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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]

 CO4A_HUMAN              Reviewed;        1744 AA.
P0C0L4; A6H8M8; A6NHJ5; A7E2V2; B0QZR6; B0V2C8; B2RUT6; B7ZVZ6;
P01028; P78445; Q13160; Q13906; Q14033; Q14835; Q4LE82; Q5JNX2;
Q5JQM8; Q6P4R1; Q6U2E5; Q6U2E8; Q6U2F0; Q6U2F3; Q6U2F4; Q6U2F6;
Q6U2F8; Q6U2G0; Q96EG2; Q96SA8; Q9NPK5; Q9UIP5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 2.
25-OCT-2017, entry version 136.
RecName: Full=Complement C4-A;
AltName: Full=Acidic complement C4;
AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2;
Contains:
RecName: Full=Complement C4 beta chain;
Contains:
RecName: Full=Complement C4-A alpha chain;
Contains:
RecName: Full=C4a anaphylatoxin;
Contains:
RecName: Full=C4b-A;
Contains:
RecName: Full=C4d-A;
Contains:
RecName: Full=Complement C4 gamma chain;
Flags: Precursor;
Name=C4A; Synonyms=CO4, CPAMD2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-418 AND
SER-1201.
TISSUE=Liver;
PubMed=6546707; DOI=10.1016/0092-8674(84)90040-0;
Belt K.T., Carroll M.C., Porter R.R.;
"The structural basis of the multiple forms of human complement
component C4.";
Cell 36:907-914(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-347; LEU-726 AND
ALA-1286.
PubMed=1988494;
Yu C.Y.;
"The complete exon-intron structure of a human complement component
C4A gene. DNA sequences, polymorphism, and linkage to the 21-
hydroxylase gene.";
J. Immunol. 146:1057-1066(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
SER-1176 AND ALA-1286.
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS TYR-347;
SER-1176 AND ALA-1286.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS TYR-347; GLY-1073 AND ALA-1286.
TISSUE=Brain;
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 1-22 AND 1056-1225.
PubMed=3838531; DOI=10.1007/BF00364869;
Belt K.T., Yu C.Y., Carroll M.C., Porter R.R.;
"Polymorphism of human complement component C4.";
Immunogenetics 21:173-180(1985).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21, AND VARIANT ASN-727.
PubMed=8012361; DOI=10.1093/hmg/3.3.481;
Sargent C.A., Anderson M.J., Hsieh S.-L., Kendall E.,
Gomez-Escobar N., Campbell R.D.;
"Characterisation of the novel gene G11 lying adjacent to the
complement C4A gene in the human major histocompatibility complex.";
Hum. Mol. Genet. 3:481-488(1994).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 448-570 AND 692-1225, AND
VARIANTS TRP-477; PRO-549; THR-907; GLY-1073; SER-1176; ALA-1207 AND
ARG-1210.
Sayer D., Puschendorf M., Wetherall J.;
"Molecular genetics of complement C4: implications for MHC evolution
and disease susceptibility gene mapping.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 680-756.
PubMed=6167582;
Moon K.E., Gorski J.P., Hugli T.E.;
"Complete primary structure of human C4a anaphylatoxin.";
J. Biol. Chem. 256:8685-8692(1981).
[10]
PROTEIN SEQUENCE OF 757-771 AND 980-990.
PubMed=1699796; DOI=10.1016/0014-5793(90)80389-Z;
Hessing M., van 't Veer C., Hackeng T.M., Bouma B.N., Iwanaga S.;
"Importance of the alpha 3-fragment of complement C4 for the binding
with C4b-binding protein.";
FEBS Lett. 271:131-136(1990).
[11]
PROTEIN SEQUENCE OF 957-1044.
PubMed=6978711; DOI=10.1042/bj1990359;
Campbell R.D., Gagnon J., Porter R.R.;
"Amino acid sequence around the thiol and reactive acyl groups of
human complement component C4.";
Biochem. J. 199:359-370(1981).
[12]
PROTEIN SEQUENCE OF 957-1336, AND VARIANTS GLY-1073; SER-1176;
ALA-1207; ARG-1210 AND ALA-1286.
PubMed=3696167; DOI=10.1016/0161-5890(87)90165-9;
Chakravarti D.N., Campbell R.D., Porter R.R.;
"The chemical structure of the C4d fragment of the human complement
component C4.";
Mol. Immunol. 24:1187-1197(1987).
[13]
PROTEIN SEQUENCE OF 990-1037.
PubMed=6950384; DOI=10.1073/pnas.78.12.7388;
Harrison R.A., Thomas M.L., Tack B.F.;
"Sequence determination of the thiolester site of the fourth component
of human complement.";
Proc. Natl. Acad. Sci. U.S.A. 78:7388-7392(1981).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1055-1225 (ALLOTYPE C4A13).
PubMed=9759862;
Martinez-Quiles N., Paz-Artal E., Moreno-Pelayo M.A., Longas J.,
Ferre-Lopez S., Rosal M., Arnaiz-Villena A.;
"C4d DNA sequences of two infrequent human allotypes (C4A13 and C4B12)
and the presence of signal sequences enhancing recombination.";
J. Immunol. 161:3438-3443(1998).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1195-1294.
PubMed=6572000; DOI=10.1073/pnas.80.1.264;
Carroll M.C., Porter R.R.;
"Cloning of a human complement component C4 gene.";
Proc. Natl. Acad. Sci. U.S.A. 80:264-267(1983).
[16]
PROTEIN SEQUENCE OF 1199-1304, AND VARIANTS ALA-1207; ARG-1210 AND
ALA-1286.
PubMed=6832377; DOI=10.1016/0014-5793(83)80188-4;
Chakravarti D.N., Campbell R.D., Gagnon J.;
"Amino acid sequence of a polymorphic segment from fragment C4d of
human complement component C4.";
FEBS Lett. 154:387-390(1983).
[17]
PROTEIN SEQUENCE OF 1405-1431, AND SULFATION AT TYR-1417; TYR-1420 AND
TYR-1422.
PubMed=3944109;
Hortin G., Sims H., Strauss A.W.;
"Identification of the site of sulfation of the fourth component of
human complement.";
J. Biol. Chem. 261:1786-1793(1986).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 1448-1474.
PubMed=6577433; DOI=10.1073/pnas.80.17.5387;
Whitehead A.S., Goldberger G., Woods D.E., Markham A.F., Colten H.R.;
"Use of a cDNA clone for the fourth component of human complement (C4)
for analysis of a genetic deficiency of C4 in guinea pig.";
Proc. Natl. Acad. Sci. U.S.A. 80:5387-5391(1983).
[19]
FUNCTION, AND INVOLVEMENT OF ASP-1125 IN IMMUNOGLOBULIN-BINDING AND
HEMOLYSIS.
PubMed=2395880; DOI=10.1073/pnas.87.17.6868;
Carroll M.C., Fathallah D.M., Bergamaschini L., Alicot E.M.,
Isenman D.E.;
"Substitution of a single amino acid (aspartic acid for histidine)
converts the functional activity of human complement C4B to C4A.";
Proc. Natl. Acad. Sci. U.S.A. 87:6868-6872(1990).
[20]
INVOLVEMENT IN C4AD.
PubMed=8473511; DOI=10.1172/JCI116377;
Barba G., Rittner C., Schneider P.M.;
"Genetic basis of human complement C4A deficiency. Detection of a
point mutation leading to nonexpression.";
J. Clin. Invest. 91:1681-1686(1993).
[21]
FUNCTION.
PubMed=8538770; DOI=10.1038/379177a0;
Dodds A.W., Ren X.D., Willis A.C., Law S.K.;
"The reaction mechanism of the internal thioester in the human
complement component C4.";
Nature 379:177-179(1996).
[22]
INVOLVEMENT IN SLE.
PubMed=10092831;
Lokki M.L., Circolo A., Ahokas P., Rupert K.L., Yu C.Y., Colten H.R.;
"Deficiency of human complement protein C4 due to identical frameshift
mutations in the C4A and C4B genes.";
J. Immunol. 162:3687-3693(1999).
[23]
REVIEW, DESCRIPTION OF ALLOTYPES, AND TISSUE SPECIFICITY.
PubMed=11367523; DOI=10.1016/S1567-5769(01)00019-4;
Blanchong C.A., Chung E.K., Rupert K.L., Yang Y., Yang Z., Zhou B.,
Moulds J.M., Yu C.Y.;
"Genetic, structural and functional diversities of human complement
components C4A and C4B and their mouse homologues, Slp and C4.";
Int. Immunopharmacol. 1:365-392(2001).
[24]
GLYCOSYLATION AT ASN-226.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1391.
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).
[26]
STRUCTURAL BASIS OF POLYMORPHISM.
PubMed=2431902;
Yu C.Y., Belt K.T., Giles C.M., Campbell R.D., Porter R.R.;
"Structural basis of the polymorphism of human complement components
C4A and C4B: gene size, reactivity and antigenicity.";
EMBO J. 5:2873-2881(1986).
[27]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-862; ASN-1328 AND
ASN-1391.
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).
[28]
INVOLVEMENT IN SLE.
PubMed=17503323; DOI=10.1086/518257;
Yang Y., Chung E.K., Wu Y.L., Savelli S.L., Nagaraja H.N., Zhou B.,
Hebert M., Jones K.N., Shu Y., Kitzmiller K., Blanchong C.A.,
McBride K.L., Higgins G.C., Rennebohm R.M., Rice R.R., Hackshaw K.V.,
Roubey R.A., Grossman J.M., Tsao B.P., Birmingham D.J., Rovin B.H.,
Hebert L.A., Yu C.Y.;
"Gene copy-number variation and associated polymorphisms of complement
component C4 in human systemic lupus erythematosus (SLE): low copy
number is a risk factor for and high copy number is a protective
factor against SLE susceptibility in European Americans.";
Am. J. Hum. Genet. 80:1037-1054(2007).
[29]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-226 AND ASN-1328.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[30]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-226; ASN-1328 AND
ASN-1391.
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).
[31]
GLYCOSYLATION AT ASN-1328.
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).
[32]
GLYCOSYLATION [LARGE SCALE ANALYSIS], AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[33]
GLYCOSYLATION AT THR-1244, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[34]
PHOSPHORYLATION AT SER-918.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[35]
POLYMORPHISM, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=26814963; DOI=10.1038/nature16549;
Schizophrenia Working Group of the Psychiatric Genomics Consortium;
Sekar A., Bialas A.R., de Rivera H., Davis A., Hammond T.R.,
Kamitaki N., Tooley K., Presumey J., Baum M., Van Doren V.,
Genovese G., Rose S.A., Handsaker R.E., Daly M.J., Carroll M.C.,
Stevens B., McCarroll S.A.;
"Schizophrenia risk from complex variation of complement component
4.";
Nature 530:177-183(2016).
[36]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 957-1323.
PubMed=12367531; DOI=10.1016/S0022-2836(02)00854-9;
van den Elsen J.M., Martin A., Wong V., Clemenza L., Rose D.R.,
Isenman D.E.;
"X-ray crystal structure of the C4d fragment of human complement
component C4.";
J. Mol. Biol. 322:1103-1115(2002).
[37]
VARIANT ALA-1286 (ALLOTYPE C4A6).
PubMed=1573268;
Anderson M.J., Milner C.M., Cotton G.H., Campbell R.D.;
"The coding sequence of the hemolytically inactive C4A6 allotype of
human complement component C4 reveals that a single arginine to
tryptophan substitution at beta-chain residue 458 is the likely cause
of the defect.";
J. Immunol. 148:2795-2802(1992).
-!- FUNCTION: Non-enzymatic component of C3 and C5 convertases and
thus essential for the propagation of the classical complement
pathway. Covalently binds to immunoglobulins and immune complexes
and enhances the solubilization of immune aggregates and the
clearance of IC through CR1 on erythrocytes. C4A isotype is
responsible for effective binding to form amide bonds with immune
aggregates or protein antigens, while C4B isotype catalyzes the
transacylation of the thioester carbonyl group to form ester bonds
with carbohydrate antigens.
-!- FUNCTION: Derived from proteolytic degradation of complement C4,
C4a anaphylatoxin is a mediator of local inflammatory process. It
induces the contraction of smooth muscle, increases vascular
permeability and causes histamine release from mast cells and
basophilic leukocytes.
-!- SUBUNIT: Circulates in blood as a disulfide-linked trimer of an
alpha, beta and gamma chain.
-!- SUBCELLULAR LOCATION: Secreted. Cell junction, synapse
{ECO:0000269|PubMed:26814963}. Cell projection, axon
{ECO:0000269|PubMed:26814963}. Cell projection, dendrite
{ECO:0000269|PubMed:26814963}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P0C0L4-1; Sequence=Displayed;
Name=2;
IsoId=P0C0L4-2; Sequence=VSP_046252;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Complement component C4 is expressed at
highest levels in the liver, at moderate levels in the adrenal
cortex, adrenal medulla, thyroid gland,and the kidney, and at
lowest levels in the heart, ovary, small intestine, thymus,
pancreas and spleen. The extra-hepatic sites of expression may be
important for the local protection and inflammatory response.
{ECO:0000269|PubMed:11367523}.
-!- PTM: Prior to secretion, the single-chain precursor is
enzymatically cleaved to yield non-identical chains alpha, beta
and gamma. During activation, the alpha chain is cleaved by C1
into C4a and C4b, and C4b stays linked to the beta and gamma
chains. Further degradation of C4b by C1 into the inactive
fragments C4c and C4d blocks the generation of C3 convertase. The
proteolytic cleavages often are incomplete so that many structural
forms can be found in plasma.
-!- PTM: N- and O-glycosylated. O-glycosylated with a core 1 or
possibly core 8 glycan. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:23234360}.
-!- POLYMORPHISM: The complement component C4 is the most polymorphic
protein of the complement system. It is the product of 2 closely
linked and highly homologous genes, C4A and C4B. Once polymorphic
variation is discounted, the 2 isotypes differ by only 4 amino
acids at positions 1120-1125: PCPVLD for C4A and LSPVIH for C4B.
The 2 isotypes bear several antigenic determinants defining
Chido/Rodgers blood group system [MIM:614374]. Rodgers
determinants are generally associated with C4A allotypes, and
Chido with C4B. Variations at these loci involve not only
nucleotide polymorphisms, but also gene number and gene size. Some
individuals may lack either C4A, or C4B gene. Partial deficiency
of C4A or C4B is the most commonly inherited immune deficiency
known in humans with a combined frequency over 31% in the normal
Caucasian population (PubMed:11367523). C4A6 allotype is deficient
in hemolytic activity. Allotype C4A13 is infrequent. Common copy-
number variants of C4A and C4B affecting expression of complement
component C4 in the brain have been associated with schizophrenia
risk (PubMed:26814963). {ECO:0000269|PubMed:11367523,
ECO:0000269|PubMed:26814963}.
-!- DISEASE: Complement component 4A deficiency (C4AD) [MIM:614380]: A
rare defect of the complement classical pathway associated with
the development of autoimmune disorders, mainly systemic lupus
with or without associated glomerulonephritis.
{ECO:0000269|PubMed:8473511}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A
chronic, relapsing, inflammatory, and often febrile multisystemic
disorder of connective tissue, characterized principally by
involvement of the skin, joints, kidneys and serosal membranes. It
is of unknown etiology, but is thought to represent a failure of
the regulatory mechanisms of the autoimmune system. The disease is
marked by a wide range of system dysfunctions, an elevated
erythrocyte sedimentation rate, and the formation of LE cells in
the blood or bone marrow. {ECO:0000269|PubMed:10092831,
ECO:0000269|PubMed:17503323}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Interindividual copy-number variation (CNV) of complement
component C4 and associated polymorphisms result in different
susceptibilities to SLE. The risk of SLE susceptibility has been
shown to be significantly increased among subjects with only two
copies of total C4. A high copy number is a protective factor
against SLE.
-!- SEQUENCE CAUTION:
Sequence=AAB59537.1; Type=Miscellaneous discrepancy; Note=During cDNA synthesis, the 5' end has been inverted (PubMed:3838531).; Evidence={ECO:0000305|PubMed:3838531};
Sequence=BAE06071.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=chrg";
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EMBL; K02403; AAB59537.1; ALT_SEQ; mRNA.
EMBL; M59815; AAA51855.1; -; Genomic_DNA.
EMBL; M59816; AAA51855.1; JOINED; Genomic_DNA.
EMBL; L26261; AAA20121.2; -; Genomic_DNA.
EMBL; AB209989; BAE06071.1; ALT_INIT; mRNA.
EMBL; AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL929593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR936924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012372; AAH12372.2; -; mRNA.
EMBL; BC063289; AAH63289.1; -; mRNA.
EMBL; BC144546; AAI44547.1; -; mRNA.
EMBL; BC146673; AAI46674.1; -; mRNA.
EMBL; BC146849; AAI46850.1; -; mRNA.
EMBL; BC151204; AAI51205.1; -; mRNA.
EMBL; BC171786; AAI71786.1; -; mRNA.
EMBL; M14824; AAA52292.1; -; Genomic_DNA.
EMBL; X77491; CAA54627.1; -; Genomic_DNA.
EMBL; AY379925; AAR89152.1; -; Genomic_DNA.
EMBL; AY379926; AAR89153.1; -; Genomic_DNA.
EMBL; AY379927; AAR89154.1; -; Genomic_DNA.
EMBL; AY379928; AAR89155.1; -; Genomic_DNA.
EMBL; AY379929; AAR89156.1; -; Genomic_DNA.
EMBL; AY379930; AAR89157.1; -; Genomic_DNA.
EMBL; AY379931; AAR89158.1; -; Genomic_DNA.
EMBL; AY379932; AAR89159.1; -; Genomic_DNA.
EMBL; AY379933; AAR89160.1; -; Genomic_DNA.
EMBL; AY379934; AAR89161.1; -; Genomic_DNA.
EMBL; AY379935; AAR89162.1; -; Genomic_DNA.
EMBL; AY379960; AAR89164.1; -; Genomic_DNA.
EMBL; AY379962; AAR89166.1; -; Genomic_DNA.
EMBL; AY379963; AAR89167.1; -; Genomic_DNA.
EMBL; AY379964; AAR89168.1; -; Genomic_DNA.
EMBL; AY379965; AAR89169.1; -; Genomic_DNA.
EMBL; AY379966; AAR89170.1; -; Genomic_DNA.
EMBL; U77886; AAK49810.1; -; Genomic_DNA.
EMBL; V00502; CAA23760.1; -; mRNA.
EMBL; K00830; AAA36229.1; -; mRNA.
CCDS; CCDS47404.1; -. [P0C0L4-1]
CCDS; CCDS59005.1; -. [P0C0L4-2]
PIR; B20807; B20807.
PIR; I56095; C4HU.
RefSeq; NP_001002029.3; NM_001002029.3.
RefSeq; NP_001239133.1; NM_001252204.1. [P0C0L4-2]
RefSeq; NP_009224.2; NM_007293.2. [P0C0L4-1]
UniGene; Hs.534847; -.
UniGene; Hs.720022; -.
PDB; 1HZF; X-ray; 2.30 A; A=957-1323.
PDB; 4FXG; X-ray; 3.75 A; A/D=20-675, B/E=680-1446, C/F=1454-1744.
PDB; 4FXK; X-ray; 3.60 A; A=20-675, B=680-1446, C=1454-1744.
PDB; 4XAM; X-ray; 4.20 A; C/E=757-1446, D/F=1454-1744.
PDB; 5JPM; X-ray; 3.75 A; A/D=20-675, B/E=680-1446, C/F=1454-1744.
PDB; 5JPN; X-ray; 3.60 A; A=20-675, B=680-1446, C=1455-1744.
PDB; 5JTW; X-ray; 3.50 A; A/D=20-675, B/E=757-1446, C/F=1454-1744.
PDBsum; 1HZF; -.
PDBsum; 4FXG; -.
PDBsum; 4FXK; -.
PDBsum; 4XAM; -.
PDBsum; 5JPM; -.
PDBsum; 5JPN; -.
PDBsum; 5JTW; -.
ProteinModelPortal; P0C0L4; -.
SMR; P0C0L4; -.
BioGrid; 107181; 24.
BioGrid; 107182; 2.
IntAct; P0C0L4; 19.
STRING; 9606.ENSP00000396688; -.
DrugBank; DB00028; Immune Globulin Human.
iPTMnet; P0C0L4; -.
PhosphoSitePlus; P0C0L4; -.
UniCarbKB; P0C0L4; -.
BioMuta; C4A; -.
DMDM; 476007827; -.
EPD; P0C0L4; -.
MaxQB; P0C0L4; -.
PaxDb; P0C0L4; -.
PeptideAtlas; P0C0L4; -.
PRIDE; P0C0L4; -.
Ensembl; ENST00000383325; ENSP00000372815; ENSG00000206340.
Ensembl; ENST00000421274; ENSP00000388662; ENSG00000227746.
Ensembl; ENST00000428956; ENSP00000396688; ENSG00000244731. [P0C0L4-1]
Ensembl; ENST00000498271; ENSP00000420212; ENSG00000244731. [P0C0L4-2]
GeneID; 720; -.
GeneID; 721; -.
KEGG; hsa:720; -.
KEGG; hsa:721; -.
UCSC; uc011doy.3; human. [P0C0L4-1]
CTD; 720; -.
CTD; 721; -.
DisGeNET; 100293534; -.
DisGeNET; 720; -.
DisGeNET; 721; -.
EuPathDB; HostDB:ENSG00000244731.7; -.
GeneCards; C4A; -.
HGNC; HGNC:1323; C4A.
HPA; CAB009811; -.
HPA; CAB032603; -.
HPA; HPA046356; -.
HPA; HPA048287; -.
HPA; HPA050103; -.
MalaCards; C4A; -.
MIM; 120790; phenotype.
MIM; 120810; gene.
MIM; 152700; phenotype.
MIM; 614374; phenotype.
MIM; 614380; phenotype.
neXtProt; NX_P0C0L4; -.
OpenTargets; ENSG00000244731; -.
Orphanet; 117; Behcet disease.
Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA25903; -.
PharmGKB; PA25904; -.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
GeneTree; ENSGT00760000118982; -.
HOGENOM; HOG000290712; -.
HOVERGEN; HBG107123; -.
InParanoid; P0C0L4; -.
KO; K03989; -.
OMA; DFACYSP; -.
OrthoDB; EOG091G00FL; -.
PhylomeDB; P0C0L4; -.
TreeFam; TF313285; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-174577; Activation of C3 and C5.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SABIO-RK; P0C0L4; -.
EvolutionaryTrace; P0C0L4; -.
GeneWiki; C4A; -.
PMAP-CutDB; B0QZR6; -.
PRO; PR:P0C0L4; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000244731; -.
Genevisible; P0C0L4; HS.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0001849; F:complement component C1q binding; IDA:BHF-UCL.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006956; P:complement activation; IGI:BHF-UCL.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IGI:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
Gene3D; 1.20.91.20; -; 1.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 2.60.40.690; -; 2.
InterPro; IPR009048; A-macroglobulin_rcpt-bd.
InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
InterPro; IPR011626; A2M_comp.
InterPro; IPR002890; A2M_N.
InterPro; IPR011625; A2M_N_2.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001599; Macroglobln_a2.
InterPro; IPR019742; MacrogloblnA2_CS.
InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR018933; Netrin_module_non-TIMP.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
Pfam; PF00207; A2M; 1.
Pfam; PF07678; A2M_comp; 1.
Pfam; PF01835; A2M_N; 1.
Pfam; PF07703; A2M_N_2; 1.
Pfam; PF07677; A2M_recep; 1.
Pfam; PF01821; ANATO; 1.
Pfam; PF01759; NTR; 1.
Pfam; PF10569; Thiol-ester_cl; 1.
PRINTS; PR00004; ANAPHYLATOXN.
SMART; SM01360; A2M; 1.
SMART; SM01359; A2M_N_2; 1.
SMART; SM01361; A2M_recep; 1.
SMART; SM00104; ANATO; 1.
SMART; SM00643; C345C; 1.
SUPFAM; SSF47686; SSF47686; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF49410; SSF49410; 1.
SUPFAM; SSF50242; SSF50242; 1.
PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PROSITE; PS50189; NTR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood group antigen;
Cell junction; Cell projection; Cleavage on pair of basic residues;
Complement pathway; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal; Sulfation; Synapse;
Systemic lupus erythematosus; Thioester bond.
SIGNAL 1 19
CHAIN 20 675 Complement C4 beta chain.
/FTId=PRO_0000005966.
PROPEP 676 679 {ECO:0000269|PubMed:6167582}.
/FTId=PRO_0000005967.
CHAIN 680 1446 Complement C4-A alpha chain.
/FTId=PRO_0000005968.
CHAIN 680 756 C4a anaphylatoxin.
/FTId=PRO_0000005969.
CHAIN 757 1446 C4b-A.
/FTId=PRO_0000005970.
CHAIN 957 1336 C4d-A.
/FTId=PRO_0000042698.
PROPEP 1447 1453
/FTId=PRO_0000005971.
CHAIN 1454 1744 Complement C4 gamma chain.
/FTId=PRO_0000005972.
DOMAIN 702 736 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1595 1742 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
SITE 1125 1125 Responsible for effective binding to form
amide bonds with immune aggregates or
protein antigens.
MOD_RES 918 918 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 1417 1417 Sulfotyrosine.
{ECO:0000269|PubMed:3944109}.
MOD_RES 1420 1420 Sulfotyrosine.
{ECO:0000269|PubMed:3944109}.
MOD_RES 1422 1422 Sulfotyrosine.
{ECO:0000269|PubMed:3944109}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19159218}.
CARBOHYD 862 862 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 1244 1244 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23234360}.
CARBOHYD 1328 1328 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 1391 1391 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
DISULFID 702 728 {ECO:0000250}.
DISULFID 703 735 {ECO:0000250}.
DISULFID 716 736 {ECO:0000250}.
DISULFID 1595 1673 {ECO:0000250}.
DISULFID 1618 1742 {ECO:0000250}.
CROSSLNK 1010 1013 Isoglutamyl cysteine thioester (Cys-Gln).
VAR_SEQ 1458 1503 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046252.
VARIANT 141 141 L -> V (in dbSNP:rs9296005).
/FTId=VAR_069154.
VARIANT 347 347 S -> Y (in allotype C4A3a, allotype C4A6;
dbSNP:rs150969927).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1988494}.
/FTId=VAR_019778.
VARIANT 418 418 V -> A (in allotype C4A4).
{ECO:0000269|PubMed:6546707}.
/FTId=VAR_069155.
VARIANT 477 477 R -> W (in allotype C4A6).
{ECO:0000269|Ref.8}.
/FTId=VAR_001987.
VARIANT 549 549 H -> P (in dbSNP:rs2229405).
{ECO:0000269|Ref.8}.
/FTId=VAR_069156.
VARIANT 726 726 P -> L (in allotype C4A3a).
{ECO:0000269|PubMed:1988494}.
/FTId=VAR_001988.
VARIANT 727 727 D -> N. {ECO:0000269|PubMed:8012361}.
/FTId=VAR_019779.
VARIANT 907 907 A -> T (in dbSNP:rs141302872).
{ECO:0000269|Ref.8}.
/FTId=VAR_019780.
VARIANT 1073 1073 D -> G (in allotype C4A1, allotype C4A2;
dbSNP:rs147162052).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3696167,
ECO:0000269|Ref.8}.
/FTId=VAR_069158.
VARIANT 1176 1176 N -> S (in allotype C4A1;
dbSNP:rs17874654).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:3696167,
ECO:0000269|Ref.3, ECO:0000269|Ref.8}.
/FTId=VAR_069159.
VARIANT 1201 1201 T -> S (in allotype C4A4).
{ECO:0000269|PubMed:6546707}.
/FTId=VAR_001992.
VARIANT 1207 1207 V -> A (in allotype C4A1, allotype C4A13;
dbSNP:rs28357075).
{ECO:0000269|PubMed:3696167,
ECO:0000269|PubMed:6832377,
ECO:0000269|Ref.8}.
/FTId=VAR_001993.
VARIANT 1210 1210 L -> R (in allotype C4A1, allotype C4A13;
dbSNP:rs28357076).
{ECO:0000269|PubMed:3696167,
ECO:0000269|PubMed:6832377,
ECO:0000269|Ref.8}.
/FTId=VAR_001994.
VARIANT 1286 1286 S -> A (in allotype C4A1, allotype C4A3a,
allotype C4A6; dbSNP:rs201016130).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1988494,
ECO:0000269|PubMed:3696167,
ECO:0000269|PubMed:6832377,
ECO:0000269|Ref.3}.
/FTId=VAR_001995.
CONFLICT 217 217 A -> V (in Ref. 5; AAI71786).
{ECO:0000305}.
CONFLICT 643 643 A -> S (in Ref. 5; AAH63289).
{ECO:0000305}.
CONFLICT 729 729 R -> W (in Ref. 5; AAH63289).
{ECO:0000305}.
CONFLICT 1013 1013 Q -> E (in Ref. 11; AA sequence, 12; AA
sequence and 13; AA sequence).
{ECO:0000305}.
CONFLICT 1109 1110 SQ -> IA (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 1182 1182 K -> I (in Ref. 5; AAH63289).
{ECO:0000305}.
CONFLICT 1245 1245 P -> Q (in Ref. 5; AAH63289).
{ECO:0000305}.
CONFLICT 1271 1271 H -> V (in Ref. 12; AA sequence and 16;
AA sequence). {ECO:0000305}.
CONFLICT 1300 1300 R -> V (in Ref. 12; AA sequence and 16;
AA sequence). {ECO:0000305}.
CONFLICT 1419 1421 Missing (in Ref. 1; AAB59537).
{ECO:0000305}.
CONFLICT 1635 1635 D -> G (in Ref. 5; AAH12372).
{ECO:0000305}.
CONFLICT 1637 1637 R -> S (in Ref. 5; AAI44547/AAI46850).
{ECO:0000305}.
CONFLICT 1678 1678 E -> G (in Ref. 5; AAI71786).
{ECO:0000305}.
CONFLICT 1704 1704 D -> E (in Ref. 5; AAH12372).
{ECO:0000305}.
STRAND 22 32 {ECO:0000244|PDB:5JTW}.
STRAND 37 45 {ECO:0000244|PDB:5JTW}.
STRAND 51 59 {ECO:0000244|PDB:5JTW}.
STRAND 67 69 {ECO:0000244|PDB:5JTW}.
STRAND 72 77 {ECO:0000244|PDB:5JTW}.
STRAND 82 87 {ECO:0000244|PDB:5JTW}.
HELIX 91 97 {ECO:0000244|PDB:5JTW}.
HELIX 99 101 {ECO:0000244|PDB:5JTW}.
STRAND 107 113 {ECO:0000244|PDB:5JTW}.
HELIX 116 119 {ECO:0000244|PDB:5JTW}.
STRAND 126 135 {ECO:0000244|PDB:5JTW}.
STRAND 139 146 {ECO:0000244|PDB:5JTW}.
STRAND 148 150 {ECO:0000244|PDB:5JTW}.
STRAND 155 163 {ECO:0000244|PDB:5JTW}.
STRAND 167 169 {ECO:0000244|PDB:5JTW}.
STRAND 174 179 {ECO:0000244|PDB:5JTW}.
STRAND 181 183 {ECO:0000244|PDB:5JTW}.
STRAND 185 191 {ECO:0000244|PDB:5JTW}.
STRAND 194 203 {ECO:0000244|PDB:5JTW}.
STRAND 210 221 {ECO:0000244|PDB:5JTW}.
STRAND 228 233 {ECO:0000244|PDB:5JTW}.
STRAND 240 253 {ECO:0000244|PDB:5JTW}.
STRAND 262 270 {ECO:0000244|PDB:5JTW}.
STRAND 278 287 {ECO:0000244|PDB:5JTW}.
STRAND 289 291 {ECO:0000244|PDB:5JTW}.
STRAND 293 295 {ECO:0000244|PDB:5JTW}.
STRAND 301 304 {ECO:0000244|PDB:5JTW}.
STRAND 309 314 {ECO:0000244|PDB:5JTW}.
HELIX 316 325 {ECO:0000244|PDB:5JTW}.
HELIX 330 332 {ECO:0000244|PDB:5JTW}.
STRAND 337 346 {ECO:0000244|PDB:5JTW}.
TURN 347 349 {ECO:0000244|PDB:5JTW}.
STRAND 352 357 {ECO:0000244|PDB:5JTW}.
STRAND 361 364 {ECO:0000244|PDB:5JTW}.
STRAND 366 370 {ECO:0000244|PDB:5JTW}.
STRAND 372 374 {ECO:0000244|PDB:5JTW}.
STRAND 382 392 {ECO:0000244|PDB:5JTW}.
STRAND 395 397 {ECO:0000244|PDB:5JTW}.
STRAND 402 409 {ECO:0000244|PDB:5JTW}.
STRAND 412 414 {ECO:0000244|PDB:5JTW}.
STRAND 417 424 {ECO:0000244|PDB:5JTW}.
STRAND 430 436 {ECO:0000244|PDB:5JTW}.
STRAND 442 450 {ECO:0000244|PDB:5JTW}.
STRAND 452 454 {ECO:0000244|PDB:5JTW}.
STRAND 456 463 {ECO:0000244|PDB:5JTW}.
STRAND 472 476 {ECO:0000244|PDB:5JTW}.
STRAND 488 498 {ECO:0000244|PDB:5JTW}.
STRAND 504 511 {ECO:0000244|PDB:5JTW}.
STRAND 514 522 {ECO:0000244|PDB:5JTW}.
STRAND 527 532 {ECO:0000244|PDB:5JTW}.
TURN 535 537 {ECO:0000244|PDB:5JTW}.
STRAND 539 549 {ECO:0000244|PDB:5JTW}.
STRAND 552 561 {ECO:0000244|PDB:5JTW}.
STRAND 571 575 {ECO:0000244|PDB:5JTW}.
STRAND 586 605 {ECO:0000244|PDB:5JTW}.
HELIX 607 611 {ECO:0000244|PDB:5JTW}.
HELIX 621 628 {ECO:0000244|PDB:5JTW}.
HELIX 629 631 {ECO:0000244|PDB:5JTW}.
HELIX 643 650 {ECO:0000244|PDB:5JTW}.
STRAND 652 655 {ECO:0000244|PDB:5JTW}.
STRAND 657 660 {ECO:0000244|PDB:5JTW}.
TURN 666 668 {ECO:0000244|PDB:5JTW}.
STRAND 780 782 {ECO:0000244|PDB:5JTW}.
STRAND 786 798 {ECO:0000244|PDB:5JTW}.
STRAND 804 814 {ECO:0000244|PDB:5JTW}.
TURN 815 817 {ECO:0000244|PDB:5JTW}.
STRAND 818 821 {ECO:0000244|PDB:5JTW}.
STRAND 825 829 {ECO:0000244|PDB:5JTW}.
STRAND 832 836 {ECO:0000244|PDB:5JTW}.
STRAND 849 851 {ECO:0000244|PDB:5JTW}.
STRAND 854 857 {ECO:0000244|PDB:5JTW}.
STRAND 859 861 {ECO:0000244|PDB:5JTW}.
STRAND 863 869 {ECO:0000244|PDB:5JTW}.
STRAND 875 877 {ECO:0000244|PDB:5JTW}.
HELIX 878 880 {ECO:0000244|PDB:5JTW}.
STRAND 885 889 {ECO:0000244|PDB:5JTW}.
STRAND 893 896 {ECO:0000244|PDB:5JTW}.
STRAND 899 903 {ECO:0000244|PDB:5JTW}.
STRAND 906 921 {ECO:0000244|PDB:5JTW}.
STRAND 924 934 {ECO:0000244|PDB:5JTW}.
STRAND 936 948 {ECO:0000244|PDB:5JTW}.
STRAND 951 961 {ECO:0000244|PDB:5JTW}.
STRAND 974 982 {ECO:0000244|PDB:5JTW}.
HELIX 997 1001 {ECO:0000244|PDB:1HZF}.
HELIX 1011 1030 {ECO:0000244|PDB:1HZF}.
HELIX 1034 1036 {ECO:0000244|PDB:5JTW}.
HELIX 1041 1057 {ECO:0000244|PDB:1HZF}.
TURN 1062 1064 {ECO:0000244|PDB:5JTW}.
HELIX 1076 1089 {ECO:0000244|PDB:1HZF}.
HELIX 1090 1092 {ECO:0000244|PDB:1HZF}.
HELIX 1097 1107 {ECO:0000244|PDB:1HZF}.
HELIX 1108 1110 {ECO:0000244|PDB:1HZF}.
STRAND 1113 1115 {ECO:0000244|PDB:5JTW}.
HELIX 1126 1132 {ECO:0000244|PDB:1HZF}.
HELIX 1137 1153 {ECO:0000244|PDB:1HZF}.
TURN 1158 1161 {ECO:0000244|PDB:1HZF}.
HELIX 1162 1185 {ECO:0000244|PDB:1HZF}.
HELIX 1190 1202 {ECO:0000244|PDB:1HZF}.
HELIX 1207 1218 {ECO:0000244|PDB:1HZF}.
STRAND 1225 1228 {ECO:0000244|PDB:5JTW}.
HELIX 1259 1275 {ECO:0000244|PDB:1HZF}.
HELIX 1280 1292 {ECO:0000244|PDB:1HZF}.
HELIX 1294 1297 {ECO:0000244|PDB:5JTW}.
HELIX 1302 1319 {ECO:0000244|PDB:1HZF}.
STRAND 1327 1335 {ECO:0000244|PDB:5JTW}.
STRAND 1338 1346 {ECO:0000244|PDB:5JTW}.
STRAND 1348 1350 {ECO:0000244|PDB:5JTW}.
STRAND 1356 1359 {ECO:0000244|PDB:5JTW}.
STRAND 1364 1373 {ECO:0000244|PDB:5JTW}.
STRAND 1376 1386 {ECO:0000244|PDB:5JTW}.
STRAND 1395 1405 {ECO:0000244|PDB:5JTW}.
STRAND 1409 1411 {ECO:0000244|PDB:5JTW}.
STRAND 1465 1475 {ECO:0000244|PDB:5JTW}.
STRAND 1484 1489 {ECO:0000244|PDB:5JTW}.
STRAND 1494 1496 {ECO:0000244|PDB:5JTW}.
HELIX 1498 1506 {ECO:0000244|PDB:5JTW}.
STRAND 1511 1518 {ECO:0000244|PDB:5JTW}.
STRAND 1521 1527 {ECO:0000244|PDB:5JTW}.
STRAND 1534 1544 {ECO:0000244|PDB:5JTW}.
STRAND 1552 1560 {ECO:0000244|PDB:5JTW}.
STRAND 1564 1570 {ECO:0000244|PDB:5JTW}.
STRAND 1573 1575 {ECO:0000244|PDB:5JTW}.
STRAND 1581 1584 {ECO:0000244|PDB:5JTW}.
STRAND 1587 1590 {ECO:0000244|PDB:5JTW}.
HELIX 1613 1618 {ECO:0000244|PDB:5JTW}.
STRAND 1624 1637 {ECO:0000244|PDB:5JTW}.
STRAND 1640 1652 {ECO:0000244|PDB:5JTW}.
STRAND 1664 1670 {ECO:0000244|PDB:5JTW}.
STRAND 1681 1687 {ECO:0000244|PDB:5JTW}.
STRAND 1708 1711 {ECO:0000244|PDB:5JTW}.
HELIX 1716 1719 {ECO:0000244|PDB:5JTW}.
HELIX 1721 1723 {ECO:0000244|PDB:5JTW}.
HELIX 1726 1740 {ECO:0000244|PDB:5JTW}.
SEQUENCE 1744 AA; 192785 MW; 9396A4CC4DA3602C CRC64;
MRLLWGLIWA SSFFTLSLQK PRLLLFSPSV VHLGVPLSVG VQLQDVPRGQ VVKGSVFLRN
PSRNNVPCSP KVDFTLSSER DFALLSLQVP LKDAKSCGLH QLLRGPEVQL VAHSPWLKDS
LSRTTNIQGI NLLFSSRRGH LFLQTDQPIY NPGQRVRYRV FALDQKMRPS TDTITVMVEN
SHGLRVRKKE VYMPSSIFQD DFVIPDISEP GTWKISARFS DGLESNSSTQ FEVKKYVLPN
FEVKITPGKP YILTVPGHLD EMQLDIQARY IYGKPVQGVA YVRFGLLDED GKKTFFRGLE
SQTKLVNGQS HISLSKAEFQ DALEKLNMGI TDLQGLRLYV AAAIIESPGG EMEEAELTSW
YFVSSPFSLD LSKTKRHLVP GAPFLLQALV REMSGSPASG IPVKVSATVS SPGSVPEVQD
IQQNTDGSGQ VSIPIIIPQT ISELQLSVSA GSPHPAIARL TVAAPPSGGP GFLSIERPDS
RPPRVGDTLN LNLRAVGSGA TFSHYYYMIL SRGQIVFMNR EPKRTLTSVS VFVDHHLAPS
FYFVAFYYHG DHPVANSLRV DVQAGACEGK LELSVDGAKQ YRNGESVKLH LETDSLALVA
LGALDTALYA AGSKSHKPLN MGKVFEAMNS YDLGCGPGGG DSALQVFQAA GLAFSDGDQW
TLSRKRLSCP KEKTTRKKRN VNFQKAINEK LGQYASPTAK RCCQDGVTRL PMMRSCEQRA
ARVQQPDCRE PFLSCCQFAE SLRKKSRDKG QAGLQRALEI LQEEDLIDED DIPVRSFFPE
NWLWRVETVD RFQILTLWLP DSLTTWEIHG LSLSKTKGLC VATPVQLRVF REFHLHLRLP
MSVRRFEQLE LRPVLYNYLD KNLTVSVHVS PVEGLCLAGG GGLAQQVLVP AGSARPVAFS
VVPTAAAAVS LKVVARGSFE FPVGDAVSKV LQIEKEGAIH REELVYELNP LDHRGRTLEI
PGNSDPNMIP DGDFNSYVRV TASDPLDTLG SEGALSPGGV ASLLRLPRGC GEQTMIYLAP
TLAASRYLDK TEQWSTLPPE TKDHAVDLIQ KGYMRIQQFR KADGSYAAWL SRDSSTWLTA
FVLKVLSLAQ EQVGGSPEKL QETSNWLLSQ QQADGSFQDP CPVLDRSMQG GLVGNDETVA
LTAFVTIALH HGLAVFQDEG AEPLKQRVEA SISKANSFLG EKASAGLLGA HAAAITAYAL
TLTKAPVDLL GVAHNNLMAM AQETGDNLYW GSVTGSQSNA VSPTPAPRNP SDPMPQAPAL
WIETTAYALL HLLLHEGKAE MADQASAWLT RQGSFQGGFR STQDTVIALD ALSAYWIASH
TTEERGLNVT LSSTGRNGFK SHALQLNNRQ IRGLEEELQF SLGSKINVKV GGNSKGTLKV
LRTYNVLDMK NTTCQDLQIE VTVKGHVEYT MEANEDYEDY EYDELPAKDD PDAPLQPVTP
LQLFEGRRNR RRREAPKVVE EQESRVHYTV CIWRNGKVGL SGMAIADVTL LSGFHALRAD
LEKLTSLSDR YVSHFETEGP HVLLYFDSVP TSRECVGFEA VQEVPVGLVQ PASATLYDYY
NPERRCSVFY GAPSKSRLLA TLCSAEVCQC AEGKCPRQRR ALERGLQDED GYRMKFACYY
PRVEYGFQVK VLREDSRAAF RLFETKITQV LHFTKDVKAA ANQMRNFLVR ASCRLRLEPG
KEYLIMGLDG ATYDLEGHPQ YLLDSNSWIE EMPSERLCRS TRQRAACAQL NDFLQEYGTQ
GCQV


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