Complement C1s subcomponent
Details
- Name
- Complement C1s subcomponent
- Synonyms
- 3.4.21.42
- C1 esterase
- Complement component 1 subcomponent s
- Gene Name
- C1S
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0011082|Complement C1s subcomponent MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIE LSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERF TGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVF TALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVF VAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTP NSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCG IPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPK CVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGN REPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVK MGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKV EKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCG TYGLYTRVKNYVDWIMKTMQENSTPRED
- Number of residues
- 688
- Molecular Weight
- 76683.905
- Theoretical pI
- 4.59
- GO Classification
- Functionscalcium ion binding / identical protein binding / serine-type endopeptidase activityProcessescomplement activation / complement activation, classical pathway / innate immune response / proteolysisComponentsblood microparticle / extracellular exosome / extracellular region
- General Function
- Serine-type endopeptidase activity
- Specific Function
- C1s B chain is a serine protease that combines with C1q and C1r 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.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0011083|Complement C1s subcomponent (C1S) 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
- Chromosome Location
- 12
- Locus
- 12p13
- External Identifiers
Resource Link UniProtKB ID P09871 UniProtKB Entry Name C1S_HUMAN GenBank Protein ID 763110 GenBank Gene ID X06596 GenAtlas ID C1S HGNC ID HGNC:1247 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
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- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- Thielens NM, Van Dorsselaer A, Gagnon J, Arlaud GJ: Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region. Biochemistry. 1990 Apr 10;29(14):3570-8. [Article]
- 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. [Article]
- Hess D, Schaller J, Rickli EE: Identification of the disulfide bonds of human complement C1s. Biochemistry. 1991 Mar 19;30(11):2827-33. [Article]
- 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. [Article]
- Rossi V, Cseh S, Bally I, Thielens NM, Jensenius JC, Arlaud GJ: Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2. J Biol Chem. 2001 Nov 2;276(44):40880-7. Epub 2001 Aug 29. [Article]
- 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. [Article]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [Article]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Gaboriaud C, Rossi V, Bally I, Arlaud GJ, Fontecilla-Camps JC: Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle. EMBO J. 2000 Apr 17;19(8):1755-65. [Article]
- Gregory LA, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C: X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement. J Biol Chem. 2003 Aug 22;278(34):32157-64. Epub 2003 Jun 4. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02371 2-(2-Hydroxy-1,1-Dihydroxymethyl-Ethylamino)-Ethanesulfonic Acid experimental unknown Details DB09228 Conestat alfa approved, investigational yes inhibitor Details DB06404 Human C1-esterase inhibitor approved yes inhibitor Details DB12831 Gabexate investigational no inhibitor Details DB09130 Copper approved, investigational unknown Details DB01593 Zinc approved, investigational unknown Details DB14487 Zinc acetate approved, investigational unknown Details DB14533 Zinc chloride approved, investigational unknown modulator Details DB14548 Zinc sulfate, unspecified form approved, experimental unknown modulator Details DB14996 Sutimlimab approved, investigational yes inhibitorantibody Details