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Protein

Major prion protein homolog

Gene

PRNP

Organism
Gallus gallus (Chicken)
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)DescriptionActionsGraphical viewLength
Metal bindingi66Copper or zinc 1By similarity1
Metal bindingi72Copper or zinc 2By similarity1
Metal bindingi78Copper or zinc 3By similarity1
Metal bindingi90Copper or zinc 4By similarity1
Metal bindingi93Copper or zinc 4; via amide nitrogen and carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionPrion
LigandCopper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Major prion protein homolog
Alternative name(s):
65-21 protein
Acetylcholine receptor-inducing activity
Short name:
ARIA
PR-LP
Gene namesi
Name:PRNP
Synonyms:PRN-P
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 22

Subcellular locationi

GO - Cellular componenti

  • amyloid-beta complex Source: Ensembl
  • anchored component of membrane Source: UniProtKB-KW
  • basal lamina Source: AgBase
  • cell Source: AgBase
  • cell surface Source: Ensembl
  • cytosol Source: Ensembl
  • dendrite Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • extracellular exosome Source: Ensembl
  • Golgi apparatus Source: Ensembl
  • inclusion body Source: Ensembl
  • membrane raft Source: Ensembl
  • nuclear membrane Source: Ensembl
  • plasma membrane Source: UniProtKB-SubCell
  • synaptic cleft Source: AgBase

Keywords - Cellular componenti

Amyloid, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000002574125 – 248Major prion protein homologAdd BLAST224
PropeptideiPRO_0000025742249 – 273Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi192 ↔ 237
Glycosylationi194N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi209N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi218N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi248GPI-anchor amidated serineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP27177.

Expressioni

Tissue specificityi

Spinal cord and brain.

Gene expression databases

BgeeiENSGALG00000000209.

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.By similarity

GO - Molecular functioni

  • glycoprotein binding Source: AgBase
  • identical protein binding Source: Ensembl
  • microtubule binding Source: Ensembl
  • protease binding Source: Ensembl
  • type 5 metabotropic glutamate receptor binding Source: Ensembl

Protein-protein interaction databases

STRINGi9031.ENSGALP00000040285.

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi134 – 136Combined sources3
Helixi157 – 167Combined sources11
Helixi185 – 200Combined sources16
Helixi219 – 246Combined sources28

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U3MNMR-A134-248[»]
ProteinModelPortaliP27177.
SMRiP27177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27177.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati42 – 4716
Repeati48 – 5326
Repeati54 – 5936
Repeati60 – 6546
Repeati66 – 7156
Repeati72 – 7766
Repeati78 – 8376
Repeati84 – 8986

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 898 X 6 AA tandem repeats of [HR]-[NQ]-P-G-Y-PAdd BLAST48

Sequence similaritiesi

Belongs to the prion family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IJMM. Eukaryota.
ENOG410YXUU. LUCA.
GeneTreeiENSGT00510000049083.
HOGENOMiHOG000232077.
HOVERGENiHBG008260.
InParanoidiP27177.
KOiK05634.
OMAiGYPHNPG.
OrthoDBiEOG091G0HMV.
PhylomeDBiP27177.
TreeFamiTF105188.

Family and domain databases

Gene3Di1.10.790.10. 1 hit.
InterProiView protein in InterPro
IPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
PANTHERiPTHR10502:SF163. PTHR10502:SF163. 1 hit.
PfamiView protein in Pfam
PF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
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.

Sequencei

Sequence statusi: Complete.

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

P27177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLLTTCCL LALLLAACTD VALSKKGKGK PSGGGWGAGS HRQPSYPRQP
60 70 80 90 100
GYPHNPGYPH NPGYPHNPGY PHNPGYPHNP GYPQNPGYPH NPGYPGWGQG
110 120 130 140 150
YNPSSGGSYH NQKPWKPPKT NFKHVAGAAA AGAVVGGLGG YAMGRVMSGM
160 170 180 190 200
NYHFDSPDEY RWWSENSARY PNRVYYRDYS SPVPQDVFVA DCFNITVTEY
210 220 230 240 250
SIGPAAKKNT SEAVAAANQT EVEMENKVVT KVIREMCVQQ YREYRLASGI
260 270
QLHPADTWLA VLLLLLTTLF AMH
Length:273
Mass (Da):29,909
Last modified:July 1, 1993 - v2
Checksum:i32D700918E787DD2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78 – 83Missing AA sequence (PubMed:1715573).Curated6
Sequence conflicti156S → R in AAA49041 (PubMed:1715573).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95404 Genomic DNA. Translation: AAC28970.1.
M61145 mRNA. Translation: AAA49041.1.
PIRiA37372.
A41280. UJCH.
A46280.
RefSeqiNP_990796.2. NM_205465.2.
XP_015152786.1. XM_015297300.1.
UniGeneiGga.3867.

Genome annotation databases

EnsembliENSGALT00000000277; ENSGALP00000040285; ENSGALG00000000209.
GeneIDi396452.
KEGGigga:396452.

Similar proteinsi

Entry informationi

Entry nameiPRIO_CHICK
AccessioniPrimary (citable) accession number: P27177
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 1, 1993
Last modified: August 30, 2017
This is version 140 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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