Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06300

- PDYN_RAT

UniProt

P06300 - PDYN_RAT

Protein

Proenkephalin-B

Gene

Pdyn

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 - Molecular functioni

    1. protein binding Source: RGD

    GO - Biological processi

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

    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

    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

    MAWSRLMLAA CLLVIPSEVA ADCLSLCSLC AVRTQDGPHP INPLICSLEC    50
    QDLVPPSEEW ETCRGFWSFL TLTASGLHGK DDLENEVALE EGYTALTKLL 100
    EPLLKELEKG QLLTSVSEEK LRGLSSRFGN GRESELLGTD LMNDEAAQAG 150
    TLHFNEEDLR KQAKRYGGFL RKYPKRSSEM TGDEDRGQDG DQVGHEDLYK 200
    RYGGFLRRIR PKLKWDNQKR YGGFLRRQFK VVTRSQENPN TYSEDLDV 248
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32784 , M32783 Genomic DNA. Translation: AAA41117.1 .
    M10088 Genomic DNA. Translation: AAA41118.1 .
    PIRi A41395. DFRTP.
    UniGenei Rn.44471.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000038921.

    Proteomic databases

    PaxDbi P06300.
    PRIDEi P06300.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:62054. rat.

    Organism-specific databases

    RGDi 62054. Pdyn.

    Phylogenomic databases

    eggNOGi NOG46156.
    HOGENOMi HOG000013003.
    HOVERGENi HBG000063.
    InParanoidi P06300.
    PhylomeDBi P06300.

    Miscellaneous databases

    PROi P06300.

    Gene expression databases

    Genevestigatori P06300.

    Family and domain databases

    InterProi IPR006024. Opioid_neupept.
    IPR000750. Proenkphlin_B.
    [Graphical view ]
    PANTHERi PTHR11438. PTHR11438. 1 hit.
    PTHR11438:SF4. PTHR11438:SF4. 1 hit.
    Pfami PF01160. Opiods_neuropep. 1 hit.
    [Graphical view ]
    PRINTSi PR01028. OPIOIDPRCRSR.
    PR01030. PENKBPRCRSR.
    PROSITEi PS01252. OPIOIDS_PRECURSOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 97 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