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Identification
HMDB Protein ID HMDBP07481
Secondary Accession Numbers
  • 13189
Name Complement C1s subcomponent precursor
Synonyms
  1. C1 esterase[Contains: Complement C1s subcomponent heavy chain
  2. Complement C1s subcomponent light chain]
Gene Name C1S
Protein Type Unknown
Biological Properties
General Function Not Available
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 Not Available
GO Classification
Component
extracellular region
Function
endopeptidase activity
serine-type endopeptidase activity
ion binding
cation binding
binding
catalytic activity
hydrolase activity
peptidase activity
calcium ion binding
Process
response to biotic stimulus
defense response
response to stimulus
humoral immune response
immune response
complement activation
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Cellular Location
  1. Cytoplasmic
Gene Properties
Chromosome Location Chromosome:12
Locus 12p13
SNPs P09871
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
Protein Properties
Number of Residues 688
Molecular Weight 76685.0
Theoretical pI 4.59
Pfam Domain Function
Signals
  • 1-15
Transmembrane Regions
  • None
Protein Sequence
>Complement C1s subcomponent precursor
MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIE
LSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERF
TGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVF
TALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVF
VAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTP
NSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCG
IPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPK
CVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGN
REPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVK
MGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKV
EKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCG
TYGLYTRVKNYVDWIMKTMQENSTPRED
GenBank ID Protein 763110
UniProtKB/Swiss-Prot ID P09871
UniProtKB/Swiss-Prot Entry Name C1S_HUMAN
PDB IDs
GenBank Gene ID X06596
GeneCard ID P09871
GenAtlas ID C1S
HGNC ID HGNC:1247
References
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:3500856 ]
  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:2831944 ]
  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:2459702 ]
  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:9794427 ]
  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:2553984 ]
  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:3007145 ]
  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:6362661 ]
  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:1854725 ]
  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:2007122 ]
  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:7779774 ]
  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:11390518 ]