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UniProtKB/Swiss-Prot entry P09871


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name C1S_HUMAN
Primary accession number P09871
Secondary accession numbers Q9UCU7 Q9UCU8 Q9UCU9 Q9UCV0 Q9UCV1 Q9UCV2 Q9UCV3 Q9UCV4 Q9UCV5 Q9UM14
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 122)
Name and origin of the protein
Protein name Complement C1s subcomponent [Precursor]
Synonyms EC 3.4.21.42
C1 esterase
Contains Complement C1s subcomponent heavy chain
Complement C1s subcomponent light chain
Gene name
Name: C1S
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3500856 [NCBI, ExPASy, EBI, Israel, Japan]
McKinnon C.M., Carter P.E., Smyth S.J., Dunbar B., Fothergill J.E.;
"Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence.";
Eur. J. Biochem. 169:547-553(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00400a004; PubMed=2831944 [NCBI, ExPASy, EBI, Israel, Japan]
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 26:8516-8524(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2459702 [NCBI, ExPASy, EBI, Israel, Japan]
Kusumoto H., Hirosawa S., Salier J.-P., Hagen F.S., Kurachi K.;
"Human genes for complement components C1r and C1s in a close tail-to-tail arrangement.";
Proc. Natl. Acad. Sci. U.S.A. 85:7307-7311(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-329.
TISSUE=Peripheral blood leukocyte;
PubMed=9794427 [NCBI, ExPASy, EBI, Israel, Japan]
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. 161:4924-4930(1998).
[6]
NUCLEOTIDE SEQUENCE OF 291-688.
DOI=10.1016/0022-2836(89)90161-7; PubMed=2553984 [NCBI, ExPASy, EBI, Israel, Japan]
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. 208:709-714(1989).
[7]
PROTEIN SEQUENCE OF 16-61; 168-219; 287-334 AND 384-445.
PubMed=3007145 [NCBI, ExPASy, EBI, Israel, Japan]
Spycher S.E., Nick H., Rickli E.E.;
"Human complement component C1s. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation.";
Eur. J. Biochem. 156:49-57(1986).
[8]
PROTEIN SEQUENCE OF 438-500; 503-534; 542-601; 617-623 AND 626-656.
PubMed=6362661 [NCBI, ExPASy, EBI, Israel, Japan]
Carter P.E., Dunbar B., Fothergill J.E.;
"The serine proteinase chain of human complement component C1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments.";
Biochem. J. 215:565-571(1983).
[9]
PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-174, AND HYDROXYLATION AT ASN-149.
DOI=10.1021/bi00466a021; PubMed=2141278 [NCBI, ExPASy, EBI, Israel, Japan]
Thielens N.M., van Dorsselaer A., Gagnon J., Arlaud G.J.;
"Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region.";
Biochemistry 29:3570-3578(1990).
[10]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Plasma;
DOI=10.1021/bi00243a014; PubMed=1854725 [NCBI, ExPASy, EBI, Israel, Japan]
Illy C., Thielens N.M., Gagnon J., Arlaud G.J.;
"Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-dependent interactions of human C1s. Location of the iodination sites.";
Biochemistry 30:7135-7141(1991).
[11]
DISULFIDE BONDS.
DOI=10.1021/bi00225a014; PubMed=2007122 [NCBI, ExPASy, EBI, Israel, Japan]
Hess D., Schaller J., Rickli E.E.;
"Identification of the disulfide bonds of human complement C1s.";
Biochemistry 30:2827-2833(1991).
[12]
PARTIAL PROTEIN SEQUENCE, AND 3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
DOI=10.1021/bi00022a004; PubMed=7779774 [NCBI, ExPASy, EBI, Israel, Japan]
Rossi V., Gaboriaud C., Lacroix M., Ulrich J., Fontecilla-Camps J.-C., Gagnon J., Arlaud G.J.;
"Structure of the catalytic region of human complement protease C1s: study by chemical cross-linking and three-dimensional homology modeling.";
Biochemistry 34:7311-7321(1995).
[13]
DISEASE.
PubMed=11390518 [NCBI, ExPASy, EBI, Israel, Japan]
Dragon-Durey M.-A., Quartier P., Fremeaux-Bacchi V., Blouin J., de Barace C., Prieur A.-M., Weiss L., Fridman W.-H.;
"Molecular basis of a selective C1s deficiency associated with early onset multiple autoimmune diseases.";
J. Immunol. 166:7612-7616(2001).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[15]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 358-688.
DOI=10.1093/emboj/19.8.1755; PubMed=10775260 [NCBI, ExPASy, EBI, Israel, Japan]
Gaboriaud C., Rossi V., Bally I., Arlaud G.J., Fontecilla-Camps J.-C.;
"Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle.";
EMBO J. 19:1755-1765(2000).
[16]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-174, CALCIUM-BINDING SITES, AND GLYCOSYLATION AT ASN-406.
DOI=10.1074/jbc.M305175200; PubMed=12788922 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory L.A., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.-C., 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. 278:32157-32164(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X06596; CAA29817.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18767; AAA51853.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04080; AAA51852.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056903; AAH56903.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009076; BAA86864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40496; C1HUS.
RefSeq NP_001725.1; -.
NP_958850.1; -.
UniGene Hs.458355
3D structure databases
PDB
1ELV; X-ray; 1.70 A; A=358-688.[ExPASy / RCSB / EBI]
1NZI; X-ray; 1.50 A; A/B=16-174.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ELV; -.
1NZI; -.
ModBase P09871.
Protein family/group databases
MEROPS S01.193; -.
PTM databases
PhosphoSite P09871; -.
Enzyme and pathway databases
Reactome REACT_6900; Signaling in Immune System.
2D gel databases
SWISS-2DPAGE P09871; -.
Organism-specific databases
H-InvDB HIX0019128; -.
HGNC HGNC:1247; C1S.
GenAtlas C1S.
HPA CAB016722; -.
MIM 120580; gene+phenotype. [NCBI / EBI]
PharmGKB PA25636; -.
GeneCards P09871.
Gene expression databases
ArrayExpress P09871; -.
GermOnline ENSG00000182326; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from experiment from Reactome).
GO:0003816; Molecular function: complement component C1s activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR016060; Complement_control_module.
IPR000859; CUB.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000436; Sushi_SCR_CCP.
Graphical view of domain structure.
Gene3D G3DSA:2.10.70.10; Complement_control_module; 1.
G3DSA:2.60.120.290; CUB; 2.
Pfam PF00431; CUB; 2.
PF00008; EGF; 1.
PF00084; Sushi; 2.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
SMART SM00032; CCP; 2.
SM00042; CUB; 2.
SM00179; EGF_CA; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS00010; ASX_HYDROXYL; 1.
PS01180; CUB; 2.
PS00022; EGF_1; FALSE_NEG.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; FALSE_NEG.
PS01187; EGF_CA; 1.
PS50923; SUSHI; 2.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; FALSE_NEG.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P09871.
Proteomic databases
PeptideAtlas P09871; -.
Genome annotation databases
Ensembl ENSG00000182326; Homo sapiens. [Contig view]
GeneID 716; -.
KEGG hsa:716; -.
Phylogenomic databases
HOVERGEN P09871; -.
Other
DrugBank DB00054; Abciximab.
DB00051; Adalimumab.
DB00074; Basiliximab.
DB00002; Cetuximab.
DB00005; Etanercept.
DB00056; Gemtuzumab ozogamicin.
DB00078; Ibritumomab.
DB00028; Immune globulin.
DB00075; Muromonab.
DB00073; Rituximab.
DB00072; Trastuzumab.
SOURCE C1S; Homo sapiens.
ProtoNet P09871.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Complement pathway; Direct protein sequencing; EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation; Immune response; Innate immunity; Metal-binding; Polymorphism; Protease; Repeat; Serine protease; Signal; Sushi.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    15  15      
CHAIN   16   688  673     Complement C1s subcomponent. PRO_0000027586
CHAIN   16   437  422     Complement C1s subcomponent heavy chain. PRO_0000027587
CHAIN   438   688  251     Complement C1s subcomponent light chain. PRO_0000027588
DOMAIN   16   130  115     CUB 1. 
DOMAIN   131   172  42     EGF-like; calcium-binding. 
DOMAIN   175   290  116     CUB 2. 
DOMAIN   292   356  65     Sushi 1. 
DOMAIN   357   423  67     Sushi 2. 
DOMAIN   438   680  243     Peptidase S1. 
ACT_SITE   475   475        Charge relay system. 
ACT_SITE   529   529        Charge relay system. 
ACT_SITE   632   632        Charge relay system. 
METAL   60    60        Calcium. 
METAL   68    68        Calcium. 
METAL   113   113        Calcium. 
METAL   131   131        Calcium. 
METAL   132   132        Calcium; via carbonyl oxygen. 
METAL   134   134        Calcium. 
METAL   149   149        Calcium. 
METAL   150   150        Calcium; via carbonyl oxygen. 
METAL   153   153        Calcium; via carbonyl oxygen. 
MOD_RES   149   149        3-hydroxyasparagine; partial. 
CARBOHYD   174   174        N-linked (GlcNAc...). 
CARBOHYD   406   406        N-linked (GlcNAc...). 
DISULFID   65    83         
DISULFID   135   147         
DISULFID   143   156         
DISULFID   158   171         
DISULFID   175   202         
DISULFID   234   251         
DISULFID   294   341         
DISULFID   321   354         
DISULFID   359   403         
DISULFID   386   421         
DISULFID   425   549        Interchain (between heavy and light chains). 
DISULFID   595   618         
DISULFID   628   659         
VARIANT   119   119  1     R -> H (in dbSNP:rs12146727 [NCBI]). VAR_033643 [3D]
VARIANT   327   327  1     V -> L (in dbSNP:rs2239170 [NCBI]). VAR_033644 
VARIANT   383   383  1     R -> H (in dbSNP:rs20573 [NCBI]). VAR_014565 
CONFLICT   294   294        C -> K (in Ref. 7; AA sequence). 
CONFLICT   513   513        G -> GG (in Ref. 6). 
CONFLICT   573   573        T -> A (in Ref. 8; AA sequence). 
CONFLICT   645   646        TK -> GR (in Ref. 8; AA sequence). 
STRAND   19    24  6      
TURN   26    29  4      
STRAND   34    43  10      
STRAND   48    58  11      
HELIX   63    65  3      
STRAND   67    73  7      
STRAND   80    82  3      
STRAND   84    86  3      
STRAND   96   112  17      
STRAND   122   131  10      
TURN   134   136  3      
STRAND   143   150  8      
STRAND   153   157  5      
STRAND   368   370  3      
STRAND   381   386  6      
TURN   388   390  3      
STRAND   391   393  3      
STRAND   399   403  5      
STRAND   409   411  3      
TURN   412   414  3      
STRAND   421   423  3      
HELIX   446   448  3      
STRAND   452   455  4      
TURN   456   459  4      
STRAND   460   466  7      
STRAND   469   472  4      
HELIX   474   477  4      
STRAND   505   510  6      
STRAND   531   537  7      
HELIX   555   557  3      
STRAND   564   570  7      
STRAND   583   590  8      
HELIX   592   596  5      
STRAND   616   620  5      
STRAND   635   639  5      
STRAND   647   655  9      
STRAND   661   667  7      
HELIX   668   671  4      
HELIX   672   681  10      
Sequence information
Length: 688 AA [This is the length of the unprocessed precursor] Molecular weight: 76684 Da [This is the MW of the unprocessed precursor] CRC64: 85522647A4C47205 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWCIVLFSLL AWVYAEPTMY GEILSPNYPQ AYPSEVEKSW DIEVPEGYGI HLYFTHLDIE 

        70         80         90        100        110        120 
LSENCAYDSV QIISGDTEEG RLCGQRSSNN PHSPIVEEFQ VPYNKLQVIF KSDFSNEERF 

       130        140        150        160        170        180 
TGFAAYYVAT DINECTDFVD VPCSHFCNNF IGGYFCSCPP EYFLHDDMKN CGVNCSGDVF 

       190        200        210        220        230        240 
TALIGEIASP NYPKPYPENS RCEYQIRLEK GFQVVVTLRR EDFDVEAADS AGNCLDSLVF 

       250        260        270        280        290        300 
VAGDRQFGPY CGHGFPGPLN IETKSNALDI IFQTDLTGQK KGWKLRYHGD PMPCPKEDTP 

       310        320        330        340        350        360 
NSVWEPAKAK YVFRDVVQIT CLDGFEVVEG RVGATSFYST CQSNGKWSNS KLKCQPVDCG 

       370        380        390        400        410        420 
IPESIENGKV EDPESTLFGS VIRYTCEEPY YYMENGGGGE YHCAGNGSWV NEVLGPELPK 

       430        440        450        460        470        480 
CVPVCGVPRE PFEEKQRIIG GSDADIKNFP WQVFFDNPWA GGALINEYWV LTAAHVVEGN 

       490        500        510        520        530        540 
REPTMYVGST SVQTSRLAKS KMLTPEHVFI HPGWKLLEVP EGRTNFDNDI ALVRLKDPVK 

       550        560        570        580        590        600 
MGPTVSPICL PGTSSDYNLM DGDLGLISGW GRTEKRDRAV RLKAARLPVA PLRKCKEVKV 

       610        620        630        640        650        660 
EKPTADAEAY VFTPNMICAG GEKGMDSCKG DSGGAFAVQD PNDKTKFYAA GLVSWGPQCG 

       670        680 
TYGLYTRVKN YVDWIMKTMQ ENSTPRED 

P09871 in FASTA format

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