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P10279 (PRIO_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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-anchorGPI-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 componentAmyloid
Cell membrane
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   LigandCopper
Metal-binding
Zinc
   Molecular functionPrion
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of T cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcineurin-NFAT signaling cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-17 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-2 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

anchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 21920025. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-7430632,EBI-7430632
PRNPP041565EBI-7430632,EBI-977302From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.18
Chain25 – 241217Major prion protein
PRO_0000025627
Propeptide242 – 26423Removed in mature form Potential
PRO_0000025628

Regions

Repeat54 – 6291
Repeat63 – 7082
Repeat71 – 7883
Repeat79 – 8684
Repeat87 – 9485
Repeat95 – 10396
Region25 – 241217Interaction with GRB2, ERI3 and SYN1 By similarity
Region54 – 103506 X 8 AA tandem repeats of P-H-G-G-G-W-G-Q

Sites

Metal binding721Copper or zinc 1 By similarity
Metal binding731Copper or zinc 1; via amide nitrogen By similarity
Metal binding741Copper or zinc 1; via amide nitrogen and carbonyl oxygen By similarity
Metal binding801Copper or zinc 2 By similarity
Metal binding811Copper or zinc 2; via amide nitrogen By similarity
Metal binding821Copper or zinc 2; via amide nitrogen and carbonyl oxygen By similarity
Metal binding881Copper or zinc 3 By similarity
Metal binding891Copper or zinc 3; via amide nitrogen By similarity
Metal binding901Copper or zinc 3; via amide nitrogen and carbonyl oxygen By similarity
Metal binding961Copper or zinc 4 By similarity
Metal binding971Copper or zinc 4; via amide nitrogen By similarity
Metal binding981Copper or zinc 4; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Lipidation2411GPI-anchor amidated alanine Potential
Glycosylation1921N-linked (GlcNAc...) Probable
Glycosylation2081N-linked (GlcNAc...) Probable
Disulfide bond190 ↔ 225

Natural variations

Natural variant601W → R. Ref.10
Natural variant71 – 788Missing in allele 2.
Natural variant84 – 9916Missing.
Natural variant92 – 998Missing.
Natural variant941Q → R. Ref.10
Natural variant981G → GGWGQPHGG.
Natural variant1541S → N. Ref.2 Ref.10
Natural variant2111E → K. Ref.9
Natural variant2341Q → R. Ref.10

Experimental info

Sequence conflict106 – 1083THG → SHS in BAA01469. Ref.2
Sequence conflict2181E → K in BAA01467. Ref.2
Sequence conflict2181E → K in BAA19253. Ref.4

Secondary structure

...................... 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10279 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: D6D214038316A231

FASTA26428,614
        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 

« Hide

References

« Hide '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.
PIRA54330.
JU0268.
RefSeqNP_001258555.1. NM_001271626.1.
NP_851358.2. NM_181015.2.
UniGeneBt.4737.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DWYNMR-A132-241[»]
1DWZNMR-A132-241[»]
1DX0NMR-A25-241[»]
1DX1NMR-A25-241[»]
1SKHNMR-A1-30[»]
2HH0X-ray2.85P107-115[»]
2RSKNMR-C/D108-119[»]
ProteinModelPortalP10279.
SMRP10279. Positions 1-30, 135-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid158758. 3 interactions.
IntActP10279. 1 interaction.
MINTMINT-1486044.

Proteomic databases

PRIDEP10279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000040292; ENSBTAP00000043233; ENSBTAG00000027937.
GeneID281427.
KEGGbta:281427.

Organism-specific databases

CTD5621.

Phylogenomic databases

eggNOGNOG41716.
GeneTreeENSGT00510000049083.
HOVERGENHBG008260.
InParanoidP10279.
KOK05634.
OMAGYPHNPG.
OrthoDBEOG7DRJ4Q.
TreeFamTF105188.

Family and domain databases

Gene3D1.10.790.10. 1 hit.
InterProIPR001610. PAC.
IPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
[Graphical view]
PANTHERPTHR11522. PTHR11522. 1 hit.
PfamPF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
[Graphical view]
PRINTSPR00341. PRION.
SMARTSM00086. PAC. 1 hit.
SM00157. PRP. 1 hit.
[Graphical view]
SUPFAMSSF54098. SSF54098. 1 hit.
PROSITEPS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10279.
NextBio20805416.

Entry information

Entry namePRIO_BOVIN
AccessionPrimary (citable) accession number: P10279
Secondary accession number(s): A1YVV9 expand/collapse secondary AC list , 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 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references