PROSITE documentation PDOC00979
Glucokinase regulatory protein family signature


The glucokinase regulatory protein (GCKR) [1] is a vertebrate protein that inhibits glucokinase by forming a complex with the enzyme, which plays a role in the control of blood glucose homeostasis. GCKR is a protein of about 70 Kd which is evolutionary related to bacterial N-acetylmuramic acid 6-phosphate etherases (MurNAc-6-P etherase, murQ) which are about half the size of GCKR and form active homodimers. MurNAc-6-P etherases catalyze the cleavage of the D-lactyl ether substituent of the bacterial cell wall sugar MurNAc and play a role in recycling of the cell wall [2]. The 3D structure of the Haemophilus influenzae HI0754/murQ protein (see <PDB:1NRI>) shows structural relationships with other sugar isomerase (SIS) domain proteins (see <PDOC51464>). In contrast to mono-SIS bacterial MurNAc-6-P etherase, mammalian GCKR is composed of two SIS domains.

As a signature pattern, we selected one of at least four well conserved regions found in those proteins.

Last update:

September 2009 / Text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

GCKR, PS01272; Glucokinase regulatory protein family signature  (PATTERN)


1AuthorsVeiga-Da-Cunha M. Detheux M. Watelet N. Van Schaftingen E.
TitleCloning and expression of a Xenopus liver cDNA encoding a fructose-phosphate-insensitive regulatory protein of glucokinase.
SourceEur. J. Biochem. 225:43-51(1994).
PubMed ID7925465

2AuthorsJaeger T. Mayer C.
TitleN-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism.
SourceCell. Mol. Life Sci. 65:928-939(2008).
PubMed ID18049859

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