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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]

 CO4B_HUMAN              Reviewed;        1744 AA.
P0C0L5; A2BHY4; P01028; P78445; Q13160; Q13906; Q14033; Q14835;
Q6U2E9; Q6U2G1; Q6U2I5; Q6U2L1; Q6U2L7; Q6U2L9; Q6U2M5; Q6VCV8;
Q96SA7; Q9NPK5; Q9UIP5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 2.
25-OCT-2017, entry version 126.
RecName: Full=Complement C4-B;
AltName: Full=Basic complement C4;
AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3;
Contains:
RecName: Full=Complement C4 beta chain;
Contains:
RecName: Full=Complement C4-B alpha chain;
Contains:
RecName: Full=C4a anaphylatoxin;
Contains:
RecName: Full=C4b-B;
Contains:
RecName: Full=C4d-B;
Contains:
RecName: Full=Complement C4 gamma chain;
Flags: Precursor;
Name=C4B; Synonyms=CO4, CPAMD3;
and
Name=C4B_2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-1317.
TISSUE=Blood;
PubMed=8575831; DOI=10.1007/BF00587313;
Ulgiati D., Townend D.C., Christiansen F.T., Dawkins R.L.,
Abraham L.J.;
"Complete sequence of the complement C4 gene from the HLA-A1, B8,
C4AQ0, C4B1, DR3 haplotype.";
Immunogenetics 43:250-252(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-347 AND ALA-907.
Rowen L., Dankers C., Baskin D., Faust J., Loretz C., Ahearn M.E.,
Banta A., Swartzell S., Smith T.M., Spies T., Hood L.;
"Sequence determination of 300 kilobases of the human class III MHC
locus.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-907 AND ASP-1073.
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS TYR-347
AND ALA-907.
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]
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).
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 956-1336, AND VARIANT ASP-1073.
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).
[8]
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).
[9]
PROTEIN SEQUENCE OF 957-1336.
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).
[10]
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).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1055-1225 (ALLOTYPE C4B12).
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).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1055-1225, AND VARIANTS ASN-1176;
VAL-1207 AND LEU-1210.
PubMed=14989716; DOI=10.1111/j.0001-2815.2004.00147.x;
Lopez-Goyanes A., Moreno M.A., Ferre S., Paz-Artal E.;
"C4d DNA sequence of complement C4B93 and recombination mechanisms for
its generation.";
Tissue Antigens 63:260-262(2004).
[13]
PROTEIN SEQUENCE OF 1199-1304.
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).
[14]
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).
[15]
INVOLVEMENT IN C4BD AND SLE.
PubMed=3265961;
Wilson W.A., Perez M.C.;
"Complete C4B deficiency in black Americans with systemic lupus
erythematosus.";
J. Rheumatol. 15:1855-1858(1988).
[16]
FUNCTION, INVOLVEMENT OF HIS-1125 IN IMMUNOGLOBULIN-BINDING AND
HEMOLYSIS, AND MUTAGENESIS OF LEU-1120; SER-1121; ILE-1124 AND
HIS-1125.
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1328.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[23]
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).
[24]
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).
[25]
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).
-!- FUNCTION: Non-enzymatic component of the 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
alpha, beta and gamma chains.
-!- SUBCELLULAR LOCATION: Secreted. Cell junction, synapse
{ECO:0000269|PubMed:26814963}. Cell projection, axon
{ECO:0000269|PubMed:26814963}. Cell projection, dendrite
{ECO:0000269|PubMed:26814963}.
-!- 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.
-!- 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. The
second copy of C4B gene present in some individuals has been
called C4B_2 by the HUGO Gene Nomenclature Committee (HGNC). 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). 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: 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.
-!- DISEASE: Complement component 4B deficiency (C4BD) [MIM:614379]: 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:3265961}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAA99717.1; Type=Erroneous gene model prediction; 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; U24578; AAA99717.1; ALT_SEQ; Genomic_DNA.
EMBL; AF019413; AAB67980.1; -; Genomic_DNA.
EMBL; AY379860; AAR89087.1; -; Genomic_DNA.
EMBL; AY379862; AAR89089.1; -; Genomic_DNA.
EMBL; AY379864; AAR89091.1; -; Genomic_DNA.
EMBL; AY379866; AAR89093.1; -; Genomic_DNA.
EMBL; AY379868; AAR89095.1; -; Genomic_DNA.
EMBL; AY379870; AAR89097.1; -; Genomic_DNA.
EMBL; AY379872; AAR89099.1; -; Genomic_DNA.
EMBL; AY379874; AAR89101.1; -; Genomic_DNA.
EMBL; AY379876; AAR89103.1; -; Genomic_DNA.
EMBL; AY379878; AAR89105.1; -; Genomic_DNA.
EMBL; AY379880; AAR89107.1; -; Genomic_DNA.
EMBL; AY379882; AAR89109.1; -; Genomic_DNA.
EMBL; AY379884; AAR89111.1; -; Genomic_DNA.
EMBL; AY379886; AAR89113.1; -; Genomic_DNA.
EMBL; AY379888; AAR89115.1; -; Genomic_DNA.
EMBL; AY379890; AAR89117.1; -; Genomic_DNA.
EMBL; AY379892; AAR89119.1; -; Genomic_DNA.
EMBL; AY379894; AAR89121.1; -; Genomic_DNA.
EMBL; AY379896; AAR89123.1; -; Genomic_DNA.
EMBL; AY379898; AAR89125.1; -; Genomic_DNA.
EMBL; AY379900; AAR89127.1; -; Genomic_DNA.
EMBL; AY379902; AAR89130.1; -; Genomic_DNA.
EMBL; AY379904; AAR89132.1; -; Genomic_DNA.
EMBL; AY379906; AAR89134.1; -; Genomic_DNA.
EMBL; AY379908; AAR89136.1; -; Genomic_DNA.
EMBL; AY379910; AAR89138.1; -; Genomic_DNA.
EMBL; AY379912; AAR89139.1; -; Genomic_DNA.
EMBL; AY379914; AAR89142.1; -; Genomic_DNA.
EMBL; AY379916; AAR89144.1; -; Genomic_DNA.
EMBL; AY379918; AAR89145.1; -; Genomic_DNA.
EMBL; AY379920; AAR89148.1; -; Genomic_DNA.
EMBL; AY379922; AAR89150.1; -; Genomic_DNA.
EMBL; AY379924; AAR89151.1; -; Genomic_DNA.
EMBL; AY379959; AAR89163.1; -; Genomic_DNA.
EMBL; AY379936; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379937; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379938; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379939; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379940; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379941; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379942; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379943; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379944; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379945; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379946; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379947; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379948; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379949; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379950; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379951; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379952; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379953; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379954; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379955; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379956; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379957; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AY379958; AAR89163.1; JOINED; Genomic_DNA.
EMBL; AL049547; CAB89302.1; -; Genomic_DNA.
EMBL; BX679671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; K02404; AAA59651.1; -; mRNA.
EMBL; U77887; AAK49811.1; -; Genomic_DNA.
EMBL; AY343497; AAQ99144.1; -; Genomic_DNA.
CCDS; CCDS47405.1; -.
PIR; B20807; B20807.
RefSeq; NP_001002029.3; NM_001002029.3.
RefSeq; NP_001229752.1; NM_001242823.2.
UniGene; Hs.534847; -.
UniGene; Hs.720022; -.
PDB; 4XAM; X-ray; 4.20 A; A/B=20-675.
PDBsum; 4XAM; -.
ProteinModelPortal; P0C0L5; -.
SMR; P0C0L5; -.
BioGrid; 107182; 2.
DIP; DIP-47260N; -.
IntAct; P0C0L5; 7.
STRING; 9606.ENSP00000415941; -.
DrugBank; DB00028; Immune Globulin Human.
MEROPS; I39.951; -.
iPTMnet; P0C0L5; -.
PhosphoSitePlus; P0C0L5; -.
DMDM; 476007828; -.
SWISS-2DPAGE; P0C0L5; -.
PaxDb; P0C0L5; -.
PeptideAtlas; P0C0L5; -.
PRIDE; P0C0L5; -.
TopDownProteomics; P0C0L5; -.
DNASU; 721; -.
Ensembl; ENST00000375177; ENSP00000364321; ENSG00000228454.
Ensembl; ENST00000411583; ENSP00000407942; ENSG00000228267.
Ensembl; ENST00000435363; ENSP00000415941; ENSG00000224389.
Ensembl; ENST00000435500; ENSP00000412786; ENSG00000233312.
Ensembl; ENST00000449788; ENSP00000414200; ENSG00000236625.
GeneID; 100293534; -.
GeneID; 721; -.
KEGG; hsa:100293534; -.
KEGG; hsa:721; -.
UCSC; uc011dpd.3; human.
CTD; 100293534; -.
CTD; 721; -.
DisGeNET; 100293534; -.
DisGeNET; 720; -.
DisGeNET; 721; -.
EuPathDB; HostDB:ENSG00000224389.8; -.
GeneCards; C4B; -.
GeneCards; C4B_2; -.
H-InvDB; HIX0164690; -.
H-InvDB; HIX0164691; -.
H-InvDB; HIX0166073; -.
H-InvDB; HIX0166340; -.
H-InvDB; HIX0166869; -.
H-InvDB; HIX0167127; -.
H-InvDB; HIX0167359; -.
H-InvDB; HIX0167360; -.
HGNC; HGNC:1324; C4B.
HGNC; HGNC:42398; C4B_2.
HPA; HPA046356; -.
HPA; HPA048287; -.
HPA; HPA050103; -.
MalaCards; C4B; -.
MIM; 120820; gene.
MIM; 152700; phenotype.
MIM; 614374; phenotype.
MIM; 614379; phenotype.
neXtProt; NX_P0C0L5; -.
OpenTargets; ENSG00000224389; -.
Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA25904; -.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
GeneTree; ENSGT00760000118982; -.
HOGENOM; HOG000290712; -.
HOVERGEN; HBG107123; -.
InParanoid; P0C0L5; -.
KO; K03989; -.
OMA; GQCHISL; -.
OrthoDB; EOG091G00FL; -.
PhylomeDB; P0C0L5; -.
TreeFam; TF313285; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-174577; Activation of C3 and C5.
Reactome; R-HSA-977606; Regulation of Complement cascade.
GeneWiki; Complement_component_4B; -.
PRO; PR:P0C0L5; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000224389; -.
ExpressionAtlas; P0C0L5; baseline and differential.
Genevisible; P0C0L5; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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:0044216; C:other organism cell; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IDA:BHF-UCL.
GO; GO:0001848; F:complement 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:0006956; P:complement activation; IGI:BHF-UCL.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0032490; P:detection of molecule of bacterial origin; IDA:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0008228; P:opsonization; TAS:BHF-UCL.
GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IGI:BHF-UCL.
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; Blood group antigen; Cell junction; Cell projection;
Cleavage on pair of basic residues; Complement pathway;
Complete proteome; Direct protein sequencing; 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_0000042699.
PROPEP 676 679 {ECO:0000269|PubMed:6167582}.
/FTId=PRO_0000042700.
CHAIN 680 1446 Complement C4-B alpha chain.
/FTId=PRO_0000042701.
CHAIN 680 756 C4a anaphylatoxin.
/FTId=PRO_0000042702.
CHAIN 757 1446 C4b-B.
/FTId=PRO_0000042703.
CHAIN 957 1336 C4d-B.
/FTId=PRO_0000042704.
PROPEP 1447 1453
/FTId=PRO_0000042705.
CHAIN 1454 1744 Complement C4 gamma chain.
/FTId=PRO_0000042706.
DOMAIN 702 736 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1595 1742 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
MOD_RES 918 918 Phosphoserine.
{ECO:0000250|UniProtKB:P0C0L4}.
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}.
CARBOHYD 862 862 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1328 1328 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16740002}.
CARBOHYD 1391 1391 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718}.
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).
VARIANT 347 347 S -> Y (in allotype C4B-long;
dbSNP:rs139889867).
{ECO:0000269|PubMed:14574404,
ECO:0000269|Ref.2}.
/FTId=VAR_023729.
VARIANT 478 478 P -> L (in allotype C4B1-hi).
/FTId=VAR_069160.
VARIANT 907 907 T -> A (in allotype C4B-long and allotype
C4B2; dbSNP:rs796750528).
{ECO:0000269|PubMed:14574404,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_023730.
VARIANT 1073 1073 G -> D (in allotype C4B2 and allotype
C4B5-Rg1; dbSNP:rs2258218).
{ECO:0000269|PubMed:6546707,
ECO:0000269|Ref.3}.
/FTId=VAR_023731.
VARIANT 1176 1176 S -> N (in allotype C4B1a;
dbSNP:rs2746414).
{ECO:0000269|PubMed:14989716}.
/FTId=VAR_023732.
VARIANT 1207 1207 A -> V (in allotype C4B5-Rg1;
dbSNP:rs200888163).
{ECO:0000269|PubMed:14989716}.
/FTId=VAR_023734.
VARIANT 1210 1210 R -> L (in allotype C4B5-Rg1;
dbSNP:rs112683215).
{ECO:0000269|PubMed:14989716}.
/FTId=VAR_023735.
VARIANT 1317 1317 I -> F (in allotype C4B1-SC01;
dbSNP:rs2023616).
{ECO:0000269|PubMed:8575831}.
/FTId=VAR_069161.
MUTAGEN 1120 1120 L->P: No effect on hemolytic activity,
nor on C1-dependent binding to IgG.
{ECO:0000269|PubMed:2395880}.
MUTAGEN 1121 1121 S->C: 30-40% decrease in hemolytic
activity and C1-dependent binding to IgG.
{ECO:0000269|PubMed:2395880}.
MUTAGEN 1124 1124 I->A: 50-60% decrease in hemolytic
activity and C1-dependent binding to IgG.
{ECO:0000269|PubMed:2395880}.
MUTAGEN 1125 1125 H->A: 20% decrease in hemolytic activity,
2-fold increase in C1-dependent binding
to IgG. {ECO:0000269|PubMed:2395880}.
MUTAGEN 1125 1125 H->D: 2.5-3 fold-decrease in hemolytic
activity, 3-fold increase in C1-dependent
binding to IgG.
{ECO:0000269|PubMed:2395880}.
CONFLICT 714 714 R -> S (in Ref. 3; AAR89101).
{ECO:0000305}.
CONFLICT 729 729 R -> Q (in Ref. 3; AAR89127).
{ECO:0000305}.
CONFLICT 980 981 VT -> LQ (in Ref. 1; AAA99717).
{ECO:0000305}.
CONFLICT 1013 1013 Q -> E (in Ref. 8; AA sequence, 9; AA
sequence and 10; AA sequence).
{ECO:0000305}.
CONFLICT 1109 1110 SQ -> IA (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 1271 1271 H -> V (in Ref. 9; AA sequence and 13; AA
sequence). {ECO:0000305}.
CONFLICT 1300 1300 R -> V (in Ref. 9; AA sequence and 13; AA
sequence). {ECO:0000305}.
CONFLICT 1654 1654 T -> RA (in Ref. 1; AAA99717).
{ECO:0000305}.
CONFLICT 1698 1698 H -> Q (in Ref. 1; AAA99717).
{ECO:0000305}.
SEQUENCE 1744 AA; 192751 MW; E724B85F7FA673C5 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
VVPTAATAVS LKVVARGSFE FPVGDAVSKV LQIEKEGAIH REELVYELNP LDHRGRTLEI
PGNSDPNMIP DGDFNSYVRV TASDPLDTLG SEGALSPGGV ASLLRLPRGC GEQTMIYLAP
TLAASRYLDK TEQWSTLPPE TKDHAVDLIQ KGYMRIQQFR KADGSYAAWL SRGSSTWLTA
FVLKVLSLAQ EQVGGSPEKL QETSNWLLSQ QQADGSFQDL SPVIHRSMQG GLVGNDETVA
LTAFVTIALH HGLAVFQDEG AEPLKQRVEA SISKASSFLG EKASAGLLGA HAAAITAYAL
TLTKAPADLR GVAHNNLMAM AQETGDNLYW GSVTGSQSNA VSPTPAPRNP SDPMPQAPAL
WIETTAYALL HLLLHEGKAE MADQAAAWLT 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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