; DOI=10.1099/0022-1317-72-10-2411;
Goldmann W., Hunter N., Benson G., Foster J.D., Hope J.;
"Different scrapie-associated fibril proteins (PrP) are encoded by
lines of sheep selected for different alleles of the Sip gene.";
J. Gen. Virol. 72:2411-2417(1991).
[16]
VARIANTS SCRAPIE THR-112; VAL-136 AND HIS-154.
PubMed=8094373; DOI=10.1006/geno.1993.1006;
Laplanche J.-L., Chatelain J., Westaway D., Thomas S., Dussaucy M.,
Brugere-Picoux J., Launay J.-M.;
"PrP polymorphisms associated with natural scrapie discovered by
denaturing gradient gel electrophoresis.";
Genomics 15:30-37(1993).
[17]
VARIANTS SCRAPIE VAL-136 AND HIS-171, AND VARIANT HIS-154.
PubMed=7897344; DOI=10.1099/0022-1317-76-3-509;
Belt P.B.G.M., Muileman I.H., Schreuder B.E.C., Bos-De Ruijter J.,
Gielkens A.L.J., Smits M.A.;
"Identification of five allelic variants of the sheep PrP gene and
their association with natural scrapie.";
J. Gen. Virol. 76:509-517(1995).
[18]
VARIANTS THR-137; PHE-141 AND GLN-211.
PubMed=8887505; DOI=10.1099/0022-1317-77-10-2669;
Bossers A., Schreuder B.E.C., Muileman I.H., Belt P.B.G.M.,
Smits M.A.;
"PrP genotype contributes to determining survival times of sheep with
natural scrapie.";
J. Gen. Virol. 77:2669-2673(1996).
-!- FUNCTION: Its primary physiological function is unclear. Has
cytoprotective activity against internal or environmental
stresses. May play a role in neuronal development and synaptic
plasticity. May be required for neuronal myelin sheath
maintenance. May play a role in iron uptake and iron homeostasis.
Soluble oligomers are toxic to cultured neuroblastoma cells and
induce apoptosis (in vitro). 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}.
-!- 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. 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. Interacts with
KIAA1191. {ECO:0000250|UniProtKB:P04156,
ECO:0000250|UniProtKB:P04925}.
-!- INTERACTION:
P04156:PRNP (xeno); NbExp=3; IntAct=EBI-7670302, EBI-977302;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P04156}. 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:0000250|UniProtKB:P04156}.
-!- DOMAIN: The normal, monomeric form has a mainly alpha-helical
structure. The disease-associated, protease-resistant form forms
amyloid fibrils containing 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. {ECO:0000250|UniProtKB:P04156}.
-!- 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:0000250|UniProtKB:P04156}.
-!- DISEASE: Note=Polymorphism at position 171 may be related to the
alleles of scrapie incubation-control (SIC) gene in this species.
{ECO:0000269|PubMed:1681027}.
-!- DISEASE: Note=Found in high quantity in the brain of humans and
animals infected with degenerative neurological diseases such as
kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler
syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE),
transmissible mink encephalopathy (TME), etc. {ECO:0000305}.
-!- DISEASE: Note=Scrapie is a transmissible neurodegenerative
disorder of sheep and goats. Most sheep that contract the disease
naturally die between 24 and 50 months of age. The incubation
period in sheep depends on the strain(s) of the infecting
pathogen, sheep age at exposure, and the sheep genotype. The
survival time is mainly determined by a single genetic locus, SIP,
which has two alleles, susceptible (sa) and resistant (pa). Short
incubation period is conferred by the partially dominant sa
allele. Scrapie can be spread between flockmates, or it can be
transmitted from an infected ewe to its lamb.
{ECO:0000269|PubMed:1681027, ECO:0000269|PubMed:7897344,
ECO:0000269|PubMed:8094373}.
-!- MISCELLANEOUS: This protein is produced by a bicistronic gene
which also produces the major prion protein/PRNP from an
overlapping reading frame.
-!- MISCELLANEOUS: The alternative prion protein/AltPrP (AC F7VJQ3)
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 (By similarity). In mouse
and hamster, the alternative initiation AUG codon is absent and is
replaced by a GUG codon. {ECO:0000250}.
-!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
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EMBL; M31313; AAB97765.1; -; Genomic_DNA.
EMBL; X79912; CAA56283.1; -; Genomic_DNA.
EMBL; U67922; AAC78726.1; -; Genomic_DNA.
EMBL; AJ223072; CAA11073.1; -; Genomic_DNA.
EMBL; AY350241; AAR14214.1; -; Genomic_DNA.
EMBL; AY350242; AAR14215.1; -; Genomic_DNA.
EMBL; AY350243; AAR14216.1; -; Genomic_DNA.
EMBL; AY350245; AAR14218.1; -; Genomic_DNA.
EMBL; AY350246; AAR14219.1; -; Genomic_DNA.
EMBL; AY350248; AAR14221.1; -; Genomic_DNA.
EMBL; AY350249; AAR14222.1; -; Genomic_DNA.
EMBL; AY350250; AAR14223.1; -; Genomic_DNA.
EMBL; AY350254; AAR14227.1; -; Genomic_DNA.
EMBL; AY350256; AAR14229.1; -; Genomic_DNA.
EMBL; AY350257; AAR14230.1; -; Genomic_DNA.
EMBL; AY350261; AAR14234.1; -; Genomic_DNA.
EMBL; AY350264; AAR14237.1; -; Genomic_DNA.
EMBL; AY350267; AAR14240.1; -; Genomic_DNA.
EMBL; AY350268; AAR14241.1; -; Genomic_DNA.
EMBL; AY350271; AAR14244.1; -; Genomic_DNA.
EMBL; AY350272; AAR14245.1; -; Genomic_DNA.
EMBL; AY350273; AAR14246.1; -; Genomic_DNA.
EMBL; AY350275; AAR14248.1; -; Genomic_DNA.
EMBL; AJ567984; CAE00186.1; -; Genomic_DNA.
EMBL; AJ567985; CAE00187.1; -; Genomic_DNA.
EMBL; AJ567986; CAE00188.2; -; Genomic_DNA.
EMBL; D38179; BAA07376.1; -; Genomic_DNA.
EMBL; AJ000680; CAA04235.1; -; Genomic_DNA.
EMBL; AJ000681; CAA04236.1; -; Genomic_DNA.
EMBL; AJ000736; CAA04274.1; -; Genomic_DNA.
EMBL; AJ000739; CAA04277.1; -; Genomic_DNA.
EMBL; AY907689; AAW88336.1; -; Genomic_DNA.
EMBL; AY907690; AAW88337.1; -; Genomic_DNA.
EMBL; AY907691; AAW88338.1; -; Genomic_DNA.
RefSeq; NP_001009481.1; NM_001009481.1.
RefSeq; XP_012043480.1; XM_012188090.2.
UniGene; Oar.765; -.
PDB; 1G04; NMR; -; A=145-169.
PDB; 1M25; NMR; -; A=145-169.
PDB; 1S4T; NMR; -; A=138-158.
PDB; 1TPX; X-ray; 2.56 A; A=114-234.
PDB; 1TQB; X-ray; 2.55 A; A=127-228.
PDB; 1TQC; X-ray; 2.80 A; A=127-228.
PDB; 1UW3; X-ray; 2.04 A; A=128-233.
PDB; 1XYU; NMR; -; A=124-234.
PDB; 1Y2S; NMR; -; A=124-234.
PDB; 2KTM; NMR; -; A=172-234.
PDB; 2MV8; NMR; -; A=103-234.
PDB; 2MV9; NMR; -; A=103-234.
PDB; 2N53; NMR; -; A=103-234.
PDB; 2RMV; NMR; -; A=145-169.
PDB; 2RMW; NMR; -; A=145-169.
PDBsum; 1G04; -.
PDBsum; 1M25; -.
PDBsum; 1S4T; -.
PDBsum; 1TPX; -.
PDBsum; 1TQB; -.
PDBsum; 1TQC; -.
PDBsum; 1UW3; -.
PDBsum; 1XYU; -.
PDBsum; 1Y2S; -.
PDBsum; 2KTM; -.
PDBsum; 2MV8; -.
PDBsum; 2MV9; -.
PDBsum; 2N53; -.
PDBsum; 2RMV; -.
PDBsum; 2RMW; -.
ProteinModelPortal; P23907; -.
SMR; P23907; -.
DIP; DIP-60917N; -.
IntAct; P23907; 1.
MINT; MINT-8302691; -.
BindingDB; P23907; -.
ChEMBL; CHEMBL2406893; -.
TCDB; 1.C.48.1.1; the prion peptide (prp) family.
Ensembl; ENSOART00000005076; ENSOARP00000004991; ENSOARG00000004668.
GeneID; 493887; -.
KEGG; oas:493887; -.
CTD; 5621; -.
GeneTree; ENSGT00510000049083; -.
HOVERGEN; HBG008260; -.
KO; K05634; -.
OMA; GYPHNPG; -.
OrthoDB; EOG091G0HMV; -.
EvolutionaryTrace; P23907; -.
PRO; PR:P23907; -.
Proteomes; UP000002356; Chromosome 13.
ExpressionAtlas; P23907; baseline.
GO; GO:0106003; C:amyloid-beta complex; IEA:Ensembl.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016234; C:inclusion body; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:1903135; F:cupric ion binding; IEA:Ensembl.
GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; ISS:AgBase.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; IEA:Ensembl.
GO; GO:0015631; F:tubulin binding; ISS:AgBase.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0090647; P:modulation of age-related behavioral decline; IEA:Ensembl.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; 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; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
Gene3D; 1.10.790.10; -; 1.
InterPro; IPR000817; Prion.
InterPro; IPR022416; Prion/Doppel_prot_b-ribbon_dom.
InterPro; IPR025860; Prion_N_dom.
PANTHER; PTHR10502:SF163; PTHR10502:SF163; 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; Amyloid; Cell membrane; Complete proteome; Copper;
Disease mutation; Disulfide bond; Glycoprotein; Golgi apparatus;
GPI-anchor; Lipoprotein; Membrane; Metal-binding; Polymorphism; Prion;
Reference proteome; Repeat; Signal; Zinc.
SIGNAL 1 24
CHAIN 25 233 Major prion protein.
/FTId=PRO_0000025727.
PROPEP 234 256 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000025728.
REPEAT 54 62 1.
REPEAT 63 70 2.
REPEAT 71 78 3.
REPEAT 79 86 4.
REPEAT 87 95 5.
REGION 25 233 Interaction with GRB2, ERI3 and SYN1.
{ECO:0000250|UniProtKB:P04925}.
REGION 54 95 5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
Q.
METAL 64 64 Copper or zinc 1.
{ECO:0000250|UniProtKB:P04156}.
METAL 65 65 Copper or zinc 1; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 66 66 Copper or zinc 1; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 72 72 Copper or zinc 2.
{ECO:0000250|UniProtKB:P04156}.
METAL 73 73 Copper or zinc 2; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 74 74 Copper or zinc 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 80 80 Copper or zinc 3.
{ECO:0000250|UniProtKB:P04156}.
METAL 81 81 Copper or zinc 3; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 82 82 Copper or zinc 3; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 88 88 Copper or zinc 4.
{ECO:0000250|UniProtKB:P04156}.
METAL 90 90 Copper or zinc 4; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 91 91 Copper or zinc 4; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
LIPID 233 233 GPI-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 182 217
VARIANT 112 112 M -> T. {ECO:0000269|PubMed:8094373}.
VARIANT 136 136 A -> V (in scrapie; short incubation; sA
allele). {ECO:0000269|PubMed:1681027,
ECO:0000269|PubMed:7897344,
ECO:0000269|PubMed:8094373}.
VARIANT 137 137 M -> T. {ECO:0000269|PubMed:8887505}.
VARIANT 141 141 L -> F. {ECO:0000269|PubMed:14769911,
ECO:0000269|PubMed:8887505,
ECO:0000269|Ref.8}.
VARIANT 154 154 R -> H. {ECO:0000269|PubMed:1681027,
ECO:0000269|PubMed:7897344,
ECO:0000269|PubMed:8094373}.
VARIANT 171 171 R -> H (in scrapie; low incidence).
{ECO:0000269|PubMed:7897344}.
VARIANT 171 171 R -> Q (linked to susceptibility to
scrapie). {ECO:0000269|PubMed:10466827,
ECO:0000269|PubMed:14769911,
ECO:0000269|PubMed:14970684,
ECO:0000269|PubMed:1681027,
ECO:0000269|PubMed:1969635,
ECO:0000269|PubMed:7926780,
ECO:0000269|PubMed:9799790,
ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
VARIANT 211 211 R -> Q. {ECO:0000269|PubMed:8887505,
ECO:0000269|Ref.8}.
HELIX 112 114 {ECO:0000244|PDB:2N53}.
HELIX 123 126 {ECO:0000244|PDB:2N53}.
STRAND 128 130 {ECO:0000244|PDB:1XYU}.
STRAND 131 133 {ECO:0000244|PDB:1Y2S}.
TURN 144 146 {ECO:0000244|PDB:1S4T}.
HELIX 147 155 {ECO:0000244|PDB:1UW3}.
HELIX 157 159 {ECO:0000244|PDB:1UW3}.
STRAND 165 167 {ECO:0000244|PDB:1G04}.
HELIX 169 171 {ECO:0000244|PDB:1UW3}.
STRAND 173 175 {ECO:0000244|PDB:1UW3}.
HELIX 176 196 {ECO:0000244|PDB:1UW3}.
HELIX 203 229 {ECO:0000244|PDB:1UW3}.
SEQUENCE 256 AA; 27915 MW; 7FFBEA6C6FDBF8BB CRC64;
MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW
GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GGWGQGGSHS QWNKPSKPKT NMKHVAGAAA
AGAVVGGLGG YMLGSAMSRP LIHFGNDYED RYYRENMYRY PNQVYYRPVD RYSNQNNFVH
DCVNITVKQH TVTTTTKGEN FTETDIKIME RVVEQMCITQ YQRESQAYYQ RGASVILFSS
PPVILLISFL IFLIVG


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