Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P01214 (PDYN_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 76. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length256 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.

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.

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

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 – 2020 Potential
Propeptide21 – 172152
PRO_0000008191
Peptide175 – 18410Alpha-neoendorphin By similarity
PRO_0000306358
Peptide175 – 1839Beta-neoendorphin
PRO_0000008192
Peptide175 – 1795Leu-enkephalin By similarity
PRO_0000306359
Propeptide186 – 20621
PRO_0000008193
Peptide209 – 24032Big dynorphin By similarity
PRO_0000306360
Peptide209 – 22517Dynorphin A(1-17)
PRO_0000306361
Peptide209 – 22113Dynorphin A(1-13) Ref.2
PRO_0000306362
Peptide209 – 2168Dynorphin A(1-8) Ref.3
PRO_0000306363
Peptide209 – 2135Leu-enkephalin By similarity
PRO_0000306364
Peptide228 – 25629Leumorphin
PRO_0000008195
Peptide228 – 24013Rimorphin
PRO_0000008196
Peptide228 – 2325Leu-enkephalin
PRO_0000008197

Natural variations

Natural variant1471G → E.
Natural variant1971R → G.

Sequences

Sequence LengthMass (Da)Tools
P01214 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 6814412E3A8DB3AE

FASTA25628,617
        10         20         30         40         50         60 
MAWQGLLLAA CLLVLPSTMA DCLSGCSLCA VKTQDGPKPI NPLICSLECQ AALQPAEEWE 

        70         80         90        100        110        120 
RCQGLLSFLA PLSLGLEGKE DLESKAALEE PSSELVKYMG PFLKELEKNR FLLSTPAEET 

       130        140        150        160        170        180 
SLSRSLVEKL RSLPGRLGEE TESELMGDAQ QNDGAMEAAA LDSSVEDPKE QVKRYGGFLR 

       190        200        210        220        230        240 
KYPKRSSEVA GEGDGDRDKV GHEDLYKRYG GFLRRIRPKL KWDNQKRYGG FLRRQFKVVT 

       250 
RSQEDPNAYY EELFDV 

« Hide

References

[1]"Cloning and sequence analysis of cDNA for porcine beta-neo-endorphin/dynorphin precursor."
Kakidani H., Furutani Y., Takahashi H., Noda M., Morimoto Y., Hirose T., Asai M., Inayama S., Nakanishi S., Numa S.
Nature 298:245-249(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hypothalamus.
[2]"Dynorphin-(1-13), an extraordinarily potent opioid peptide."
Goldstein A., Tachibana S., Lowney L.I., Hunkapiller M., Hood L.
Proc. Natl. Acad. Sci. U.S.A. 76:6666-6670(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 209-221, IDENTIFICATION, CHARACTERIZATION OF DYNORPHIN A(1-13).
[3]"A new opioid octapeptide related to dynorphin from porcine hypothalamus."
Minamino N., Kangawa K., Fukuda A., Matsuo H., Iagarashi M.
Biochem. Biophys. Res. Commun. 95:1475-1481(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 209-216, IDENTIFICATION OF DYNORPHIN A(1-8).
Tissue: Hypothalamus.
[4]"Leumorphin is a novel endogenous opioid peptide derived from preproenkephalin B."
Nakao K., Suda M., Sakamoto M., Yoshimasa T., Morii N., Ikeda Y., Yanaihara C., Yanaihara N., Numa S., Imura H.
Biochem. Biophys. Res. Commun. 117:695-701(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF LEUMORPHIN AND RIMORPHIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01362 mRNA. Translation: CAA24650.1.
PIRDFPG. A93280.
RefSeqNP_001004040.1. NM_001004040.1.
UniGeneSsc.121.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000007643.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID445529.
KEGGssc:445529.

Organism-specific databases

CTD5173.

Phylogenomic databases

eggNOGNOG46156.
HOGENOMHOG000013003.
HOVERGENHBG000063.
KOK15840.

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...

Entry information

Entry namePDYN_PIG
AccessionPrimary (citable) accession number: P01214
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 13, 2013
This is version 76 of the entry and version 1 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