Summary: Granin (chromogranin or secretogranin)
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Granin Edit Wikipedia article
| Granin (chromogranin or secretogranin) | |||||||||
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Structure of SS-cyclized catestatin fragment from chromogranin A.[1]
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| Identifiers | |||||||||
| Symbol | Granin | ||||||||
| Pfam | PF01271 | ||||||||
| InterPro | IPR001990 | ||||||||
| PROSITE | PDOC00365 | ||||||||
| SCOP | 1cfk | ||||||||
| SUPERFAMILY | 1cfk | ||||||||
| OPM superfamily | 328 | ||||||||
| OPM protein | 1lv4 | ||||||||
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Granin (chromogranin and secretogranin) is a protein family of regulated secretory proteins ubiquitously found in the cores of amine and peptide hormone and neurotransmitter dense-core secretory vesicles.[2]
Contents
Function
Granins (chromogranins or secretogranins) are acidic proteins and are present in the secretory granules of a wide variety of endocrine and neuro-endocrine cells. The exact function(s) of these proteins is not yet settled but there is evidence that granins function as pro-hormones, giving rise to an array of peptide fragments for which autocrine, paracrine, and endocrine activities have been demonstrated in vitro and in vivo. The intracellular biochemistry of granins includes binding of Ca2+, ATP and catecholamines (epinephrine, norepinephrine) within the hormone storage vesicle core. There is also evidence that CgA, and perhaps other granins, regulate the biogenesis of dense-core secretory vesicles and hormone sequestration in neuroendocrine cells.
Structure
Apart from their subcellular location and the abundance of acidic residues (Asp and Glu), these proteins do not share many structural similarities. Only one short region, located in the C-terminal section, is conserved in all these proteins. Chromogranins and secretogranins together share a C-terminal motif, whereas chromogranins A and B share a region of high similarity in their N-terminal section; this region includes two cysteine residues involved in a disulfide bond.
There are considerable differences in the amino acid composition between different animals. Commercial assays for measuring human CGA can usually not be used for measuring CGA in samples from other species. Some specific parts of the molecule have a higher degree of amino acid homology and methods where the antibodies are directed against specific epitopes can be used to measure samples from different animals.[3] Region-specific assays measuring defined parts of CGA, CGB and SG2 can be used for measurements in samples from cats and dogs.[4][5][6][7]
Members
Chromogranins
- chromogranin A (CgA)
- chromogranin B (CgB)
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Secretogranins
- secretogranin II (SgII) (see also secretoneurin)
- secretogranin III (SgIII)
- secretogranin V (SgV)
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Two other proteins (secretogranin IV and VI) are also proposed to belong to the granins on the basis of their physico-chemical properties.
References
- ^ Preece NE, Nguyen M, Mahata M, Mahata SK, Mahapatra NR, Tsigelny I, O'Connor DT (April 2004). "Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A". Regulatory Peptides. 118 (1-2): 75–87. PMID 14759560. doi:10.1016/j.regpep.2003.10.035.
- ^ Huttner WB, Gerdes HH, Rosa P (January 1991). "The granin (chromogranin/secretogranin) family". Trends in Biochemical Sciences. 16 (1): 27–30. PMID 2053134. doi:10.1016/0968-0004(91)90012-K.
- ^ Stridsberg M, Angeletti RH, Helle KB (June 2000). "Characterisation of N-terminal chromogranin A and chromogranin B in mammals by region-specific radioimmunoassays and chromatographic separation methods". The Journal of Endocrinology. 165 (3): 703–14. PMID 10828855. doi:10.1677/joe.0.1650703.
- ^ Stridsberg M, Pettersson A, Hagman R, Westin C, Höglund O (June 2014). "Chromogranins can be measured in samples from cats and dogs". BMC Research Notes. 7 (1): 336. PMC 4055239
. PMID 24899097. doi:10.1186/1756-0500-7-336. - ^ Höglund OV, Hagman R, Stridsberg M (27 March 2015). "Chromogranin A and cortisol at intraoperative repeated noxious stimuli: Surgical stress in a dog model" (PDF). SAGE Open Medicine. 3 (0): 2050312115576432. PMC 4679230 . PMID 26770773. doi:10.1177/2050312115576432.
- ^ Srithunyarat T, Höglund OV, Hagman R, Olsson U, Stridsberg M, Lagerstedt AS, Pettersson A (August 2016). "Catestatin, vasostatin, cortisol, temperature, heart rate, respiratory rate, scores of the short form of the Glasgow composite measure pain scale and visual analog scale for stress and pain behavior in dogs before and after ovariohysterectomy". BMC Research Notes. 9 (1): 381. PMC 4969733 . PMID 27484122. doi:10.1186/s13104-016-2193-1.
- ^ Srithunyarat T, Hagman R, Höglund OV, Olsson U, Stridsberg M, Jitpean S, Lagerstedt AS, Pettersson A (January 2017). "Catestatin and vasostatin concentrations in healthy dogs". Acta Veterinaria Scandinavica. 59 (1): 1. PMID 28049540. doi:10.1186/s13028-016-0274-8.
External links
- Chromogranins at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the public domain Pfam and InterPro IPR001990
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Granin (chromogranin or secretogranin) Provide feedback
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External database links
| PROSITE: | PDOC00365 |
| SCOP: | 1cfk |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001990
Granins (chromogranins or secretogranins) [PUBMED:2053134] are a family of acidic proteins present in the secretory granules of a wide variety of endocrine and neuro-endocrine cells. The exact function(s) of these proteins is not yet known but they seem to be the precursors of biologically active peptides and/or they may act as helper proteins in the packaging of peptide hormones and neuropeptides. Apart from their subcellular location and the abundance of acidic residues (Asp and Glu), these proteins do not share many structural similarities. Only one short region, located in the C-terminal section, is conserved in all these proteins.
Chromogranins and secretogranins together share a C-terminal motif, whereas chromogranins A and B share a region of high similarity in their N-terminal section; this region includes two cysteine residues involved in a disulphide bond.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | secretory granule (GO:0030141) |
Domain organisation
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Alignments
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| Seed (8) |
Full (370) |
Representative proteomes | UniProt (518) |
NCBI (1235) |
Meta (0) |
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| RP15 (33) |
RP35 (88) |
RP55 (218) |
RP75 (315) |
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| PP/heatmap | 1 | ||||||||
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| Seed (8) |
Full (370) |
Representative proteomes | UniProt (518) |
NCBI (1235) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|---|
| RP15 (33) |
RP35 (88) |
RP55 (218) |
RP75 (315) |
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| Gzipped | |||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
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.
Note: You can also download the data file for the tree.
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: | 8 |
| Number in full: | 370 |
| Average length of the domain: | 374.40 aa |
| Average identity of full alignment: | 23 % |
| Average coverage of the sequence by the domain: | 90.71 % |
HMM information
| HMM build commands: |
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 586 | ||||||||||||
| Family (HMM) version: | 16 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Colour assignments
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Granin domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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