The domain within your query sequence starts at position 87 and ends at position 463; the E-value for the Granin domain shown below is 1.7e-95.

AKERAQQPLKQQQPPKQQQQQQQQQQQEQQHSSFEDELSEVFENQSPDAKHRDAAAEVPS
RDTMEKRKDSDKGQQDGFEATTEGPRPQAFPEPNQESPMMGDSESPGEDTATNTQSPTSL
PSQEHVDPQATGDSERGLSAQQQARKAKQEEKEEEEEEEAVAREKAGPEEVPTAASSSHF
HAGYKAIQKDDGQSDSQAVDGDGKTEASEALPSEGKGELEHSQQEEDGEEAMVGTPQGLF
PQGGKGRELEHKQEEEEEEEERLSREWEDKRWSRMDQLAKELTAEKRLEGEDDPDRSMKL
SFRTRAYGFRDPGPQLRRGWRPSSREDSVEARSDFEEKKEEEGSANRRAEDQELESLSAI
EAELEKVAHQLQALRRG

Granin

Granin
PFAM accession number:PF01271
Interpro abstract (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.

GO component:secretory granule (GO:0030141)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Granin