Summary: Vertebrate endogenous opioids neuropeptide

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

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Opioid peptide Edit Wikipedia article

Vertebrate endogenous opioids neuropeptide

Identifiers

Symbol

Opiods_neuropep

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

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]

[edit] Opioid peptides produced by the body

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

The nucleotide sequence of the human gene for proopiomelanocortin (POMC) was characterized in 1980.^[2] The POMC gene codes for endogenous opiates such as Î²-endorphin and gamma-endorphin.^[3] The peptides with opiate activity that are derived from proopiomelanocortin comprise the class of endogenous opioid peptides called "endorphins".
The human gene for enkephalins was isolated and its sequence described in 1982.^[4]
The human gene for dynorphins (originally called the "Enkephalin B" gene because of sequence similarity to the enkephalin gene) was isolated and its sequence described in 1983.^[5]
The PNOC gene encoding prepronociceptin, which is cleaved into nociceptin and potentially two additional neuropeptides.^[1]
Adrenorphin, amidorphin, and leumorphin were discovered in the 1980s.
Opiorphin and spinorphin, enkephalinase inhibitors (i.e., prevent the metabolism of enkephalins).
Hemorphins, hemoglobin-derived opioid peptides, including hemorphin-4, valorphin, and spinorphin, among others.

[edit] Opioid food peptides

[edit] Microbial opioid peptides

Deltorphin I and II (fungal)
Dermorphin (from an unknown microbe)

[edit] References

^ ^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): 8666â70. doi:10.1073/pnas.93.16.8666. PMC 38730. PMID 8710928.
^ 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): 4890â4. doi:10.1073/pnas.77.8.4890. PMC 349954. PMID 6254047.
^ 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): 3942â6. doi:10.1073/pnas.73.11.3942. PMC 431275. PMID 1069261.
^ 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): 431â4. doi:10.1038/297431a0. PMID 6281660.
^ 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): 611â4. doi:10.1038/306611a0. PMID 6316163.

[edit] External links

Opioid Peptides at the US National Library of Medicine Medical Subject Headings (MeSH)

Peptides: neuropeptides

Hormones

see hormones

Opioid peptides

Dynorphin	Big dynorphin Dynorphin A Dynorphin B

Endorphins	Beta-endorphin Alpha-endorphin Gamma-endorphin Î±-neo-endorphin Î²-neo-endorphin

Enkephalin	Met-enkephalin Leu-enkephalin

Others	Adrenorphin Amidorphin Leumorphin Nociceptin Opiorphin Spinorphin

Other
neuropeptides

Kinins	Bradykinin Tachykinins: mammal Substance P Neurokinin A Neurokinin B amphibian Kassinin Physalaemin

Neuromedins	B N S U

Other	Angiotensin Bombesin Calcitonin gene-related peptide Carnosine Cocaine and amphetamine regulated transcript Delta sleep-inducing peptide FMRFamide Galanin Galanin-like peptide Gastrin releasing peptide Neuropeptide S Neuropeptide Y Neurophysins Neurotensin Pancreatic polypeptide Pituitary adenylate cyclase activating peptide RVD-HpÎ± VGF

B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

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

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Vertebrate endogenous opioids neuropeptide Provide feedback

No Pfam abstract.

External database links

PANDIT:	PF01160
PROSITE:	PDOC00964
Pseudofam:	PF01160
SYSTERS:	Opiods_neuropep

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

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Biological process

neuropeptide signaling pathway (GO:0007218)

Domain organisation

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Alignments

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There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.

Alignment types

We make a range of alignments for each Pfam-A family:

seed: the curated alignment from which the HMM for the family is built
full: the alignment generated by searching the sequence database using the HMM
RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
NCBI: alignment generated by searching the NCBI sequence database using the family HMM
meta: alignment generated by searching the metagenomics sequence database using the family HMM

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PP/Heatmap: an HTML-based representation of the alignment, coloured according to the posterior-probability (PP) values from the HMM. As for the standard HTML view, heatmap alignments can also be very large and slow to render.
Pfam viewer: an HTML-based viewer that uses DAS to retrieve alignment fragments on request

Reformatting

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You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

	Seed (31)	Full (202)	Representative proteomes				NCBI (181)	Meta (0)
	Seed (31)	Full (202)	RP15 (3)	RP35 (11)	RP55 (26)	RP75 (73)	NCBI (181)	Meta (0)
Jalview	View	View	View	View	View	View	View
HTML	View	View	View	View	View	View
PP/heatmap	₁	View	View	View	View	View
Pfam viewer	View	View

¹Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, — not available.

Format an alignment

	Seed (31)	Full (202)	Representative proteomes				NCBI (181)	Meta (0)
	Seed (31)	Full (202)	RP15 (3)	RP35 (11)	RP55 (26)	RP75 (73)	NCBI (181)	Meta (0)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

	Seed (31)	Full (202)	Representative proteomes				NCBI (181)	Meta (0)
	Seed (31)	Full (202)	RP15 (3)	RP35 (11)	RP55 (26)	RP75 (73)	NCBI (181)	Meta (0)
Raw Stockholm	Download	Download	Download	Download	Download	Download	Download
Gzipped	Download	Download	Download	Download	Download	Download	Download

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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Trees

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation

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

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

Download:

download the raw HMM for this family

Species distribution

Sunburst
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How the sunburst is generated

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The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.

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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.

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Interactive tree

For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.

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Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: Opiods_neuropep (PF01160)

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