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7  structures 208  species 0  interactions 921  sequences 7  architectures

Family: Granin (PF01271)

Summary: Granin (chromogranin or secretogranin)

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Granin Edit Wikipedia article

Granin (chromogranin or secretogranin)
PDB 1n2y EBI.jpg
Structure of SS-cyclized catestatin fragment from chromogranin A.[1]
OPM superfamily282
OPM protein1lv4

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]


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.


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]



chromogranin A
(parathyroid secretory protein 1)
Alt. symbolsCGA
NCBI gene1113
Other data
LocusChr. 14 q32
chromogranin B
(secretogranin 1)
Alt. symbolsSCG1
NCBI gene1114
Other data
LocusChr. 20 pter-p12


secretogranin II
(chromogranin C)
Alt. symbolsCHGC, SgII
NCBI gene7857
Other data
LocusChr. 2 q35-q36
secretogranin III
Alt. symbolsSGIII
NCBI gene29106
Other data
LocusChr. 15 q21.3
secretogranin V
(7B2 protein)
Alt. symbolsSGNE1
NCBI gene6447
Other data
LocusChr. 15 q13-q14

Extended group

Some other proteins are also proposed to belong to the granins based on their physico-chemical properties. These include NESP55 (SgVI), VGF (SgVII), and ProSAAS (SgVIII).[8]


  1. ^ 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. doi:10.1016/j.regpep.2003.10.035. PMID 14759560.
  2. ^ Huttner WB, Gerdes HH, Rosa P (January 1991). "The granin (chromogranin/secretogranin) family". Trends in Biochemical Sciences. 16 (1): 27–30. doi:10.1016/0968-0004(91)90012-K. PMID 2053134.
  3. ^ 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. doi:10.1677/joe.0.1650703. PMID 10828855.
  4. ^ 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. doi:10.1186/1756-0500-7-336. PMC 4055239. PMID 24899097.
  5. ^ Höglund OV, Hagman R, Stridsberg M (27 March 2015). "Chromogranin A and cortisol at intraoperative repeated noxious stimuli: Surgical stress in a dog model". SAGE Open Medicine. 3: 2050312115576432. doi:10.1177/2050312115576432. PMC 4679230. PMID 26770773.
  6. ^ 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. doi:10.1186/s13104-016-2193-1. PMC 4969733. PMID 27484122.
  7. ^ 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. doi:10.1186/s13028-016-0274-8. PMC 5210291. PMID 28049540.
  8. ^ Bartolomucci A, Possenti R, Mahata SK, Fischer-Colbrie R, Loh YP, Salton SR (December 2011). "The extended granin family: structure, function, and biomedical implications". Endocrine Reviews. 32 (6): 755–97. doi:10.1210/er.2010-0027. PMC 3591675. PMID 21862681.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR001990

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

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Granin (chromogranin or secretogranin) Provide feedback

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External database links

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, such as:

  • Chromogranin A (CGA): CGA is a protein of about 420 residues; it is the precursor of the peptide pancreastatin which strongly inhibits glucose- induced insulin release from the pancreas.
  • Secretogranin 1 (chromogranin B): A sulfated protein of about 600 residues.
  • Secretogranin 2 (chromogranin C): A sulfated protein of about 650 residues.

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

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Seed source: Prosite
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD , Bateman A
Number in seed: 8
Number in full: 921
Average length of the domain: 347.90 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 86.32 %

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HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.0 25.0
Noise cut-off 24.9 24.6
Model length: 586
Family (HMM) version: 19
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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 7 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 sequence.

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