CLV_PCSK_KEX2_1
ELM server details
ELM
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Functional site class:
 PCSK cleavage site
Functional site description:
 The subtilisin-like proprotein convertases are expressed extensively in mammalian neural and endocrine cells and play a major role in the proteolytic processing of both neuropeptide and peptide hormone precursors.
ELM(s): CLV_PCSK_PC1ET2_1, CLV_PCSK_SKI1_1, CLV_PCSK_KEX2_1, CLV_PCSK_FUR_1, CLV_PCSK_PC7_1
CLV_PCSK_KEX2_1 description: Yeast kexin 2 cleavage site (Lys-Arg-|-Xaa or Arg-Arg-|-Xaa)
Pattern: [KR]R.
Present in taxon(s): Metazoa  
Not represented in taxon(s): Vertebrata  

o Abstract

The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products.
The prohormone-processing yeast KEX2 protease can act as an intracellular membrane protein or a soluble, secreted endopeptidase. The protein is required for processing of precursors of alpha-factor and killer toxin.
PCSK1 (proprotein convertase 1, NEC1) and PCSK2 (proprotein convertase 2, NEC2) are type I proinsulin-processing enzymes that play a key role in regulating insulin biosynthesis. They are also known to cleave proopiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and progastrin.
PACE4 (paired basic amino acid cleaving system 4, SPC4) is a calcium-dependent serine endoprotease that can cleave precursor
protein at their paired basic amino acid processing sites. Some of its substrates are - transforming growth factor beta related proteins, proalbumin, and von Willebrand factor.
Furin (PACE, paired basic amino acid cleaving enzyme, membrane associated receptor protein) is serine endoprotease responsible for
processing variety of substrates (proparathyroid hormone, transforming growth factor beta 1 precursor, proalbumin, pro-beta-secretase, membrane type-1 matrix metalloproteinase, beta subunit of pro-nerve growth factor and von Willebrand factor).
PC7 (proprotein convertase subtilisin/kexin type 7) is a closely related to PACE and PACE4. This calcium-dependent serine endoprotease is concentrated in the trans-Golgi network, associated with the membranes, and is not secreted. It can process proalbumin. PC7 and furin are also thought to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 and gp140.

o Selected references

Brenner C, Fuller RS
Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease.
Proc Natl Acad Sci U S A 1992 Feb 1;89(3) : 922-6.
PMID: 1736307

Fuller RS, Brake A, Thorner J
Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease.
Proc Natl Acad Sci U S A 1989 Mar;86(5) : 1434-8.
PMID: 2646633

Germain D, Dumas F, Vernet T, Bourbonnais Y, Thomas DY, Boileau G
The pro-region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self-processing.
FEBS Lett 1992 Mar 16;299(3) : 283-6.
PMID: 1544507

Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H
Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases.
Biochem Biophys Res Commun 1988 Oct 14;156(1) : 246-54.
PMID: 2845974

o This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.

Biological Process
  proteolysis and peptidolysis
Cellular Component
  extracellular
  Golgi apparatus
Molecular Function
  kexin

 

o Instances for CLV_PCSK_KEX2_1

No instances annotated