Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST.
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS. To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017. From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
The vitamin K-dependent blood coagulation factor IX as well as several
extracellular regulatory proteins require vitamin K for the posttranslational
synthesis of γ-carboxyglutamic acid, an amino acid clustered in the
N-terminal Gla domain of these proteins [1,2]. The Gla domain is a membrane
binding motif which, in the presence of calcium ions, interacts with
phospholipid membranes that include phosphatidylserine.
The 3D structure of the Gla domain has been solved (see for example
<PDB:1CFH>) [3,4]. Calcium ions induce conformational changes in the Gla
domain and are necessary for the Gla domain to fold properly. A common
structural feature of functional Gla domains is the clustering of N-terminal
hydrophobic residues into a hydrophobic patch that mediates interaction with
the cell surface membrane .
Proteins known to contain a Gla domain are listed below:
A number of plasma proteins involved in blood coagulation. These proteins
are prothrombin, coagulation factors VII, IX and X, proteins C, S, and Z.
Two proteins that occur in calcified tissues: osteocalcin (also known as
bone-Gla protein, BGP), and matrix Gla-protein (MGP).
Cone snail venom peptides: conantokin-G and -T, and conotoxin GS .
The pattern we developed start with the conserved Gla-x(3)-Gla-x-Cys motif
found in the middle of the domain which seems to be important for substrate
recognition by the carboxylase  and end with the last conserved position of
the domain (an aromatic residue). We also developed a profile that covers the
whole Gla domain.
All glutamic residues present in the domain are potential carboxylation
sites; in coagulation proteins, all are modified to Gla, while in BGP and MGP
some are not.
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.