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UniProtKB - P23907 (PRIO_SHEEP)

Entry version 152 (16 Oct 2019)
Sequence version 1 (01 Nov 1991)
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Protein

Major prion protein

Gene

PRNP

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi64Copper or zinc 1By similarity1
Metal bindingi65Copper or zinc 1; via amide nitrogenBy similarity1
Metal bindingi66Copper or zinc 1; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi72Copper or zinc 2By similarity1
Metal bindingi73Copper or zinc 2; via amide nitrogenBy similarity1
Metal bindingi74Copper or zinc 2; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi80Copper or zinc 3By similarity1
Metal bindingi81Copper or zinc 3; via amide nitrogenBy similarity1
Metal bindingi82Copper or zinc 3; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi88Copper or zinc 4By similarity1
Metal bindingi90Copper or zinc 4; via amide nitrogenBy similarity1
Metal bindingi91Copper or zinc 4; via amide nitrogen and carbonyl oxygenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionPrion
LigandCopper, Metal-binding, Zinc

Protein family/group databases

Transport Classification Database

More...TCDBi		1.C.48.1.1 the prion peptide (prp) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Major prion protein
Short name:
PrP
Alternative name(s):
CD_antigen: CD230
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PRNP
Synonyms:PRP, SIP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiOvis aries (Sheep)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9940 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002356 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Cell membrane, Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Polymorphism at position 171 may be related to the alleles of scrapie incubation-control (SIC) gene in this species.1 Publication
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.Curated
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.3 Publications

Keywords - Diseasei

Disease mutation

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2406893

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Add BLAST24
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002572725 – 233Major prion proteinAdd BLAST209
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000025728234 – 256Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi182 ↔ 217
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi184N-linked (GlcNAc...) asparagineCurated1
Glycosylationi200N-linked (GlcNAc...) asparagineCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi233GPI-anchor amidated alanineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P23907 baseline

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-60917N

Protein interaction database and analysis system

More...IntActi		P23907, 1 interactor

Molecular INTeraction database

More...MINTi		P23907

STRING: functional protein association networks

More...STRINGi		9940.ENSOARP00000004991

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P23907

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1256
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P23907

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P23907

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati54 – 6219
Repeati63 – 7028
Repeati71 – 7838
Repeati79 – 8648
Repeati87 – 9559

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni25 – 233Interaction with GRB2, ERI3 and SYN1By similarityAdd BLAST209
Regioni54 – 955 X 8 AA tandem repeats of P-H-G-G-G-W-G-QAdd BLAST42

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the prion family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00510000049083

KEGG Orthology (KO)

More...KOi		K05634

Identification of Orthologs from Complete Genome Data

More...OMAi		DVGLCKK

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.790.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000817 Prion
IPR036924 Prion/Doppel_b-ribbon_dom_sf
IPR022416 Prion/Doppel_prot_b-ribbon_dom
IPR025860 Prion_N_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00377 Prion, 1 hit
PF11587 Prion_bPrPp, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00341 PRION

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00157 PRP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54098 SSF54098, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00291 PRION_1, 1 hit
PS00706 PRION_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7FFBEA6C6FDBF8BB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti112M → T1 Publication1
Natural varianti136A → V in scrapie; short incubation; sA allele. 3 Publications1
Natural varianti137M → T1 Publication1
Natural varianti141L → F3 Publications1
Natural varianti154R → H3 Publications1
Natural varianti171R → H in scrapie; low incidence. 1 Publication1
Natural varianti171R → Q Linked to susceptibility to scrapie. 9 Publications1
Natural varianti211R → Q2 Publications1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

NCBI Reference Sequences

More...RefSeqi		NP_001009481.1, NM_001009481.1
XP_012043480.1, XM_012188090.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSOART00000005076; ENSOARP00000004991; ENSOARG00000004668

Database of genes from NCBI RefSeq genomes

More...GeneIDi		493887

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		oas:493887

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
2N53NMR-A103-234[»]
2RMVNMR-A145-169[»]
2RMWNMR-A145-169[»]
SMRiP23907
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-60917N
IntActiP23907, 1 interactor
MINTiP23907
STRINGi9940.ENSOARP00000004991

Chemistry databases

BindingDBiP23907
ChEMBLiCHEMBL2406893

Protein family/group databases

TCDBi1.C.48.1.1 the prion peptide (prp) family

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P23907

Genome annotation databases

EnsembliENSOART00000005076; ENSOARP00000004991; ENSOARG00000004668
GeneIDi493887
KEGGioas:493887

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5621

Phylogenomic databases

GeneTreeiENSGT00510000049083
KOiK05634
OMAiDVGLCKK

Miscellaneous databases

EvolutionaryTraceiP23907

Protein Ontology

More...PROi		PR:P23907

Gene expression databases

ExpressionAtlasiP23907 baseline

Family and domain databases

Gene3Di1.10.790.10, 1 hit
InterProiView protein in InterPro
IPR000817 Prion
IPR036924 Prion/Doppel_b-ribbon_dom_sf
IPR022416 Prion/Doppel_prot_b-ribbon_dom
IPR025860 Prion_N_dom
PfamiView protein in Pfam
PF00377 Prion, 1 hit
PF11587 Prion_bPrPp, 1 hit
PRINTSiPR00341 PRION
SMARTiView protein in SMART
SM00157 PRP, 1 hit
SUPFAMiSSF54098 SSF54098, 1 hit
PROSITEiView protein in PROSITE
PS00291 PRION_1, 1 hit
PS00706 PRION_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPRIO_SHEEP
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P23907
Secondary accession number(s): Q5ECG0
, Q6V638, Q6V654, Q712W2, Q712W3, Q7JGT4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 16, 2019
This is version 152 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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