GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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.
07-APR-2021, entry version 153.
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]
INTERACTION WITH CR1.
PubMed=2972794; DOI=10.1084/jem.168.5.1699;
Klickstein L.B., Bartow T.J., Miletic V., Rabson L.D., Smith J.A.,
Fearon D.T.;
"Identification of distinct C3b and C4b recognition sites in the human
C3b/C4b receptor (CR1, CD35) by deletion mutagenesis.";
J. Exp. Med. 168:1699-1717(1988).
[17]
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).
[18]
INTERACTION WITH CR1.
PubMed=8175757;
Krych M., Clemenza L., Howdeshell D., Hauhart R., Hourcade D.,
Atkinson J.P.;
"Analysis of the functional domains of complement receptor type 1 (C3b/C4b
receptor; CD35) by substitution mutagenesis.";
J. Biol. Chem. 269:13273-13278(1994).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
STRUCTURAL BASIS OF POLYMORPHISM.
PubMed=2431902; DOI=10.1002/j.1460-2075.1986.tb04582.x;
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).
[26]
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).
[27]
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. C4b interacts with CR1 (via Sushi 1 and Sushi 2
domains). {ECO:0000269|PubMed:2972794, ECO:0000269|PubMed:8175757}.
-!- INTERACTION:
PRO_0000042699; O00187: MASP2; NbExp=4; IntAct=EBI-26369106, EBI-7965040;
-!- 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 variants 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 variants 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";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
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.
PDB; 4XAM; X-ray; 4.20 A; A/B=20-675.
PDB; 6YSQ; X-ray; 3.30 A; A/B=1-1744.
PDBsum; 4XAM; -.
PDBsum; 6YSQ; -.
SMR; P0C0L5; -.
BioGRID; 107182; 5.
ComplexPortal; CPX-6156; Classical and lectin pathway C3 convertase complex C4b2a-B.
DIP; DIP-47260N; -.
IntAct; P0C0L5; 11.
MINT; P0C0L5; -.
STRING; 9606.ENSP00000415941; -.
DrugBank; DB09130; Copper.
DrugBank; DB00028; Human immunoglobulin G.
DrugBank; DB01593; Zinc.
DrugBank; DB14487; Zinc acetate.
DrugBank; DB14533; Zinc chloride.
DrugBank; DB14548; Zinc sulfate, unspecified form.
MEROPS; I39.951; -.
GlyConnect; 1146; 32 N-Linked glycans (4 sites).
GlyGen; P0C0L5; 4 sites, 7 N-linked glycans (3 sites).
iPTMnet; P0C0L5; -.
PhosphoSitePlus; P0C0L5; -.
BioMuta; C4B; -.
DMDM; 476007828; -.
SWISS-2DPAGE; P0C0L5; -.
CPTAC; non-CPTAC-1107; -.
EPD; P0C0L5; -.
jPOST; P0C0L5; -.
MassIVE; P0C0L5; -.
PaxDb; P0C0L5; -.
PeptideAtlas; P0C0L5; -.
PRIDE; P0C0L5; -.
ProteomicsDB; 435; -.
ProteomicsDB; 52293; -.
ProteomicsDB; 67395; -.
TopDownProteomics; P0C0L5; -.
Antibodypedia; 35326; 330 antibodies.
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; 721; -.
GeneCards; C4B; -.
GeneCards; C4B_2; -.
HGNC; HGNC:1324; C4B.
HGNC; HGNC:42398; C4B_2.
HPA; ENSG00000224389; Group enriched (adrenal gland, liver).
MalaCards; C4B; -.
MIM; 120820; gene.
MIM; 152700; phenotype.
MIM; 614374; phenotype.
MIM; 614379; phenotype.
neXtProt; NX_P0C0L5; -.
OpenTargets; ENSG00000224389; -.
Orphanet; 169147; Immunodeficiency due to a classical component pathway complement deficiency.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA25904; -.
VEuPathDB; HostDB:ENSG00000224389.8; -.
eggNOG; KOG1366; Eukaryota.
GeneTree; ENSGT00940000155739; -.
InParanoid; P0C0L5; -.
OMA; HACFFPT; -.
OrthoDB; 28894at2759; -.
PhylomeDB; P0C0L5; -.
TreeFam; TF313285; -.
PathwayCommons; P0C0L5; -.
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.
SABIO-RK; P0C0L5; -.
BioGRID-ORCS; 100293534; 3 hits in 44 CRISPR screens.
BioGRID-ORCS; 721; 4 hits in 598 CRISPR screens.
ChiTaRS; C4B; human.
GeneWiki; Complement_component_4B; -.
Pharos; P0C0L5; Tbio.
PRO; PR:P0C0L5; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; P0C0L5; protein.
Bgee; ENSG00000224389; Expressed in right lobe of liver and 113 other tissues.
ExpressionAtlas; P0C0L5; baseline and differential.
Genevisible; P0C0L5; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
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: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.
CDD; cd00017; ANATO; 1.
Gene3D; 2.40.50.120; -; 1.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 2.60.40.690; -; 1.
InterPro; IPR009048; A-macroglobulin_rcpt-bd.
InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
InterPro; IPR011625; A2M_N_BRD.
InterPro; IPR011626; Alpha-macroglobulin_TED.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
InterPro; IPR037569; Complement_C4A.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001599; Macroglobln_a2.
InterPro; IPR019742; MacrogloblnA2_CS.
InterPro; IPR002890; MG2.
InterPro; IPR041555; MG3.
InterPro; IPR040839; MG4.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR018933; Netrin_module_non-TIMP.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
PANTHER; PTHR11412:SF86; PTHR11412:SF86; 1.
Pfam; PF00207; A2M; 1.
Pfam; PF07703; A2M_BRD; 1.
Pfam; PF07677; A2M_recep; 1.
Pfam; PF01821; ANATO; 1.
Pfam; PF01835; MG2; 1.
Pfam; PF17791; MG3; 1.
Pfam; PF17789; MG4; 1.
Pfam; PF01759; NTR; 1.
Pfam; PF07678; TED_complement; 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;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Phosphoprotein; Reference proteome;
Secreted; Signal; Sulfation; Synapse; Systemic lupus erythematosus;
Thioester bond.
SIGNAL 1..19
CHAIN 20..675
/note="Complement C4 beta chain"
/id="PRO_0000042699"
PROPEP 676..679
/evidence="ECO:0000269|PubMed:6167582"
/id="PRO_0000042700"
CHAIN 680..1446
/note="Complement C4-B alpha chain"
/id="PRO_0000042701"
CHAIN 680..756
/note="C4a anaphylatoxin"
/id="PRO_0000042702"
CHAIN 757..1446
/note="C4b-B"
/id="PRO_0000042703"
CHAIN 957..1336
/note="C4d-B"
/id="PRO_0000042704"
PROPEP 1447..1453
/id="PRO_0000042705"
CHAIN 1454..1744
/note="Complement C4 gamma chain"
/id="PRO_0000042706"
DOMAIN 702..736
/note="Anaphylatoxin-like"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
DOMAIN 1595..1742
/note="NTR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
MOD_RES 918
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P0C0L4"
MOD_RES 1417
/note="Sulfotyrosine"
/evidence="ECO:0000269|PubMed:3944109"
MOD_RES 1420
/note="Sulfotyrosine"
/evidence="ECO:0000269|PubMed:3944109"
MOD_RES 1422
/note="Sulfotyrosine"
/evidence="ECO:0000269|PubMed:3944109"
CARBOHYD 226
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:12754519"
CARBOHYD 862
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1328
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16740002"
CARBOHYD 1391
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:14760718"
DISULFID 702..728
/evidence="ECO:0000250"
DISULFID 703..735
/evidence="ECO:0000250"
DISULFID 716..736
/evidence="ECO:0000250"
DISULFID 1595..1673
/evidence="ECO:0000250"
DISULFID 1618..1742
/evidence="ECO:0000250"
CROSSLNK 1010..1013
/note="Isoglutamyl cysteine thioester (Cys-Gln)"
VARIANT 347
/note="S -> Y (in allotype C4B-long; dbSNP:rs139889867)"
/evidence="ECO:0000269|PubMed:14574404, ECO:0000269|Ref.2"
/id="VAR_023729"
VARIANT 478
/note="P -> L (in allotype C4B1-hi)"
/id="VAR_069160"
VARIANT 907
/note="T -> A (in allotype C4B-long and allotype C4B2;
dbSNP:rs796750528)"
/evidence="ECO:0000269|PubMed:14574404, ECO:0000269|Ref.2,
ECO:0000269|Ref.3"
/id="VAR_023730"
VARIANT 1073
/note="G -> D (in allotype C4B2 and allotype C4B5-Rg1;
dbSNP:rs2258218)"
/evidence="ECO:0000269|PubMed:6546707, ECO:0000269|Ref.3"
/id="VAR_023731"
VARIANT 1176
/note="S -> N (in allotype C4B1a; dbSNP:rs2746414)"
/evidence="ECO:0000269|PubMed:14989716"
/id="VAR_023732"
VARIANT 1207
/note="A -> V (in allotype C4B5-Rg1; dbSNP:rs2229403)"
/evidence="ECO:0000269|PubMed:14989716"
/id="VAR_023734"
VARIANT 1210
/note="R -> L (in allotype C4B5-Rg1; dbSNP:rs2229409)"
/evidence="ECO:0000269|PubMed:14989716"
/id="VAR_023735"
VARIANT 1317
/note="I -> F (in allotype C4B1-SC01; dbSNP:rs2023616)"
/evidence="ECO:0000269|PubMed:8575831"
/id="VAR_069161"
MUTAGEN 1120
/note="L->P: No effect on hemolytic activity, nor on C1-
dependent binding to IgG."
/evidence="ECO:0000269|PubMed:2395880"
MUTAGEN 1121
/note="S->C: 30-40% decrease in hemolytic activity and C1-
dependent binding to IgG."
/evidence="ECO:0000269|PubMed:2395880"
MUTAGEN 1124
/note="I->A: 50-60% decrease in hemolytic activity and C1-
dependent binding to IgG."
/evidence="ECO:0000269|PubMed:2395880"
MUTAGEN 1125
/note="H->A: 20% decrease in hemolytic activity, 2-fold
increase in C1-dependent binding to IgG."
/evidence="ECO:0000269|PubMed:2395880"
MUTAGEN 1125
/note="H->D: 2.5-3 fold-decrease in hemolytic activity, 3-
fold increase in C1-dependent binding to IgG."
/evidence="ECO:0000269|PubMed:2395880"
CONFLICT 714
/note="R -> S (in Ref. 3; AAR89101)"
/evidence="ECO:0000305"
CONFLICT 729
/note="R -> Q (in Ref. 3; AAR89127)"
/evidence="ECO:0000305"
CONFLICT 980..981
/note="VT -> LQ (in Ref. 1; AAA99717)"
/evidence="ECO:0000305"
CONFLICT 1013
/note="Q -> E (in Ref. 8; AA sequence, 9; AA sequence and
10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 1109..1110
/note="SQ -> IA (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 1271
/note="H -> V (in Ref. 9; AA sequence and 13; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 1300
/note="R -> V (in Ref. 9; AA sequence and 13; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 1654
/note="T -> RA (in Ref. 1; AAA99717)"
/evidence="ECO:0000305"
CONFLICT 1698
/note="H -> Q (in Ref. 1; AAA99717)"
/evidence="ECO:0000305"
STRAND 22..32
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 37..45
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 52..60
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 66..69
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 72..76
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 78..80
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 82..87
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 91..97
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 107..113
/evidence="ECO:0007744|PDB:6YSQ"
TURN 115..120
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 126..135
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 139..146
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 148..150
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 155..163
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 167..169
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 174..179
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 181..183
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 185..191
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 194..203
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 210..221
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 228..233
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 240..250
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 252..254
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 262..270
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 278..287
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 293..295
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 301..304
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 309..314
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 316..325
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 330..332
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 337..346
/evidence="ECO:0007744|PDB:6YSQ"
TURN 347..349
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 352..357
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 361..364
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 366..370
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 384..392
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 402..409
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 412..414
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 417..424
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 430..435
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 443..450
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 452..454
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 456..463
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 472..476
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 488..498
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 504..511
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 514..522
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 525..532
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 535..537
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 539..549
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 552..561
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 571..574
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 586..605
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 608..611
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 622..628
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 629..631
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 641..643
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 644..650
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 652..655
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 780..782
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 786..798
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 804..814
/evidence="ECO:0007744|PDB:6YSQ"
TURN 815..817
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 818..821
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 825..829
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 832..837
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 849..851
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 853..857
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 859..861
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 863..869
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 878..880
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 885..889
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 894..896
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 899..903
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 906..921
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 924..934
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 936..948
/evidence="ECO:0007744|PDB:6YSQ"
TURN 950..953
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 954..960
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 973..981
/evidence="ECO:0007744|PDB:6YSQ"
TURN 997..1000
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1001..1003
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1011..1030
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1035..1037
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1040..1053
/evidence="ECO:0007744|PDB:6YSQ"
TURN 1054..1057
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1068..1072
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1076..1088
/evidence="ECO:0007744|PDB:6YSQ"
TURN 1089..1092
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1097..1101
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1103..1109
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1113..1115
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1137..1151
/evidence="ECO:0007744|PDB:6YSQ"
TURN 1152..1155
/evidence="ECO:0007744|PDB:6YSQ"
TURN 1158..1160
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1162..1183
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1190..1202
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1207..1219
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1261..1275
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1276..1278
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1282..1292
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1303..1318
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1326..1335
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1338..1350
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1354..1356
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1362..1364
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1366..1370
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1372..1374
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1376..1386
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1395..1405
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1465..1474
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1484..1489
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1494..1496
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1498..1501
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1502..1504
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1506..1509
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1512..1517
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1519..1527
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1534..1536
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1539..1544
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1554..1560
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1564..1567
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1573..1575
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1581..1584
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1587..1590
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1613..1618
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1625..1634
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1640..1652
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1664..1670
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1681..1687
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1695..1699
/evidence="ECO:0007744|PDB:6YSQ"
STRAND 1708..1711
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1715..1718
/evidence="ECO:0007744|PDB:6YSQ"
HELIX 1724..1739
/evidence="ECO:0007744|PDB:6YSQ"
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


Related products :

Catalog number Product name Quantity
E0389h ELISA Basic complement C4,C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3,C4B,CO4,Complement C4-B,CPAMD3,Homo sapiens,Human 96T
E0389h ELISA kit Basic complement C4,C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3,C4B,CO4,Complement C4-B,CPAMD3,Homo sapiens,Human 96T
U0389h CLIA Basic complement C4,C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3,C4B,CO4,Complement C4-B,CPAMD3,Homo sapiens,Human 96T
E0389h ELISA Acidic complement C4,C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2,C4A,CO4,Complement C4-A,CPAMD2,Homo sapiens,Human 96T
E0389h ELISA kit Acidic complement C4,C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2,C4A,CO4,Complement C4-A,CPAMD2,Homo sapiens,Human 96T
U0389h CLIA Acidic complement C4,C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2,C4A,CO4,Complement C4-A,CPAMD2,Homo sapiens,Human 96T
E1970h ELISA kit C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Homo sapiens,Human 96T
U1970Rb CLIA kit C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Oryctolagus cuniculus,Rabbit 96T
E1970Rb ELISA kit C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Oryctolagus cuniculus,Rabbit 96T
E1970Rb ELISA C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Oryctolagus cuniculus,Rabbit 96T
E1970h ELISA C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Homo sapiens,Human 96T
U1970h CLIA kit C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Homo sapiens,Human 96T
U1970h CLIA C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Homo sapiens,Human 96T
U1970Rb CLIA C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Oryctolagus cuniculus,Rabbit 96T
U1970m CLIA C8a,Complement component 8 subunit alpha,Complement component C8 alpha chain,Mouse,Mus musculus 96T
U1970m CLIA kit C8a,Complement component 8 subunit alpha,Complement component C8 alpha chain,Mouse,Mus musculus 96T
E1970m ELISA C8a,Complement component 8 subunit alpha,Complement component C8 alpha chain,Mouse,Mus musculus 96T
E1970m ELISA kit C8a,Complement component 8 subunit alpha,Complement component C8 alpha chain,Mouse,Mus musculus 96T
LF-MA0198 anti-Complement C4 β-chain (52H10), Mouse monoclonal to Complement C4 β-chain, Isotype IgG1, Host Mouse 100 ul
LF-MA0188 anti-Complement C4 (γ-chain), Mouse monoclonal to Complement C4 (γ-chain), Isotype IgG2b, Host Mouse 100 ul
LF-MA0187 anti-Complement C4 (β-chain), Mouse monoclonal to Complement C4 (β-chain), Isotype IgG1, Host Mouse 100 ul
EIAAB08424 C8B,Complement component 8 subunit beta,Complement component C8 beta chain,Homo sapiens,Human
EIAAB08425 C8B,Complement component 8 subunit beta,Complement component C8 beta chain,Oryctolagus cuniculus,Rabbit
EIAAB08423 C8b,Complement component 8 subunit beta,Complement component C8 beta chain,Mouse,Mus musculus
EIAAB08422 C8b,Complement component 8 subunit beta,Complement component C8 beta chain,Rat,Rattus norvegicus