KEGG   ENZYME: 3.4.21.42Help
Entry
EC 3.4.21.42                Enzyme                                 

Name
complement subcomponent C_overbar_1s_;
C1 esterase;
activated complement C1s;
complement C_overbar_1r_
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Cleavage of Arg!Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)!Lys bond in complement component C2 to form C2a and C2b: the "classical" pathway C3 convertase
Comment
Activated from proenzyme C1s in plasma by complement subcomponent C_overbar_1r_. In peptidase family S1 (trypsin family)
History
EC 3.4.21.42 created 1981
Orthology
K01331  complement component 1, s subcomponent
Genes
HSA: 716(C1S)
PTR: 451808(C1S)
PPS: 100991971(C1S)
GGO: 101145266(C1S)
PON: 100455685(C1S)
NLE: 100599399(C1S)
MCC: 714589(C1S)
MCF: 102134687 102137207(C1S)
CSAB: 103218499 103218857(C1S)
RRO: 104659255 104660154 104664861 104681691(C1S) 104681692
CJC: 100412274(C1S)
SBQ: 101034947(C1S)
MMU: 317677(C1s2) 50908(C1s1)
RNO: 192262(C1s)
CGE: 100759777(C1s)
NGI: 103727488(C1s)
HGL: 101697979(C1s)
CCAN: 109682778(C1s)
OCU: 100348898(C1S)
TUP: 102487452 102496444(C1S)
CFA: 486714(C1S)
AML: 100472516(C1S)
UMR: 103656176(C1S)
ORO: 101377797(C1S)
FCA: 101088676(C1S)
PTG: 102948650(C1S)
AJU: 106965335(C1S)
BTA: 767827(C1S)
BOM: 102285301(C1S)
BIU: 109558903(C1S)
PHD: 102326599(C1S)
CHX: 102189289(C1S)
OAS: 101107688(C1S)
SSC: 397274(C1S)
CFR: 102513921(C1S)
CDK: 105098188(C1S)
BACU: 103003533(C1S)
LVE: 103085588(C1S)
OOR: 101269409(C1S)
ECB: 100060261(C1S)
EPZ: 103563702(C1S)
EAI: 106847309(C1S)
MYB: 102255615(C1S)
MYD: 102755154(C1S)
HAI: 109373658(C1S)
RSS: 109459715(C1S)
PALE: 102897110(C1S)
LAV: 100676140(C1S)
TMU: 101344169
MDO: 100016766(C1S)
SHR: 100917190(C1S)
OAA: 100085003(C1S)
GGA: 418294(C1S)
MGP: 100549400(C1S)
CJO: 107318599(C1S)
APLA: 101791779(C1S)
ACYG: 106047861(C1S)
TGU: 100222051(C1S)
GFR: 102043120(C1S)
FAB: 101809291(C1S)
PHI: 102112114(C1S)
PMAJ: 107207087(C1S)
CCAE: 111938155(C1S)
CCW: 104687135(C1S)
FPG: 101915039(C1S)
FCH: 102049047(C1S)
CLV: 102093208(C1S)
EGZ: 104126544(C1S)
AAM: 106497286(C1S)
ASN: 102373441(C1S)
AMJ: 102572422(C1S)
CMY: 102946599(C1S)
CPIC: 101944626(C1S)
ACS: 100558615(c1s) 100560720
PVT: 110084650(C1S)
PBI: 103065043(C1S)
XLA: 733422(c1s.L)
XTR: 613055(c1s)
NPR: 108784394(C1S)
CCAR: 109104855
AMEX: 103027368
TRU: 101072918
NCC: 104941464
MZE: 105940904
LCF: 108880738
BPEC: 110163037
ELS: 105009774
LCM: 102354579(C1S)
 » show all
Taxonomy
Reference
1  [PMID:6281620]
  Authors
Sim RB.
  Title
The human complement system serine proteases C1r and C1s and their proenzymes.
  Journal
Methods Enzymol 80 Pt C:26-42 (1981)
Reference
2  [PMID:3500856]
  Authors
Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE.
  Title
Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence.
  Journal
Eur J Biochem 169:547-53 (1987)
DOI:10.1111/j.1432-1033.1987.tb13644.x
  Sequence
[hsa:716]
Reference
3  [PMID:3052276]
  Authors
Muller-Eberhard HJ.
  Title
Molecular organization and function of the complement system.
  Journal
Annu Rev Biochem 57:321-47 (1988)
DOI:10.1146/annurev.bi.57.070188.001541
Reference
4  [PMID:2500154]
  Authors
Skoog MT, Mehdi S, Wiseman JS, Bey P.
  Title
The specificity of two proteinases that cleave adjacent to arginine, C1 esterase and acrosin, for peptide p-nitroanilide substrates.
  Journal
Biochim Biophys Acta 996:89-94 (1989)
DOI:10.1016/0167-4838(89)90099-X
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.42
IUBMB Enzyme Nomenclature: 3.4.21.42
ExPASy - ENZYME nomenclature database: 3.4.21.42
BRENDA, the Enzyme Database: 3.4.21.42
CAS: 80295-70-1

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