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Granin

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Granin (chromogranin or secretogranin)
Structure of SS-cyclized catestatin fragment from chromogranin A.[1]
Identifiers
SymbolGranin
PfamPF01271
InterProIPR001990
PROSITEPDOC00365
SCOP21cfk / SCOPe / SUPFAM
OPM superfamily328
OPM protein1lv4
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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]

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.

Members

Chromogranins

chromogranin A
(parathyroid secretory protein 1)
Identifiers
SymbolCHGA
Alt. symbolsCGA
NCBI gene1113
HGNC1929
OMIM118910
RefSeqNM_001275
UniProtP10645
Other data
LocusChr. 14 q32
Search for
StructuresSwiss-model
DomainsInterPro
chromogranin B
(secretogranin 1)
Identifiers
SymbolCHGB
Alt. symbolsSCG1
NCBI gene1114
HGNC1930
OMIM118920
RefSeqNM_001819
UniProtP05060
Other data
LocusChr. 20 pter-p12
Search for
StructuresSwiss-model
DomainsInterPro


Secretogranins

secretogranin II
(chromogranin C)
Identifiers
SymbolSCG2
Alt. symbolsCHGC, SgII
NCBI gene7857
HGNC10575
OMIM118930
RefSeqNM_003469
UniProtP13521
Other data
LocusChr. 2 q35-q36
Search for
StructuresSwiss-model
DomainsInterPro
secretogranin III
(FLJ90833)
Identifiers
SymbolSCG3
Alt. symbolsSGIII
NCBI gene29106
HGNC13707
OMIM611796
RefSeqNM_013243
UniProtQ8WXD2
Other data
LocusChr. 15 q21.3
Search for
StructuresSwiss-model
DomainsInterPro
secretogranin V
(7B2 protein)
Identifiers
SymbolSCG5
Alt. symbolsSGNE1
NCBI gene6447
HGNC10816
OMIM173120
RefSeqNM_003020
UniProtP05408
Other data
LocusChr. 15 q13-q14
Search for
StructuresSwiss-model
DomainsInterPro


Two other proteins (secretogranin IV and VI) are also proposed to belong to the granins on the basis of their physico-chemical properties.

References

  1. ^ Preece NE, Nguyen M, Mahata M; et al. (2004). "Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A". Regul. Pept. 118 (1–2): 75–87. doi:10.1016/j.regpep.2003.10.035. PMID 14759560. {{cite journal}}: Explicit use of et al. in: |author= (help); Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ Huttner WB, Gerdes HH, Rosa P (1991). "The granin (chromogranin/secretogranin) family". Trends Biochem. Sci. 16 (1): 27–30. doi:10.1016/0968-0004(91)90012-K. PMID 2053134. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
This article incorporates text from the public domain Pfam and InterPro: IPR001990