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)
NLE: 100591992(FURIN)
MCC: 715813(FURIN)
MCF: 102120129(FURIN)
CSAB: 103231185(FURIN)
RRO: 104679270(FURIN)
RBB: 108517214(FURIN)
CJC: 100396662(FURIN)
SBQ: 101030569(FURIN)
MMU: 18550(Furin)
RNO: 54281(Furin)
CGE: 100682534(Furin)
NGI: 103749884(Furin)
HGL: 101717888(Furin)
CCAN: 109695073(Furin)
OCU: 100009442(FURIN)
TUP: 102470724(FURIN)
CFA: 488746(FURIN)
AML: 100475645(FURIN)
UMR: 103660267(FURIN)
ORO: 101370688(FURIN)
FCA: 101100308(FURIN)
PTG: 102959189(FURIN)
AJU: 106965942(FURIN)
BTA: 281374(FURIN)
BOM: 102282121(FURIN)
BIU: 109575483(FURIN)
PHD: 102341327(FURIN)
CHX: 102187990(FURIN)
OAS: 780454(FURIN)
SSC: 100156882(FURIN)
CFR: 102513312(FURIN)
CDK: 105094698(FURIN)
BACU: 103020203(FURIN)
LVE: 103076349(FURIN)
OOR: 101273219(FURIN)
ECB: 100068931(FURIN)
EPZ: 103546212(FURIN)
EAI: 106832050(FURIN)
MYB: 102239137(FURIN)
MYD: 102765324(FURIN)
HAI: 109381481(FURIN)
RSS: 109437119(FURIN)
PALE: 102887466(FURIN)
LAV: 100670249(FURIN)
TMU: 101356016
MDO: 100014434(FURIN)
SHR: 100921198(FURIN)
GGA: 395457(FURIN)
MGP: 100551066(FURIN)
CJO: 107318976(FURIN)
APLA: 101790528
ACYG: 106048640(FURIN)
TGU: 100220259(FURIN)
GFR: 102041810(FURIN)
FAB: 101807647(FURIN)
PHI: 102101328(FURIN)
PMAJ: 107209435(FURIN)
CCAE: 111933939(FURIN)
CCW: 104683851(FURIN)
FPG: 101912812(FURIN)
FCH: 102047991(FURIN)
CLV: 102090604(FURIN)
EGZ: 104125996(FURIN)
ASN: 102382421(FURIN)
CMY: 102933713(FURIN)
CPIC: 101931781(FURIN)
ACS: 100551704(furin)
PBI: 103051998(FURIN)
GJA: 107109710(FURIN)
XLA: 397747(furin.S) 398345(furin.L)
XTR: 100327238(furin)
NPR: 108799145(FURIN)
DRE: 566557(furina) 566591(furinb)
IPU: 108270701 108274716(furin)
TRU: 101061571(furin) 101078322
LCO: 104925266(furin) 104927319
NCC: 104944022(furin) 104964234
MZE: 101479014 101482852(furin)
OLA: 100049240 101158353(furin)
XMA: 102222459 102231939(furin)
PRET: 103462559 103466119(furin)
NFU: 107381331 107388981(furin)
KMR: 108228577 108239969(furin)
LCF: 108875306(furin) 108877754
SDU: 111221567 111228587(furin)
HCQ: 109525872 109530490(furin)
BPEC: 110165934(furin) 110175436
MALB: 109962881 109968745(furin)
ELS: 105016086 105018383(furin)
SFM: 108941070 108942037(furin)
LCM: 102359471(FURIN)
CMK: 103173138 103188561(furin)
CIN: 100175968
SPU: 574878
APLC: 110987280
DME: Dmel_CG10772(Fur1) Dmel_CG18734(Fur2)
DSI: Dsimw501_GD18200(Dsim_GD18200)
MDE: 101893498
AAG: 5578803
BIM: 100740609
BTER: 100650142
SOC: 105194571
AEC: 105149511
ACEP: 105626928
PBAR: 105430658
HST: 105188026
DQU: 106743879
CFO: 105254895
LHU: 105678951
PGC: 109853364
PCF: 106785371
MDL: 103580708
TCA: 661907
DPA: 109541004
NVL: 108560582
BMOR: 692448
PMAC: 106718570
PRAP: 111004261
HAW: 110373817
API: 100166619
DNX: 107162048
CLEC: 106663869
ZNE: 110835312
CEL: CELE_F11A6.1(kpc-1)
CBR: CBG12593(Cbr-bli-4) CBG15803(Cbr-kpc-1)
TSP: Tsp_12023
MYI: 110447249
OBI: 106882877
ADF: 107345646
 » 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 14:265-75 (1990)
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 45:257-70 (1991)
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) 111:296-301 (1992)
Reference
4  [PMID:18407092]
  Authors
Seidah NG, Chretien M
  Title
Proprotein and prohormone convertases of the subtilisin family Recent developments and future perspectives.
  Journal
Trends Endocrinol Metab 3:133-40 (1992)
DOI:10.1016/1043-2760(92)90102-7
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 267:23435-8 (1992)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.75
IUBMB Enzyme Nomenclature: 3.4.21.75
ExPASy - ENZYME nomenclature database: 3.4.21.75
BRENDA, the Enzyme Database: 3.4.21.75
CAS: 141760-45-4

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