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Major prion protein (PrP) (CD antigen CD230)

 PRIO_RAT                Reviewed;         254 AA.
P13852; Q549H6;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
31-JAN-2018, entry version 153.
RecName: Full=Major prion protein;
Short=PrP;
AltName: CD_antigen=CD230;
Flags: Precursor;
Name=Prnp; Synonyms=Prn, Prp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SJ/D, and Zitter; TISSUE=Liver;
PubMed=7909925; DOI=10.1016/0304-3940(94)90478-2;
Gomi H., Ikeda T., Kunieda T., Itohara S., Prusiner S.B.,
Yamanouchi K.;
"Prion protein (PrP) is not involved in the pathogenesis of spongiform
encephalopathy in zitter rats.";
Neurosci. Lett. 166:171-174(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Wistar; TISSUE=Liver;
PubMed=8879116; DOI=10.1007/BF00369996;
Saeki K., Matsumoto Y., Hirota Y., Matsumoto Y., Onodera T.;
"Three-exon structure of the gene encoding the rat prion protein and
its expression in tissues.";
Virus Genes 12:15-20(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=10373359; DOI=10.1006/jmbi.1999.2831;
Wopfner F., Weidenhofer G., Schneider R., von Brunn A., Gilch S.,
Schwarz T.F., Werner T., Schatzl H.M.;
"Analysis of 27 mammalian and 9 avian PrPs reveals high conservation
of flexible regions of the prion protein.";
J. Mol. Biol. 289:1163-1178(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 29-254.
PubMed=2889848;
Liao Y.-C., Tokes Z., Lim E., Lackey A., Woo C.H., Button J.D.,
Clawson G.A.;
"Cloning of rat 'prion-related protein' cDNA.";
Lab. Invest. 57:370-374(1987).
[6]
PROTEIN SEQUENCE OF 209-229, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
-!- 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}.
-!- 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; S69654; AAB30728.2; -; Genomic_DNA.
EMBL; D50093; BAA08790.1; -; Genomic_DNA.
EMBL; AF117322; AAD19993.1; -; Genomic_DNA.
EMBL; BC072692; AAH72692.1; -; mRNA.
EMBL; M20313; AAA41947.1; -; mRNA.
PIR; A53892; A53892.
RefSeq; NP_036763.1; NM_012631.2.
RefSeq; XP_006235124.1; XM_006235062.3.
UniGene; Rn.3936; -.
ProteinModelPortal; P13852; -.
SMR; P13852; -.
BioGrid; 246818; 2.
STRING; 10116.ENSRNOP00000028881; -.
iPTMnet; P13852; -.
PhosphoSitePlus; P13852; -.
PaxDb; P13852; -.
PRIDE; P13852; -.
Ensembl; ENSRNOT00000028881; ENSRNOP00000028881; ENSRNOG00000021259.
GeneID; 24686; -.
KEGG; rno:24686; -.
UCSC; RGD:3410; rat.
CTD; 5621; -.
RGD; 3410; Prnp.
eggNOG; ENOG410IJMM; Eukaryota.
eggNOG; ENOG410YXUU; LUCA.
GeneTree; ENSGT00510000049083; -.
HOGENOM; HOG000232077; -.
HOVERGEN; HBG008260; -.
InParanoid; P13852; -.
KO; K05634; -.
OMA; GYPHNPG; -.
OrthoDB; EOG091G0HMV; -.
PhylomeDB; P13852; -.
TreeFam; TF105188; -.
PRO; PR:P13852; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000021259; -.
Genevisible; P13852; RN.
GO; GO:0106003; C:amyloid-beta complex; IEA:Ensembl.
GO; GO:0046658; C:anchored component of plasma membrane; TAS:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
GO; GO:0016234; C:inclusion body; ISO:RGD.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; ISO:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:ARUK-UCL.
GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
GO; GO:0043008; F:ATP-dependent protein binding; IPI:RGD.
GO; GO:0051087; F:chaperone binding; IPI:RGD.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:1903135; F:cupric ion binding; ISO:RGD.
GO; GO:1903136; F:cuprous ion binding; ISO:RGD.
GO; GO:0005539; F:glycosaminoglycan binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0044325; F:ion channel binding; IPI:RGD.
GO; GO:0005521; F:lamin binding; IPI:RGD.
GO; GO:0008017; F:microtubule binding; ISO:RGD.
GO; GO:0002020; F:protease binding; ISO:RGD.
GO; GO:0032403; F:protein complex binding; ISO:RGD.
GO; GO:0004872; F:receptor activity; ISO:RGD.
GO; GO:0004871; F:signal transducer activity; ISO:RGD.
GO; GO:0015631; F:tubulin binding; ISO:RGD.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IPI:ARUK-UCL.
GO; GO:0032147; P:activation of protein kinase activity; ISO:RGD.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
GO; GO:0071280; P:cellular response to copper ion; ISO:RGD.
GO; GO:0035690; P:cellular response to drug; ISO:RGD.
GO; GO:0007611; P:learning or memory; IMP:RGD.
GO; GO:0090647; P:modulation of age-related behavioral decline; ISO:RGD.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISO:RGD.
GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; ISO:RGD.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISO:RGD.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:ARUK-UCL.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; ISO:RGD.
GO; GO:0043433; P:negative regulation of DNA binding transcription factor activity; ISO:RGD.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:RGD.
GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:RGD.
GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:RGD.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IDA:ARUK-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:RGD.
GO; GO:1990535; P:neuron projection maintenance; ISO:RGD.
GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:RGD.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:RGD.
GO; GO:0031648; P:protein destabilization; ISO:RGD.
GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; ISO:RGD.
GO; GO:1902938; P:regulation of intracellular calcium activated chloride channel activity; ISO:RGD.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:RGD.
GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
GO; GO:0046686; P:response to cadmium ion; IDA:RGD.
GO; GO:0046688; P:response to copper ion; IDA:RGD.
GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
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;
Amyloid; Cell membrane; Complete proteome; Copper;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Golgi apparatus; GPI-anchor; Lipoprotein; Membrane; Metal-binding;
Prion; Reference proteome; Repeat; Signal; Zinc.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 231 Major prion protein.
/FTId=PRO_0000025723.
PROPEP 232 254 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000025724.
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.
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 231 231 GPI-anchor amidated serine.
{ECO:0000250|UniProtKB:P04273}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 179 214 {ECO:0000250|UniProtKB:P04273}.
SEQUENCE 254 AA; 27804 MW; 28F424D13BEFA2C6 CRC64;
MANLGYWLLA LFVTTCTDVG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQSGGTWGQP
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWS QGGGTHNQWN KPSKPKTNLK HVAGAAAAGA
VVGGLGGYML GSAMSRPMLH FGNDWEDRYY RENMYRYPNQ VYYRPVDQYS NQNNFVHDCV
NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCVTQYQK ESQAYYDGRR SSAVLFSSPP
VILLISFLIF LIVG


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