Xenbase is undergoing scheduled maintenance Wednesday, June 14 and Thursday, June 15, 2023. Xenbase will be unavailable on those days.

Click on this message to dismiss it.
Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Int J Pept Protein Res 1995 Nov 01;465:419-23. doi: 10.1111/j.1399-3011.1995.tb01076.x.
Show Gene links Show Anatomy links

Amino-acid sequence of bone Gla protein from the African clawed toad Xenopus laevis and the fish Sparus aurata.

Cancela ML , Williamson MK , Price PA .

As an initial step in the analysis of bone Gla protein (BGP; osteocalcin) function in lower vertebrates, we have developed a simple and rapid method for the isolation of BGP from bone and have applied this to the isolation of BGP from the African clawed toad Xenopus laevis and the fish Sparus aurata. We have also determined the complete amino-acid sequence of Sparus and Xenopus BGP, including the identification of the sites of y-carboxylation. Since the addition of Xenopus and Sparus BGP sequences significantly extends the range of species whose BGP structures are known, we have compared the 18 presently known BGP sequences. Twelve amino acids are invariant in these 18 BGP sequences and are therefore presumably critical to BGP conformation or function. Eight of these 12 invariant amino acids are also invariant in all presently known matrix Gla protein sequences (shark, mouse, rat, cow, human), an observation which strongly supports the evolutionary relationship between these two vitamin K-dependent bone proteins and suggests that the proteins may adapt similar tertiary structures.

PubMed ID: 8567186
Article link: Int J Pept Protein Res
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: bglap2 gla mgp nat8.5