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:

"
Peptidase S8/S53 domain
".

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 10272: Proprotein convertase subtilisin/kexin type

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
Furin. [EC: 3.4.21.75]
Release of mature proteins from their proproteins by cleavage of -Arg- Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.
  • Activated by calcium.
  • Belongs to peptidase family S8.
32 A0A024RC70 A0A024RC70 B7PMP4 B7PMP4 B7PPF6 B7PPF6 C1LG70 C1LG70 C1LG71 C1LG71
(22 more...)
Proprotein convertase 2. [EC: 3.4.21.94]
Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
  • A calcium dependent enzyme, maximally active at about pH 5.5.
  • Specificity is broader than that of prohormone convertase 1.
  • Substrates include pro-opiomelanocortin, proenkephalin, prodynorphin, proinsulin and proluteinizing-hormone-releasing hormone.
  • Unlike prohormone convertase 1, does not cleave prorenin or prosomatostatin.
  • Usually processing of prodynorphin occurs at a bond in which P2 is Thr.
  • Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 1.
  • Belongs to peptidase family S8.
30 A1IHD0 A1IHD0 B2ZRZ7 B2ZRZ7 B7Q266 B7Q266 C1LEI4 C1LEI4 E0VP88 E0VP88
(20 more...)
Kexin. [EC: 3.4.21.61]
Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors.
  • Calcium activated.
  • Inhibited by p-mercuribenzoate.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.22.23.
30 A0A075FQ13 A0A075FQ13 A0A0F4YH34 A0A0F4YH34 A0A0J5Q4U6 A0A0J5Q4U6 A0A0L8VI93 A0A0L8VI93 A2Q9N6 A2Q9N6
(20 more...)
Proprotein convertase 1. [EC: 3.4.21.93]
Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
  • A calcium dependent enzyme, maximally active at about pH 5.5.
  • Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin.
  • Unlike prohormone convertase 2, does not cleave proluteinizing- hormone-releasing hormone.
  • Usually processing of prodynorphin occurs at a bond in which P2 is Thr.
  • Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 2.
  • Belongs to peptidase family S8.
16 B7PYT9 B7PYT9 E0VJJ3 E0VJJ3 P28840 P28840 P29120 P29120 P63239 P63239
(6 more...)
Mitogen-activated protein kinase. [EC: 2.7.11.24]
ATP + a protein = ADP + a phosphoprotein.
  • Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2 is necessary for enzyme activation.
  • Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline.
  • A distinguishing feature of all MAPKs is the conserved sequence Thr- Xaa-Tyr (TXY).
  • Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation.
  • Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischemeic injury.
  • Formerly EC 2.7.1.37.
2 A0A177BA79 A0A177BA79