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PROSITE documentation PDOC00756 |
A variety of GPI-linked cell-surface glycoproteins are composed of one or more copies of a conserved domain of about 100 amino-acid residues [1,2]. These proteins are:
U-PAR contains three tandem copies of the domain, while all the others are made up of a single domain.
As shown in the following schematic, this conserved domain contains 10 cysteine residues involved in five disulfide bonds - in u-PAR, the first copy of the domain lacks the fourth disulfide bond.
+------+ +------------------------+ +---+ | | | | | | xCxxCxxxxxxCxxxxxCxxxxxCxxxxxxxxxxxxxxxxxxCxxxxCxxxxxxxxxxxxxxCCxxxCxxxxxxxx | | | | +---------------------+ +--------------+
'C': conserved cysteine involved in a disulfide bond.
The signature pattern that detects this domain starts towards its extremity and ends at the sixth cysteine.
Last update:May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Behrendt N. Ploug M. Patthy L. Houen G. Blasi F. Dano K. |
Title | The ligand-binding domain of the cell surface receptor for urokinase-type plasminogen activator. | |
Source | J. Biol. Chem. 266:7842-7847(1991). | |
PubMed ID | 1850423 |
2 | Authors | Ploug M. Kjalke M. Ronne E. Weidle U. Hoyer-Hansen G. Dano K. |
Title | Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator. A domain structure belonging to a novel superfamily of glycolipid-anchored membrane proteins. | |
Source | J. Biol. Chem. 268:17539-17546(1993). | |
PubMed ID | 8394346 |