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Protein

Proenkephalin-B

Gene

Pdyn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. neuropeptide signaling pathway Source: UniProtKB-KW
  2. regulation of neurotransmitter secretion Source: RGD
  3. synaptic transmission Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endorphin, Neuropeptide, Neurotransmitter, Opioid peptide

Names & Taxonomyi

Protein namesi
Recommended name:
Proenkephalin-B
Alternative name(s):
Beta-neoendorphin-dynorphin
Preprodynorphin
Cleaved into the following 9 chains:
Big dynorphin
Short name:
Big Dyn
Dynorphin A(1-17)
Short name:
Dyn-A17
Short name:
Dynorphin A
Alternative name(s):
Dynorphin B
Short name:
Dyn-B
Dynorphin B(1-13)
Alternative name(s):
Dynorphin B-29
Gene namesi
Name:Pdyn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi62054. Pdyn.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 163142PRO_0000008198Add
BLAST
Peptidei166 – 17510Alpha-neoendorphinPRO_0000306365
Peptidei166 – 1749Beta-neoendorphinPRO_0000008199
Peptidei166 – 1705Leu-enkephalinPRO_0000008200
Propeptidei177 – 19923PRO_0000008201Add
BLAST
Peptidei202 – 23332Big dynorphinBy similarityPRO_0000306366Add
BLAST
Peptidei202 – 21817Dynorphin A(1-17)PRO_0000008202Add
BLAST
Peptidei202 – 21413Dynorphin A(1-13)By similarityPRO_0000306367Add
BLAST
Peptidei202 – 2098Dynorphin A(1-8)By similarityPRO_0000306368
Peptidei202 – 2065Leu-enkephalinPRO_0000008203
Peptidei221 – 24828LeumorphinPRO_0000008204Add
BLAST
Peptidei221 – 23313RimorphinBy similarityPRO_0000306369Add
BLAST
Peptidei221 – 2255Leu-enkephalinPRO_0000008205

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP06300.
PRIDEiP06300.

Expressioni

Gene expression databases

GenevestigatoriP06300.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000038921.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG46156.
HOGENOMiHOG000013003.
HOVERGENiHBG000063.
InParanoidiP06300.
PhylomeDBiP06300.

Family and domain databases

InterProiIPR006024. Opioid_neupept.
IPR000750. Proenkphlin_B.
[Graphical view]
PANTHERiPTHR11438. PTHR11438. 1 hit.
PTHR11438:SF4. PTHR11438:SF4. 1 hit.
PfamiPF01160. Opiods_neuropep. 1 hit.
[Graphical view]
PRINTSiPR01028. OPIOIDPRCRSR.
PR01030. PENKBPRCRSR.
PROSITEiPS01252. OPIOIDS_PRECURSOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWSRLMLAA CLLVIPSEVA ADCLSLCSLC AVRTQDGPHP INPLICSLEC
60 70 80 90 100
QDLVPPSEEW ETCRGFWSFL TLTASGLHGK DDLENEVALE EGYTALTKLL
110 120 130 140 150
EPLLKELEKG QLLTSVSEEK LRGLSSRFGN GRESELLGTD LMNDEAAQAG
160 170 180 190 200
TLHFNEEDLR KQAKRYGGFL RKYPKRSSEM TGDEDRGQDG DQVGHEDLYK
210 220 230 240
RYGGFLRRIR PKLKWDNQKR YGGFLRRQFK VVTRSQENPN TYSEDLDV
Length:248
Mass (Da):28,079
Last modified:November 1, 1997 - v2
Checksum:i899F1B24CA3D1E91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811T → A in AAA41118 (PubMed:3858883).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32784, M32783 Genomic DNA. Translation: AAA41117.1.
M10088 Genomic DNA. Translation: AAA41118.1.
PIRiA41395. DFRTP.
UniGeneiRn.44471.

Genome annotation databases

UCSCiRGD:62054. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32784, M32783 Genomic DNA. Translation: AAA41117.1.
M10088 Genomic DNA. Translation: AAA41118.1.
PIRiA41395. DFRTP.
UniGeneiRn.44471.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000038921.

Proteomic databases

PaxDbiP06300.
PRIDEiP06300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:62054. rat.

Organism-specific databases

RGDi62054. Pdyn.

Phylogenomic databases

eggNOGiNOG46156.
HOGENOMiHOG000013003.
HOVERGENiHBG000063.
InParanoidiP06300.
PhylomeDBiP06300.

Miscellaneous databases

PROiP06300.

Gene expression databases

GenevestigatoriP06300.

Family and domain databases

InterProiIPR006024. Opioid_neupept.
IPR000750. Proenkphlin_B.
[Graphical view]
PANTHERiPTHR11438. PTHR11438. 1 hit.
PTHR11438:SF4. PTHR11438:SF4. 1 hit.
PfamiPF01160. Opiods_neuropep. 1 hit.
[Graphical view]
PRINTSiPR01028. OPIOIDPRCRSR.
PR01030. PENKBPRCRSR.
PROSITEiPS01252. OPIOIDS_PRECURSOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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.

Entry informationi

Entry nameiPDYN_RAT
AccessioniPrimary (citable) accession number: P06300
Secondary accession number(s): Q63193
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.