KEGG   ENZYME: 3.4.21.75Help
Entry
EC 3.4.21.75                Enzyme                                 

Name
furin;
prohormone convertase;
dibasic processing enzyme;
PACE;
paired basic amino acid cleaving enzyme;
paired basic amino acid converting enzyme;
serine proteinase PACE;
PC1;
SPC3;
proprotein convertase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg! bonds, where Xaa can by any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors
Comment
One of a group of peptidases in peptidase family S8 (subtilisin family) that is structurally and functionally similar to kexin. All are activated by Ca2+, contain Cys near the active site His, and are inhibited by p-mercuribenzoate. At least three related enzymes are recognized in mammals: PC2, PC3 and PC4, which have somewhat different specificities
History
EC 3.4.21.75 created 1993
Orthology
K01349  
furin
Genes
HSA: 
5045(FURIN)
PTR: 
453652(FURIN)
PPS: 
100978848(FURIN)
GGO: 
101128325(FURIN)
PON: 
100448725(FURIN)
MCC: 
715813(FURIN)
MCF: 
102120129(FURIN)
MMU: 
18550(Furin)
RNO: 
54281(Furin)
CGE: 
100682534(Furin)
HGL: 
101717888(Furin)
TUP: 
102470724(FURIN)
CFA: 
488746(FURIN)
AML: 
100475645(FURIN)
FCA: 
101100308(FURIN)
PTG: 
102959189(FURIN)
BTA: 
281374(FURIN)
BOM: 
102282121(FURIN)
PHD: 
102341327(FURIN)
CHX: 
102187990(FURIN)
OAS: 
780454(FURIN)
SSC: 
100156882(FURIN)
CFR: 
102513312(FURIN)
BACU: 
103020203(FURIN)
LVE: 
103076349(FURIN)
ECB: 
100068931(FURIN)
MYB: 
102239137(FURIN)
MYD: 
102765324(FURIN)
PALE: 
102887466(FURIN)
MDO: 
100014434(FURIN)
SHR: 
100921198(FURIN)
GGA: 
395457(FURIN)
MGP: 
TGU: 
100220259(FURIN)
FAB: 
101807647(FURIN)
PHI: 
102101328(FURIN)
APLA: 
101790528(FURIN)
FPG: 
101912812(FURIN)
FCH: 
102047991(FURIN)
CLV: 
102090604(FURIN)
ASN: 
102382421(FURIN)
AMJ: 
102566936(FURIN)
CMY: 
102933713(FURIN)
ACS: 
100551704(furin)
PBI: 
103051998(FURIN)
XLA: 
397747(Furin-1) 398345(furin)
XTR: 
100327238(furin)
DRE: 
566557(furina) 566591(furinb)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102359471(FURIN)
CMK: 
BFO: 
CIN: 
SPU: 
574878(furin)
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
725466(Fur1)
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CBR: 
CBG12593(Cbr-bli-4) CBG15803(Cbr-kpc-1)
BMY: 
LOA: 
TSP: 
AQU: 
ACAN: 
 » show all
Taxonomy
Reference
1  [PMID:2094803]
  Authors
van de Ven WJ, Voorberg J, Fontijn R, Pannekoek H, van den Ouweland AM, van Duijnhoven HL, Roebroek AJ, Siezen RJ.
  Title
Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes.
  Journal
Mol. Biol. Rep. 14 (1990) 265-75.
Reference
2  [PMID:1843280]
  Authors
Van de Ven WJ, Creemers JW, Roebroek AJ.
  Title
Furin: the prototype mammalian subtilisin-like proprotein-processing enzyme. Endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway.
  Journal
Enzyme. 45 (1991) 257-70.
Reference
3  [PMID:1587790]
  Authors
Hatsuzawa K, Murakami K, Nakayama K.
  Title
Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites.
  Journal
J. Biochem. (Tokyo). 111 (1992) 296-301.
Reference
4
  Authors
Seidah, N.G. and Chretien, M.
  Title
Proprotein and prohormone convertases of the subtilisin family: recent developments and future perspectives.
  Journal
Trends Endocrinol. Metab. 3 (1992) 133-140.
Reference
5  [PMID:1429684]
  Authors
Steiner DF, Smeekens SP, Ohagi S, Chan SJ.
  Title
The new enzymology of precursor processing endoproteases.
  Journal
J. Biol. Chem. 267 (1992) 23435-8.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
141760-45-4

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