Reviewed, UniProtKB/Swiss-Prot O46501 (PRIO_CANFA)

Names and origin

Protein names

Recommended name:
    Major prion protein
      Short name=PrP
Alternative name(s):
    CD_antigen=CD230

Gene names

Name:	PRNP
Synonyms:	PRP

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The function of PrP is not known. PrP is encoded in the host genome and is expressed both in normal and infected cells.
Subunit structure	PrP has a tendency to aggregate yielding polymers called "rods". Interacts with GRB2, ERI3/PRNPIP and SYN1 By similarity.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor. Golgi apparatus By similarity.
Involvement in disease	PrP is found in high quantity in the brain of humans and animals infected with the degenerative neurological diseases kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.
Sequence similarities	Belongs to the prion family.

Ontologies

Keywords
Cellular component	Amyloid Cell membrane Golgi apparatus Membrane
Domain	Repeat Signal
Molecular function	Prion
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein homooligomerization Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

By similarity

Chain

25 – 232

208

Major prion protein

PRO_0000025639

Propeptide

233 – 255

23

Removed in mature form Potential

PRO_0000025640

Regions

Repeat

54 – 62

9

1

Repeat

63 – 70

8

2

Repeat

71 – 78

8

3

Repeat

79 – 86

8

4

Repeat

87 – 94

8

5

Region

25 – 232

208

Interaction with GRB2, ERI3 and SYN1 By similarity

Region

54 – 94

41

5 X 8 AA tandem repeats of P-H-G-G-G-W-G-Q

Amino acid modifications

Lipidation

232

1

GPI-anchor amidated alanine Potential

Glycosylation

174

1

N-linked (GlcNAc...) Potential

Glycosylation

184

1

N-linked (GlcNAc...) Potential

Glycosylation

199

1

N-linked (GlcNAc...) Potential

Disulfide bond

182 ↔ 216

By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

255

Helix Strand Turn

Details...

Helix

147 – 154

8

Helix

157 – 159

3

Beta strand

173 – 176

4

Helix

177 – 196

20

Helix

202 – 222

21

Helix

224 – 227

4

Sequences

	Sequence		Length	Mass (Da)
	O46501-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 70E80411BD6B1F63	FASTA	255	27,704
	10 20 30 40 50 60 MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW 70 80 90 100 110 120 GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GGWGQGGTHS QWNKPSKPKT NMKHVAGAAA 130 140 150 160 170 180 AGAVVGGLGG YLLGSAMSRP LIHFGNDCED RYYRENMYRY PNQVYYRSVD QYNNQSTFVH 190 200 210 220 230 240 DCVNITVKQH TVTTTKGENF TETDIKMMER VVEQMCITQY QRESEAYYQR GASVILFSSP 250 PVILLVSFLI FLIVG

References

[1]	Rohwer R.G., Edelman D. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Prion protein NMR structures of cats, dogs, pigs, and sheep." 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. Proc. Natl. Acad. Sci. U.S.A. 102:640-645(2005) [PubMed: 15647367] [Abstract] Cited for: STRUCTURE BY NMR OF 124-233.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF022714 Genomic DNA. Translation: AAB94585.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XYK	NMR	-	A	124-233	[»]

SMR

O46501. Positions 1-30.

ModBase

Search...

Phylogenomic databases

HOVERGEN

O46501.

InParanoid

O46501.

Family and domain databases

InterPro

IPR000817. Prion.
[Graphical view]

Gene3D

G3DSA:1.10.790.10. Prion. 1 hit.

PANTHER

PTHR11522. Prion. 1 hit.

Pfam

PF00377. Prion. 1 hit.
[Graphical view]

PRINTS

PR00341. PRION.

SMART

SM00157. PRP. 1 hit.
[Graphical view]

PROSITE

PS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRIO_CANFA

Accession

Primary (citable) accession number: O46501

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 1, 1998
Last modified:	January 19, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)