Complement component 1s

C1S
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1ELV, 1NZI, 4J1Y, 4LMF, 4LOR, 4LOS, 4LOT
Identifiers
Aliases	C1S, EDSPD2, complement C1s
External IDs	OMIM: 120580 MGI: 3644269 HomoloGene: 1314 GeneCards: C1S
EC number	3.4.21.42
Gene location (Human)
Chr.	Chromosome 12 (human)[1]
End	7,071,032 bp[1]
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)[2]
End	124,636,085 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• calcium ion binding; • peptidase activity; • serine-type peptidase activity; • GO:0001948 protein binding; • hydrolase activity; • metal ion binding; • identical protein binding; • serine-type endopeptidase activity;
Cellular component	• blood microparticle; • extracellular exosome; • extracellular region; • extracellular;
Biological process	• proteolysis; • classical complement pathway; • immune system process; • innate immune system; • complement activation, lectin pathway; • complement activation; • regulation of complement activation;
	Sources:Amigo / QuickGO
Orthologs
	716
	317677
	ENSG00000182326
	ENSMUSG00000079343
	P09871
	Q8CFG8
	NM_001734; NM_201442; NM_001346850
	NM_173864
	NP_001333779; NP_001725; NP_958850
	NP_776289
	Wikidata
View/Edit Human	View/Edit Mouse

Complement component 1s (EC 3.4.21.42, C1 esterase, activated complement C1s, complement C overbar 1r, C1s) is a protein involved in the complement system. C1s is part of the C1 complex.[5][6][7][8] In humans, it is encoded by the C1S gene.[9]

C1s cleaves C4 and C2, which eventually leads to the production of the classical pathway C3-convertase.

Classical pathway. (Some labels are in Polish.)

References

GRCh38: Ensembl release 89: ENSG00000182326 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000079343 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Sim RB (1981). "The human complement system serine proteases C1r and C1s and their proenzymes". Methods in Enzymology. 80 Pt C: 26–42. doi:10.1016/s0076-6879(81)80006-7. PMID 6281620.
Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE (December 1987). "Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence". European Journal of Biochemistry. 169 (3): 547–53. doi:10.1111/j.1432-1033.1987.tb13644.x. PMID 3500856.
Müller-Eberhard HJ (1988). "Molecular organization and function of the complement system". Annual Review of Biochemistry. 57: 321–47. doi:10.1146/annurev.bi.57.070188.001541. PMID 3052276.
Skoog MT, Mehdi S, Wiseman JS, Bey P (June 1989). "The specificity of two proteinases that cleave adjacent to arginine, C1 esterase and acrosin, for peptide p-nitroanilide substrates". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 996 (1–2): 89–94. doi:10.1016/0167-4838(89)90099-x. PMID 2500154.
"Entrez Gene: C1S Complement component 1, s subcomponent".

Luo C, Thielens NM, Gagnon J, Gal P, Sarvari M, Tseng Y, Tosi M, Zavodszky P, Arlaud GJ, Schumaker VN (May 1992). "Recombinant human complement subcomponent C1s lacking beta-hydroxyasparagine, sialic acid, and one of its two carbohydrate chains still reassembles with C1q and C1r to form a functional C1 complex". Biochemistry. 31 (17): 4254–62. doi:10.1021/bi00132a015. PMID 1533159.
Illy C, Thielens NM, Gagnon J, Arlaud GJ (July 1991). "Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-dependent interactions of human C1s. Location of the iodination sites". Biochemistry. 30 (29): 7135–41. doi:10.1021/bi00243a014. PMID 1854725.
Hess D, Schaller J, Rickli EE (March 1991). "Identification of the disulfide bonds of human complement C1s". Biochemistry. 30 (11): 2827–33. doi:10.1021/bi00225a014. PMID 2007122.
Thielens NM, Van Dorsselaer A, Gagnon J, Arlaud GJ (April 1990). "Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region". Biochemistry. 29 (14): 3570–8. doi:10.1021/bi00466a021. PMID 2141278.
Busby TF, Ingham KC (May 1990). "NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- with C1q". Biochemistry. 29 (19): 4613–8. doi:10.1021/bi00471a016. PMID 2372546.
Kusumoto H, Hirosawa S, Salier JP, Hagen FS, Kurachi K (October 1988). "Human genes for complement components C1r and C1s in a close tail-to-tail arrangement". Proceedings of the National Academy of Sciences of the United States of America. 85 (19): 7307–11. doi:10.1073/pnas.85.19.7307. PMC 282175. PMID 2459702.
Katz Y, Strunk RC (March 1989). "Synthesis and regulation of C1 inhibitor in human skin fibroblasts". Journal of Immunology. 142 (6): 2041–5. PMID 2537870.
Tosi M, Duponchel C, Meo T, Couture-Tosi E (August 1989). "Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin". Journal of Molecular Biology. 208 (4): 709–14. doi:10.1016/0022-2836(89)90161-7. PMID 2553984.
Tosi M, Duponchel C, Meo T, Julier C (December 1987). "Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr". Biochemistry. 26 (26): 8516–24. doi:10.1021/bi00400a004. PMID 2831944.
Nguyen VC, Tosi M, Gross MS, Cohen-Haguenauer O, Jegou-Foubert C, de Tand MF, Meo T, Frézal J (April 1988). "Assignment of the complement serine protease genes C1r and C1s to chromosome 12 region 12p13". Human Genetics. 78 (4): 363–8. doi:10.1007/BF00291737. PMID 2834284. S2CID 30582112.
Spycher SE, Nick H, Rickli EE (April 1986). "Human complement component C1s. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation". European Journal of Biochemistry. 156 (1): 49–57. doi:10.1111/j.1432-1033.1986.tb09546.x. PMID 3007145.
Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE (December 1987). "Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence". European Journal of Biochemistry. 169 (3): 547–53. doi:10.1111/j.1432-1033.1987.tb13644.x. PMID 3500856.
Kauffman D, Hofmann T, Bennick A, Keller P (May 1986). "Basic proline-rich proteins from human parotid saliva: complete covalent structures of proteins IB-1 and IB-6". Biochemistry. 25 (9): 2387–92. doi:10.1021/bi00357a013. PMID 3521730.
Bock SC, Skriver K, Nielsen E, Thøgersen HC, Wiman B, Donaldson VH, Eddy RL, Marrinan J, Radziejewska E, Huber R (July 1986). "Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization". Biochemistry. 25 (15): 4292–301. doi:10.1021/bi00363a018. PMID 3756141.
Carter PE, Dunbar B, Fothergill JE (December 1983). "The serine proteinase chain of human complement component C1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments". The Biochemical Journal. 215 (3): 565–71. doi:10.1042/bj2150565. PMC 1152437. PMID 6362661.
Nilsson T, Sjöholm I, Wiman B (September 1983). "Structural and circular-dichroism studies on the interaction between human C1-esterase inhibitor and C1s". The Biochemical Journal. 213 (3): 617–24. doi:10.1042/bj2130617. PMC 1152176. PMID 6604523.
Rossi V, Gaboriaud C, Lacroix M, Ulrich J, Fontecilla-Camps JC, Gagnon J, Arlaud GJ (June 1995). "Structure of the catalytic region of human complement protease C1s: study by chemical cross-linking and three-dimensional homology modeling". Biochemistry. 34 (22): 7311–21. doi:10.1021/bi00022a004. PMID 7779774.
Bersch B, Hernandez JF, Marion D, Arlaud GJ (February 1998). "Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family". Biochemistry. 37 (5): 1204–14. doi:10.1021/bi971851v. PMID 9477945.
Endo Y, Takahashi M, Nakao M, Saiga H, Sekine H, Matsushita M, Nonaka M, Fujita T (November 1998). "Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates". Journal of Immunology. 161 (9): 4924–30. PMID 9794427.
Inoue N, Saito T, Masuda R, Suzuki Y, Ohtomi M, Sakiyama H (October 1998). "Selective complement C1s deficiency caused by homozygous four-base deletion in the C1s gene". Human Genetics. 103 (4): 415–8. doi:10.1007/s004390050843. PMID 9856483. S2CID 7689382.

External links

Complement+C1s at the US National Library of Medicine Medical Subject Headings (MeSH)
Human C1S genome location and C1S gene details page in the UCSC Genome Browser.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000182326 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000079343 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Sim RB (1981). "The human complement system serine proteases C1r and C1s and their proenzymes". Methods in Enzymology. 80 Pt C: 26–42. doi:10.1016/s0076-6879(81)80006-7. PMID 6281620.

[6] Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE (December 1987). "Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence". European Journal of Biochemistry. 169 (3): 547–53. doi:10.1111/j.1432-1033.1987.tb13644.x. PMID 3500856.

[7] Müller-Eberhard HJ (1988). "Molecular organization and function of the complement system". Annual Review of Biochemistry. 57: 321–47. doi:10.1146/annurev.bi.57.070188.001541. PMID 3052276.

[8] Skoog MT, Mehdi S, Wiseman JS, Bey P (June 1989). "The specificity of two proteinases that cleave adjacent to arginine, C1 esterase and acrosin, for peptide p-nitroanilide substrates". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 996 (1–2): 89–94. doi:10.1016/0167-4838(89)90099-x. PMID 2500154.

[9] "Entrez Gene: C1S Complement component 1, s subcomponent".

Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Complement component 1s

See also

References

Further reading

External links