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Complement C1s subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s) [Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain]

 C1S_HUMAN               Reviewed;         688 AA.
P09871; D3DUT4; Q9UCU7; Q9UCU8; Q9UCU9; Q9UCV0; Q9UCV1; Q9UCV2;
Q9UCV3; Q9UCV4; Q9UCV5; Q9UM14;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
22-NOV-2017, entry version 219.
RecName: Full=Complement C1s subcomponent;
EC=3.4.21.42;
AltName: Full=C1 esterase;
AltName: Full=Complement component 1 subcomponent s;
Contains:
RecName: Full=Complement C1s subcomponent heavy chain;
Contains:
RecName: Full=Complement C1s subcomponent light chain;
Flags: Precursor;
Name=C1S;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3500856; DOI=10.1111/j.1432-1033.1987.tb13644.x;
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].
PubMed=2831944; DOI=10.1021/bi00400a004;
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; DOI=10.1073/pnas.85.19.7307;
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 GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-329.
TISSUE=Peripheral blood leukocyte;
PubMed=9794427;
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).
[7]
NUCLEOTIDE SEQUENCE OF 291-688.
PubMed=2553984; DOI=10.1016/0022-2836(89)90161-7;
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).
[8]
PROTEIN SEQUENCE OF 16-61; 168-219; 287-334 AND 384-445.
PubMed=3007145; DOI=10.1111/j.1432-1033.1986.tb09546.x;
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).
[9]
PROTEIN SEQUENCE OF 438-500; 503-534; 542-601; 617-623 AND 626-656.
PubMed=6362661; DOI=10.1042/bj2150565;
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).
[10]
PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-174, AND HYDROXYLATION
AT ASN-149.
PubMed=2141278; DOI=10.1021/bi00466a021;
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).
[11]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Plasma;
PubMed=1854725; DOI=10.1021/bi00243a014;
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).
[12]
DISULFIDE BONDS.
PubMed=2007122; DOI=10.1021/bi00225a014;
Hess D., Schaller J., Rickli E.E.;
"Identification of the disulfide bonds of human complement C1s.";
Biochemistry 30:2827-2833(1991).
[13]
PARTIAL PROTEIN SEQUENCE, AND 3D-STRUCTURE MODELING OF CATALYTIC
DOMAIN.
PubMed=7779774; DOI=10.1021/bi00022a004;
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).
[14]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
REGULATION.
PubMed=11527969; DOI=10.1074/jbc.M105934200;
Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C.,
Arlaud G.J.;
"Substrate specificities of recombinant mannan-binding lectin-
associated serine proteases-1 and -2.";
J. Biol. Chem. 276:40880-40887(2001).
[15]
INVOLVEMENT IN COMPLEMENT COMPONENT C1S DEFICIENCY.
PubMed=11390518; DOI=10.4049/jimmunol.166.12.7612;
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).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
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).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174 AND ASN-406.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
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. 8:651-661(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
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 96:253-262(2014).
[19]
INVOLVEMENT IN EDSPD2, AND VARIANTS EDSPD2 ARG-294 AND VAL-316 DEL.
PubMed=27745832; DOI=10.1016/j.ajhg.2016.08.019;
Molecular Basis of Periodontal EDS Consortium;
Kapferer-Seebacher I., Pepin M., Werner R., Aitman T.J., Nordgren A.,
Stoiber H., Thielens N., Gaboriaud C., Amberger A., Schossig A.,
Gruber R., Giunta C., Bamshad M., Bjoerck E., Chen C., Chitayat D.,
Dorschner M., Schmitt-Egenolf M., Hale C.J., Hanna D., Hennies H.C.,
Heiss-Kisielewsky I., Lindstrand A., Lundberg P., Mitchell A.L.,
Nickerson D.A., Reinstein E., Rohrbach M., Romani N., Schmuth M.,
Silver R., Taylan F., Vandersteen A., Vandrovcova J., Weerakkody R.,
Yang M., Pope F.M., Byers P.H., Zschocke J.;
"Periodontal Ehlers-Danlos syndrome is caused by mutations in C1R and
C1S, which encode subcomponents C1r and C1s of complement.";
Am. J. Hum. Genet. 99:1005-1014(2016).
[20]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 358-688.
PubMed=10775260; DOI=10.1093/emboj/19.8.1755;
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).
[21]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-174, CALCIUM-BINDING
SITES, AND GLYCOSYLATION AT ASN-406.
PubMed=12788922; DOI=10.1074/jbc.M305175200;
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).
-!- 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.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000269|PubMed:11527969}.
-!- ENZYME REGULATION: Inhibited by SERPING1.
{ECO:0000269|PubMed:11527969}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12.3 uM for complement component C2 (at 37 degrees Celsius)
{ECO:0000269|PubMed:11527969};
KM=1.9 uM for complement component C4 (at 37 degrees Celsius)
{ECO:0000269|PubMed:11527969};
Note=Less efficient than MASP2 in C4 cleavage.;
-!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q,
C1r and C1s in the molar ration of 1:2:2. Activated C1s is an
disulfide-linked heterodimer of a heavy chain and a light chain.
{ECO:0000269|PubMed:2007122}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2810045, EBI-2810045;
P00736:C1R; NbExp=4; IntAct=EBI-2810045, EBI-3926504;
O43889-2:CREB3; NbExp=3; IntAct=EBI-2810045, EBI-625022;
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:2141278}.
-!- DISEASE: Complement component C1s deficiency (C1SD) [MIM:613783]:
A rare defect resulting in C1 deficiency and impaired activation
of the complement classical pathway. C1 deficiency generally leads
to severe immune complex disease with features of systemic lupus
erythematosus and glomerulonephritis.
{ECO:0000269|PubMed:11390518}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Ehlers-Danlos syndrome, periodontal type, 2 (EDSPD2)
[MIM:617174]: A form of Ehlers-Danlos syndrome, a connective
tissue disorder characterized by hyperextensible skin, atrophic
cutaneous scars due to tissue fragility and joint hyperlaxity.
EDSPD2 is characterized by the association of typical features of
Ehlers-Danlos syndrome with gingival recession and severe early-
onset periodontal disease, leading to premature loss of permanent
teeth. EDSPD2 transmission pattern is consistent with autosomal
dominant inheritance. {ECO:0000269|PubMed:27745832}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=C1Sbase; Note=C1S mutation db;
URL="http://structure.bmc.lu.se/idbase/C1Sbase/";
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EMBL; X06596; CAA29817.1; -; mRNA.
EMBL; M18767; AAA51853.1; -; mRNA.
EMBL; J04080; AAA51852.1; -; mRNA.
EMBL; CH471116; EAW88689.1; -; Genomic_DNA.
EMBL; CH471116; EAW88690.1; -; Genomic_DNA.
EMBL; BC056903; AAH56903.1; -; mRNA.
EMBL; AB009076; BAA86864.1; -; Genomic_DNA.
CCDS; CCDS31735.1; -.
PIR; A40496; C1HUS.
RefSeq; NP_001333779.1; NM_001346850.1.
RefSeq; NP_001725.1; NM_001734.4.
RefSeq; NP_958850.1; NM_201442.3.
RefSeq; XP_005253817.1; XM_005253760.1.
UniGene; Hs.458355; -.
PDB; 1ELV; X-ray; 1.70 A; A=356-688.
PDB; 1NZI; X-ray; 1.50 A; A/B=16-174.
PDB; 4J1Y; X-ray; 2.66 A; A/B=292-688.
PDB; 4LMF; X-ray; 2.92 A; A/B/C/D=17-292.
PDB; 4LOR; X-ray; 2.50 A; A=17-292.
PDB; 4LOS; X-ray; 2.00 A; A=172-358.
PDB; 4LOT; X-ray; 2.92 A; A=175-423.
PDBsum; 1ELV; -.
PDBsum; 1NZI; -.
PDBsum; 4J1Y; -.
PDBsum; 4LMF; -.
PDBsum; 4LOR; -.
PDBsum; 4LOS; -.
PDBsum; 4LOT; -.
ProteinModelPortal; P09871; -.
SMR; P09871; -.
BioGrid; 107177; 7.
IntAct; P09871; 9.
MINT; MINT-4655918; -.
STRING; 9606.ENSP00000328173; -.
BindingDB; P09871; -.
ChEMBL; CHEMBL3913; -.
DrugBank; DB00054; Abciximab.
DrugBank; DB00051; Adalimumab.
DrugBank; DB00074; Basiliximab.
DrugBank; DB06404; C1 Esterase Inhibitor (Human).
DrugBank; DB09228; C1 Esterase Inhibitor (Recombinant).
DrugBank; DB00002; Cetuximab.
DrugBank; DB00005; Etanercept.
DrugBank; DB00056; Gemtuzumab ozogamicin.
DrugBank; DB00078; Ibritumomab tiuxetan.
DrugBank; DB00075; Muromonab.
DrugBank; DB00073; Rituximab.
DrugBank; DB00072; Trastuzumab.
GuidetoPHARMACOLOGY; 2335; -.
MEROPS; S01.193; -.
iPTMnet; P09871; -.
PhosphoSitePlus; P09871; -.
BioMuta; C1S; -.
DMDM; 115205; -.
SWISS-2DPAGE; P09871; -.
MaxQB; P09871; -.
PaxDb; P09871; -.
PeptideAtlas; P09871; -.
PRIDE; P09871; -.
Ensembl; ENST00000328916; ENSP00000328173; ENSG00000182326.
Ensembl; ENST00000360817; ENSP00000354057; ENSG00000182326.
Ensembl; ENST00000406697; ENSP00000385035; ENSG00000182326.
GeneID; 716; -.
KEGG; hsa:716; -.
UCSC; uc001qsj.4; human.
CTD; 716; -.
DisGeNET; 716; -.
EuPathDB; HostDB:ENSG00000182326.14; -.
GeneCards; C1S; -.
HGNC; HGNC:1247; C1S.
HPA; CAB016722; -.
HPA; HPA018852; -.
MalaCards; C1S; -.
MIM; 120580; gene.
MIM; 613783; phenotype.
MIM; 617174; phenotype.
neXtProt; NX_P09871; -.
OpenTargets; ENSG00000182326; -.
Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
PharmGKB; PA25636; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOVERGEN; HBG000559; -.
InParanoid; P09871; -.
KO; K01331; -.
OMA; FGPYCGN; -.
OrthoDB; EOG091G02DS; -.
PhylomeDB; P09871; -.
TreeFam; TF330373; -.
BRENDA; 3.4.21.42; 2681.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SABIO-RK; P09871; -.
ChiTaRS; C1S; human.
EvolutionaryTrace; P09871; -.
GeneWiki; C1S; -.
GenomeRNAi; 716; -.
PMAP-CutDB; P09871; -.
PRO; PR:P09871; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000182326; -.
ExpressionAtlas; P09871; baseline and differential.
Genevisible; P09871; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
GO; GO:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00033; CCP; 2.
CDD; cd00041; CUB; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.60.120.290; -; 2.
InterPro; IPR035708; Complement_C1s_subcomponent.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24255:SF18; PTHR24255:SF18; 1.
Pfam; PF00431; CUB; 2.
Pfam; PF00084; Sushi; 2.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00032; CCP; 2.
SMART; SM00042; CUB; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57535; SSF57535; 2.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS01180; CUB; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complement pathway; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
EGF-like domain; Ehlers-Danlos syndrome; Glycoprotein; Hydrolase;
Hydroxylation; Immunity; Innate immunity; Metal-binding; Polymorphism;
Protease; Reference proteome; Repeat; Serine protease; Signal; Sushi.
SIGNAL 1 15 {ECO:0000269|PubMed:3007145}.
CHAIN 16 688 Complement C1s subcomponent.
/FTId=PRO_0000027586.
CHAIN 16 437 Complement C1s subcomponent heavy chain.
/FTId=PRO_0000027587.
CHAIN 438 688 Complement C1s subcomponent light chain.
/FTId=PRO_0000027588.
DOMAIN 16 130 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 131 172 EGF-like; calcium-binding.
DOMAIN 175 290 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 292 356 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 357 423 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 438 680 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
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 (3R)-3-hydroxyasparagine.
{ECO:0000269|PubMed:2141278}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2141278}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12788922,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
DISULFID 65 83 {ECO:0000269|PubMed:2007122}.
DISULFID 135 147 {ECO:0000269|PubMed:2007122}.
DISULFID 143 156 {ECO:0000269|PubMed:2007122}.
DISULFID 158 171 {ECO:0000269|PubMed:2007122}.
DISULFID 175 202 {ECO:0000269|PubMed:2007122}.
DISULFID 234 251 {ECO:0000269|PubMed:2007122}.
DISULFID 294 341 {ECO:0000269|PubMed:2007122}.
DISULFID 321 354 {ECO:0000269|PubMed:2007122}.
DISULFID 359 403 {ECO:0000269|PubMed:2007122}.
DISULFID 386 421 {ECO:0000269|PubMed:2007122}.
DISULFID 425 549 Interchain (between heavy and light
chains). {ECO:0000255|PROSITE-
ProRule:PRU00059, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00302,
ECO:0000269|PubMed:2007122}.
DISULFID 595 618 {ECO:0000269|PubMed:2007122}.
DISULFID 628 659 {ECO:0000269|PubMed:2007122}.
VARIANT 119 119 R -> H (in dbSNP:rs12146727).
/FTId=VAR_033643.
VARIANT 294 294 C -> R (in EDSPD2).
{ECO:0000269|PubMed:27745832}.
/FTId=VAR_077120.
VARIANT 316 316 Missing (in EDSPD2; unknown pathological
significance).
{ECO:0000269|PubMed:27745832}.
/FTId=VAR_077121.
VARIANT 327 327 V -> L (in dbSNP:rs2239170).
/FTId=VAR_033644.
VARIANT 383 383 R -> H (in dbSNP:rs20573).
/FTId=VAR_014565.
CONFLICT 294 294 C -> K (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 513 513 G -> GG (in Ref. 7). {ECO:0000305}.
CONFLICT 573 573 T -> A (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 645 646 TK -> GR (in Ref. 9; AA sequence).
{ECO:0000305}.
STRAND 19 24 {ECO:0000244|PDB:1NZI}.
TURN 26 29 {ECO:0000244|PDB:1NZI}.
STRAND 34 43 {ECO:0000244|PDB:1NZI}.
STRAND 48 58 {ECO:0000244|PDB:1NZI}.
HELIX 63 65 {ECO:0000244|PDB:1NZI}.
STRAND 67 73 {ECO:0000244|PDB:1NZI}.
STRAND 75 77 {ECO:0000244|PDB:1NZI}.
STRAND 80 82 {ECO:0000244|PDB:1NZI}.
STRAND 84 86 {ECO:0000244|PDB:1NZI}.
STRAND 96 112 {ECO:0000244|PDB:1NZI}.
STRAND 122 131 {ECO:0000244|PDB:1NZI}.
TURN 134 136 {ECO:0000244|PDB:1NZI}.
STRAND 137 140 {ECO:0000244|PDB:4LOR}.
STRAND 143 150 {ECO:0000244|PDB:1NZI}.
STRAND 153 157 {ECO:0000244|PDB:1NZI}.
STRAND 162 164 {ECO:0000244|PDB:4LOR}.
STRAND 171 173 {ECO:0000244|PDB:4LOR}.
STRAND 176 180 {ECO:0000244|PDB:4LOS}.
STRAND 182 188 {ECO:0000244|PDB:4LOS}.
TURN 190 193 {ECO:0000244|PDB:4LOS}.
STRAND 201 207 {ECO:0000244|PDB:4LOS}.
STRAND 212 217 {ECO:0000244|PDB:4LOS}.
HELIX 220 222 {ECO:0000244|PDB:4LOS}.
STRAND 223 225 {ECO:0000244|PDB:4LOS}.
STRAND 235 242 {ECO:0000244|PDB:4LOS}.
STRAND 245 250 {ECO:0000244|PDB:4LOS}.
STRAND 252 254 {ECO:0000244|PDB:4LOS}.
STRAND 259 262 {ECO:0000244|PDB:4LOS}.
STRAND 265 273 {ECO:0000244|PDB:4LOS}.
STRAND 282 291 {ECO:0000244|PDB:4LOS}.
STRAND 300 306 {ECO:0000244|PDB:4LOS}.
STRAND 309 312 {ECO:0000244|PDB:4J1Y}.
STRAND 316 321 {ECO:0000244|PDB:4LOS}.
STRAND 325 331 {ECO:0000244|PDB:4LOS}.
STRAND 334 341 {ECO:0000244|PDB:4LOS}.
TURN 348 351 {ECO:0000244|PDB:4LOS}.
STRAND 353 356 {ECO:0000244|PDB:4LOS}.
STRAND 368 370 {ECO:0000244|PDB:1ELV}.
STRAND 381 386 {ECO:0000244|PDB:1ELV}.
TURN 388 390 {ECO:0000244|PDB:1ELV}.
STRAND 391 393 {ECO:0000244|PDB:1ELV}.
STRAND 395 397 {ECO:0000244|PDB:4LOT}.
STRAND 399 403 {ECO:0000244|PDB:1ELV}.
TURN 405 407 {ECO:0000244|PDB:4LOT}.
STRAND 409 411 {ECO:0000244|PDB:1ELV}.
TURN 412 414 {ECO:0000244|PDB:1ELV}.
STRAND 421 423 {ECO:0000244|PDB:1ELV}.
HELIX 446 448 {ECO:0000244|PDB:1ELV}.
STRAND 452 455 {ECO:0000244|PDB:1ELV}.
TURN 456 459 {ECO:0000244|PDB:1ELV}.
STRAND 460 466 {ECO:0000244|PDB:1ELV}.
STRAND 469 472 {ECO:0000244|PDB:1ELV}.
HELIX 474 477 {ECO:0000244|PDB:1ELV}.
STRAND 490 492 {ECO:0000244|PDB:4J1Y}.
HELIX 494 499 {ECO:0000244|PDB:4J1Y}.
STRAND 505 510 {ECO:0000244|PDB:1ELV}.
HELIX 520 522 {ECO:0000244|PDB:4J1Y}.
STRAND 531 537 {ECO:0000244|PDB:1ELV}.
HELIX 555 557 {ECO:0000244|PDB:1ELV}.
STRAND 564 570 {ECO:0000244|PDB:1ELV}.
STRAND 576 578 {ECO:0000244|PDB:4J1Y}.
STRAND 583 590 {ECO:0000244|PDB:1ELV}.
HELIX 592 596 {ECO:0000244|PDB:1ELV}.
STRAND 616 620 {ECO:0000244|PDB:1ELV}.
HELIX 627 629 {ECO:0000244|PDB:4J1Y}.
STRAND 635 639 {ECO:0000244|PDB:1ELV}.
STRAND 647 655 {ECO:0000244|PDB:1ELV}.
STRAND 661 667 {ECO:0000244|PDB:1ELV}.
HELIX 668 671 {ECO:0000244|PDB:1ELV}.
HELIX 672 681 {ECO:0000244|PDB:1ELV}.
SEQUENCE 688 AA; 76684 MW; 85522647A4C47205 CRC64;
MWCIVLFSLL AWVYAEPTMY GEILSPNYPQ AYPSEVEKSW DIEVPEGYGI HLYFTHLDIE
LSENCAYDSV QIISGDTEEG RLCGQRSSNN PHSPIVEEFQ VPYNKLQVIF KSDFSNEERF
TGFAAYYVAT DINECTDFVD VPCSHFCNNF IGGYFCSCPP EYFLHDDMKN CGVNCSGDVF
TALIGEIASP NYPKPYPENS RCEYQIRLEK GFQVVVTLRR EDFDVEAADS AGNCLDSLVF
VAGDRQFGPY CGHGFPGPLN IETKSNALDI IFQTDLTGQK KGWKLRYHGD PMPCPKEDTP
NSVWEPAKAK YVFRDVVQIT CLDGFEVVEG RVGATSFYST CQSNGKWSNS KLKCQPVDCG
IPESIENGKV EDPESTLFGS VIRYTCEEPY YYMENGGGGE YHCAGNGSWV NEVLGPELPK
CVPVCGVPRE PFEEKQRIIG GSDADIKNFP WQVFFDNPWA GGALINEYWV LTAAHVVEGN
REPTMYVGST SVQTSRLAKS KMLTPEHVFI HPGWKLLEVP EGRTNFDNDI ALVRLKDPVK
MGPTVSPICL PGTSSDYNLM DGDLGLISGW GRTEKRDRAV RLKAARLPVA PLRKCKEVKV
EKPTADAEAY VFTPNMICAG GEKGMDSCKG DSGGAFAVQD PNDKTKFYAA GLVSWGPQCG
TYGLYTRVKN YVDWIMKTMQ ENSTPRED


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