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P27177 (PRIO_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Major prion protein homolog
Alternative name(s):
65-21 protein
Acetylcholine receptor-inducing activity
Short name=ARIA
PR-LP
Gene names
Name:PRNP
Synonyms:PRN-P
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates the synthesis of acetylcholine receptors in cultured chicken myotubes. May serve normally to regulate the chemoreceptor number at the neuromuscular junction and perhaps in the central nervous system as well.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Tissue specificity

Spinal cord and brain.

Sequence similarities

Belongs to the prion family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.2
Chain25 – 248224Major prion protein homolog
PRO_0000025741
Propeptide249 – 27325Removed in mature form Potential
PRO_0000025742

Regions

Repeat42 – 4761
Repeat48 – 5362
Repeat54 – 5963
Repeat60 – 6564
Repeat66 – 7165
Repeat72 – 7766
Repeat78 – 8367
Repeat84 – 8968
Region42 – 89488 X 6 AA tandem repeats of [HR]-[NQ]-P-G-Y-P

Amino acid modifications

Lipidation2481GPI-anchor amidated serine Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Disulfide bond192 ↔ 237

Experimental info

Sequence conflict78 – 836Missing AA sequence Ref.2
Sequence conflict1561S → R in AAA49041. Ref.2

Secondary structure

......... 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27177 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 32D700918E787DD2

FASTA27329,909
        10         20         30         40         50         60 
MARLLTTCCL LALLLAACTD VALSKKGKGK PSGGGWGAGS HRQPSYPRQP GYPHNPGYPH 

        70         80         90        100        110        120 
NPGYPHNPGY PHNPGYPHNP GYPQNPGYPH NPGYPGWGQG YNPSSGGSYH NQKPWKPPKT 

       130        140        150        160        170        180 
NFKHVAGAAA AGAVVGGLGG YAMGRVMSGM NYHFDSPDEY RWWSENSARY PNRVYYRDYS 

       190        200        210        220        230        240 
SPVPQDVFVA DCFNITVTEY SIGPAAKKNT SEAVAAANQT EVEMENKVVT KVIREMCVQQ 

       250        260        270 
YREYRLASGI QLHPADTWLA VLLLLLTTLF AMH 

« Hide

References

[1]"Molecular cloning of a candidate chicken prion protein."
Gabriel J.M., Oesch B., Kretzschmar H., Scott M., Prusiner S.B.
Proc. Natl. Acad. Sci. U.S.A. 89:9097-9101(1992) [PubMed: 1409608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity."
Harris D.A., Falls D.L., Johnson F.A., Fischbach G.D.
Proc. Natl. Acad. Sci. U.S.A. 88:7664-7668(1991) [PubMed: 1715573] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-51.
Tissue: Brain.
[3]"Mr 42,000 ARIA: a protein that may regulate the accumulation of acetylcholine receptors at developing chick neuromuscular junctions."
Falls D.L., Harris D.A., Johnson F.A., Morgan M.M., Corfas G., Fischbach G.D.
Cold Spring Harb. Symp. Quant. Biol. 55:397-406(1990) [PubMed: 2132829] [Abstract]
Cited for: REVIEW.
[4]"Prion protein NMR structures of chickens, turtles, and frogs."
Calzolai L., Lysek D.A., Perez D.R., Guentert P., Wuethrich K.
Proc. Natl. Acad. Sci. U.S.A. 102:651-655(2005) [PubMed: 15647366] [Abstract]
Cited for: STRUCTURE BY NMR OF 134-248.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95404 Genomic DNA. Translation: AAC28970.1.
M61145 mRNA. Translation: AAA49041.1.
IPIIPI00597864.
PIRA37372.
UJCH. A41280.
A46280.
RefSeqNP_990796.1. NM_205465.1.
UniGeneGga.3867.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U3MNMR-A134-248[»]
ProteinModelPortalP27177.
SMRP27177. Positions 132-248.
ModBaseSearch...

Protein-protein interaction databases

STRINGP27177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000000277; ENSGALP00000040285; ENSGALG00000000209.
GeneID396452.
KEGGgga:396452.

Organism-specific databases

CTD5621.

Phylogenomic databases

eggNOGveNOG19845.
HOGENOMHBG278973.
HOVERGENHBG008260.
InParanoidP27177.
OMAPNQVYYR.
OrthoDBEOG4HDSW2.

Family and domain databases

InterProIPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
[Graphical view]
Gene3DG3DSA:1.10.790.10. Prion. 1 hit.
KOK05634.
PANTHERPTHR11522. Prion. 1 hit.
PfamPF00377. Prion. 1 hit.
[Graphical view]
SMARTSM00157. PRP. 1 hit.
[Graphical view]
SUPFAMSSF54098. Prion. 1 hit.
PROSITEPS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRIO_CHICK
AccessionPrimary (citable) accession number: P27177
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 1, 1993
Last modified: November 16, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families