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0  structures 67  species 0  interactions 202  sequences 1  architecture

Family: Opiods_neuropep (PF01160)

Summary: Vertebrate endogenous opioids neuropeptide

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This is the Wikipedia entry entitled "Opioid peptide". More...

Opioid peptide Edit Wikipedia article

Vertebrate endogenous opioids neuropeptide
Identifiers
Symbol Opiods_neuropep
Pfam PF01160
InterPro IPR006024
PROSITE PDOC00964

Opioid peptides are short sequences of amino acids that bind to opioid receptors in the brain; opiates and opioids mimic the effect of these peptides. Opioid peptides may be produced by the body itself, for example endorphins. The effects of these peptides vary, but they all resemble opiates. Brain opioid peptide systems are known to play an important role in motivation, emotion, attachment behaviour, the response to stress and pain, and the control of food intake.

Opioid-like peptides may also be absorbed from partially digested food (casomorphins, exorphins, and rubiscolins), but have limited physiological activity. The opioid food peptides have lengths of typically 4-8 amino acids. The body's own opioids are generally much longer.

Opioid peptides are released by post-translational proteolytic cleavage of precursor proteins. The precursors consist of the following components: a signal sequence that precedes a conserved region of about 50 residues; a variable-length region; and the sequence of the neuropeptides themselves. Sequence analysis reveals that the conserved N-terminal region of the precursors contains 6 cysteines, which are probably involved in disulfide bond formation. It is speculated that this region might be important for neuropeptide processing.[1]

Opioid peptides produced by the body[edit]

The human genome contains several homologous genes that are known to code for endogenous opioid peptides.

Opioid food peptides[edit]

Microbial opioid peptides[edit]

References[edit]

  1. ^ a b Mollereau C, Simons MJ, Soularue P, Liners F, Vassart G, Meunier JC, Parmentier M (August 1996). "Structure, tissue distribution, and chromosomal localization of the prepronociceptin gene". Proc. Natl. Acad. Sci. U.S.A. 93 (16): 8666–70. doi:10.1073/pnas.93.16.8666. PMC 38730. PMID 8710928. 
  2. ^ Chang AC, Cochet M, Cohen SN (August 1980). "Structural organization of human genomic DNA encoding the pro-opiomelanocortin peptide". Proc. Natl. Acad. Sci. U.S.A. 77 (8): 4890–4. doi:10.1073/pnas.77.8.4890. PMC 349954. PMID 6254047. 
  3. ^ Ling N, Burgus R, Guillemin R (November 1976). "Isolation, primary structure, and synthesis of alpha-endorphin and gamma-endorphin, two peptides of hypothalamic-hypophysial origin with morphinomimetic activity". Proc. Natl. Acad. Sci. U.S.A. 73 (11): 3942–6. doi:10.1073/pnas.73.11.3942. PMC 431275. PMID 1069261. 
  4. ^ Noda M, Teranishi Y, Takahashi H, Toyosato M, Notake M, Nakanishi S, Numa S (June 1982). "Isolation and structural organization of the human preproenkephalin gene." Nature". 1982 Jun 3;' 297 (5865): 431–4. doi:10.1038/297431a0. PMID 6281660. 
  5. ^ Horikawa S, Takai T, Toyosato M, Takahashi H, Noda M, Kakidani H et al. (Dec 1983). "Isolation and structural organization of the human preproenkephalin B gene". Nature 306 (5943): 611–4. doi:10.1038/306611a0. PMID 6316163. 

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR006024

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Vertebrate endogenous opioids neuropeptide Provide feedback

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006024

Vertebrate endogenous opioid neuropeptides are released by post-translational proteolytic cleavage of precursor proteins. The precursors consist of the following components: a signal sequence that precedes a conserved region of about 50 residues; a variable-length region; and the sequence of the neuropeptide itself. Three types of precursor are known: preproenkephalin A (gene PENK), which is processed to produce 6 copies of Met-enkephalin, plus Leu-enkephalin; preproenkephalin B (gene PDYN), which is processed to produce neoendorphin, dynorphin, leumorphin, rimorphin and Leu-enkephalin; and prepronocipeptin (gene PNOC), whose processing produces nociceptin (orphanin FQ) and two other potential neuropeptides.

Sequence analysis reveals that the conserved N-terminal region of the precursors contains 6 cysteines, which are probably involved in disulphide bond formation. It is speculated that this region might be important for neuropeptide processing [PUBMED:8710928].

Gene Ontology

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Domain organisation

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Full
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Representative proteomes NCBI
(181)
Meta
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RP15
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RP35
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RP55
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RP75
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  Seed
(31)
Full
(202)
Representative proteomes NCBI
(181)
Meta
(0)
RP15
(3)
RP35
(11)
RP55
(26)
RP75
(73)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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Seed source: Prosite
Previous IDs: none
Type: Family
Author: Finn RD, Bateman A
Number in seed: 31
Number in full: 202
Average length of the domain: 44.50 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 20.36 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 21.0 21.5
Noise cut-off 19.6 18.4
Model length: 49
Family (HMM) version: 13
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