Summary: Opioids neuropeptide

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Wikipedia: Proopiomelanocortin
Pfam
InterPro

This is the Wikipedia entry entitled "Proopiomelanocortin". More...

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Proopiomelanocortin Edit Wikipedia article

Proopiomelanocortin

Identifiers

Symbols

POMC; ACTH; CLIP; LPH; MSH; NPP; POC

External IDs

OMIM: 176830 MGI: 97742 HomoloGene: 723 GeneCards: POMC Gene

Gene Ontology
Molecular function	• G-protein coupled receptor binding • receptor binding • hormone activity • type 3 melanocortin receptor binding • type 4 melanocortin receptor binding • type 1 melanocortin receptor binding
Cellular component	• extracellular region • extracellular space • cytoplasm • peroxisome • peroxisomal matrix • secretory granule
Biological process	• generation of precursor metabolites and energy • signal transduction • neuropeptide signaling pathway • cell-cell signaling • regulation of blood pressure • peptide hormone processing • regulation of appetite • negative regulation of tumor necrosis factor production • cellular pigmentation • cellular nitrogen compound metabolic process • small molecule metabolic process • positive regulation of transcription from RNA polymerase II promoter
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
25.38 – 25.39 Mb

Chr 12:
3.95 – 3.96 Mb

PubMed search

[1]

[2]

Opioids neuropeptide

Identifiers

Symbol

Op_neuropeptide

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

Pro-opiomelanocortin (POMC) is a precursor polypeptide with 241 amino acid residues. POMC is synthesized from the 285-amino acid long polypeptide precursor, pre-pro-opiomelanocortin (pre-POMC), by the removal of a 44-amino acid long signal peptide sequence during translation.

The POMC gene is located on chromosome 2p23.3. The POMC gene is expressed in both the anterior and intermediate lobes of the pituitary gland. This gene encodes a 285-amino acid polypeptide hormone precursor that undergoes extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. The encoded protein is synthesized mainly in corticotroph cells of the anterior pituitary where four cleavage sites are used; adrenocorticotrophin (ACTH), essential for normal steroidogenesis and the maintenance of normal adrenal weight, and β-lipotropin are the major end products. However, there are at least eight potential cleavage sites within the polypeptide precursor and, depending on tissue type and the available convertases, processing may yield as many as ten biologically active peptides involved in diverse cellular functions. Cleavage sites consist of the sequences, Arg-Lys, Lys-Arg or Lys-Lys. Enzymes responsible for processing of POMC peptides include prohormone convertase 1 (PC1), prohormone convertase 2 (PC2), carboxypeptidase E (CPE), peptidyl α-amidating monooxygenase (PAM), N-acetyltransferase (N-AT), and prolylcarboxypeptidase (PRCP).

The processing of POMC involves glycosylations, acetylations, and extensive proteolytic cleavage at sites shown to contain regions of basic protein sequences. However, the proteases that recognize these cleavage sites are tissue-specific. In some tissues, including the hypothalamus, placenta, and epithelium, all cleavage sites may be used, giving rise to peptides with roles in pain and energy homeostasis, melanocyte stimulation, and immune modulation. These include several distinct melanotropins, lipotropins, and endorphins that are contained within the adrenocorticotrophin and β-lipotropin peptides.

Mutations in this gene have been associated with early onset obesity, adrenal insufficiency, and red hair pigmentation. Alternatively spliced transcript variants encoding the same protein have been described.^[1]^[2]

[edit] Production

It is synthesized by:

Corticotrope cells of the anterior pituitary gland
Melanotrope cells of the intermediate lobe of the pituitary gland
3,148±62 neurons in the arcuate nucleus of the hypothalamus^[3]
Smaller populations of neurons in the dorsomedial hypothalamus and brainstem
Melanocytes in the skin

[edit] Derivatives

proopiomelanocortin derivatives
POMC

γ-MSH	ACTH		β-lipotropin

	α-MSH	CLIP	γ-lipotropin		β-endorphin

				β-MSH

The large molecule of POMC is the source of several important biologically active substances. POMC can be cleaved enzymatically into the following peptides:

N-Terminal Peptide of Proopiomelanocortin (NPP, or pro-γ-MSH)
γ-Melanotropin (γ-MSH)
Corticotropin (Adrenocorticotropic Hormone, or ACTH)
α-Melanotropin (α-Melanocyte-Stimulating Hormone, or α-MSH)
Corticotropin-like Intermediate Peptide (CLIP)
β-Lipotropin (β-LPH)
Lipotropin Gamma (γ-LPH)
β-Melanotropin (β-MSH)
β-Endorphin
[Met]Enkephalin

Although the N-terminal 5 amino acids of β-endorphin are identical to the sequence of [Met]enkephalin, it is not generally thought that β-endorphin is converted into [Met]enkephalin. Instead, [Met]enkephalin is produced from its own precursor, proenkephalin A.

The production of β-MSH occurs in humans but not in mice or rats due to the absence of the enzymatic processing site in the rodent POMC.

[edit] Function

Each of these peptides is packaged in large dense-core vesicles that are released from the cells by exocytosis in response to appropriate stimulation:

α-MSH produced by neurons in the arcuate nucleus has important roles in the regulation of appetite and sexual behavior, while α-MSH secreted from the intermediate lobe of the pituitary regulates the production of melanin.
ACTH is a peptide hormone that regulates the secretion of glucocorticoids from the adrenal cortex.
β-endorphin and [Met]enkephalin are endogenous opioid peptides with widespread actions in the brain.

[edit] Interactions

Proopiomelanocortin has been shown to interact with Melanocortin 4 receptor.^[4]^[5]

[edit] See also

[edit] References

^ "Entrez Gene: POMC proopiomelanocortin (adrenocorticotropin/ beta-lipotropin/ alpha-melanocyte stimulating hormone/ beta-melanocyte stimulating hormone/ beta-endorphin)".
^ Kuehnen, Peter; Mischke, Mona, Wiegand, Susanna, Sers, Christine, Horsthemke, Bernhard, Lau, Susanne, Keil, Thomas, Lee, Young-Ae, Grueters, Annette, Krude, Heiko, Yeo, Giles S. H. (NaN undefined NaN). "An Alu Element–Associated Hypermethylation Variant of the POMC Gene Is Associated with Childhood Obesity". PLoS Genetics 8 (3): e1002543. doi:10.1371/journal.pgen.1002543.
^ Cowley et al, Leptin activates anorexigenic POMC neurons through a neural network in the arcuate nucleus, Nature. 2001 May 24;411(6836):480-4.
^ Yang, Y K; Fong T M, Dickinson C J, Mao C, Li J Y, Tota M R, Mosley R, Van Der Ploeg L H, Gantz I (December 2000). "Molecular determinants of ligand binding to the human melanocortin-4 receptor". Biochemistry (UNITED STATES) 39 (48): 14900–11. doi:10.1021/bi001684q. ISSN 0006-2960. PMID 11101306.
^ Yang, Y K; Ollmann M M, Wilson B D, Dickinson C, Yamada T, Barsh G S, Gantz I (March 1997). "Effects of recombinant agouti-signaling protein on melanocortin action". Mol. Endocrinol. (UNITED STATES) 11 (3): 274–80. doi:10.1210/me.11.3.274. ISSN 0888-8809. PMID 9058374.

[edit] Further reading

Millington GW (May 2006). "Proopiomelanocortin (POMC): the cutaneous roles of its melanocortin products and receptors". Clin. Exp. Dermatol. 31 (3): 407–12. doi:10.1111/j.1365-2230.2006.02128.x. PMID 16681590.
Millington GW (2007). "The role of proopiomelanocortin (POMC) neurones in feeding behaviour". Nutr Metab (Lond) 4: 18. doi:10.1186/1743-7075-4-18. PMC 2018708. PMID 17764572.
Bhardwaj RS, Luger TA (1995). "Proopiomelanocortin production by epidermal cells: evidence for an immune neuroendocrine network in the epidermis". Arch. Dermatol. Res. 287 (1): 85–90. doi:10.1007/BF00370724. PMID 7726641.
Raffin-Sanson ML, de Keyzer Y, Bertagna X (2003). "Proopiomelanocortin, a polypeptide precursor with multiple functions: from physiology to pathological conditions". Eur. J. Endocrinol. 149 (2): 79–90. doi:10.1530/eje.0.1490079. PMID 12887283.
Dores RM, Lecaude S (2005). "Trends in the evolution of the proopiomelanocortin gene". Gen. Comp. Endocrinol. 142 (1–2): 81–93. doi:10.1016/j.ygcen.2005.02.003. PMID 15862552.
König S, Luger TA, Scholzen TE (2006). "Monitoring neuropeptide-specific proteases: processing of the proopiomelanocortin peptides adrenocorticotropin and alpha-melanocyte-stimulating hormone in the skin". Exp. Dermatol. 15 (10): 751–61. doi:10.1111/j.1600-0625.2006.00472.x. PMID 16984256.
Farooqi S, O'Rahilly S (2007). "Genetics of obesity in humans". Endocr. Rev. 27 (7): 710–18. doi:10.1210/er.2006-0040. PMID 17122358.

[edit] External links

Pro-Opiomelanocortin at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates public domain material from websites or documents of the National Center for Biotechnology Information (Reference Sequence collection).

Endocrine system: hormones (Peptide hormones · Steroid hormones)

Endocrine
glands

Hypothalamic-
pituitary

Hypothalamus	GnRH · TRH · Dopamine · CRH · GHRH/Somatostatin · Melanin concentrating hormone

Posterior pituitary	Vasopressin · Oxytocin

Anterior pituitary	α (FSH FSHB, LH LHB, TSH TSHB, CGA) · Prolactin · POMC (CLIP, ACTH, MSH, Endorphins, Lipotropin) · GH

Adrenal axis

Adrenal cortex: aldosterone · cortisol · DHEA
Adrenal medulla: epinephrine · norepinephrine

Thyroid axis

Thyroid: thyroid hormone (T₃ and T₄) · calcitonin
Parathyroid: PTH

Gonadal axis

Testis: testosterone · AMH · inhibin

Ovary: estradiol · progesterone · activin and inhibin · relaxin (pregnancy)

Placenta: hCG · HPL · estrogen · progesterone

Islet-Acinar
Axis

Pancreas: glucagon · insulin · amylin · somatostatin · pancreatic polypeptide

Pineal gland

Pineal gland: melatonin

Non-end.
glands

Thymus: Thymosin (Thymosin α1, Thymosin beta) · Thymopoietin · Thymulin

Digestive system: Stomach: gastrin · ghrelin · Duodenum: CCK · Incretins (GIP, GLP-1) · secretin · motilin · VIP · Ileum: enteroglucagon · peptide YY · Liver/other: Insulin-like growth factor (IGF-1, IGF-2)

Adipose tissue: leptin · adiponectin · resistin

Skeleton: Osteocalcin

Kidney: JGA (renin) · peritubular cells (EPO) · calcitriol · prostaglandin

Heart: Natriuretic peptide (ANP, BNP)

M: END

anat/phys/devp/horm

noco (d)/cong/tumr, sysi/epon

proc, drug (A10/H1/H2/H3/H5)

Peptides: neuropeptides

Hormones

see hormones

Opioid peptides

Dynorphin	Big dynorphin Dynorphin A Dynorphin B

Endorphins	Beta-endorphin Alpha-endorphin Gamma-endorphin α-neo-endorphin β-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-Hpα 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 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.

Opioids neuropeptide Provide feedback

This family corresponds to the conserved YGG motif that is found in a wide variety of opioid neuropeptides such as enkephalin.

Internal database links

SCOOP:

NPP

External database links

PANDIT:	PF08035
PROSITE:	PDOC00964
Pseudofam:	PF08035
SYSTERS:	Op_neuropeptide

This tab holds annotation information from the InterPro database.

InterPro entry IPR013532

Pro-opiomelanocortin is present in high levels in the pituitary and is processed into 3 major peptide families: adrenocorticotrophin (ACTH); alpha-, beta- and gamma-melanocyte- stimulating hormones (MSH); and beta-endorphin [PUBMED:2266117]. ACTH regulates the synthesis and release of glucocorticoids and, to some extent, aldosterone in the adrenal cortex. It is synthesised and released in response to corticotrophin-releasing factor at times of stress (i.e. heat, cold, infection, etc.), its release leading to increased metabolism. The action of MSH in man is poorly understood, but it may be involved in temperature regulation [PUBMED:2266117]. Full activity of ACTH resides in the first 20 N-terminal amino acids, the first 13 of which are identical to alpha-MSH [PUBMED:2266117, PUBMED:2839146].

This region corresponds to the conserved YGG motif that is found in a wide variety of opioid neuropeptides such as enkephalin

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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.

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

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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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	Seed (14)	Full (584)	Representative proteomes				NCBI (585)	Meta (0)
	Seed (14)	Full (584)	RP15 (1)	RP35 (4)	RP55 (9)	RP75 (25)	NCBI (585)	Meta (0)
Jalview	View	View	View	View	View	View	View
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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 (14)	Full (584)	Representative proteomes				NCBI (585)	Meta (0)
	Seed (14)	Full (584)	RP15 (1)	RP35 (4)	RP55 (9)	RP75 (25)	NCBI (585)	Meta (0)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

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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 (14)	Full (584)	Representative proteomes				NCBI (585)	Meta (0)
	Seed (14)	Full (584)	RP15 (1)	RP35 (4)	RP55 (9)	RP75 (25)	NCBI (585)	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

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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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:

Bateman A, Lee SC

Number in seed:

14

Number in full:

584

Average length of the domain:

23.60 aa

Average identity of full alignment:

87 %

Average coverage of the sequence by the domain:

11.63 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	20.4	20.4
Trusted cut-off	20.4	22.5
Noise cut-off	20.3	19.6

Model length:

31

Family (HMM) version:

6

Download:

download the raw HMM for this family

Species distribution

Sunburst
Tree

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order
family
genus
species

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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: Op_neuropeptide (PF08035)

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