InterPro : IPR000001

Name  Kringle Short Name  Kringle
Type  Domain Description  Kringles are autonomous structural domains, found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity [, , ]. Kringle domains [, , ]are characterised by a triple loop, 3-disulphide bridge structure, whose conformation is defined by a number of hydrogen bonds and small pieces of anti-parallel beta-sheet. They are found in a varying number of copies in some plasma proteins including prothrombin and urokinase-type plasminogen activator, which are serine proteases belonging to MEROPS peptidase family S1A.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR018056 Kringle, conserved site Kringle_CS Conserved_site

5 Found In

Id Name Short Name Type
IPR001314 Peptidase S1A, chymotrypsin-type Peptidase_S1A Family
IPR003966 Prothrombin/thrombin Prothrombin/thrombin Family
IPR016247 Tyrosine-protein kinase, receptor ROR Tyr_kinase_rcpt_ROR Family
IPR014394 Coagulation factor XIIa/hepatocyte growth factor activator Coagulation_fac_XIIa/HGFA Family
IPR017076 Kremen Kremen Family

1 Parent Features

Id Name Short Name Type
IPR013806 Kringle-like fold Kringle-like Domain

6 Publications

First Author Title Year Journal Volume Pages
Patthy L Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. 1985 Cell 41 657-63
Patthy L Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases. 1984 FEBS Lett 171 131-6
Ikeo K Evolutionary origin of numerous kringles in human and simian apolipoprotein(a). 1991 FEBS Lett 287 146-8
McMullen BA Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). 1985 J Biol Chem 260 5328-41
Atkinson RA Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry. 1990 J Mol Biol 212 541-52
Castellino FJ The genetic relationships between the kringle domains of human plasminogen, prothrombin, tissue plasminogen activator, urokinase, and coagulation factor XII. 1987 J Mol Evol 26 358-69



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)