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Complement C1s subcomponent

ID 2782
Name Complement C1s subcomponent
Synonyms
  • EC 3.4.21.42
  • C1 esterase
  • Complement C1s subcomponent precursor
Gene Name C1S
Protein Sequence
>Complement C1s subcomponent precursor
MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIE
LSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERF
TGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVF
TALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVF
VAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTP
NSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCG
IPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPK
CVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGN
REPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVK
MGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKV
EKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCG
TYGLYTRVKNYVDWIMKTMQENSTPRED
Number of Residues 688
Molecular Weight 76685
Theoretical pI 4.59
GO Classification
Component
extracellular region
Function
calcium ion binding
peptidase activity
endopeptidase activity
binding
serine-type endopeptidase activity
catalytic activity
ion binding
cation binding
hydrolase activity
Process
physiological process
proteolysis
response to stimulus
response to biotic stimulus
metabolism
defense response
immune response
macromolecule metabolism
humoral immune response
protein metabolism
complement activation
cellular protein metabolism
General Function Involved in calcium ion binding
Specific Function C1s B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4
Pathways Not Available
Reactions
  • 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
Pfam Domain Function
Signals 1-15
Transmembrane Regions None
Essentiality Non-Essential
GenBank Protein ID 763110 Link_out
UniProtKB ID P09871 Link_out
UniProtKB Entry Name C1S_HUMAN Link_out
PDB ID 1ELV Link_out
PDB File show
3D Structure View 3D Structure
Cellular Location Cytoplasmic
Gene Sequence
>2067 bp
ATGTGGTGCATTGTCCTGTTTTCACTTTTGGCATGGGTTTATGCTGAGCCTACCATGTAT
GGGGAGATCCTGTCCCCTAACTATCCTCAGGCATATCCCAGTGAGGTAGAGAAATCTTGG
GACATAGAAGTTCCTGAAGGGTATGGGATTCACCTCTACTTCACCCATCTGGACATTGAG
CTGTCAGAGAACTGTGCGTATGACTCAGTGCAGATAATCTCAGGAGACACTGAAGAAGGG
AGGCTCTGTGGACAGAGGAGCAGTAACAATCCCCACTCTCCAATTGTGGAAGAGTTCCAA
GTCCCATACAACAAACTCCAGGTGATCTTTAAGTCAGACTTTTCCAATGAAGAGCGTTTT
ACGGGGTTTGCTGCATACTATGTTGCCACAGACATAAATGAATGCACAGATTTTGTAGAT
GTCCCTTGTAGCCACTTCTGCAACAATTTCATTGGTGGTTACTTCTGCTCCTGCCCCCCG
GAATATTTCCTCCATGATGACATGAAGAATTGCGGAGTTAATTGCAGTGGGGATGTATTC
ACTGCACTGATTGGGGAGATTGCAAGTCCCAATTATCCCAAACCATATCCAGAGAACTCA
AGGTGTGAATACCAGATCCGGTTGGAGAAAGGGTTCCAAGTGGTGGTGACCTTGCGGAGA
GAAGATTTTGATGTGGAAGCAGCTGACTCAGCGGGAAACTGCCTTGACAGTTTAGTTTTT
GTTGCAGGAGATCGGCAATTTGGTCCTTACTGTGGTCATGGATTCCCTGGGCCTCTAAAT
ATTGAAACCAAGAGTAATGCTCTTGATATCATCTTCCAAACTGATCTAACAGGGCAAAAA
AAGGGCTGGAAACTTCGCTATCATGGAGATCCAATGCCCTGCCCTAAGGAAGACACTCCC
AATTCTGTTTGGGAGCCTGCGAAGGCAAAATATGTCTTTAGAGATGTGGTGCAGATAACC
TGTCTGGATGGGTTTGAAGTTGTGGAGGGACGTGTTGGTGCAACATCTTTCTATTCGACT
TGTCAAAGCAATGGAAAGTGGAGTAATTCCAAACTGAAATGTCAACCTGTGGACTGTGGC
ATTCCTGAATCCATTGAGAATGGTAAAGTTGAAGACCCAGAGAGCACTTTGTTTGGTTCT
GTCATCCGCTACACTTGTGAGGAGCCATATTACTACATGGAAAATGGAGGAGGTGGGGAG
TATCACTGTGCTGGTAACGGGAGCTGGGTGAATGAGGTGCTGGGCCCGGAGCTGCCGAAA
TGTGTTCCAGTCTGTGGAGTCCCCAGAGAACCCTTTGAAGAAAAACAGAGGATAATTGGA
GGATCCGATGCAGATATTAAAAACTTCCCCTGGCAAGTCTTCTTTGACAACCCATGGGCT
GGTGGAGCGCTCATTAATGAGTACTGGGTGCTGACGGCTGCTCATGTTGTGGAGGGAAAC
AGGGAGCCAACAATGTATGTTGGGTCCACCTCAGTGCAGACCTCACGGCTGGCAAAATCC
AAGATGCTCACTCCTGAGCATGTGTTTATTCATCCGGGATGGAAGCTGCTGGAAGTCCCA
GAAGGACGAACCAATTTTGATAATGACATTGCACTGGTGCGGCTGAAAGACCCAGTGAAA
ATGGGACCCACCGTCTCTCCCATCTGCCTACCAGGCACCTCTTCCGACTACAACCTCATG
GATGGGGACCTGGGACTGATCTCAGGCTGGGGCCGAACAGAGAAGAGAGATCGTGCTGTT
CGCCTCAAGGCGGCAAGGTTACCTGTAGCTCCTTTAAGAAAATGCAAAGAAGTGAAAGTG
GAGAAACCCACAGCAGATGCAGAGGCCTATGTTTTCACTCCTAACATGATCTGTGCTGGA
GGAGAGAAGGGCATGGATAGCTGTAAAGGGGACAGTGGTGGGGCCTTTGCTGTACAGGAT
CCCAATGACAAGACCAAATTCTACGCAGCTGGCCTGGTGTCCTGGGGGCCCCAGTGTGGG
ACCTATGGGCTCTACACACGGGTAAAGAACTATGTTGACTGGATAATGAAGACTATGCAG
GAAAATAGCACCCCCCGTGAGGACTAA
GenBank Gene ID X06596 Link_out
GeneCard ID C1S Link_out
GenAtlas ID C1S Link_out
HGNC ID HGNC:1247 Link_out
HPRD ID 00397
IUPHAR ID Not Available
Guide to Pharmacology ID Not Available
Chromosome Location Not Available
Locus 12p13
SNPs C1S Link_out
General References
  1. Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE: Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence. Eur J Biochem. 1987 Dec 15;169(3):547-53. Pubmed
  2. Tosi M, Duponchel C, Meo T, Julier C: Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr. Biochemistry. 1987 Dec 29;26(26):8516-24. Pubmed
  3. Kusumoto H, Hirosawa S, Salier JP, Hagen FS, Kurachi K: Human genes for complement components C1r and C1s in a close tail-to-tail arrangement. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7307-11. Pubmed
  4. Endo Y, Takahashi M, Nakao M, Saiga H, Sekine H, Matsushita M, Nonaka M, Fujita T: Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates. J Immunol. 1998 Nov 1;161(9):4924-30. Pubmed
  5. Tosi M, Duponchel C, Meo T, Couture-Tosi E: Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin. J Mol Biol. 1989 Aug 20;208(4):709-14. Pubmed
  6. Spycher SE, Nick H, Rickli EE: Human complement component C1s. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation. Eur J Biochem. 1986 Apr 1;156(1):49-57. Pubmed
  7. Carter PE, Dunbar B, Fothergill JE: The serine proteinase chain of human complement component C1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments. Biochem J. 1983 Dec 1;215(3):565-71. Pubmed
  8. Illy C, Thielens NM, Gagnon J, Arlaud GJ: Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-dependent interactions of human C1s. Location of the iodination sites. Biochemistry. 1991 Jul 23;30(29):7135-41. Pubmed
  9. Hess D, Schaller J, Rickli EE: Identification of the disulfide bonds of human complement C1s. Biochemistry. 1991 Mar 19;30(11):2827-33. Pubmed
  10. Rossi V, Gaboriaud C, Lacroix M, Ulrich J, Fontecilla-Camps JC, Gagnon J, Arlaud GJ: Structure of the catalytic region of human complement protease C1s: study by chemical cross-linking and three-dimensional homology modeling. Biochemistry. 1995 Jun 6;34(22):7311-21. Pubmed
  11. Dragon-Durey MA, Quartier P, Fremeaux-Bacchi V, Blouin J, de Barace C, Prieur AM, Weiss L, Fridman WH: Molecular basis of a selective C1s deficiency associated with early onset multiple autoimmune diseases. J Immunol. 2001 Jun 15;166(12):7612-6. Pubmed
Drugs
# DrugBank ID Drug Name Drug Type Drug Groups
1 DB02371 2-(2-Hydroxy-1,1-Dihydroxymethyl-Ethylamino)-Ethanesulfonic Acid small molecule experimental
2 DB00054 Abciximab biotech approved
3 DB00051 Adalimumab biotech approved
4 DB00074 Basiliximab biotech approved, investigational
5 DB00002 Cetuximab biotech approved
6 DB00005 Etanercept biotech approved, investigational
7 DB00056 Gemtuzumab ozogamicin biotech approved, investigational
8 DB00078 Ibritumomab biotech approved
9 DB00075 Muromonab biotech approved
10 DB00073 Rituximab biotech approved
11 DB00072 Trastuzumab biotech approved, investigational