CPLM-002193

Genbank Nucleotide ID

Protein Synonyms/Alias

PrP; PrP27-30; PrP33-35C; CD230

Mus musculus (Mouse)

Position	Peptide	Type	References
203	NFTETDVKMMERVVE	ubiquitination	[1]

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

Functional Description

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) (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.

REPEAT 51 58 1.
REPEAT 59 66 2.
REPEAT 67 74 3.
REPEAT 75 82 4.
REPEAT 83 90 5.
REGION 23 231 Interaction with GRB2, ERI3 and SYN1.
REGION 51 90 5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
METAL 60 60 Copper or zinc 1 (By similarity).
METAL 61 61 Copper or zinc 1; via amide nitrogen (By
METAL 62 62 Copper or zinc 1; via amide nitrogen and
METAL 68 68 Copper or zinc 2 (By similarity).
METAL 69 69 Copper or zinc 2; via amide nitrogen (By
METAL 70 70 Copper or zinc 2; via amide nitrogen and
METAL 76 76 Copper or zinc 3 (By similarity).
METAL 77 77 Copper or zinc 3; via amide nitrogen (By
METAL 78 78 Copper or zinc 3; via amide nitrogen and
METAL 84 84 Copper or zinc 4 (By similarity).
METAL 85 85 Copper or zinc 4; via amide nitrogen (By
METAL 86 86 Copper or zinc 4; via amide nitrogen and
MOD_RES 44 44 Hydroxyproline.
LIPID 230 230 GPI-anchor amidated serine (By
CARBOHYD 180 180 N-linked (GlcNAc...) (Probable).
CARBOHYD 196 196 N-linked (GlcNAc...).
DISULFID 178 213

3D-structure; Amyloid; Cell membrane; Complete proteome; Copper; Direct protein sequencing; Disulfide bond; Glycoprotein; Golgi apparatus; GPI-anchor; Hydroxylation; Lipoprotein; Membrane; Metal-binding; Polymorphism; Prion; Reference proteome; Repeat; Signal; Zinc.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO:0005794; C:Golgi apparatus; IDA:MGI.
GO:0045121; C:membrane raft; IDA:MGI.
GO:0005730; C:nucleolus; IEA:Compara.
GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO:0006878; P:cellular copper ion homeostasis; TAS:MGI.
GO:0007611; P:learning or memory; IEA:Compara.
GO:0046007; P:negative regulation of activated T cell proliferation; IMP:BHF-UCL.
GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL.
GO:0032689; P:negative regulation of interferon-gamma production; IMP:BHF-UCL.
GO:0032700; P:negative regulation of interleukin-17 production; IMP:BHF-UCL.
GO:0032703; P:negative regulation of interleukin-2 production; IMP:BHF-UCL.
GO:0001933; P:negative regulation of protein phosphorylation; IMP:BHF-UCL.
GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:BHF-UCL.
GO:0006139; P:nucleobase-containing compound metabolic process; TAS:MGI.
GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO:0046686; P:response to cadmium ion; IEA:Compara.
GO:0046688; P:response to copper ion; IEA:Compara.
GO:0006979; P:response to oxidative stress; IDA:MGI.

IPR000817; Prion.
IPR022416; Prion/Doppel_prot_b-ribbon_dom.
IPR025860; Prion_N_dom.

PF00377; Prion
PF11587; Prion_bPrPp

PS00291; PRION_1
PS00706; PRION_2