{PDOC00634} {PS00799; GRANULINS} {BEGIN} *********************** * Granulins signature * *********************** Granulins [1] are a family of cysteine-rich peptides of about 6 Kd which may have multiple biological activity. A precursor protein (known as acrogranin) potentially encodes seven different forms of granulin (grnA to grnG) which are probably released by post-translational proteolytic processing. A schematic representation of the structure of a granulin is shown below: xxxCxxxxxCxxxxxCCxxxxxxxxCCxxxxxxCCxxxxxCCxxxxxCxxxxxxCx ************** 'C': conserved cysteine probably involved in a disulfide bond. '*': position of the pattern. Granulins are evolutionary related to a PMP-D1, a peptide extracted from the pars intercerebralis of migratory locusts [2]. -Consensus pattern: C-x-D-x(2)-H-C-C-P-x(4)-C [The 4 C's may be involved in disulfide bonds] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: May 2004 / Text revised. [ 1] Bhandari V., Palfree R.G., Bateman A. "Isolation and sequence of the granulin precursor cDNA from human bone marrow reveals tandem cysteine-rich granulin domains." Proc. Natl. Acad. Sci. U.S.A. 89:1715-1719(1992). PubMed=1542665 [ 2] Nakakura N., Hietter H., Van Dorsselaer A., Luu B. "Isolation and structural determination of three peptides from the insect Locusta migratoria. Identification of a deoxyhexose-linked peptide." Eur. J. Biochem. 204:147-153(1992). PubMed=1740125 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}