InterPro : IPR013806

Name  Kringle-like fold Short Name  Kringle-like
Type  Domain Description  This entry represents proteins displaying a Kringle-like structure, which consists of a nearly all-beta, disulphide-rich fold. Proteins displaying this fold include both Kringle modules as well as fibronectin type II modules, the latter displaying a shorter two-disulphide version of the Kringle module.Kringle modules occur in blood clotting and fibrinolytic proteins, such as plasminogen, prothrombin, meizothrombin, and urokinase-type plasminogen activator, as well as in apolipoprotein and hepatocyte growth factor. 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 [, ].Fibronectin type II modules occur in fibronectin, as well as in gelatinase A (MMP-2), gelatinase B (MMP-9), and the collagen-binding domain of PDC-109. Fibronectin is a multi-domain glycoprotein, found in a soluble form in plasma, and in an insoluble form in loose connective tissue and basement membranes, that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin []. Fibronectins are involved in a number of important functions e.g., wound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis. Gelatinases A and B are members of the matrix metalloproteinase family that act as neutral proteinases in the breakdown and remodelling of the extracellular matrix. These gelatinases play important roles in the pathogenesis of inflammation, infection and in neoplastic diseases []. In gelatinase A, the three fibronectin-like modules are inserted within a catalytic domain, these modules acting to target the enzyme to matrix macromolecules [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR000562 Fibronectin, type II, collagen-binding FN_type2_col-bd Domain
IPR000001 Kringle Kringle Domain

1 Contains

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

2 Found In

Id Name Short Name Type
IPR003966 Prothrombin/thrombin Prothrombin/thrombin Family
IPR016247 Tyrosine-protein kinase, receptor ROR Tyr_kinase_rcpt_ROR Family

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
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
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
Skorstengaard K Complete primary structure of bovine plasma fibronectin. 1986 Eur J Biochem 161 441-53
Chakrabarti S Matrix metalloproteinase-2 (MMP-2) and MMP-9 in pulmonary pathology. 2005 Exp Lung Res 31 599-621
Hornebeck W Fibronectin type II (FnII)-like modules regulate gelatinase A activity. 2005 Pathol Biol (Paris) 53 405-10

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)