P10279 (PRIO_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Major prion protein
Short name=PrP

Alternative name(s):
Major scrapie-associated fibril protein 1
CD_antigen=CD230

Gene names

Name:	PRNP
Synonyms:	PRP

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	264 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	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 Cu2+ or ZN2+ for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains By similarity.
Subunit structure	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 By similarity. Interacts with KIAA1191 By similarity.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor By similarity. Golgi apparatus By similarity. Note: Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of CU2+, to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis By similarity.
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 By similarity. 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 By similarity.
Involvement in disease	Variations in PRNP are responsible of transmissible bovine spongiform encephalopathies (BSE), a class of neurodegenerative diseases that affect various mammals. These diseases are caused by abnormally folded prion proteins. BSE can be subdivided into at least three groups: classical, H-type and L-type, with the latter 2 collectively referred to as atypical BSE. Susceptibility or resistance to a BSE disease can be influenced by at least 3 factors related to the host prion protein: protein expression levels, number of octapeptide repeats, and specific polymorphisms. In cattle, as in humans, BSEs can occur as infectious, spontaneous and genetic diseases.
Miscellaneous	This protein is produced by a bicistronic gene which also produces the major prion protein/PRNP from an overlapping reading frame. The alternative prion protein/AltPrP (AC F7VJQ2) and PRNP have no apparent direct functional relation since a mutation that removes the start codon of the AltPrP has no apparent effect on the biology of PRNP By similarity. In mouse and hamster, the alternative initiation AUG codon is absent and is replaced by a GUG codon.
Sequence similarities	Belongs to the prion family.

Ontologies

Keywords
Cellular component	Amyloid Cell membrane Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Prion
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of T cell receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of activated T cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of calcineurin-NFAT signaling cascade Inferred from electronic annotation. Source: Compara negative regulation of interferon-gamma production Inferred from electronic annotation. Source: Compara negative regulation of interleukin-17 production Inferred from electronic annotation. Source: Compara negative regulation of interleukin-2 production Inferred from electronic annotation. Source: Compara negative regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara negative regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: InterPro response to oxidative stress Inferred from electronic annotation. Source: Compara signal transduction 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-KW endoplasmic reticulum Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.18

Chain

25 – 241

217

Major prion protein

PRO_0000025627

Propeptide

242 – 264

23

Removed in mature form Potential

PRO_0000025628

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

Repeat

95 – 103

9

6

Region

25 – 241

217

Interaction with GRB2, ERI3 and SYN1 By similarity

Region

54 – 103

50

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

Sites

Metal binding

72

1

Copper or zinc 1 By similarity

Metal binding

73

1

Copper or zinc 1; via amide nitrogen By similarity

Metal binding

74

1

Copper or zinc 1; via amide nitrogen and carbonyl oxygen By similarity

Metal binding

80

1

Copper or zinc 2 By similarity

Metal binding

81

1

Copper or zinc 2; via amide nitrogen By similarity

Metal binding

82

1

Copper or zinc 2; via amide nitrogen and carbonyl oxygen By similarity

Metal binding

88

1

Copper or zinc 3 By similarity

Metal binding

89

1

Copper or zinc 3; via amide nitrogen By similarity

Metal binding

90

1

Copper or zinc 3; via amide nitrogen and carbonyl oxygen By similarity

Metal binding

96

1

Copper or zinc 4 By similarity

Metal binding

97

1

Copper or zinc 4; via amide nitrogen By similarity

Metal binding

98

1

Copper or zinc 4; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Lipidation

241

1

GPI-anchor amidated alanine Potential

Glycosylation

192

1

N-linked (GlcNAc...) Probable

Glycosylation

208

1

N-linked (GlcNAc...) Probable

Disulfide bond

190 ↔ 225

Natural variations

Natural variant

60

1

W → R. Ref.10

Natural variant

71 – 78

8

Missing in allele 2.

Natural variant

84 – 99

16

Missing.

Natural variant

92 – 99

8

Missing.

Natural variant

94

1

Q → R. Ref.10

Natural variant

98

1

G → GGWGQPHGG.

Natural variant

154

1

S → N. Ref.2 Ref.10

Natural variant

211

1

E → K. Ref.9

Natural variant

234

1

Q → R. Ref.10

Experimental info

Sequence conflict

106 – 108

3

THG → SHS in BAA01469. Ref.2

Sequence conflict

218

1

E → K in BAA01467. Ref.2

Sequence conflict

218

1

E → K in BAA19253. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

264

Helix Strand Turn

Details...

Turn

3 – 8

6

Helix

9 – 21

13

Beta strand

24 – 26

3

Beta strand

109 – 111

3

Helix

136 – 138

3

Beta strand

139 – 141

3

Helix

155 – 162

8

Helix

165 – 167

3

Beta strand

177 – 179

3

Helix

184 – 203

20

Turn

204 – 206

3

Helix

211 – 237

27

Sequences

	Sequence		Length	Mass (Da)
	P10279 [UniParc]. Last modified November 1, 1991. Version 2. Checksum: D6D214038316A231	FASTA	264	28,614
	10 20 30 40 50 60 MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW 70 80 90 100 110 120 GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GWGQPHGGGG WGQGGTHGQW NKPSKPKTNM 130 140 150 160 170 180 KHVAGAAAAG AVVGGLGGYM LGSAMSRPLI HFGSDYEDRY YRENMHRYPN QVYYRPVDQY 190 200 210 220 230 240 SNQNNFVHDC VNITVKEHTV TTTTKGENFT ETDIKMMERV VEQMCITQYQ RESQAYYQRG 250 260 ASVILFSSPP VILLISFLIF LIVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon." Goldmann W., Hunter N., Martin T., Dawson M., Hope J. J. Gen. Virol. 72:201-204(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Holstein-Friesian.
[2]	"Comparative sequence analysis and expression of bovine PrP gene in mouse L-929 cells." Yoshimoto J., Iinuma T., Ishiguro N., Horiuchi M., Imamura M., Shinagawa M. Virus Genes 6:343-356(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS 92-TRP--GLY 99 DEL AND ASN-154. Strain: Holstein-Friesian. Tissue: Brain.
[3]	"Immunologic and molecular biologic studies of prion proteins in bovine spongiform encephalopathy." Prusiner S.B., Fuzi M., Scott M., Serban D., Serban H., Taraboulos A., Gabriel J.M., Wells G.A., Wilesmith J.W., Bradley R. J. Infect. Dis. 167:602-613(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Genomic organization of bovine PrP gene and complete nucleotide sequence of bovine PrP cDNA." Horiuchi M., Ishiguro N., Nagasawa H., Toyoda Y., Shinagawa M. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Holstein-Friesian. Tissue: Brain.
[5]	"Complete genomic sequence of the bovine prion gene (PRNP) and polymorphism in its promoter region." Hills D., Comincini S., Schlaepfer J., Dolf G., Ferretti L., Williams J.L. Anim. Genet. 32:231-232(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Jersey.
[6]	"Bovine PrP gene for prion protein." Naharro G., Yugueros J., Temprano A. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT 98-GLY-GLY-TRP-GLY-GLN-PRO-HIS-GLY-GLY INS.
[7]	"Nucleotide sequence of PrP cDNA in Korean cattle." Yoo H.S., Kang S.G., Choi I.S., Kang S.K., Hwang W.S. Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Korean.
[8]	"Prion gene sequence variation within diverse groups of U.S. sheep, beef cattle, and deer." Heaton M.P., Leymaster K.A., Freking B.A., Hawk D.A., Smith T.P., Keele J.W., Snelling W.M., Fox J.M., Chitko-McKown C.G., Laegreid W.W. Mamm. Genome 14:765-777(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]	"Prevalence of the prion protein gene E211K variant in U.S. cattle." Heaton M.P., Keele J.W., Harhay G.P., Richt J.A., Koohmaraie M., Wheeler T.L., Shackelford S.D., Casas E., King D.A., Sonstegard T.S., Van Tassell C.P., Neibergs H.L., Chase C.C. Jr., Kalbfleisch T.S., Smith T.P.L., Clawson M.L., Laegreid W.W. BMC Vet. Res. 4:25-25(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 211, VARIANT LYS-211.
[10]	"Cloning and sequence analysis of bovine prion protein gene." Wu R., Xie Q.G., Liu X.T., Chen H.T., Cheng J. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-60; ARG-94; ASN-154 AND ARG-234. Strain: Holstein-Friesian and Qinchuan. Tissue: Blood.
[11]	"Prion protein gene (PRNP) variants and evidence for strong purifying selection in functionally important regions of bovine exon 3." Seabury C.M., Honeycutt R.L., Rooney A.P., Halbert N.D., Derr J.N. Proc. Natl. Acad. Sci. U.S.A. 101:15142-15147(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS 84-TRP--GLY 99 DEL; 92-TRP--GLY 99 DEL AND 98-GLY-GLY-TRP-GLY-GLN-PRO-HIS-GLY-GLY INS.
[12]	"Genomic characterization of the bovine PRN loci (PRNP, PRND and PRNT)." Uboldi C., Bertoni A., Del Vecchio I., Comincini S., Hills D., Schlaepfer J., Dolf G., Williams J.L., Ferretti L. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[13]	"Comparative genomic organization of the human and bovine PRNP locus." Choi S.-H., Kim I.-C., Kim D.-S., Kim D.-W., Chae S.-H., Choi H.-H., Choi I., Yeo J.-S., Song M.-N., Park H.-S. Genomics 87:598-607(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[14]	"Frequencies of bovine PrP gene polymorphisms in Japanese-black and Holstein bulls in japan." Abe T., Hasebe H., Kobayashi E. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Holstein and Japanese black. Tissue: Semen.
[15]	"Detection of prion protein in various animal species by a new set of monoclonal antibodies." Barbieri I., Brocchi E., Borre A., Moretti M., Gelmetti D., Capucci L. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[16]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Hypothalamus.
[17]	"Characterization of bovine PrP promoter region." Tanaka M., Inoue S., Ikeda T., Horiuchi M., Ishiguro N., Shinagawa M. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
[18]	"Fibrils from brains of cows with new cattle disease contain scrapie-associated protein." Hope J., Reekie L.J.D., Hunter N., Multhaup G., Beyreuther K., White H., Scott A.C., Stack M.J., Dawson M., Wells G.A. Nature 336:390-392(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-36.
[19]	"NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein." Biverstahl H., Andersson A., Graslund A., Maler L. Biochemistry 43:14940-14947(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-30.
[20]	"NMR structure of the bovine prion protein." Lopez Garcia F., Zahn R., Riek R., Wuethrich K. Proc. Natl. Acad. Sci. U.S.A. 97:8334-8339(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 132-241.
[21]	"Directed evolution of an anti-prion protein scFv fragment to an affinity of 1 pM and its structural interpretation." Luginbuhl B., Kanyo Z., Jones R.M., Fletterick R.J., Prusiner S.B., Cohen F.E., Williamson R.A., Burton D.R., Pluckthun A. J. Mol. Biol. 363:75-97(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 107-115 IN COMPLEX WITH ANTIBODY FRAGMENT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X55882 Genomic DNA. Translation: CAA39368.1.
D10612 mRNA. Translation: BAA01467.1.
D10613 Genomic DNA. Translation: BAA01468.1.
D10614 Genomic DNA. Translation: BAA01469.1.
S55629 mRNA. Translation: AAB25514.1.
AB001468 mRNA. Translation: BAA19253.1.
AJ298878 Genomic DNA. Translation: CAC37367.1.
AF455119 Genomic DNA. Translation: AAM73856.1.
AF517842 mRNA. Translation: AAM66709.1.
AY335912 Genomic DNA. Translation: AAP84097.2.
AY367638 Genomic DNA. Translation: AAQ64645.1.
AY367639 Genomic DNA. Translation: AAQ64646.1.
AY367640 Genomic DNA. Translation: AAQ64647.1.
AY367641 Genomic DNA. Translation: AAQ64648.1.
AY367642 Genomic DNA. Translation: AAQ64649.1.
AY367643 Genomic DNA. Translation: AAQ64650.1.
AY720445 Genomic DNA. Translation: AAV30252.1.
AY720446 Genomic DNA. Translation: AAV30253.1.
AY720448 Genomic DNA. Translation: AAV30255.1.
AY720449 Genomic DNA. Translation: AAV30256.1.
AY720450 Genomic DNA. Translation: AAV30257.1.
AY720451 Genomic DNA. Translation: AAV30258.1.
AY720452 Genomic DNA. Translation: AAV30259.1.
AY720453 Genomic DNA. Translation: AAV30260.1.
AY720454 Genomic DNA. Translation: AAV30261.1.
AY720455 Genomic DNA. Translation: AAV30262.1.
AY720458 Genomic DNA. Translation: AAV30265.1.
AY720459 Genomic DNA. Translation: AAV30266.1.
AY720460 Genomic DNA. Translation: AAV30267.1.
AY720461 Genomic DNA. Translation: AAV30268.1.
AY720462 Genomic DNA. Translation: AAV30269.1.
AY720463 Genomic DNA. Translation: AAV30270.1.
AY720464 Genomic DNA. Translation: AAV30271.1.
AY720465 Genomic DNA. Translation: AAV30272.1.
AY720466 Genomic DNA. Translation: AAV30273.1.
AY720467 Genomic DNA. Translation: AAV30274.1.
AY720468 Genomic DNA. Translation: AAV30275.1.
AY720469 Genomic DNA. Translation: AAV30276.1.
AY720470 Genomic DNA. Translation: AAV30277.1.
AY720471 Genomic DNA. Translation: AAV30278.1.
AY720472 Genomic DNA. Translation: AAV30279.1.
AY720473 Genomic DNA. Translation: AAV30280.1.
AY720474 Genomic DNA. Translation: AAV30281.1.
AY720475 Genomic DNA. Translation: AAV30282.1.
AY720476 Genomic DNA. Translation: AAV30283.1.
AY720477 Genomic DNA. Translation: AAV30284.1.
AY720478 Genomic DNA. Translation: AAV30285.1.
AY720479 Genomic DNA. Translation: AAV30286.1.
AY720480 Genomic DNA. Translation: AAV30287.1.
AY720481 Genomic DNA. Translation: AAV30288.1.
AY720482 Genomic DNA. Translation: AAV30289.1.
AY720483 Genomic DNA. Translation: AAV30290.1.
AY720484 Genomic DNA. Translation: AAV30291.1.
AY720485 Genomic DNA. Translation: AAV30292.1.
AY720486 Genomic DNA. Translation: AAV30293.1.
AY720488 Genomic DNA. Translation: AAV30295.1.
AY720489 Genomic DNA. Translation: AAV30296.1.
AY720492 Genomic DNA. Translation: AAV30299.1.
AY720493 Genomic DNA. Translation: AAV30300.1.
AY720494 Genomic DNA. Translation: AAV30301.1.
AY720495 Genomic DNA. Translation: AAV30302.1.
AY720496 Genomic DNA. Translation: AAV30303.1.
AY720497 Genomic DNA. Translation: AAV30304.1.
AY720498 Genomic DNA. Translation: AAV30305.1.
AY720503 Genomic DNA. Translation: AAV30310.1.
AY720504 Genomic DNA. Translation: AAV30311.1.
AY720505 Genomic DNA. Translation: AAV30312.1.
AY720506 Genomic DNA. Translation: AAV30313.1.
AY720507 Genomic DNA. Translation: AAV30314.1.
AY720508 Genomic DNA. Translation: AAV30315.1.
AY720509 Genomic DNA. Translation: AAV30316.1.
AY720510 Genomic DNA. Translation: AAV30317.1.
AY720511 Genomic DNA. Translation: AAV30318.1.
AY720512 Genomic DNA. Translation: AAV30319.1.
AY720513 Genomic DNA. Translation: AAV30320.1.
AY720514 Genomic DNA. Translation: AAV30321.1.
AY720525 Genomic DNA. Translation: AAV30332.1.
AY720530 Genomic DNA. Translation: AAV30337.1.
AY720531 Genomic DNA. Translation: AAV30338.1.
AY720532 Genomic DNA. Translation: AAV30339.1.
AY720533 Genomic DNA. Translation: AAV30340.1.
AY720534 Genomic DNA. Translation: AAV30341.1.
AY720535 Genomic DNA. Translation: AAV30342.1.
AY720540 Genomic DNA. Translation: AAV30347.1.
AY720541 Genomic DNA. Translation: AAV30348.1.
AY720544 Genomic DNA. Translation: AAV30351.1.
AY720545 Genomic DNA. Translation: AAV30352.1.
AY720546 Genomic DNA. Translation: AAV30353.1.
AY720547 Genomic DNA. Translation: AAV30354.1.
AY720548 Genomic DNA. Translation: AAV30355.1.
AY720549 Genomic DNA. Translation: AAV30356.1.
AY720550 Genomic DNA. Translation: AAV30357.1.
AY720551 Genomic DNA. Translation: AAV30358.1.
AY720552 Genomic DNA. Translation: AAV30359.1.
AY720553 Genomic DNA. Translation: AAV30360.1.
AY720554 Genomic DNA. Translation: AAV30361.1.
AY720555 Genomic DNA. Translation: AAV30362.1.
AY720556 Genomic DNA. Translation: AAV30363.1.
AY720557 Genomic DNA. Translation: AAV30364.1.
AY720558 Genomic DNA. Translation: AAV30365.1.
AY720559 Genomic DNA. Translation: AAV30366.1.
AY720560 Genomic DNA. Translation: AAV30367.1.
AY720561 Genomic DNA. Translation: AAV30368.1.
AY720562 Genomic DNA. Translation: AAV30369.1.
AY720563 Genomic DNA. Translation: AAV30370.1.
AY720564 Genomic DNA. Translation: AAV30371.1.
AY720565 Genomic DNA. Translation: AAV30372.1.
AY720566 Genomic DNA. Translation: AAV30373.1.
AY720567 Genomic DNA. Translation: AAV30374.1.
AY720568 Genomic DNA. Translation: AAV30375.1.
AY720569 Genomic DNA. Translation: AAV30376.1.
AY720570 Genomic DNA. Translation: AAV30377.1.
AY720571 Genomic DNA. Translation: AAV30378.1.
AY720572 Genomic DNA. Translation: AAV30379.1.
AY720573 Genomic DNA. Translation: AAV30380.1.
AY720574 Genomic DNA. Translation: AAV30381.1.
AY720581 Genomic DNA. Translation: AAV30388.1.
AY720582 Genomic DNA. Translation: AAV30389.1.
AY720583 Genomic DNA. Translation: AAV30390.1.
AY720584 Genomic DNA. Translation: AAV30391.1.
AY720585 Genomic DNA. Translation: AAV30392.1.
AY720588 Genomic DNA. Translation: AAV30395.1.
AY720591 Genomic DNA. Translation: AAV30398.1.
AY720594 Genomic DNA. Translation: AAV30401.1.
AY720595 Genomic DNA. Translation: AAV30402.1.
AY720596 Genomic DNA. Translation: AAV30403.1.
AY720597 Genomic DNA. Translation: AAV30404.1.
AY720600 Genomic DNA. Translation: AAV30407.1.
AY720601 Genomic DNA. Translation: AAV30408.1.
AY720602 Genomic DNA. Translation: AAV30409.1.
AY720603 Genomic DNA. Translation: AAV30410.1.
AY720604 Genomic DNA. Translation: AAV30411.1.
AY720605 Genomic DNA. Translation: AAV30412.1.
AY720606 Genomic DNA. Translation: AAV30413.1.
AY720607 Genomic DNA. Translation: AAV30414.1.
AY720608 Genomic DNA. Translation: AAV30415.1.
AY720609 Genomic DNA. Translation: AAV30416.1.
AY720610 Genomic DNA. Translation: AAV30417.1.
AY720611 Genomic DNA. Translation: AAV30418.1.
AY720612 Genomic DNA. Translation: AAV30419.1.
AY720613 Genomic DNA. Translation: AAV30420.1.
AY720622 Genomic DNA. Translation: AAV30429.1.
AY720623 Genomic DNA. Translation: AAV30430.1.
AY720624 Genomic DNA. Translation: AAV30431.1.
AY720625 Genomic DNA. Translation: AAV30432.1.
AY720626 Genomic DNA. Translation: AAV30433.1.
AY720627 Genomic DNA. Translation: AAV30434.1.
AY720628 Genomic DNA. Translation: AAV30435.1.
AY720629 Genomic DNA. Translation: AAV30436.1.
AY720630 Genomic DNA. Translation: AAV30437.1.
AY720631 Genomic DNA. Translation: AAV30438.1.
AY720632 Genomic DNA. Translation: AAV30439.1.
AY720633 Genomic DNA. Translation: AAV30440.1.
AY720634 Genomic DNA. Translation: AAV30441.1.
AY720635 Genomic DNA. Translation: AAV30442.1.
AY720636 Genomic DNA. Translation: AAV30443.1.
AY720637 Genomic DNA. Translation: AAV30444.1.
AY720640 Genomic DNA. Translation: AAV30447.1.
AY720641 Genomic DNA. Translation: AAV30448.1.
AY720642 Genomic DNA. Translation: AAV30449.1.
AY720643 Genomic DNA. Translation: AAV30450.1.
AY720644 Genomic DNA. Translation: AAV30451.1.
AY720645 Genomic DNA. Translation: AAV30452.1.
AY720648 Genomic DNA. Translation: AAV30455.1.
AY720649 Genomic DNA. Translation: AAV30456.1.
AY720650 Genomic DNA. Translation: AAV30457.1.
AY720651 Genomic DNA. Translation: AAV30458.1.
AY720652 Genomic DNA. Translation: AAV30459.1.
AY720653 Genomic DNA. Translation: AAV30460.1.
AY720654 Genomic DNA. Translation: AAV30461.1.
AY720655 Genomic DNA. Translation: AAV30462.1.
AY720656 Genomic DNA. Translation: AAV30463.1.
AY720657 Genomic DNA. Translation: AAV30464.1.
AY720662 Genomic DNA. Translation: AAV30469.1.
AY720663 Genomic DNA. Translation: AAV30470.1.
AY720664 Genomic DNA. Translation: AAV30471.1.
AY720667 Genomic DNA. Translation: AAV30474.1.
AY720668 Genomic DNA. Translation: AAV30475.1.
AY720669 Genomic DNA. Translation: AAV30476.1.
AY720670 Genomic DNA. Translation: AAV30477.1.
AY720671 Genomic DNA. Translation: AAV30478.1.
AY720672 Genomic DNA. Translation: AAV30479.1.
AY720673 Genomic DNA. Translation: AAV30480.1.
AY720674 Genomic DNA. Translation: AAV30481.1.
AY720675 Genomic DNA. Translation: AAV30482.1.
AY720676 Genomic DNA. Translation: AAV30483.1.
AY720677 Genomic DNA. Translation: AAV30484.1.
AY720678 Genomic DNA. Translation: AAV30485.1.
DQ205538 Genomic DNA. Translation: ABB51165.1.
AY944236 Genomic DNA. Translation: AAY21624.1.
AB248079 Genomic DNA. Translation: BAE78586.1.
AB247937 Genomic DNA. Translation: BAE78583.1.
EF139165 Genomic DNA. Translation: ABL75501.1.
BC119821 mRNA. Translation: AAI19822.1.
D26151 Genomic DNA. Translation: BAA05138.1.

IPI

IPI00702852.

PIR

A54330.
JU0268.

RefSeq

NP_001258555.1. NM_001271626.1.
NP_851358.2. NM_181015.2.

UniGene

Bt.4737.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DWY	NMR	-	A	132-241	[»]
1DWZ	NMR	-	A	132-241	[»]
1DX0	NMR	-	A	25-241	[»]
1DX1	NMR	-	A	25-241	[»]
1SKH	NMR	-	A	1-30	[»]
2HH0	X-ray	2.85	P	107-115	[»]
2RSK	NMR	-	C/D	108-119	[»]

ProteinModelPortal

P10279.

SMR

P10279. Positions 1-30, 135-238.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1486044.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000040292; ENSBTAP00000043233; ENSBTAG00000027937.

GeneID

281427.

KEGG

bta:281427.

Organism-specific databases

CTD

5621.

Phylogenomic databases

eggNOG

NOG41716.

GeneTree

ENSGT00510000049083.

HOVERGEN

HBG008260.

InParanoid

P10279.

KO

K05634.

OMA

GYPHNPG.

OrthoDB

EOG4HDSW2.

Gene expression databases

ArrayExpress

P10279.

Family and domain databases

Gene3D

1.10.790.10. 1 hit.

InterPro

IPR001610. PAC.
IPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
[Graphical view]

PANTHER

PTHR11522. PTHR11522. 1 hit.

Pfam

PF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
[Graphical view]

PRINTS

PR00341. PRION.

SMART

SM00086. PAC. 1 hit.
SM00157. PRP. 1 hit.
[Graphical view]

SUPFAM

SSF54098. Prion. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P10279.

NextBio

20805416.

Entry information

Entry name

PRIO_BOVIN

Accession

Primary (citable) accession number: P10279
Secondary accession number(s): A1YVV9 , Q01880, Q0VD57, Q5UJJ5, Q5UJM6, Q5UK69, Q5UK71, Q6UL03, Q6UL04, Q6UL05, Q6UL06, Q7YRN3, Q8MJI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1991
Last modified:	April 3, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program