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P06300 (PDYN_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proenkephalin-B
Alternative name(s):
Beta-neoendorphin-dynorphin
Preprodynorphin

Cleaved into the following 9 chains:

  1. Alpha-neoendorphin
  2. Beta-neoendorphin
  3. Big dynorphin
    Short name=Big Dyn
  4. Dynorphin A(1-17)
    Short name=Dyn-A17
    Short name=Dynorphin A
  5. Dynorphin A(1-13)
  6. Dynorphin A(1-8)
  7. Leu-enkephalin
  8. Rimorphin
    Alternative name(s):
    Dynorphin B
    Short name=Dyn-B
    Dynorphin B(1-13)
  9. Leumorphin
    Alternative name(s):
    Dynorphin B-29
Gene names
Name:Pdyn
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress By similarity. Ref.7

Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin By similarity. Ref.7

Leumorphin has a typical opiod activity and may have anti-apoptotic effect By similarity. Ref.7

Subcellular location

Secreted.

Post-translational modification

The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.

Sequence similarities

Belongs to the opioid neuropeptide precursor family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 163142
PRO_0000008198
Peptide166 – 17510Alpha-neoendorphin
PRO_0000306365
Peptide166 – 1749Beta-neoendorphin
PRO_0000008199
Peptide166 – 1705Leu-enkephalin
PRO_0000008200
Propeptide177 – 19923
PRO_0000008201
Peptide202 – 23332Big dynorphin By similarity
PRO_0000306366
Peptide202 – 21817Dynorphin A(1-17)
PRO_0000008202
Peptide202 – 21413Dynorphin A(1-13) By similarity
PRO_0000306367
Peptide202 – 2098Dynorphin A(1-8) By similarity
PRO_0000306368
Peptide202 – 2065Leu-enkephalin
PRO_0000008203
Peptide221 – 24828Leumorphin
PRO_0000008204
Peptide221 – 23313Rimorphin By similarity
PRO_0000306369
Peptide221 – 2255Leu-enkephalin
PRO_0000008205

Experimental info

Sequence conflict1811T → A in AAA41118. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P06300 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 899F1B24CA3D1E91

FASTA24828,079
        10         20         30         40         50         60 
MAWSRLMLAA CLLVIPSEVA ADCLSLCSLC AVRTQDGPHP INPLICSLEC QDLVPPSEEW 

        70         80         90        100        110        120 
ETCRGFWSFL TLTASGLHGK DDLENEVALE EGYTALTKLL EPLLKELEKG QLLTSVSEEK 

       130        140        150        160        170        180 
LRGLSSRFGN GRESELLGTD LMNDEAAQAG TLHFNEEDLR KQAKRYGGFL RKYPKRSSEM 

       190        200        210        220        230        240 
TGDEDRGQDG DQVGHEDLYK RYGGFLRRIR PKLKWDNQKR YGGFLRRQFK VVTRSQENPN 


TYSEDLDV 

« Hide

References

[1]"Characterization of the rat prodynorphin gene."
Douglass J., McMurray C.T., Garrett J.E., Adelman J.P., Calavetta L.
Mol. Endocrinol. 3:2070-2078(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence and expression of the rat prodynorphin gene."
Civelli O., Douglass J., Goldstein A., Herbert E.
Proc. Natl. Acad. Sci. U.S.A. 82:4291-4295(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 45-248.
Tissue: Hypothalamus.
[3]"Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate forms. Cleavage at a single arginine residue."
Dupuy A., Lindberg I., Zhou Y., Akil H., Lazure C., Chretien M., Seidah N.G., Day R.
FEBS Lett. 337:60-65(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 235-248.
[4]"Identification of the tridecapeptide dynorphin B (rimorphin) within perikarya of rat duodenum."
Wolter H.J.
Life Sci. 39:727-730(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RIMORPHIN.
[5]"Neuropeptide processing by single-step cleavage: conversion of leumorphin (dynorphin B-29) to dynorphin B."
Devi L., Goldstein A.
Biochem. Biophys. Res. Commun. 130:1168-1176(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: CONVERSION OF LEUMORPHIN TO RIMORPHIN.
[6]"Bridge peptide is a cleavage product of pro-dynorphin processing in the rat anterior pituitary."
Day R., Akil H.
NIDA Res. Monogr. 75:244-246(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF BRIDGE PEPTIDE.
[7]"Leumorphin has an anti-apoptotic effect by activating epidermal growth factor receptor kinase in rat pheochromocytoma PC12 cells."
Lee B.D., Kim S., Hur E.M., Park Y.S., Kim Y.H., Lee T.G., Kim K.T., Suh P.G., Ryu S.H.
J. Neurochem. 95:56-67(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF LEUMORPHIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32784, M32783 Genomic DNA. Translation: AAA41117.1.
M10088 Genomic DNA. Translation: AAA41118.1.
PIRDFRTP. A41395.
UniGeneRn.44471.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000038921.

Proteomic databases

PaxDbP06300.
PRIDEP06300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:62054. rat.

Organism-specific databases

RGD62054. Pdyn.

Phylogenomic databases

eggNOGNOG46156.
HOGENOMHOG000013003.
HOVERGENHBG000063.
InParanoidP06300.
PhylomeDBP06300.

Gene expression databases

GenevestigatorP06300.

Family and domain databases

InterProIPR006024. Opioid_neupept.
IPR000750. Proenkphlin_B.
[Graphical view]
PANTHERPTHR11438. PTHR11438. 1 hit.
PTHR11438:SF4. PTHR11438:SF4. 1 hit.
PfamPF01160. Opiods_neuropep. 1 hit.
[Graphical view]
PRINTSPR01028. OPIOIDPRCRSR.
PR01030. PENKBPRCRSR.
PROSITEPS01252. OPIOIDS_PRECURSOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP06300.

Entry information

Entry namePDYN_RAT
AccessionPrimary (citable) accession number: P06300
Secondary accession number(s): Q63193
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 96 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