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Complement component C9 [Cleaved into: Complement component C9a; Complement component C9b]

 CO9_HUMAN               Reviewed;         559 AA.
P02748;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
13-FEB-2019, entry version 196.
RecName: Full=Complement component C9;
Contains:
RecName: Full=Complement component C9a;
Contains:
RecName: Full=Complement component C9b;
Flags: Precursor;
Name=C9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=4018030;
Stanley K.K., Kocher H.-P., Luzio J.P., Jackson P., Tschopp J.;
"The sequence and topology of human complement component C9.";
EMBO J. 4:375-382(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-559, AND PROTEIN SEQUENCE OF
N-TERMINUS.
PubMed=6095282; DOI=10.1073/pnas.81.23.7298;
Discipio R.G., Gehring M.R., Podack E.R., Kan C.C., Hugli T.E.,
Fey G.H.;
"Nucleotide sequence of cDNA and derived amino acid sequence of human
complement component C9.";
Proc. Natl. Acad. Sci. U.S.A. 81:7298-7302(1984).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-159.
PubMed=3219351; DOI=10.1021/bi00417a050;
Marazziti D., Eggertsen G., Fey G.H., Stanley K.K.;
"Relationships between the gene and protein structure in human
complement component C9.";
Biochemistry 27:6529-6534(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-559, VARIANT C9D GLY-119,
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9634479; DOI=10.1007/s002510050415;
Witzel-Schloemp K., Hobart M.J., Fernie B.A., Orren A., Wuerzner R.,
Rittner C., Kaufmann T., Schneider P.M.;
"Heterogeneity in the genetic basis of human complement C9
deficiency.";
Immunogenetics 48:144-147(1998).
[6]
PARTIAL PROTEIN SEQUENCE, ELECTRON MICROSCOPY, FUNCTION, SUBCELLULAR
LOCATION, PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION AT ASN-277 AND
ASN-415.
PubMed=4055801;
DiScipio R.G., Hugli T.E.;
"The architecture of complement component C9 and poly(C9).";
J. Biol. Chem. 260:14802-14809(1985).
[7]
DISULFIDE BONDS, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8603752; DOI=10.1016/0014-5793(95)01541-8;
Lengweiler S., Schaller J., Rickli E.E.;
"Identification of disulfide bonds in the ninth component (C9) of
human complement.";
FEBS Lett. 380:8-12(1996).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9212048; DOI=10.1203/00006450-199707000-00020;
Lassiter H.A., Walz B.M., Wilson J.L., Jung E., Calisi C.R.,
Goldsmith L.J., Wilson R.A., Morgan B.P., Feldhoff R.C.;
"The administration of complement component C9 enhances the survival
of neonatal rats with Escherichia coli sepsis.";
Pediatr. Res. 42:128-136(1997).
[9]
GLYCOSYLATION AT TRP-48 AND TRP-51.
PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
"The four terminal components of the complement system are C-
mannosylated on multiple tryptophan residues.";
J. Biol. Chem. 274:32786-32794(1999).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
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).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
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).
[14]
GLYCOSYLATION AT ASN-415.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[15]
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).
[16]
3D-STRUCTURE MODELING OF MEMBRANE-SPANNING DOMAIN (MSB).
PubMed=2395434; DOI=10.1016/0161-5890(90)90001-G;
Peitsch M.C., Amiguet P., Guy R., Brunner J., Maizel J.V. Jr.,
Tschopp J.;
"Localization and molecular modelling of the membrane-inserted domain
of the ninth component of human complement and perforin.";
Mol. Immunol. 27:589-602(1990).
[17]
ELECTRON MICROSCOPY, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22832194; DOI=10.1016/j.celrep.2012.02.003;
Hadders M.A., Bubeck D., Roversi P., Hakobyan S., Forneris F.,
Morgan B.P., Pangburn M.K., Llorca O., Lea S.M., Gros P.;
"Assembly and regulation of the membrane attack complex based on
structures of C5b6 and sC5b9.";
Cell Rep. 1:200-207(2012).
[18]
STRUCTURE BY ELECTRON MICROSCOPY (6.70 ANGSTROMS) OF 39-544, FUNCTION,
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=26841934; DOI=10.1038/ncomms10588;
Dudkina N.V., Spicer B.A., Reboul C.F., Conroy P.J., Lukoyanova N.,
Elmlund H., Law R.H., Ekkel S.M., Kondos S.C., Goode R.J., Ramm G.,
Whisstock J.C., Saibil H.R., Dunstone M.A.;
"Structure of the poly-C9 component of the complement membrane attack
complex.";
Nat. Commun. 7:10588-10588(2016).
[19] {ECO:0000244|PDB:6DLW}
STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 22-559, FUNCTION,
SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF
PHE-283 AND VAL-426.
PubMed=30111885; DOI=10.1038/s41467-018-05717-0;
Spicer B.A., Law R.H.P., Caradoc-Davies T.T., Ekkel S.M.,
Bayly-Jones C., Pang S.S., Conroy P.J., Ramm G., Radjainia M.,
Venugopal H., Whisstock J.C., Dunstone M.A.;
"The first transmembrane region of complement component-9 acts as a
brake on its self-assembly.";
Nat. Commun. 9:3266-3266(2018).
[20]
VARIANT ARMD15 SER-167.
PubMed=24036952; DOI=10.1038/ng.2741;
Seddon J.M., Yu Y., Miller E.C., Reynolds R., Tan P.L.,
Gowrisankar S., Goldstein J.I., Triebwasser M., Anderson H.E.,
Zerbib J., Kavanagh D., Souied E., Katsanis N., Daly M.J.,
Atkinson J.P., Raychaudhuri S.;
"Rare variants in CFI, C3 and C9 are associated with high risk of
advanced age-related macular degeneration.";
Nat. Genet. 45:1366-1370(2013).
-!- FUNCTION: Constituent of the membrane attack complex (MAC) that
plays a key role in the innate and adaptive immune response by
forming pores in the plasma membrane of target cells
(PubMed:9634479, PubMed:9212048, PubMed:26841934). C9 is the pore-
forming subunit of the MAC (PubMed:4055801, PubMed:26841934,
PubMed:30111885). {ECO:0000269|PubMed:26841934,
ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:4055801,
ECO:0000269|PubMed:9212048, ECO:0000269|PubMed:9634479}.
-!- SUBUNIT: Component of the membrane attack complex (MAC). MAC
assembly is initiated by proteolytic cleavage of C5 into C5a and
C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the
pore-forming subunit C9 (PubMed:22832194). About 20 C9 chains
oligomerize to give rise to a huge beta-barrel that forms a 100
Angstrom diameter pore in target membranes (PubMed:26841934,
PubMed:30111885). {ECO:0000269|PubMed:22832194,
ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22832194,
ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:8603752,
ECO:0000269|PubMed:9212048, ECO:0000269|PubMed:9634479}. Target
cell membrane {ECO:0000269|PubMed:26841934,
ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:9212048}; Multi-
pass membrane protein {ECO:0000269|PubMed:26841934}. Note=Secreted
as soluble monomer. Oligomerizes at target membranes, forming a
pre-pore. A conformation change then leads to the formation of a
100 Angstrom diameter pore. {ECO:0000269|PubMed:26841934,
ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:4055801,
ECO:0000269|PubMed:9634479}.
-!- TISSUE SPECIFICITY: Plasma (at protein level).
{ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841934,
ECO:0000269|PubMed:8603752, ECO:0000269|PubMed:9212048,
ECO:0000269|PubMed:9634479}.
-!- PTM: Thrombin cleaves factor C9 to produce C9a and C9b.
{ECO:0000269|PubMed:4055801}.
-!- PTM: Phosphorylation sites are present in the extracellular
medium.
-!- PTM: Initially, positions and connectivity of disulfide bonds were
based on peptide sequencing done for the human protein
(PubMed:8603752). The crystal structures for the human and mouse
proteins corrected the positions and connectivities of the
disulfide bonds (PubMed:30111885). The distance between Cys-57 and
Cys-94 in the monomeric mouse protein precludes formation of a
disulfide bond, contrary to what is seen in the structure of the
human polymeric form of the protein (Probable).
{ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:8603752,
ECO:0000305|PubMed:30111885}.
-!- DISEASE: Complement component 9 deficiency (C9D) [MIM:613825]: A
rare defect of the complement classical pathway associated with
susceptibility to severe recurrent infections predominantly by
Neisseria gonorrhoeae or Neisseria meningitidis. Some patients may
develop dermatomyositis. {ECO:0000269|PubMed:9634479}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Macular degeneration, age-related, 15 (ARMD15)
[MIM:615591]: A form of age-related macular degeneration, a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world. In most patients,
the disease is manifest as ophthalmoscopically visible yellowish
accumulations of protein and lipid that lie beneath the retinal
pigment epithelium and within an elastin-containing structure
known as Bruch membrane. {ECO:0000269|PubMed:24036952}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=C9base; Note=C9 mutation db;
URL="http://structure.bmc.lu.se/idbase/C9base/";
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EMBL; X02176; CAA26117.1; -; mRNA.
EMBL; BC020721; AAH20721.1; -; mRNA.
EMBL; K02766; AAA51889.1; -; mRNA.
EMBL; J02833; AAA51890.1; -; Genomic_DNA.
EMBL; Y08545; CAA69849.1; -; Genomic_DNA.
EMBL; Y08546; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08547; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08548; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08549; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08550; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08551; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08552; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08553; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08554; CAA69849.1; JOINED; Genomic_DNA.
CCDS; CCDS3929.1; -.
PIR; A59363; C9HU.
RefSeq; NP_001728.1; NM_001737.4.
UniGene; Hs.654443; -.
PDB; 5FMW; EM; 6.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=39-544.
PDB; 6DLW; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=22-559.
PDB; 6H03; EM; 5.60 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=22-559.
PDB; 6H04; EM; 5.60 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=22-559.
PDBsum; 5FMW; -.
PDBsum; 6DLW; -.
PDBsum; 6H03; -.
PDBsum; 6H04; -.
ProteinModelPortal; P02748; -.
SMR; P02748; -.
BioGrid; 107196; 6.
DIP; DIP-1124N; -.
ELM; P02748; -.
STRING; 9606.ENSP00000263408; -.
GlyConnect; 1150; -.
iPTMnet; P02748; -.
PhosphoSitePlus; P02748; -.
BioMuta; C9; -.
DMDM; 1352108; -.
jPOST; P02748; -.
MaxQB; P02748; -.
PaxDb; P02748; -.
PeptideAtlas; P02748; -.
PRIDE; P02748; -.
ProteomicsDB; 51564; -.
DNASU; 735; -.
Ensembl; ENST00000263408; ENSP00000263408; ENSG00000113600.
GeneID; 735; -.
KEGG; hsa:735; -.
UCSC; uc003jlv.5; human.
CTD; 735; -.
DisGeNET; 735; -.
EuPathDB; HostDB:ENSG00000113600.10; -.
GeneCards; C9; -.
HGNC; HGNC:1358; C9.
HPA; CAB002151; -.
HPA; HPA029577; -.
MalaCards; C9; -.
MIM; 120940; gene.
MIM; 613825; phenotype.
MIM; 615591; phenotype.
neXtProt; NX_P02748; -.
OpenTargets; ENSG00000113600; -.
Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency.
Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
PharmGKB; PA25968; -.
eggNOG; ENOG410IH3C; Eukaryota.
eggNOG; ENOG410XT9A; LUCA.
GeneTree; ENSGT00940000159777; -.
HOGENOM; HOG000111869; -.
HOVERGEN; HBG106792; -.
InParanoid; P02748; -.
KO; K04000; -.
OMA; GINILGM; -.
OrthoDB; 787014at2759; -.
PhylomeDB; P02748; -.
TreeFam; TF330498; -.
Reactome; R-HSA-166665; Terminal pathway of complement.
Reactome; R-HSA-977606; Regulation of Complement cascade.
ChiTaRS; C9; human.
GenomeRNAi; 735; -.
PRO; PR:P02748; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113600; Expressed in 60 organ(s), highest expression level in liver.
Genevisible; P02748; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001906; P:cell killing; IDA:UniProtKB.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00112; LDLa; 1.
Gene3D; 2.20.100.10; -; 1.
InterPro; IPR037567; Complement_C9.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR001862; MAC_perforin.
InterPro; IPR020864; MACPF.
InterPro; IPR020863; MACPF_CS.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
PANTHER; PTHR19325:SF362; PTHR19325:SF362; 1.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF01823; MACPF; 1.
Pfam; PF00090; TSP_1; 1.
PRINTS; PR00764; COMPLEMENTC9.
SMART; SM00192; LDLa; 1.
SMART; SM00457; MACPF; 1.
SMART; SM00209; TSP1; 1.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57424; SSF57424; 1.
SUPFAM; SSF82895; SSF82895; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 1.
PROSITE; PS00279; MACPF_1; 1.
PROSITE; PS51412; MACPF_2; 1.
PROSITE; PS50092; TSP1; 1.
1: Evidence at protein level;
3D-structure; Age-related macular degeneration;
Complement alternate pathway; Complement pathway; Complete proteome;
Cytolysis; Direct protein sequencing; Disease mutation;
Disulfide bond; EGF-like domain; Glycoprotein; Immunity;
Innate immunity; Membrane; Membrane attack complex; Phosphoprotein;
Polymorphism; Reference proteome; Secreted; Signal;
Target cell membrane; Target membrane; Transmembrane;
Transmembrane beta strand.
SIGNAL 1 21 {ECO:0000269|PubMed:6095282}.
CHAIN 22 559 Complement component C9.
/FTId=PRO_0000023602.
CHAIN 22 265 Complement component C9a.
/FTId=PRO_0000023603.
CHAIN 266 559 Complement component C9b.
/FTId=PRO_0000023604.
TRANSMEM 314 330 Beta stranded. {ECO:0000255}.
TRANSMEM 335 354 Beta stranded. {ECO:0000255}.
DOMAIN 42 95 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 99 136 LDL-receptor class A.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 138 509 MACPF. {ECO:0000255|PROSITE-
ProRule:PRU00745}.
DOMAIN 510 540 EGF-like.
SITE 265 266 Cleavage; by thrombin.
CARBOHYD 48 48 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 51 51 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:4055801}.
CARBOHYD 415 415 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:4055801}.
DISULFID 43 78 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885,
ECO:0000269|PubMed:8603752}.
DISULFID 54 88 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885}.
DISULFID 57 94 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885}.
DISULFID 101 112 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885,
ECO:0000269|PubMed:8603752}.
DISULFID 107 125 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885,
ECO:0000269|PubMed:8603752}.
DISULFID 119 134 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885,
ECO:0000269|PubMed:8603752}.
DISULFID 142 181 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885,
ECO:0000269|PubMed:8603752}.
DISULFID 510 526 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885,
ECO:0000269|PubMed:8603752}.
DISULFID 513 528 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885,
ECO:0000269|PubMed:8603752}.
DISULFID 530 539 {ECO:0000244|PDB:6DLW,
ECO:0000269|PubMed:30111885,
ECO:0000269|PubMed:8603752}.
VARIANT 5 5 R -> W (in dbSNP:rs700233).
/FTId=VAR_022024.
VARIANT 119 119 C -> G (in C9D; dbSNP:rs121909593).
{ECO:0000269|PubMed:9634479}.
/FTId=VAR_012648.
VARIANT 127 127 D -> Y (in dbSNP:rs696763).
/FTId=VAR_050481.
VARIANT 167 167 P -> S (in ARMD15; dbSNP:rs34882957).
{ECO:0000269|PubMed:24036952}.
/FTId=VAR_070940.
VARIANT 203 203 I -> V (in dbSNP:rs13361416).
/FTId=VAR_027651.
VARIANT 279 279 T -> S (in dbSNP:rs34625111).
/FTId=VAR_033802.
VARIANT 427 427 S -> T (in dbSNP:rs34421659).
/FTId=VAR_061503.
MUTAGEN 283 283 F->C: Creates an artifactual disulfide
bond that prevents the conformation
change required for oligomerization and
pore formation; when associated with C-
427. {ECO:0000269|PubMed:30111885}.
MUTAGEN 426 426 V->C: Creates an artifactual disulfide
bond that prevents the conformation
change required for oligomerization and
pore formation; when associated with C-
283. {ECO:0000269|PubMed:30111885}.
CONFLICT 43 43 C -> R (in Ref. 3; AAA51889).
{ECO:0000305}.
CONFLICT 314 314 Missing (in Ref. 3; AAA51889).
{ECO:0000305}.
CONFLICT 417 417 T -> P (in Ref. 3; AAA51889).
{ECO:0000305}.
SEQUENCE 559 AA; 63173 MW; 7403F6AD77B3ECE1 CRC64;
MSACRSFAVA ICILEISILT AQYTTSYDPE LTESSGSASH IDCRMSPWSE WSQCDPCLRQ
MFRSRSIEVF GQFNGKRCTD AVGDRRQCVP TEPCEDAEDD CGNDFQCSTG RCIKMRLRCN
GDNDCGDFSD EDDCESEPRP PCRDRVVEES ELARTAGYGI NILGMDPLST PFDNEFYNGL
CNRDRDGNTL TYYRRPWNVA SLIYETKGEK NFRTEHYEEQ IEAFKSIIQE KTSNFNAAIS
LKFTPTETNK AEQCCEETAS SISLHGKGSF RFSYSKNETY QLFLSYSSKK EKMFLHVKGE
IHLGRFVMRN RDVVLTTTFV DDIKALPTTY EKGEYFAFLE TYGTHYSSSG SLGGLYELIY
VLDKASMKRK GVELKDIKRC LGYHLDVSLA FSEISVGAEF NKDDCVKRGE GRAVNITSEN
LIDDVVSLIR GGTRKYAFEL KEKLLRGTVI DVTDFVNWAS SINDAPVLIS QKLSPIYNLV
PVKMKNAHLK KQNLERAIED YINEFSVRKC HTCQNGGTVI LMDGKCLCAC PFKFEGIACE
ISKQKISEGL PALEFPNEK


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Kits Elisa; taq POLYMERASE

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Pathways :
WP1056: Complement and Coagulation Cascades
WP1095: Complement Activation, Classical Pathway
WP1172: Complement and Coagulation Cascades
WP1624: Bacterial secretion system
WP1692: Protein export
WP1713: Two-component system
WP1798: Complement cascade
WP200: Complement Activation, Classical Pathway
WP2328: Allograft rejection
WP449: Complement and Coagulation Cascades
WP545: Complement Activation, Classical Pathway
WP547: Complement and Coagulation Cascades
WP558: Complement and Coagulation Cascades
WP751: Complement Activation, Classical Pathway
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Related Genes :
[C9] Complement component C9 [Cleaved into: Complement component C9a; Complement component C9b]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[C8B] Complement component C8 beta chain (Complement component 8 subunit beta)
[C8A] Complement component C8 alpha chain (Complement component 8 subunit alpha)
[C3 CPAMD1] Complement C3 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C1S] 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]
[C7] Complement component C7
[C1R] Complement C1r subcomponent (EC 3.4.21.41) (Complement component 1 subcomponent r) [Cleaved into: Complement C1r subcomponent heavy chain; Complement C1r subcomponent light chain]
[C6] Complement component C6
[C5 CPAMD4] Complement C5 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4) [Cleaved into: Complement C5 beta chain; Complement C5 alpha chain; C5a anaphylatoxin; Complement C5 alpha' chain]
[C3] Complement C3 (HSE-MSF) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc) (Neutrophil chemotactic factor-2) (ENCF-2); Complement C3 alpha chain; C3a anaphylatoxin (Neutrophil chemotactic factor-1) (ENCF-1); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; C3-beta-c (C3bc); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[c3] Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] (Fragment)
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C4A CO4 CPAMD2] Complement C4-A (Acidic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2) [Cleaved into: Complement C4 beta chain; Complement C4-A alpha chain; C4a anaphylatoxin; C4b-A; C4d-A; Complement C4 gamma chain]
[C4B CO4 CPAMD3; C4B_2] Complement C4-B (Basic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3) [Cleaved into: Complement C4 beta chain; Complement C4-B alpha chain; C4a anaphylatoxin; C4b-B; C4d-B; Complement C4 gamma chain]
[MASP1 CRARF CRARF1 PRSS5] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[PSMA4 HC9 PSC9] Proteasome subunit alpha type-4 (EC 3.4.25.1) (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CLU APOJ CLI KUB1 AAG4] Clusterin (Aging-associated gene 4 protein) (Apolipoprotein J) (Apo-J) (Complement cytolysis inhibitor) (CLI) (Complement-associated protein SP-40,40) (Ku70-binding protein 1) (NA1/NA2) (Testosterone-repressed prostate message 2) (TRPM-2) [Cleaved into: Clusterin beta chain (ApoJalpha) (Complement cytolysis inhibitor a chain); Clusterin alpha chain (ApoJbeta) (Complement cytolysis inhibitor b chain)]
[CD93 C1QR1 MXRA4] Complement component C1q receptor (C1q/MBL/SPA receptor) (C1qR) (C1qR(p)) (C1qRp) (CDw93) (Complement component 1 q subcomponent receptor 1) (Matrix-remodeling-associated protein 4) (CD antigen CD93)

Bibliography :
[30508672] Molecular characterization, expression analysis, and ontogeny of complement component C9 in southern catfish (Silurus meridionalis).
[30148749] INCREASED COMPLEMENT LEVELS IN HUMAN VITREOUS ASPIRATES OF PROLIFERATIVE DIABETIC RETINOPATHY AND RETINAL DETACHMENT EYES.
[29767720] Functional analyses of rare genetic variants in complement component C9 identified in patients with age-related macular degeneration.
[29600944] Investigation of serum biomarkers in primary gout patients using iTRAQ-based screening.
[29513714] Identification of blood biomarkers in glioblastoma by SWATH mass spectrometry and quantitative targeted absolute proteomics.
[28918156] Exploration of the bovine colostrum proteome and effects of heat treatment time on colostrum protein profile.
[28823846] iTRAQ based investigation of plasma proteins in HIV infected and HIV/HBV coinfected patients - C9 and KLK are related to HIV/HBV coinfection.
[28221766] Proteoform Profile Mapping of the Human Serum Complement Component C9 Revealing Unexpected New Features of N-, O-, and C-Glycosylation.
[26709396] Proteomic analysis for the identification of serum diagnostic markers for joint hypermobility syndrome.
[26404905] Serum Glycoprotein Biomarker Discovery and Qualification Pipeline Reveals Novel Diagnostic Biomarker Candidates for Esophageal Adenocarcinoma.