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CATH Superfamily 4.10.400.10

Low-density Lipoprotein Receptor

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Low-density Lipoprotein Receptor
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 12090: Low-density lipoprotein receptor-related protein

There are 5 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Complement factor I. [EC: 3.4.21.45]
Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage.
  • Cleavage of complement subcomponent C3b requires its binding to cofactor H or complement receptor CR1; cleavage of iC3b requires complement receptor CR1; cleavage of C4b requires C4b-binding protein.
  • Belongs to peptidase family S1.
 9 B7P761 B7P761 B7P761 B7P9Y0 B7PJ49 B7PJ49 B7PJ49 B7QBX8 B7QKE3
Receptor protein-tyrosine kinase. [EC: 2.7.10.1]
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
  • The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans.
  • In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies.
  • Formerly EC 2.7.1.112.
 5 A0A0P5CPS6 B7PJ49 B7PJ49 B7PJ49 B7QBX8
Enteropeptidase. [EC: 3.4.21.9]
Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.
  • Activates trypsinogen.
  • Not inhibited by protein inhibitors of trypsin.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.8.
 5 B7P761 B7P761 B7P761 B7P9Y0 B7QBX8
Procollagen C-endopeptidase. [EC: 3.4.24.19]
Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III.
  • The activity is increased by calcium and by an enhancer glycoprotein.
 3 B7PJ49 B7PJ49 B7PJ49
Coagulation factor Xa. [EC: 3.4.21.6]
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
  • A blood coagulation factor formed from the proenzyme factor X by limited proteolysis.
  • Factor X is a glycoprotein composed of a heavy chain and a light chain, which are generated from a precursor protein by the excision of the tripeptide RKR and held together by one or more disulfide bonds.
  • The activated factor Xa converts prothrombin to thrombin in the presence of factor Va, Ca(2+) and phospholipids.
  • Scutelarin (EC 3.4.21.60) has similar specificity, but does not require factor Va.
  • Belongs to peptidase family S1.
 1 B7QKE3