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Protein

Major prion protein

Gene

PRNP

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. 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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Copper or zinc 1By similarity
Metal bindingi65 – 651Copper or zinc 1; via amide nitrogenBy similarity
Metal bindingi66 – 661Copper or zinc 1; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi72 – 721Copper or zinc 2By similarity
Metal bindingi73 – 731Copper or zinc 2; via amide nitrogenBy similarity
Metal bindingi74 – 741Copper or zinc 2; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi80 – 801Copper or zinc 3By similarity
Metal bindingi81 – 811Copper or zinc 3; via amide nitrogenBy similarity
Metal bindingi82 – 821Copper or zinc 3; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi88 – 881Copper or zinc 4By similarity
Metal bindingi90 – 901Copper or zinc 4; via amide nitrogenBy similarity
Metal bindingi91 – 911Copper or zinc 4; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Prion

Keywords - Ligandi

Copper, Metal-binding, Zinc

Protein family/group databases

TCDBi1.C.48.1.1. the prion peptide fragment (prp-f) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Major prion protein
Short name:
PrP
Alternative name(s):
CD_antigen: CD230
Gene namesi
Name:PRNP
Synonyms:PRP, SIP
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Chromosome 13

Subcellular locationi

  • Cell membrane By similarity; 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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Polymorphism at position 171 may be related to the alleles of scrapie incubation-control (SIC) gene in this species.

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.

Scrapie is a transmissible neurodegenerative disorder of sheep and goats. Most sheep that contract the disease naturally die between 24 and 50 months of age. The incubation period in sheep depends on the strain(s) of the infecting pathogen, sheep age at exposure, and the sheep genotype. The survival time is mainly determined by a single genetic locus, SIP, which has two alleles, susceptible (sa) and resistant (pa). Short incubation period is conferred by the partially dominant sa allele. Scrapie can be spread between flockmates, or it can be transmitted from an infected ewe to its lamb.

Keywords - Diseasei

Disease mutation

Chemistry

ChEMBLiCHEMBL2406893.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 233209Major prion proteinPRO_0000025727Add
BLAST
Propeptidei234 – 25623Removed in mature formSequence analysisPRO_0000025728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi182 ↔ 217
Glycosylationi184 – 1841N-linked (GlcNAc...)Curated
Glycosylationi200 – 2001N-linked (GlcNAc...)Curated
Lipidationi233 – 2331GPI-anchor amidated alanineSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Gene expression databases

ExpressionAtlasiP23907. baseline.

Interactioni

Subunit structurei

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. Interacts with KIAA1191.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PRNPP041563EBI-7670302,EBI-977302From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-60917N.
IntActiP23907. 1 interaction.
MINTiMINT-8302691.

Chemistry

BindingDBiP23907.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi128 – 1303Combined sources
Beta strandi131 – 1333Combined sources
Turni144 – 1463Combined sources
Helixi147 – 1559Combined sources
Helixi157 – 1593Combined sources
Beta strandi165 – 1673Combined sources
Helixi169 – 1713Combined sources
Beta strandi173 – 1753Combined sources
Helixi176 – 19621Combined sources
Helixi203 – 22927Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G04NMR-A145-169[»]
1M25NMR-A145-169[»]
1S4TNMR-A138-158[»]
1TPXX-ray2.56A114-234[»]
1TQBX-ray2.55A127-228[»]
1TQCX-ray2.80A127-228[»]
1UW3X-ray2.04A128-233[»]
1XYUNMR-A124-234[»]
1Y2SNMR-A124-234[»]
2KTMNMR-A172-234[»]
2MV8NMR-A103-234[»]
2MV9NMR-A103-234[»]
2RMVNMR-A145-169[»]
2RMWNMR-A145-169[»]
ProteinModelPortaliP23907.
SMRiP23907. Positions 1-30, 127-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23907.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati54 – 6291
Repeati63 – 7082
Repeati71 – 7883
Repeati79 – 8684
Repeati87 – 9595

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 233209Interaction with GRB2, ERI3 and SYN1By similarityAdd
BLAST
Regioni54 – 95425 X 8 AA tandem repeats of P-H-G-G-G-W-G-QAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the prion family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG008260.
KOiK05634.
OMAiHNPGYPH.

Family and domain databases

Gene3Di1.10.790.10. 1 hit.
InterProiIPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
[Graphical view]
PfamiPF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
[Graphical view]
PRINTSiPR00341. PRION.
SMARTiSM00157. PRP. 1 hit.
[Graphical view]
SUPFAMiSSF54098. SSF54098. 1 hit.
PROSITEiPS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23907-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN
60 70 80 90 100
RYPPQGGGGW GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GGWGQGGSHS
110 120 130 140 150
QWNKPSKPKT NMKHVAGAAA AGAVVGGLGG YMLGSAMSRP LIHFGNDYED
160 170 180 190 200
RYYRENMYRY PNQVYYRPVD RYSNQNNFVH DCVNITVKQH TVTTTTKGEN
210 220 230 240 250
FTETDIKIME RVVEQMCITQ YQRESQAYYQ RGASVILFSS PPVILLISFL

IFLIVG
Length:256
Mass (Da):27,915
Last modified:November 1, 1991 - v1
Checksum:i7FFBEA6C6FDBF8BB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121M → T.1 Publication
Natural varianti136 – 1361A → V in scrapie; short incubation; sA allele. 3 Publications
Natural varianti137 – 1371M → T.1 Publication
Natural varianti141 – 1411L → F.3 Publications
Natural varianti154 – 1541R → H.3 Publications
Natural varianti171 – 1711R → H in scrapie; low incidence. 1 Publication
Natural varianti171 – 1711R → Q Linked to susceptibility to scrapie. 9 Publications
Natural varianti211 – 2111R → Q.2 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31313 Genomic DNA. Translation: AAB97765.1.
X79912 Genomic DNA. Translation: CAA56283.1.
U67922 Genomic DNA. Translation: AAC78726.1.
AJ223072 Genomic DNA. Translation: CAA11073.1.
AY350241 Genomic DNA. Translation: AAR14214.1.
AY350242 Genomic DNA. Translation: AAR14215.1.
AY350243 Genomic DNA. Translation: AAR14216.1.
AY350245 Genomic DNA. Translation: AAR14218.1.
AY350246 Genomic DNA. Translation: AAR14219.1.
AY350248 Genomic DNA. Translation: AAR14221.1.
AY350249 Genomic DNA. Translation: AAR14222.1.
AY350250 Genomic DNA. Translation: AAR14223.1.
AY350254 Genomic DNA. Translation: AAR14227.1.
AY350256 Genomic DNA. Translation: AAR14229.1.
AY350257 Genomic DNA. Translation: AAR14230.1.
AY350261 Genomic DNA. Translation: AAR14234.1.
AY350264 Genomic DNA. Translation: AAR14237.1.
AY350267 Genomic DNA. Translation: AAR14240.1.
AY350268 Genomic DNA. Translation: AAR14241.1.
AY350271 Genomic DNA. Translation: AAR14244.1.
AY350272 Genomic DNA. Translation: AAR14245.1.
AY350273 Genomic DNA. Translation: AAR14246.1.
AY350275 Genomic DNA. Translation: AAR14248.1.
AJ567984 Genomic DNA. Translation: CAE00186.1.
AJ567985 Genomic DNA. Translation: CAE00187.1.
AJ567986 Genomic DNA. Translation: CAE00188.2.
D38179 Genomic DNA. Translation: BAA07376.1.
AJ000680 Genomic DNA. Translation: CAA04235.1.
AJ000681 Genomic DNA. Translation: CAA04236.1.
AJ000736 Genomic DNA. Translation: CAA04274.1.
AJ000739 Genomic DNA. Translation: CAA04277.1.
AY907689 Genomic DNA. Translation: AAW88336.1.
AY907690 Genomic DNA. Translation: AAW88337.1.
AY907691 Genomic DNA. Translation: AAW88338.1.
RefSeqiNP_001009481.1. NM_001009481.1.
XP_012043480.1. XM_012188090.2.
UniGeneiOar.765.

Genome annotation databases

EnsembliENSOART00000005076; ENSOARP00000004991; ENSOARG00000004668.
GeneIDi493887.
KEGGioas:493887.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31313 Genomic DNA. Translation: AAB97765.1.
X79912 Genomic DNA. Translation: CAA56283.1.
U67922 Genomic DNA. Translation: AAC78726.1.
AJ223072 Genomic DNA. Translation: CAA11073.1.
AY350241 Genomic DNA. Translation: AAR14214.1.
AY350242 Genomic DNA. Translation: AAR14215.1.
AY350243 Genomic DNA. Translation: AAR14216.1.
AY350245 Genomic DNA. Translation: AAR14218.1.
AY350246 Genomic DNA. Translation: AAR14219.1.
AY350248 Genomic DNA. Translation: AAR14221.1.
AY350249 Genomic DNA. Translation: AAR14222.1.
AY350250 Genomic DNA. Translation: AAR14223.1.
AY350254 Genomic DNA. Translation: AAR14227.1.
AY350256 Genomic DNA. Translation: AAR14229.1.
AY350257 Genomic DNA. Translation: AAR14230.1.
AY350261 Genomic DNA. Translation: AAR14234.1.
AY350264 Genomic DNA. Translation: AAR14237.1.
AY350267 Genomic DNA. Translation: AAR14240.1.
AY350268 Genomic DNA. Translation: AAR14241.1.
AY350271 Genomic DNA. Translation: AAR14244.1.
AY350272 Genomic DNA. Translation: AAR14245.1.
AY350273 Genomic DNA. Translation: AAR14246.1.
AY350275 Genomic DNA. Translation: AAR14248.1.
AJ567984 Genomic DNA. Translation: CAE00186.1.
AJ567985 Genomic DNA. Translation: CAE00187.1.
AJ567986 Genomic DNA. Translation: CAE00188.2.
D38179 Genomic DNA. Translation: BAA07376.1.
AJ000680 Genomic DNA. Translation: CAA04235.1.
AJ000681 Genomic DNA. Translation: CAA04236.1.
AJ000736 Genomic DNA. Translation: CAA04274.1.
AJ000739 Genomic DNA. Translation: CAA04277.1.
AY907689 Genomic DNA. Translation: AAW88336.1.
AY907690 Genomic DNA. Translation: AAW88337.1.
AY907691 Genomic DNA. Translation: AAW88338.1.
RefSeqiNP_001009481.1. NM_001009481.1.
XP_012043480.1. XM_012188090.2.
UniGeneiOar.765.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G04NMR-A145-169[»]
1M25NMR-A145-169[»]
1S4TNMR-A138-158[»]
1TPXX-ray2.56A114-234[»]
1TQBX-ray2.55A127-228[»]
1TQCX-ray2.80A127-228[»]
1UW3X-ray2.04A128-233[»]
1XYUNMR-A124-234[»]
1Y2SNMR-A124-234[»]
2KTMNMR-A172-234[»]
2MV8NMR-A103-234[»]
2MV9NMR-A103-234[»]
2RMVNMR-A145-169[»]
2RMWNMR-A145-169[»]
ProteinModelPortaliP23907.
SMRiP23907. Positions 1-30, 127-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60917N.
IntActiP23907. 1 interaction.
MINTiMINT-8302691.

Chemistry

BindingDBiP23907.
ChEMBLiCHEMBL2406893.

Protein family/group databases

TCDBi1.C.48.1.1. the prion peptide fragment (prp-f) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOART00000005076; ENSOARP00000004991; ENSOARG00000004668.
GeneIDi493887.
KEGGioas:493887.

Organism-specific databases

CTDi5621.

Phylogenomic databases

HOVERGENiHBG008260.
KOiK05634.
OMAiHNPGYPH.

Miscellaneous databases

EvolutionaryTraceiP23907.
PROiP23907.

Gene expression databases

ExpressionAtlasiP23907. baseline.

Family and domain databases

Gene3Di1.10.790.10. 1 hit.
InterProiIPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
[Graphical view]
PfamiPF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
[Graphical view]
PRINTSiPR00341. PRION.
SMARTiSM00157. PRP. 1 hit.
[Graphical view]
SUPFAMiSSF54098. SSF54098. 1 hit.
PROSITEiPS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-171.
    Strain: Suffolk.
    Tissue: Spleen.
  2. "Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie."
    Westaway D., Zuliani V., Cooper C.M., da Costa M., Neuman S., Jenny A.L., Detwiler L., Prusiner S.B.
    Genes Dev. 8:959-969(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-171.
    Strain: Suffolk.
    Tissue: Brain.
  3. "Complete genomic sequence and analysis of the prion protein gene region from three mammalian species."
    Lee I.Y., Westaway D., Smit A.F.A., Wang K., Seto J., Chen L., Acharya C., Ankener M., Baskin D., Cooper C., Yao H., Prusiner S.B., Hood L.E.
    Genome Res. 8:1022-1037(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-171.
    Tissue: Brain.
  4. "PrP (prion) gene expression in sheep may be modulated by alternative polyadenylation of its messenger RNA."
    Goldmann W., O'Neill G., Cheung F., Charleson F., Ford P., Hunter N.
    J. Gen. Virol. 80:2275-2283(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-171.
  5. "Identification of a novel ovine PrP polymorphism and scrapie-resistant genotypes for St. Croix White and a related composite breed."
    Seabury C.M., Derr J.N.
    Cytogenet. Genome Res. 102:85-88(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-171.
  6. "Prion protein gene polymorphisms in healthy and scrapie affected sheep in Greece."
    Billinis C., Psychas V., Leontides L., Spyrou V., Argyroudis S., Vlemmas I., Leontides S., Sklaviadis T., Papadopoulos O.
    J. Gen. Virol. 85:547-554(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-141 AND GLN-171.
  7. Inoue S., Watanabe A., Horiuchi M., Ishiguro N., Shinagawa M.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  8. "PrP allelic variants associated with natural scrapie."
    Bossers A.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-141; GLN-171 AND GLN-211.
  9. "A set of genotyping controls for 15 haplotype combinations of ovine PRNP codons 136, 154, and 171."
    Heaton M.P., Leymaster K.A., Clawson M.L., Laegreid W.W.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-171.
  10. "The epididymal soluble prion protein forms a high-molecular-mass complex in association with hydrophobic proteins."
    Ecroyd H., Belghazi M., Dacheux J.-L., Gatti J.-L.
    Biochem. J. 392:211-219(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH CES5A; CLU; BPI; MANBA AND GLB1.
    Tissue: Epididymis.
  11. "The crystal structure of the globular domain of sheep prion protein."
    Haire L.F., Whyte S.M., Vasisht N., Gill A.C., Verma C., Dodson E.J., Dodson G.G., Bayley P.M.
    J. Mol. Biol. 336:1175-1183(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 128-233.
  12. "Insight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants."
    Eghiaian F., Grosclaude J., Lesceu S., Debey P., Doublet B., Treguer E., Rezaei H., Knossow M.
    Proc. Natl. Acad. Sci. U.S.A. 101:10254-10259(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 115-234 IN COMPLEX WITH ANTIBODY.
  13. Cited for: STRUCTURE BY NMR OF 124-234.
  14. "Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3."
    Adrover M., Pauwels K., Prigent S., de Chiara C., Xu Z., Chapuis C., Pastore A., Rezaei H.
    J. Biol. Chem. 285:21004-21012(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 167-234, SUBUNIT, DOMAIN.
  15. "Different scrapie-associated fibril proteins (PrP) are encoded by lines of sheep selected for different alleles of the Sip gene."
    Goldmann W., Hunter N., Benson G., Foster J.D., Hope J.
    J. Gen. Virol. 72:2411-2417(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCRAPIE VAL-136; HIS-154 AND GLN-171, POLYMORPHISM.
  16. "PrP polymorphisms associated with natural scrapie discovered by denaturing gradient gel electrophoresis."
    Laplanche J.-L., Chatelain J., Westaway D., Thomas S., Dussaucy M., Brugere-Picoux J., Launay J.-M.
    Genomics 15:30-37(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCRAPIE THR-112; VAL-136 AND HIS-154.
  17. "Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie."
    Belt P.B.G.M., Muileman I.H., Schreuder B.E.C., Bos-De Ruijter J., Gielkens A.L.J., Smits M.A.
    J. Gen. Virol. 76:509-517(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCRAPIE VAL-136 AND HIS-171, VARIANT HIS-154.
  18. "PrP genotype contributes to determining survival times of sheep with natural scrapie."
    Bossers A., Schreuder B.E.C., Muileman I.H., Belt P.B.G.M., Smits M.A.
    J. Gen. Virol. 77:2669-2673(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-137; PHE-141 AND GLN-211.

Entry informationi

Entry nameiPRIO_SHEEP
AccessioniPrimary (citable) accession number: P23907
Secondary accession number(s): Q5ECG0
, Q6V638, Q6V654, Q712W2, Q712W3, Q7JGT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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 F7VJQ3) 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.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.