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

 PRIO_MESAU              Reviewed;         254 AA.
P04273;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
25-OCT-2017, entry version 141.
RecName: Full=Major prion protein;
Short=PrP;
AltName: Full=PrP27-30;
AltName: Full=PrP33-35C;
AltName: CD_antigen=CD230;
Flags: Precursor;
Name=PRNP; Synonyms=PRP;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2873895; DOI=10.1016/0092-8674(86)90662-8;
Basler K., Oesch B., Scott M., Westaway D., Waelchli M., Groth D.F.,
McKinley M.P., Prusiner S.B., Weissmann C.;
"Scrapie and cellular PrP isoforms are encoded by the same chromosomal
gene.";
Cell 46:417-428(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-254.
PubMed=2859120; DOI=10.1016/0092-8674(85)90333-2;
Oesch B., Westaway D., Walchli M., McKinley M.P., Kent S.B.H.,
Aebersold R., Barry R.A., Tempst P., Teplow D.B., Hood L.E.,
Prusiner S.B., Weissmann C.;
"A cellular gene encodes scrapie PrP 27-30 protein.";
Cell 40:735-746(1985).
[3]
GLYCOSYLATION AT ASN-181 AND ASN-197, AND DISULFIDE BONDS.
PubMed=3138115; DOI=10.1111/j.1432-1033.1988.tb14246.x;
Turk E., Teplow D.B., Hood L.E., Prusiner S.B.;
"Purification and properties of the cellular and scrapie hamster prion
proteins.";
Eur. J. Biochem. 176:21-30(1988).
[4]
GPI-ANCHOR.
PubMed=2444340; DOI=10.1016/0092-8674(87)90150-4;
Stahl N., Borchelt D.R., Hasiao K., Prusiner S.B.;
"Scrapie prion protein contains a phosphatidylinositol glycolipid.";
Cell 51:229-240(1987).
[5]
GPI-ANCHOR AT SER-231.
PubMed=1980209; DOI=10.1021/bi00490a001;
Stahl N., Baldwin M.A., Burlingame A.L., Prusiner S.B.;
"Identification of glycoinositol phospholipid linked and truncated
forms of the scrapie prion protein.";
Biochemistry 29:8879-8884(1990).
[6]
MUTAGENESIS OF THR-183 AND THR-199.
PubMed=1983782; DOI=10.1093/glycob/1.1.101;
Rogers M., Taraboulos A., Scott M., Groth D., Prusiner S.B.;
"Intracellular accumulation of the cellular prion protein after
mutagenesis of its Asn-linked glycosylation sites.";
Glycobiology 1:101-109(1990).
[7]
COPPER- OR ZINC-BINDING SITES, AND DOMAIN.
PubMed=12779334; DOI=10.1021/bi027138+;
Burns C.S., Aronoff-Spencer E., Legname G., Prusiner S.B.,
Antholine W.E., Gerfen G.J., Peisach J., Millhauser G.L.;
"Copper coordination in the full-length, recombinant prion protein.";
Biochemistry 42:6794-6803(2003).
[8]
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).
[9]
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).
[10]
ALTERNATIVE INITIATION (ISOFORM 2), SUBCELLULAR LOCATION, MUTAGENESIS
OF MET-1 AND MET-15, AND SUMOYLATION.
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).
[11]
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).
[12]
STRUCTURE BY NMR OF 90-231.
PubMed=9294167; DOI=10.1073/pnas.94.19.10086;
James T.L., Liu H., Ulyanov N.B., Farr-Jones S., Zhang H., Donne D.G.,
Kaneko K., Groth D., Mehlhorn I., Prusiner S.B., Cohen F.E.;
"Solution structure of a 142-residue recombinant prion protein
corresponding to the infectious fragment of the scrapie isoform.";
Proc. Natl. Acad. Sci. U.S.A. 94:10086-10091(1997).
[13]
STRUCTURE BY NMR OF 29-231.
PubMed=9391046; DOI=10.1073/pnas.94.25.13452;
Donne D.G., Viles J.H., Groth D., Mehlhorn I., James T.L., Cohen F.E.,
Prusiner S.B., Wright P.E., Dyson H.J.;
"Structure of the recombinant full-length hamster prion protein
PrP(29-231): the N-terminus is highly flexible.";
Proc. Natl. Acad. Sci. U.S.A. 94:13452-13457(1997).
-!- 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}.
-!- 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 (By similarity). Mislocalized cytosolically
exposed PrP interacts with MGRN1; this interaction alters MGRN1
subcellular location and causes lysosomal enlargement (By
similarity). Interacts with APP. Interacts with KIAA1191 (By
similarity). Interacts with ADGRG6 (By similarity).
{ECO:0000250|UniProtKB:P04156, ECO:0000250|UniProtKB:P04925}.
-!- INTERACTION:
Self; NbExp=10; IntAct=EBI-986426, EBI-986426;
Q8CJG0:Ago2 (xeno); NbExp=2; IntAct=EBI-986426, EBI-528299;
-!- 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}.
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1;
IsoId=P04273-1; Sequence=Displayed;
Name=2; Synonyms=PrP(M15);
IsoId=P04273-2; Sequence=VSP_039046;
-!- 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}.
-!- PTM: Isoform 2 is sumoylated with SUMO1.
{ECO:0000269|PubMed:19059915}.
-!- 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}.
-!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
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EMBL; M14054; AAA37091.1; -; Genomic_DNA.
EMBL; K02234; AAA37092.1; -; mRNA.
PIR; I48168; UJHYIH.
RefSeq; XP_005068717.1; XM_005068660.2. [P04273-1]
RefSeq; XP_012967855.1; XM_013112401.1. [P04273-1]
PDB; 1B10; NMR; -; A=90-231.
PDB; 2KKG; NMR; -; A=23-106.
PDB; 2LH8; NMR; -; A=125-228.
PDB; 3NVE; X-ray; 1.70 A; A/B=138-143.
PDB; 4YXL; X-ray; 2.60 A; A=90-232.
PDBsum; 1B10; -.
PDBsum; 2KKG; -.
PDBsum; 2LH8; -.
PDBsum; 3NVE; -.
PDBsum; 4YXL; -.
DisProt; DP00187; -.
ProteinModelPortal; P04273; -.
SMR; P04273; -.
DIP; DIP-1081N; -.
IntAct; P04273; 1.
ChEMBL; CHEMBL1293203; -.
iPTMnet; P04273; -.
UniCarbKB; P04273; -.
Ensembl; ENSMAUT00000026964; ENSMAUP00000022959; ENSMAUG00000020251.
GeneID; 101829062; -.
CTD; 5621; -.
HOVERGEN; HBG008260; -.
OrthoDB; EOG091G0HMV; -.
EvolutionaryTrace; P04273; -.
Proteomes; UP000189706; Genome assembly.
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; IMP:CAFA.
GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; IEA:Ensembl.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IEA:UniProtKB-KW.
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: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:1990535; P:neuron projection maintenance; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
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; 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; 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; Cell cycle;
Cell membrane; Complete proteome; Copper; Cytoplasm; Disulfide bond;
Glycoprotein; Golgi apparatus; GPI-anchor; Growth arrest; Lipoprotein;
Membrane; Metal-binding; Nucleus; Prion; Reference proteome; Repeat;
Signal; Ubl conjugation; Zinc.
SIGNAL 1 22
CHAIN 23 231 Major prion protein.
/FTId=PRO_0000025695.
PROPEP 232 254 Removed in mature form.
{ECO:0000269|PubMed:1980209}.
/FTId=PRO_0000025696.
REPEAT 51 59 1.
REPEAT 60 67 2.
REPEAT 68 75 3.
REPEAT 76 83 4.
REPEAT 84 91 5.
REGION 23 231 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.
REGION 90 231 PrP27-30 (protease resistant core).
METAL 61 61 Copper or zinc 1.
METAL 62 62 Copper or zinc 1; via amide nitrogen.
METAL 63 63 Copper or zinc 1; via amide nitrogen and
carbonyl oxygen.
METAL 69 69 Copper or zinc 2.
METAL 70 70 Copper or zinc 2; via amide nitrogen.
METAL 71 71 Copper or zinc 2; via amide nitrogen and
carbonyl.
METAL 71 71 Copper or zinc 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 77 77 Copper or zinc 3.
METAL 78 78 Copper or zinc 3; via amide nitrogen.
METAL 79 79 Copper or zinc 3; via amide nitrogen and
carbonyl oxygen.
METAL 85 85 Copper or zinc 4.
METAL 86 86 Copper or zinc 4; via amide nitrogen.
METAL 87 87 Copper or zinc 4; via amide nitrogen and
carbonyl oxygen.
LIPID 231 231 GPI-anchor amidated serine.
{ECO:0000269|PubMed:1980209}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3138115}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3138115}.
DISULFID 179 214 {ECO:0000269|PubMed:3138115}.
VAR_SEQ 1 14 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_039046.
MUTAGEN 1 1 M->S: Protein detected. No protein
detected; when associated with S-15.
{ECO:0000269|PubMed:19059915}.
MUTAGEN 15 15 M->S: No protein detected; when
associated with S-1.
{ECO:0000269|PubMed:19059915}.
MUTAGEN 183 183 T->A: Accumulates intracellularly.
{ECO:0000269|PubMed:1983782}.
MUTAGEN 199 199 T->A: Accumulates intracellularly.
{ECO:0000269|PubMed:1983782}.
STRAND 61 63 {ECO:0000244|PDB:2KKG}.
STRAND 69 71 {ECO:0000244|PDB:2KKG}.
STRAND 73 75 {ECO:0000244|PDB:2KKG}.
STRAND 77 79 {ECO:0000244|PDB:2KKG}.
STRAND 81 83 {ECO:0000244|PDB:2KKG}.
STRAND 85 87 {ECO:0000244|PDB:2KKG}.
STRAND 129 133 {ECO:0000244|PDB:1B10}.
STRAND 139 141 {ECO:0000244|PDB:3NVE}.
HELIX 144 153 {ECO:0000244|PDB:4YXL}.
HELIX 154 156 {ECO:0000244|PDB:4YXL}.
STRAND 160 163 {ECO:0000244|PDB:1B10}.
HELIX 166 168 {ECO:0000244|PDB:4YXL}.
HELIX 172 193 {ECO:0000244|PDB:4YXL}.
HELIX 200 222 {ECO:0000244|PDB:4YXL}.
SEQUENCE 254 AA; 27919 MW; 442C0E3ED4D20672 CRC64;
MANLSYWLLA LFVAMWTDVG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGTWGQP
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHNQWN KPSKPKTNMK HMAGAAAAGA
VVGGLGGYML GSAMSRPMMH FGNDWEDRYY RENMNRYPNQ VYYRPVDQYN NQNNFVHDCV
NITIKQHTVT TTTKGENFTE TDIKIMERVV EQMCTTQYQK ESQAYYDGRR SSAVLFSSPP
VILLISFLIF LMVG


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