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

 PRIO_RABIT              Reviewed;         252 AA.
Q95211;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
30-AUG-2017, entry version 124.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=New Zealand white;
PubMed=9031631; DOI=10.1016/S0378-1119(96)00598-7;
Loftus B., Rogers M.;
"Characterization of a prion protein (PrP) gene from rabbit; a species
with apparent resistance to infection by prions.";
Gene 184:215-219(1997).
[2]
STRUCTURE BY NMR OF 91-228 OF WILD TYPE AND MUTANT ASN-173, AND
DISULFIDE BOND.
PubMed=20639199; DOI=10.1074/jbc.M110.118844;
Wen Y., Li J., Yao W., Xiong M., Hong J., Peng Y., Xiao G., Lin D.;
"Unique structural characteristics of the rabbit prion protein.";
J. Biol. Chem. 285:31682-31693(2010).
-!- 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}.
-!- 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=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; U28334; AAC48697.1; -; Genomic_DNA.
PIR; JC6175; JC6175.
RefSeq; XP_008254357.1; XM_008256135.2.
RefSeq; XP_008254358.1; XM_008256136.2.
UniGene; Ocu.6364; -.
PDB; 2FJ3; NMR; -; A=91-228.
PDB; 2JOH; NMR; -; A=91-228.
PDB; 2JOM; NMR; -; A=91-228.
PDB; 4HLS; X-ray; 1.45 A; A/B=119-229.
PDB; 4HMM; X-ray; 1.50 A; A/B=119-229.
PDB; 4HMR; X-ray; 1.60 A; A/B=119-229.
PDBsum; 2FJ3; -.
PDBsum; 2JOH; -.
PDBsum; 2JOM; -.
PDBsum; 4HLS; -.
PDBsum; 4HMM; -.
PDBsum; 4HMR; -.
ProteinModelPortal; Q95211; -.
SMR; Q95211; -.
DIP; DIP-59794N; -.
STRING; 9986.ENSOCUP00000001797; -.
Ensembl; ENSOCUT00000002082; ENSOCUP00000001797; ENSOCUG00000002086.
GeneID; 100008658; -.
CTD; 5621; -.
eggNOG; ENOG410IJMM; Eukaryota.
eggNOG; ENOG410YXUU; LUCA.
GeneTree; ENSGT00510000049083; -.
HOVERGEN; HBG008260; -.
InParanoid; Q95211; -.
OMA; GYPHNPG; -.
OrthoDB; EOG091G0HMV; -.
TreeFam; TF105188; -.
EvolutionaryTrace; Q95211; -.
Proteomes; UP000001811; Chromosome 4.
Bgee; ENSOCUG00000002086; -.
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; IEA:Ensembl.
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: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; IPR020949; Prion_copper_b_octapeptide.
InterPro; IPR025860; Prion_N_dom.
PANTHER; PTHR10502:SF163; PTHR10502:SF163; 1.
Pfam; PF00377; Prion; 1.
Pfam; PF11587; Prion_bPrPp; 1.
Pfam; PF03991; Prion_octapep; 5.
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;
Disulfide bond; Glycoprotein; Golgi apparatus; GPI-anchor;
Lipoprotein; Membrane; Metal-binding; Prion; Reference proteome;
Repeat; Signal; Zinc.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 229 Major prion protein.
/FTId=PRO_0000025721.
PROPEP 230 252 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000025722.
REPEAT 51 59 1.
REPEAT 60 67 2.
REPEAT 68 75 3.
REPEAT 76 83 4.
REPEAT 84 92 5.
REGION 23 229 Interaction with GRB2, ERI3 and SYN1.
{ECO:0000250|UniProtKB:P04925}.
REGION 51 92 5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
Q.
METAL 61 61 Copper or zinc 1.
{ECO:0000250|UniProtKB:P04156}.
METAL 62 62 Copper or zinc 1; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 63 63 Copper or zinc 1; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 69 69 Copper or zinc 2.
{ECO:0000250|UniProtKB:P04156}.
METAL 70 70 Copper or zinc 2; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 71 71 Copper or zinc 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 77 77 Copper or zinc 3.
{ECO:0000250|UniProtKB:P04156}.
METAL 78 78 Copper or zinc 3; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 79 79 Copper or zinc 3; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 85 85 Copper or zinc 4.
{ECO:0000250|UniProtKB:P04156}.
METAL 86 86 Copper or zinc 4; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 87 87 Copper or zinc 4; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
LIPID 229 229 GPI-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 178 213 {ECO:0000269|PubMed:20639199}.
STRAND 128 130 {ECO:0000244|PDB:2FJ3}.
TURN 131 134 {ECO:0000244|PDB:2JOH}.
HELIX 143 152 {ECO:0000244|PDB:4HLS}.
HELIX 153 155 {ECO:0000244|PDB:4HLS}.
STRAND 161 163 {ECO:0000244|PDB:4HMM}.
HELIX 165 167 {ECO:0000244|PDB:4HLS}.
HELIX 171 191 {ECO:0000244|PDB:4HLS}.
TURN 192 194 {ECO:0000244|PDB:4HLS}.
HELIX 199 220 {ECO:0000244|PDB:4HLS}.
HELIX 222 228 {ECO:0000244|PDB:4HLS}.
SEQUENCE 252 AA; 27432 MW; 2E177AAF38B23A54 CRC64;
MAHLGYWMLL LFVATWSDVG LCKKRPKPGG GWNTGGSRYP GQSSPGGNRY PPQGGGWGQP
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGTHNQWGK PSKPKTSMKH VAGAAAAGAV
VGGLGGYMLG SAMSRPLIHF GNDYEDRYYR ENMYRYPNQV YYRPVDQYSN QNSFVHDCVN
ITVKQHTVTT TTKGENFTET DIKIMERVVE QMCITQYQQE SQAAYQRAAG VLLFSSPPVI
LLISFLIFLI VG


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