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Complement C3 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]

 CO3_HUMAN               Reviewed;        1663 AA.
P01024; A7E236;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
25-OCT-2017, entry version 220.
RecName: Full=Complement C3;
AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1;
Contains:
RecName: Full=Complement C3 beta chain;
Contains:
RecName: Full=C3-beta-c;
Short=C3bc;
Contains:
RecName: Full=Complement C3 alpha chain;
Contains:
RecName: Full=C3a anaphylatoxin;
Contains:
RecName: Full=Acylation stimulating protein;
Short=ASP;
AltName: Full=C3adesArg;
Contains:
RecName: Full=Complement C3b alpha' chain;
Contains:
RecName: Full=Complement C3c alpha' chain fragment 1;
Contains:
RecName: Full=Complement C3dg fragment;
Contains:
RecName: Full=Complement C3g fragment;
Contains:
RecName: Full=Complement C3d fragment;
Contains:
RecName: Full=Complement C3f fragment;
Contains:
RecName: Full=Complement C3c alpha' chain fragment 2;
Flags: Precursor;
Name=C3; Synonyms=CPAMD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-314.
PubMed=2579379; DOI=10.1073/pnas.82.3.708;
de Bruijn M.H.L., Fey G.H.;
"Human complement component C3: cDNA coding sequence and derived
primary structure.";
Proc. Natl. Acad. Sci. U.S.A. 82:708-712(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-102; LEU-314;
LYS-863; ASP-1224 AND THR-1367.
SeattleSNPs variation discovery resource;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY,
AND FUNCTION.
PubMed=8376604; DOI=10.1172/JCI116733;
Baldo A., Sniderman A.D., St-Luce S., Avramoglu R.K., Maslowska M.,
Hoang B., Monge J.C., Bell A., Mulay S., Cianflone K.;
"The adipsin-acylation stimulating protein system and regulation of
intracellular triglyceride synthesis.";
J. Clin. Invest. 92:1543-1547(1993).
[6]
PROTEIN SEQUENCE OF 672-748.
PubMed=1238393;
Hugli T.E.;
"Human anaphylatoxin (C3a) from the third component of complement.
Primary structure.";
J. Biol. Chem. 250:8293-8301(1975).
[7]
PROTEIN SEQUENCE OF 955-966, AND SUBUNIT.
TISSUE=Serum;
PubMed=7539791; DOI=10.1074/jbc.270.23.13645;
Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I.,
Stigbrand T., Gleich G.J., Sottrup-Jensen L.;
"Identification of angiotensinogen and complement C3dg as novel
proteins binding the proform of eosinophil major basic protein in
human pregnancy serum and plasma.";
J. Biol. Chem. 270:13645-13651(1995).
[8]
PROTEIN SEQUENCE OF 988-1036.
PubMed=6175959; DOI=10.1073/pnas.79.4.1054;
Thomas M.L., Janatova J., Gray W.R., Tack B.F.;
"Third component of human complement: localization of the internal
thiolester bond.";
Proc. Natl. Acad. Sci. U.S.A. 79:1054-1058(1982).
[9]
PROTEIN SEQUENCE OF 1409-1563.
PubMed=3279119;
Daoudaki M.E., Becherer J.D., Lambris J.D.;
"A 34-amino acid peptide of the third component of complement mediates
properdin binding.";
J. Immunol. 140:1577-1580(1988).
[10]
INTERACTION WITH HERPES SIMPLEX VIRUS HHV-1 AND HHV-2 GYCOPROTEIN C.
PubMed=2849025; DOI=10.1016/0882-4010(87)90012-X;
Eisenberg R.J., Ponce de Leon M., Friedman H.M., Fries L.F.,
Frank M.M., Hastings J.C., Cohen G.H.;
"Complement component C3b binds directly to purified glycoprotein C of
herpes simplex virus types 1 and 2.";
Microb. Pathog. 3:423-435(1987).
[11]
FUNCTION.
PubMed=2909530;
Cianflone K.M., Sniderman A.D., Walsh M.J., Vu H.T., Gagnon J.,
Rodriguez M.A.;
"Purification and characterization of acylation stimulating protein.";
J. Biol. Chem. 264:426-430(1989).
[12]
MUTAGENESIS OF THE THIOESTER BOND REGION.
PubMed=1577777;
Isaac L., Isenman D.E.;
"Structural requirements for thioester bond formation in human
complement component C3. Reassessment of the role of thioester bond
integrity on the conformation of C3.";
J. Biol. Chem. 267:10062-10069(1992).
[13]
DISULFIDE BONDS.
PubMed=8416818; DOI=10.1016/0014-5793(93)81139-Q;
Dolmer K., Sottrup-Jensen L.;
"Disulfide bridges in human complement component C3b.";
FEBS Lett. 315:85-90(1993).
[14]
FUNCTION.
PubMed=9059512; DOI=10.1016/S0005-2760(96)00144-0;
Tao Y., Cianflone K., Sniderman A.D., Colby-Germinario S.P.,
Germinario R.J.;
"Acylation-stimulating protein (ASP) regulates glucose transport in
the rat L6 muscle cell line.";
Biochim. Biophys. Acta 1344:221-229(1997).
[15]
IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=9555951;
Saleh J., Summers L.K., Cianflone K., Fielding B.A., Sniderman A.D.,
Frayn K.N.;
"Coordinated release of acylation stimulating protein (ASP) and
triacylglycerol clearance by human adipose tissue in vivo in the
postprandial period.";
J. Lipid Res. 39:884-891(1998).
[16]
FUNCTION.
PubMed=10432298; DOI=10.1042/bj3420041;
Murray I., Kohl J., Cianflone K.;
"Acylation-stimulating protein (ASP): structure-function determinants
of cell surface binding and triacylglycerol synthetic activity.";
Biochem. J. 342:41-48(1999).
[17]
INTERACTION WITH C5AR2.
PubMed=11773063; DOI=10.1074/jbc.C100714200;
Cain S.A., Monk P.N.;
"The orphan receptor C5L2 has high affinity binding sites for
complement fragments C5a and C5a des Arg(74).";
J. Biol. Chem. 277:7165-7169(2002).
[18]
INTERACTION WITH C5AR2.
PubMed=12540846; DOI=10.1074/jbc.M206169200;
Kalant D., Cain S.A., Maslowska M., Sniderman A.D., Cianflone K.,
Monk P.N.;
"The chemoattractant receptor-like protein C5L2 binds the C3a des-
Arg77/acylation-stimulating protein.";
J. Biol. Chem. 278:11123-11129(2003).
[19]
GLYCOSYLATION AT ASN-85.
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).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-939.
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).
[21]
EFFECTS OF EXERCISE.
PubMed=15809665; DOI=10.1038/sj.ijo.0802949;
Schrauwen P., Hesselink M.K., Jain M., Cianflone K.;
"Acylation-stimulating protein: effect of acute exercise and endurance
training.";
Int. J. Obes. Relat. Metab. Disord. 29:632-638(2005).
[22]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15833747; DOI=10.1074/jbc.M406921200;
Kalant D., MacLaren R., Cui W., Samanta R., Monk P.N., Laporte S.A.,
Cianflone K.;
"C5L2 is a functional receptor for acylation-stimulating protein.";
J. Biol. Chem. 280:23936-23944(2005).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85; ASN-939 AND ASN-1617.
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).
[24]
ASSOCIATION WITH TYPE 2 DIABETES.
PubMed=16302015; DOI=10.1038/sj.ijo.0803173;
Yang Y., Lu H.L., Zhang J., Yu H.Y., Wang H.W., Zhang M.X.,
Cianflone K.;
"Relationships among acylation stimulating protein, adiponectin and
complement C3 in lean vs obese type 2 diabetes.";
Int. J. Obes. Relat. Metab. Disord. 30:439-446(2006).
[25]
IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
PubMed=16333141; DOI=10.1194/jlr.M500500-JLR200;
Maslowska M., Legakis H., Assadi F., Cianflone K.;
"Targeting the signaling pathway of acylation stimulating protein.";
J. Lipid Res. 47:643-652(2006).
[26]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[27]
ASSOCIATION WITH OBESITY.
PubMed=18805911; DOI=10.1530/EJE-08-0467;
Wamba P.C., Mi J., Zhao X.Y., Zhang M.X., Wen Y., Cheng H., Hou D.Q.,
Cianflone K.;
"Acylation stimulating protein but not complement C3 associates with
metabolic syndrome components in Chinese children and adolescents.";
Eur. J. Endocrinol. 159:781-790(2008).
[28]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
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).
[29]
FUNCTION.
PubMed=19615750; DOI=10.1016/j.molimm.2009.06.007;
Cui W., Simaan M., Laporte S., Lodge R., Cianflone K.;
"C5a- and ASP-mediated C5L2 activation, endocytosis and recycling are
lost in S323I-C5L2 mutation.";
Mol. Immunol. 46:3086-3098(2009).
[30]
MUTAGENESIS OF ASP-1029; GLU-1030; GLU-1032; GLU-1035; ARG-1042;
ASP-1140; GLU-1153; ASP-1156; GLU-1159; GLU-1160; ASN-1163 AND
LYS-1284, AND INTERACTION WITH CR2 AND S.AUREUS SBI.
PubMed=20083651; DOI=10.4049/jimmunol.0902919;
Isenman D.E., Leung E., Mackay J.D., Bagby S., van den Elsen J.M.;
"Mutational analyses reveal that the staphylococcal immune evasion
molecule Sbi and complement receptor 2 (CR2) share overlapping contact
residues on C3d: implications for the controversy regarding the
CR2/C3d cocrystal structure.";
J. Immunol. 184:1946-1955(2010).
[31]
MUTAGENESIS OF ASP-1029; GLU-1030; GLU-1032; GLU-1110; ASP-1115;
ASP-1121; ASP-1140; GLU-1153; ASP-1156; GLU-1159; GLU-1160 AND
ASN-1163, AND INTERACTION WITH CR2.
PubMed=20951140; DOI=10.1016/j.jmb.2010.10.005;
Shaw C.D., Storek M.J., Young K.A., Kovacs J.M., Thurman J.M.,
Holers V.M., Hannan J.P.;
"Delineation of the complement receptor type 2-C3d complex by site-
directed mutagenesis and molecular docking.";
J. Mol. Biol. 404:697-710(2010).
[32]
ASSOCIATION WITH CORONARY HEART DISEASE.
PubMed=19913840; DOI=10.1016/j.metabol.2009.09.006;
Onat A., Hergenc G., Can G., Kaya Z., Yuksel H.;
"Serum complement C3: a determinant of cardiometabolic risk, additive
to the metabolic syndrome, in middle-aged population.";
Metabolism 59:628-634(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
PHOSPHORYLATION AT SER-38; SER-70; SER-297; SER-303; SER-672; SER-968;
SER-1321 AND SER-1573.
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).
[36]
STRUCTURE BY NMR OF C3A.
PubMed=3260670; DOI=10.1073/pnas.85.14.5036;
Nettesheim D.G., Edalji R.P., Mollison K.W., Greer J.,
Zuiderweg E.R.P.;
"Secondary structure of complement component C3a anaphylatoxin in
solution as determined by NMR spectroscopy: differences between
crystal and solution conformations.";
Proc. Natl. Acad. Sci. U.S.A. 85:5036-5040(1988).
[37]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF C3D.
PubMed=9596584; DOI=10.1126/science.280.5367.1277;
Nagar B., Jones R.G., Diefenbach R.J., Isenman D.E., Rini J.M.;
"X-ray crystal structure of C3d: a C3 fragment and ligand for
complement receptor 2.";
Science 280:1277-1281(1998).
[38]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF C3D IN COMPLEX WITH CR2, AND
MUTAGENESIS OF 1108-ILE-LEU-1109 AND ASN-1163.
PubMed=11387479; DOI=10.1126/science.1059118;
Szakonyi G., Guthridge J.M., Li D., Young K., Holers V.M., Chen X.S.;
"Structure of complement receptor 2 in complex with its C3d ligand.";
Science 292:1725-1728(2001).
[39]
X-RAY SCATTERING SOLUTION STRUCTURE OF C3D IN COMPLEX WITH CR2.
PubMed=15713468; DOI=10.1016/j.jmb.2004.12.006;
Gilbert H.E., Eaton J.T., Hannan J.P., Holers V.M., Perkins S.J.;
"Solution structure of the complex between CR2 SCR 1-2 and C3d of
human complement: an X-ray scattering and sedimentation modelling
study.";
J. Mol. Biol. 346:859-873(2005).
[40]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF C3C, AND X-RAY
CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF C3.
PubMed=16177781; DOI=10.1038/nature04005;
Janssen B.J.C., Huizinga E.G., Raaijmakers H.C.A., Roos A., Daha M.R.,
Nilsson-Ekdahl K., Nilsson B., Gros P.;
"Structures of complement component C3 provide insights into the
function and evolution of immunity.";
Nature 437:505-511(2005).
[41]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF C3B.
PubMed=17051160; DOI=10.1038/nature05172;
Janssen B.J.C., Christodoulidou A., McCarthy A., Lambris J.D.,
Gros P.;
"Structure of C3b reveals conformational changes that underlie
complement activity.";
Nature 444:213-216(2006).
[42]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF C3C IN COMPLEX WITH VSIG4,
X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF C3B IN COMPLEX WITH VSIG4,
AND GLYCOSYLATION AT ASN-85 AND ASN-939.
PubMed=17051150; DOI=10.1038/nature05263;
Wiesmann C., Katschke K.J., Yin J., Helmy K.Y., Steffek M.,
Fairbrother W.J., McCallum S.A., Embuscado L., DeForge L., Hass P.E.,
van Lookeren Campagne M.;
"Structure of C3b in complex with CRIg gives insights into regulation
of complement activation.";
Nature 444:217-220(2006).
[43]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-936 AND 1321-1663 IN
COMPLEX WITH INHIBITOR COMPSTATIN, DISULFIDE BONDS, AND GLYCOSYLATION
AT ASN-85.
PubMed=17684013; DOI=10.1074/jbc.M704587200;
Janssen B.J., Halff E.F., Lambris J.D., Gros P.;
"Structure of compstatin in complex with complement component C3c
reveals a new mechanism of complement inhibition.";
J. Biol. Chem. 282:29241-29247(2007).
[44]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 996-1287 IN COMPLEX WITH
S.AUREUS FIB.
PubMed=17351618; DOI=10.1038/ni1450;
Hammel M., Sfyroera G., Ricklin D., Magotti P., Lambris J.D.,
Geisbrecht B.V.;
"A structural basis for complement inhibition by Staphylococcus
aureus.";
Nat. Immunol. 8:430-437(2007).
[45]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 996-1303 IN COMPLEX WITH
S.AUREUS SBI, AND SUBUNIT.
PubMed=21055811; DOI=10.1016/j.molimm.2010.09.017;
Clark E.A., Crennell S., Upadhyay A., Zozulya A.V., Mackay J.D.,
Svergun D.I., Bagby S., van den Elsen J.M.;
"A structural basis for Staphylococcal complement subversion: X-ray
structure of the complement-binding domain of Staphylococcus aureus
protein Sbi in complex with ligand C3d.";
Mol. Immunol. 48:452-462(2011).
[46]
X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 996-1303 IN COMPLEX WITH
CR2, AND INTERACTION WITH CR2.
PubMed=21527715; DOI=10.1126/science.1201954;
van den Elsen J.M., Isenman D.E.;
"A crystal structure of the complex between human complement receptor
2 and its ligand C3d.";
Science 332:608-611(2011).
[47]
VARIANT C3S ASN-1216.
PubMed=2473125;
Poznansky M.C., Clissold P.M., Lachmann P.J.;
"The difference between human C3F and C3S results from a single amino
acid change from an asparagine to an aspartate residue at position
1216 on the alpha-chain of the complement component, C3.";
J. Immunol. 143:1254-1258(1989).
[48]
ERRATUM, AND RETRACTION.
PubMed=2584723;
Poznansky M.C., Clissold P.M., Lachmann P.J.;
J. Immunol. 143:3860-3862(1989).
[49]
VARIANTS GLY-102 AND LEU-314.
PubMed=1976733; DOI=10.1084/jem.172.4.1011;
Botto M., Yong Fong K., So A.K., Koch C., Walport M.J.;
"Molecular basis of polymorphisms of human complement component C3.";
J. Exp. Med. 172:1011-1017(1990).
[50]
VARIANT C3D ASN-549.
PubMed=7961791;
Singer L., Whitehead W.T., Akama H., Katz Y., Fishelson Z.,
Wetsel R.A.;
"Inherited human complement C3 deficiency. An amino acid substitution
in the beta-chain (Asp549 to Asn) impairs C3 secretion.";
J. Biol. Chem. 269:28494-28499(1994).
[51]
ASSOCIATION OF VARIANT GLY-102 WITH ARMD9.
PubMed=17634448; DOI=10.1056/NEJMoa072618;
Yates J.R.W., Sepp T., Matharu B.K., Khan J.C., Thurlby D.A.,
Shahid H., Clayton D.G., Hayward C., Morgan J., Wright A.F.,
Armbrecht A.M., Dhillon B., Deary I.J., Redmond E., Bird A.C.,
Moore A.T.;
"Complement C3 variant and the risk of age-related macular
degeneration.";
N. Engl. J. Med. 357:553-561(2007).
[52]
VARIANTS AHUS5 GLN-592; TRP-592; TRP-735; VAL-1094; ASN-1115;
TRP-1158; LYS-1161 AND ASP-1464, AND CHARACTERIZATION OF VARIANTS
AHUS5 GLN-592; TRP-592; VAL-1094; ASN-1115 AND LYS-1161.
PubMed=18796626; DOI=10.1182/blood-2008-01-133702;
Fremeaux-Bacchi V., Miller E.C., Liszewski M.K., Strain L., Blouin J.,
Brown A.L., Moghal N., Kaplan B.S., Weiss R.A., Lhotta K., Kapur G.,
Mattoo T., Nivet H., Wong W., Gie S., Hurault de Ligny B.,
Fischbach M., Gupta R., Hauhart R., Meunier V., Loirat C.,
Dragon-Durey M.A., Fridman W.H., Janssen B.J., Goodship T.H.,
Atkinson J.P.;
"Mutations in complement C3 predispose to development of atypical
hemolytic uremic syndrome.";
Blood 112:4948-4952(2008).
[53]
VARIANTS AHUS5 VAL-603 AND LEU-1042.
PubMed=20513133; DOI=10.1002/humu.21256;
Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.;
"Mutations in alternative pathway complement proteins in American
patients with atypical hemolytic uremic syndrome.";
Hum. Mutat. 31:E1445-E1460(2010).
[54]
VARIANT ASN-549, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22028381; DOI=10.1093/jmcb/mjr024;
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
Lin X., Zeng R., Wu J.R.;
"Quantitative detection of single amino acid polymorphisms by targeted
proteomics.";
J. Mol. Cell Biol. 3:309-315(2011).
[55]
CHARACTERIZATION OF VARIANT GLY-102.
PubMed=21555552; DOI=10.1073/pnas.1019338108;
Heurich M., Martinez-Barricarte R., Francis N.J., Roberts D.L.,
Rodriguez de Cordoba S., Morgan B.P., Harris C.L.;
"Common polymorphisms in C3, factor B, and factor H collaborate to
determine systemic complement activity and disease risk.";
Proc. Natl. Acad. Sci. U.S.A. 108:8761-8766(2011).
[56]
VARIANT ARMD9 GLN-155, AND CHARACTERIZATION OF VARIANT ARMD9 GLN-155.
PubMed=24036952; DOI=10.1038/ng.2741;
Seddon J.M., Yu Y., Miller E.C., Reynolds R., Tan P.L.,
Gowrisankar S., Goldstein J.I., Triebwasser M., Anderson H.E.,
Zerbib J., Kavanagh D., Souied E., Katsanis N., Daly M.J.,
Atkinson J.P., Raychaudhuri S.;
"Rare variants in CFI, C3 and C9 are associated with high risk of
advanced age-related macular degeneration.";
Nat. Genet. 45:1366-1370(2013).
-!- FUNCTION: C3 plays a central role in the activation of the
complement system. Its processing by C3 convertase is the central
reaction in both classical and alternative complement pathways.
After activation C3b can bind covalently, via its reactive
thioester, to cell surface carbohydrates or immune aggregates.
-!- FUNCTION: Derived from proteolytic degradation of complement C3,
C3a anaphylatoxin is a mediator of local inflammatory process. In
chronic inflammation, acts as a chemoattractant for neutrophils
(By similarity). It induces the contraction of smooth muscle,
increases vascular permeability and causes histamine release from
mast cells and basophilic leukocytes. {ECO:0000250}.
-!- FUNCTION: C3-beta-c: Acts as a chemoattractant for neutrophils in
chronic inflammation. {ECO:0000250}.
-!- FUNCTION: Acylation stimulating protein: adipogenic hormone that
stimulates triglyceride (TG) synthesis and glucose transport in
adipocytes, regulating fat storage and playing a role in
postprandial TG clearance. Appears to stimulate TG synthesis via
activation of the PLC, MAPK and AKT signaling pathways. Ligand for
C5AR2. Promotes the phosphorylation, ARRB2-mediated
internalization and recycling of C5AR2 (PubMed:8376604,
PubMed:2909530, PubMed:9059512, PubMed:10432298, PubMed:15833747,
PubMed:16333141, PubMed:19615750). {ECO:0000269|PubMed:10432298,
ECO:0000269|PubMed:15833747, ECO:0000269|PubMed:16333141,
ECO:0000269|PubMed:19615750, ECO:0000269|PubMed:2909530,
ECO:0000269|PubMed:8376604, ECO:0000269|PubMed:9059512}.
-!- SUBUNIT: C3 precursor is first processed by the removal of 4 Arg
residues, forming two chains, beta and alpha, linked by a
disulfide bond. C3 convertase activates C3 by cleaving the alpha
chain, releasing C3a anaphylatoxin and generating C3b (beta chain
+ alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi
domains 1 and 2). During pregnancy, C3dg exists as a complex
(probably a 2:2:2 heterohexamer) with AGT and the proform of PRG2.
Interacts with VSIG4. C3b interacts with herpes simplex virus 1
(HHV-1) and herpes simplex virus 2 (HHV-2) envelope glycoprotein
C; this interaction inhibits the activation of the complement
system. Interacts with S.aureus immunoglobulin-binding protein
sbi, this prevents interaction between C3dg and CR2. Interacts
with S.aureus fib. Interacts (both C3a and ASP) with C5AR2; the
interaction occurs with higher affinity for ASP, enhancing the
phosphorylation and activation of C5AR2, recruitment of ARRB2 to
the cell surface and endocytosis of GRP77.
{ECO:0000269|PubMed:11387479, ECO:0000269|PubMed:11773063,
ECO:0000269|PubMed:12540846, ECO:0000269|PubMed:17051150,
ECO:0000269|PubMed:17351618, ECO:0000269|PubMed:17684013,
ECO:0000269|PubMed:20083651, ECO:0000269|PubMed:20951140,
ECO:0000269|PubMed:21055811, ECO:0000269|PubMed:21527715,
ECO:0000269|PubMed:2849025, ECO:0000269|PubMed:7539791}.
-!- INTERACTION:
P00751:CFB; NbExp=3; IntAct=EBI-905851, EBI-1223668;
P08603:CFH; NbExp=5; IntAct=EBI-905851, EBI-1223708;
Q9Y279-1:VSIG4; NbExp=5; IntAct=EBI-905851, EBI-903144;
Q9Y279-2:VSIG4; NbExp=2; IntAct=EBI-905851, EBI-903148;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma. The acylation stimulating protein
(ASP) is expressed in adipocytes and released into the plasma
during both the fasting and postprandial periods.
{ECO:0000269|PubMed:15833747, ECO:0000269|PubMed:9555951}.
-!- PTM: C3b is rapidly split in two positions by factor I and a
cofactor to form iC3b (inactivated C3b) and C3f which is released.
Then iC3b is slowly cleaved (possibly by factor I) to form C3c
(beta chain + alpha' chain fragment 1 + alpha' chain fragment 2),
C3dg and C3f. Other proteases produce other fragments such as C3d
or C3g. C3a is further processed by carboxypeptidases to release
the C-terminal arginine residue generating the acylation
stimulating protein (ASP). Levels of ASP are increased in
adipocytes in the postprandial period and by insulin and dietary
chylomicrons.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- POLYMORPHISM: There are two alleles: C3S (C3 slow), the most
common allele in all races and C3F (C3 fast), relatively frequent
in Caucasians, less common in Black Americans, extremely rare in
Orientals.
-!- DISEASE: Complement component 3 deficiency (C3D) [MIM:613779]: A
rare defect of the complement classical pathway. Patients develop
recurrent, severe, pyogenic infections because of ineffective
opsonization of pathogens. Some patients may also develop
autoimmune disorders, such as arthralgia and vasculitic rashes,
lupus-like syndrome and membranoproliferative glomerulonephritis.
{ECO:0000269|PubMed:7961791}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Macular degeneration, age-related, 9 (ARMD9)
[MIM:611378]: A form of age-related macular degeneration, a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world. In most patients,
the disease is manifest as ophthalmoscopically visible yellowish
accumulations of protein and lipid that lie beneath the retinal
pigment epithelium and within an elastin-containing structure
known as Bruch membrane. {ECO:0000269|PubMed:17634448,
ECO:0000269|PubMed:24036952}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Hemolytic uremic syndrome atypical 5 (AHUS5)
[MIM:612925]: An atypical form of hemolytic uremic syndrome. It is
a complex genetic disease characterized by microangiopathic
hemolytic anemia, thrombocytopenia, renal failure and absence of
episodes of enterocolitis and diarrhea. In contrast to typical
hemolytic uremic syndrome, atypical forms have a poorer prognosis,
with higher death rates and frequent progression to end-stage
renal disease. {ECO:0000269|PubMed:18796626,
ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Other genes may play a role in modifying the phenotype.
-!- DISEASE: Note=Increased levels of C3 and its cleavage product ASP,
are associated with obesity, diabetes and coronary heart disease.
Short-term endurance training reduces baseline ASP levels and
subsequently fat storage.
-!- CAUTION: According to PubMed:21527715, the interaction surface
between C3 and CR2 reported in PubMed:11387479 is artifactual and
can be ascribed to the presence of zinc acetate in the buffer.
{ECO:0000305}.
-!- WEB RESOURCE: Name=C3base; Note=C3 mutation db;
URL="http://structure.bmc.lu.se/idbase/C3base/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Complement C3 entry;
URL="https://en.wikipedia.org/wiki/Complement_c3";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/c3/";
-----------------------------------------------------------------------
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EMBL; K02765; AAA85332.1; -; mRNA.
EMBL; AY513239; AAR89906.1; -; Genomic_DNA.
EMBL; CH471139; EAW69071.1; -; Genomic_DNA.
EMBL; BC150179; AAI50180.1; -; mRNA.
EMBL; BC150200; AAI50201.1; -; mRNA.
CCDS; CCDS32883.1; -.
PIR; A94065; C3HU.
RefSeq; NP_000055.2; NM_000064.3.
UniGene; Hs.529053; -.
PDB; 1C3D; X-ray; 1.80 A; A=996-1287.
PDB; 1GHQ; X-ray; 2.04 A; A=996-1300.
PDB; 1W2S; X-ray; -; A=996-1299.
PDB; 2A73; X-ray; 3.30 A; A=23-665, B=673-1663.
PDB; 2A74; X-ray; 2.40 A; A/D=23-665, B/E=749-936, C/F=1321-1663.
PDB; 2GOX; X-ray; 2.20 A; A/C=996-1287.
PDB; 2I07; X-ray; 4.00 A; A=23-667, B=749-1663.
PDB; 2ICE; X-ray; 3.10 A; A/D=23-664, B/E=749-954, C/F=1321-1663.
PDB; 2ICF; X-ray; 4.10 A; A=23-664, B=749-1663.
PDB; 2NOJ; X-ray; 2.70 A; A/C/E/G=996-1287.
PDB; 2QKI; X-ray; 2.40 A; A/D=23-665, B/E=749-936, C/F=1321-1663.
PDB; 2WII; X-ray; 2.70 A; A=23-667, B=749-1663.
PDB; 2WIN; X-ray; 3.90 A; A/C/E/G=23-667, B/D/F/H=749-1663.
PDB; 2WY7; X-ray; 1.70 A; A=996-1303.
PDB; 2WY8; X-ray; 1.70 A; A=996-1303.
PDB; 2XQW; X-ray; 2.31 A; A/B=996-1287.
PDB; 2XWB; X-ray; 3.49 A; A/C=23-664, B/D=752-1663.
PDB; 2XWJ; X-ray; 4.00 A; A/C/E/G=23-667, B/D/F/H=749-1663.
PDB; 3D5R; X-ray; 2.10 A; A/B=996-1287.
PDB; 3D5S; X-ray; 2.30 A; A/B=996-1287.
PDB; 3G6J; X-ray; 3.10 A; A/C=23-666, B/D=749-1663.
PDB; 3L3O; X-ray; 3.40 A; A/D=23-667, B/E=749-954, C/F=1321-1663.
PDB; 3L5N; X-ray; 7.54 A; A=23-667, B=749-1663.
PDB; 3NMS; X-ray; 4.10 A; A=23-667, B=749-954, C=1321-1663.
PDB; 3OED; X-ray; 3.16 A; A/B=996-1303.
PDB; 3OHX; X-ray; 3.50 A; A/D=23-667, B/E=749-954, C/F=1321-1663.
PDB; 3OXU; X-ray; 2.10 A; A/B/C=996-1303.
PDB; 3RJ3; X-ray; 2.35 A; A/B/C=996-1303.
PDB; 3T4A; X-ray; 3.40 A; A/D=23-667, B/E=749-954, C/F=1321-1663.
PDB; 4HW5; X-ray; 2.25 A; A/B=672-748.
PDB; 4HWJ; X-ray; 2.60 A; A=672-747.
PDB; 4I6O; X-ray; 2.14 A; A=672-748.
PDB; 4M76; X-ray; 2.80 A; A=994-1288.
PDB; 4ONT; X-ray; 2.15 A; A/B/C=996-1303.
PDB; 4ZH1; X-ray; 2.24 A; A/B/C=996-1303.
PDB; 5FO7; X-ray; 2.80 A; A=23-667, B=749-1663.
PDB; 5FO8; X-ray; 2.40 A; A=23-667, B=749-1663.
PDB; 5FO9; X-ray; 3.30 A; A/D=23-667, B/E=749-1663.
PDB; 5FOA; X-ray; 4.19 A; A/C=23-667, B/D=749-1663.
PDB; 5FOB; X-ray; 2.60 A; A=23-667, B=749-1663.
PDB; 5M6W; X-ray; 6.00 A; A/G=23-667, B/H=751-1663.
PDB; 5O32; X-ray; 4.21 A; A/E=23-667, B/F=749-1663.
PDB; 5O35; X-ray; 4.20 A; A=23-667, B=749-1663.
PDBsum; 1C3D; -.
PDBsum; 1GHQ; -.
PDBsum; 1W2S; -.
PDBsum; 2A73; -.
PDBsum; 2A74; -.
PDBsum; 2GOX; -.
PDBsum; 2I07; -.
PDBsum; 2ICE; -.
PDBsum; 2ICF; -.
PDBsum; 2NOJ; -.
PDBsum; 2QKI; -.
PDBsum; 2WII; -.
PDBsum; 2WIN; -.
PDBsum; 2WY7; -.
PDBsum; 2WY8; -.
PDBsum; 2XQW; -.
PDBsum; 2XWB; -.
PDBsum; 2XWJ; -.
PDBsum; 3D5R; -.
PDBsum; 3D5S; -.
PDBsum; 3G6J; -.
PDBsum; 3L3O; -.
PDBsum; 3L5N; -.
PDBsum; 3NMS; -.
PDBsum; 3OED; -.
PDBsum; 3OHX; -.
PDBsum; 3OXU; -.
PDBsum; 3RJ3; -.
PDBsum; 3T4A; -.
PDBsum; 4HW5; -.
PDBsum; 4HWJ; -.
PDBsum; 4I6O; -.
PDBsum; 4M76; -.
PDBsum; 4ONT; -.
PDBsum; 4ZH1; -.
PDBsum; 5FO7; -.
PDBsum; 5FO8; -.
PDBsum; 5FO9; -.
PDBsum; 5FOA; -.
PDBsum; 5FOB; -.
PDBsum; 5M6W; -.
PDBsum; 5O32; -.
PDBsum; 5O35; -.
ProteinModelPortal; P01024; -.
SMR; P01024; -.
BioGrid; 107179; 29.
CORUM; P01024; -.
DIP; DIP-35180N; -.
IntAct; P01024; 20.
MINT; MINT-5003988; -.
STRING; 9606.ENSP00000245907; -.
BindingDB; P01024; -.
ChEMBL; CHEMBL4917; -.
DrugBank; DB00028; Immune Globulin Human.
DrugBank; DB01915; S-Hydroxycysteine.
MEROPS; I39.950; -.
iPTMnet; P01024; -.
PhosphoSitePlus; P01024; -.
UniCarbKB; P01024; -.
BioMuta; C3; -.
DMDM; 119370332; -.
DOSAC-COBS-2DPAGE; P01024; -.
SWISS-2DPAGE; P01024; -.
EPD; P01024; -.
PaxDb; P01024; -.
PeptideAtlas; P01024; -.
PRIDE; P01024; -.
Ensembl; ENST00000245907; ENSP00000245907; ENSG00000125730.
GeneID; 718; -.
KEGG; hsa:718; -.
CTD; 718; -.
DisGeNET; 718; -.
EuPathDB; HostDB:ENSG00000125730.16; -.
GeneCards; C3; -.
GeneReviews; C3; -.
H-InvDB; HIX0020036; -.
HGNC; HGNC:1318; C3.
HPA; CAB004209; -.
HPA; HPA003563; -.
HPA; HPA020432; -.
MalaCards; C3; -.
MIM; 120700; gene.
MIM; 611378; phenotype.
MIM; 612925; phenotype.
MIM; 613779; phenotype.
neXtProt; NX_P01024; -.
OpenTargets; ENSG00000125730; -.
Orphanet; 279; Age-related macular degeneration.
Orphanet; 93575; Atypical hemolytic-uremic syndrome with C3 anomaly.
Orphanet; 280133; Complement component 3 deficiency.
PharmGKB; PA25897; -.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
GeneTree; ENSGT00760000118982; -.
HOGENOM; HOG000286028; -.
HOVERGEN; HBG005110; -.
InParanoid; P01024; -.
KO; K03990; -.
OMA; INTHPSQ; -.
OrthoDB; EOG091G00FJ; -.
PhylomeDB; P01024; -.
TreeFam; TF313285; -.
BRENDA; 3.4.21.47; 2681.
Reactome; R-HSA-173736; Alternative complement activation.
Reactome; R-HSA-174577; Activation of C3 and C5.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
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-418594; G alpha (i) signalling events.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P01024; -.
ChiTaRS; C3; human.
EvolutionaryTrace; P01024; -.
GeneWiki; Complement_component_3; -.
GenomeRNAi; 718; -.
PMAP-CutDB; P01024; -.
PRO; PR:P01024; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000125730; -.
CleanEx; HS_C3; -.
ExpressionAtlas; P01024; baseline and differential.
Genevisible; P01024; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0072562; C:blood microparticle; 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:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; IDA:UniProtKB.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006956; P:complement activation; IMP:BHF-UCL.
GO; GO:0006957; P:complement activation, alternative pathway; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
GO; GO:0001970; P:positive regulation of activation of membrane attack complex; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IMP:BHF-UCL.
GO; GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
GO; GO:0010828; P:positive regulation of glucose transport; IDA:UniProtKB.
GO; GO:0010884; P:positive regulation of lipid storage; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IEA:Ensembl.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0010866; P:regulation of triglyceride biosynthetic process; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd03583; NTR_complement_C3; 1.
Gene3D; 1.20.91.20; -; 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; 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; IPR035711; Complement_C3-like.
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; IPR035815; NTR_complement_C3.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
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; Age-related macular degeneration;
Cleavage on pair of basic residues; Complement alternate pathway;
Complement pathway; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Fatty acid metabolism; Glycoprotein;
Hemolytic uremic syndrome; Immunity; Inflammatory response;
Innate immunity; Lipid metabolism; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal; Thioester bond.
SIGNAL 1 22 {ECO:0000269|PubMed:8376604}.
CHAIN 23 1663 Complement C3.
/FTId=PRO_0000005907.
CHAIN 23 667 Complement C3 beta chain.
/FTId=PRO_0000005908.
CHAIN 569 667 C3-beta-c. {ECO:0000250}.
/FTId=PRO_0000430430.
CHAIN 672 1663 Complement C3 alpha chain.
/FTId=PRO_0000005909.
CHAIN 672 748 C3a anaphylatoxin.
/FTId=PRO_0000005910.
CHAIN 672 747 Acylation stimulating protein.
/FTId=PRO_0000419935.
CHAIN 749 1663 Complement C3b alpha' chain.
/FTId=PRO_0000005911.
CHAIN 749 954 Complement C3c alpha' chain fragment 1.
/FTId=PRO_0000005912.
CHAIN 955 1303 Complement C3dg fragment.
/FTId=PRO_0000005913.
CHAIN 955 1001 Complement C3g fragment.
/FTId=PRO_0000005914.
CHAIN 1002 1303 Complement C3d fragment.
/FTId=PRO_0000005915.
PEPTIDE 1304 1320 Complement C3f fragment.
{ECO:0000269|PubMed:8376604}.
/FTId=PRO_0000005916.
CHAIN 1321 1663 Complement C3c alpha' chain fragment 2.
/FTId=PRO_0000273948.
DOMAIN 693 728 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1518 1661 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 1424 1456 Properdin-binding.
SITE 747 748 Cleavage; by carboxypeptidases.
SITE 748 749 Cleavage; by C3 convertase.
SITE 954 955 Cleavage; by factor I. {ECO:0000255}.
SITE 1303 1304 Cleavage; by factor I.
SITE 1320 1321 Cleavage; by factor I.
MOD_RES 38 38 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 70 70 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 297 297 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 303 303 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 672 672 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 968 968 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 1321 1321 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 1573 1573 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17051150,
ECO:0000269|PubMed:17684013,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2579379}.
CARBOHYD 939 939 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17051150}.
CARBOHYD 1617 1617 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 559 816 Interchain (between beta and alpha
chains).
DISULFID 627 662
DISULFID 693 720 {ECO:0000269|PubMed:8416818}.
DISULFID 694 727
DISULFID 707 728
DISULFID 873 1513
DISULFID 1101 1158
DISULFID 1358 1489
DISULFID 1389 1458
DISULFID 1506 1511
DISULFID 1518 1590
DISULFID 1537 1661
DISULFID 1637 1646
CROSSLNK 1010 1013 Isoglutamyl cysteine thioester (Cys-Gln).
VARIANT 102 102 R -> G (in allele C3F; associated with
susceptibility to ARMD9; results in
decreased binding affinity for regulator
factor H; results in reduced sensitivity
to cleavage by factor I;
dbSNP:rs2230199).
{ECO:0000269|PubMed:1976733,
ECO:0000269|PubMed:21555552,
ECO:0000269|Ref.2}.
/FTId=VAR_001983.
VARIANT 155 155 K -> Q (in ARMD9; results in resistance
to proteolytic inactivation by CFH and
CFI; dbSNP:rs147859257).
{ECO:0000269|PubMed:24036952}.
/FTId=VAR_070941.
VARIANT 314 314 P -> L (in dbSNP:rs1047286).
{ECO:0000269|PubMed:1976733,
ECO:0000269|PubMed:2579379,
ECO:0000269|Ref.2}.
/FTId=VAR_001984.
VARIANT 469 469 E -> D (in dbSNP:rs11569422).
/FTId=VAR_020262.
VARIANT 549 549 D -> N (in C3D; impairs secretion;
variant confirmed at protein level).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:7961791}.
/FTId=VAR_001985.
VARIANT 592 592 R -> Q (in AHUS5; leads to impaired
binding to the regulator CD46/MCP and
resistance to cleavage by factor I;
dbSNP:rs121909583).
{ECO:0000269|PubMed:18796626}.
/FTId=VAR_063213.
VARIANT 592 592 R -> W (in AHUS5; leads to impaired
binding to the regulator CD46/MCP and
resistance to cleavage by factor I;
dbSNP:rs771353792).
{ECO:0000269|PubMed:18796626}.
/FTId=VAR_063214.
VARIANT 603 603 F -> V (in AHUS5).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063654.
VARIANT 735 735 R -> W (in AHUS5; dbSNP:rs117793540).
{ECO:0000269|PubMed:18796626}.
/FTId=VAR_063215.
VARIANT 863 863 R -> K (in dbSNP:rs11569472).
{ECO:0000269|Ref.2}.
/FTId=VAR_019206.
VARIANT 1042 1042 R -> L (in AHUS5).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063655.
VARIANT 1094 1094 A -> V (in AHUS5; leads to impaired
binding to the regulator CD46/MCP and
resistance to cleavage by factor I;
dbSNP:rs121909584).
{ECO:0000269|PubMed:18796626}.
/FTId=VAR_063216.
VARIANT 1115 1115 D -> N (in AHUS5; leads to impaired
binding to the regulator CD46/MCP and
resistance to cleavage by factor I;
dbSNP:rs121909585).
{ECO:0000269|PubMed:18796626}.
/FTId=VAR_063217.
VARIANT 1158 1158 C -> W (in AHUS5).
{ECO:0000269|PubMed:18796626}.
/FTId=VAR_063218.
VARIANT 1161 1161 Q -> K (in AHUS5; leads to impaired
binding to the regulator CD46/MCP and
resistance to cleavage by factor I).
{ECO:0000269|PubMed:18796626}.
/FTId=VAR_063219.
VARIANT 1216 1216 D -> N (in C3S).
{ECO:0000269|PubMed:2473125}.
/FTId=VAR_022761.
VARIANT 1224 1224 G -> D (in dbSNP:rs11569534).
{ECO:0000269|Ref.2}.
/FTId=VAR_019207.
VARIANT 1367 1367 I -> T (in dbSNP:rs11569541).
{ECO:0000269|Ref.2}.
/FTId=VAR_019208.
VARIANT 1464 1464 H -> D (in AHUS5).
{ECO:0000269|PubMed:18796626}.
/FTId=VAR_063220.
VARIANT 1521 1521 Q -> R (in dbSNP:rs7256789).
/FTId=VAR_029792.
VARIANT 1601 1601 H -> N (in dbSNP:rs1803225).
/FTId=VAR_029793.
VARIANT 1619 1619 S -> R (in dbSNP:rs2230210).
/FTId=VAR_029326.
MUTAGEN 1029 1029 D->A: Minor effect on binding of C3d to
CR2. {ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1030 1030 E->A: Impaired binding of C3d to CR2.
{ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1032 1032 E->A: Impaired binding of C3d to CR2.
{ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1035 1035 E->A: No effect on binding of C3d to CR2.
{ECO:0000269|PubMed:20083651}.
MUTAGEN 1042 1042 R->M: Impaired binding of C3d to CR2.
{ECO:0000269|PubMed:20083651}.
MUTAGEN 1108 1109 IL->RR: Impaired binding of C3d to CR2;
when associated with A-1163.
{ECO:0000269|PubMed:11387479}.
MUTAGEN 1110 1110 E->A: No effect on binding of C3d to CR2.
{ECO:0000269|PubMed:20951140}.
MUTAGEN 1115 1115 D->A: No effect on binding of C3d to CR2.
{ECO:0000269|PubMed:20951140}.
MUTAGEN 1121 1121 D->A: No effect on binding of C3d to CR2.
{ECO:0000269|PubMed:20951140}.
MUTAGEN 1140 1140 D->A: No effect on binding of C3d to CR2.
{ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1153 1153 E->A: Impaired binding of C3d to CR2.
{ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1156 1156 D->A: Impaired binding of C3d to CR2.
{ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1159 1159 E->A: Impaired binding of C3d to CR2.
{ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1160 1160 E->A: Minor effect on binding of C3d to
CR2. {ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1163 1163 N->A: No effect on binding of C3d to CR2.
Impaired binding of C3d to CR2; when
associated with 1108-R-R-1109.
{ECO:0000269|PubMed:11387479,
ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1163 1163 N->R: Impaired binding of C3d to CR2.
{ECO:0000269|PubMed:11387479,
ECO:0000269|PubMed:20083651,
ECO:0000269|PubMed:20951140}.
MUTAGEN 1284 1284 K->A: Impaired binding of C3d to CR2.
{ECO:0000269|PubMed:20083651}.
CONFLICT 681 681 D -> N (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 700 700 E -> Q (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1026 1026 H -> S (in Ref. 8; AA sequence).
{ECO:0000305}.
STRAND 25 29 {ECO:0000244|PDB:2A74}.
STRAND 31 34 {ECO:0000244|PDB:2A74}.
STRAND 36 41 {ECO:0000244|PDB:2A74}.
STRAND 43 47 {ECO:0000244|PDB:2A74}.
STRAND 53 64 {ECO:0000244|PDB:2A74}.
STRAND 67 69 {ECO:0000244|PDB:2ICE}.
STRAND 73 76 {ECO:0000244|PDB:2A74}.
HELIX 78 80 {ECO:0000244|PDB:2A74}.
STRAND 87 89 {ECO:0000244|PDB:2A74}.
HELIX 94 97 {ECO:0000244|PDB:2ICE}.
STRAND 105 112 {ECO:0000244|PDB:2A74}.
STRAND 115 123 {ECO:0000244|PDB:2A74}.
STRAND 129 135 {ECO:0000244|PDB:2A74}.
STRAND 137 139 {ECO:0000244|PDB:2A74}.
STRAND 144 152 {ECO:0000244|PDB:2A74}.
STRAND 162 168 {ECO:0000244|PDB:2A74}.
STRAND 174 176 {ECO:0000244|PDB:2A74}.
STRAND 179 181 {ECO:0000244|PDB:2A74}.
TURN 183 187 {ECO:0000244|PDB:2A74}.
STRAND 188 194 {ECO:0000244|PDB:2A74}.
STRAND 202 210 {ECO:0000244|PDB:2A74}.
STRAND 214 216 {ECO:0000244|PDB:2XWB}.
STRAND 218 224 {ECO:0000244|PDB:2A74}.
STRAND 231 244 {ECO:0000244|PDB:2A74}.
STRAND 251 259 {ECO:0000244|PDB:2A74}.
STRAND 267 277 {ECO:0000244|PDB:2A74}.
STRAND 280 294 {ECO:0000244|PDB:2A74}.
STRAND 297 302 {ECO:0000244|PDB:2A74}.
HELIX 304 309 {ECO:0000244|PDB:2A74}.
STRAND 311 313 {ECO:0000244|PDB:5FO9}.
HELIX 316 319 {ECO:0000244|PDB:2A74}.
STRAND 323 332 {ECO:0000244|PDB:2A74}.
STRAND 338 352 {ECO:0000244|PDB:2A74}.
STRAND 354 356 {ECO:0000244|PDB:2A74}.
STRAND 358 360 {ECO:0000244|PDB:2A73}.
STRAND 362 364 {ECO:0000244|PDB:2A74}.
STRAND 370 377 {ECO:0000244|PDB:2A74}.
STRAND 379 381 {ECO:0000244|PDB:3T4A}.
STRAND 388 393 {ECO:0000244|PDB:2A74}.
HELIX 395 397 {ECO:0000244|PDB:2QKI}.
STRAND 398 400 {ECO:0000244|PDB:2ICE}.
STRAND 405 411 {ECO:0000244|PDB:2A74}.
STRAND 415 417 {ECO:0000244|PDB:5FO8}.
STRAND 420 426 {ECO:0000244|PDB:2A74}.
TURN 429 431 {ECO:0000244|PDB:2A74}.
HELIX 433 435 {ECO:0000244|PDB:2A74}.
STRAND 439 445 {ECO:0000244|PDB:2A74}.
HELIX 449 451 {ECO:0000244|PDB:2A74}.
STRAND 455 459 {ECO:0000244|PDB:2A74}.
STRAND 470 478 {ECO:0000244|PDB:2A74}.
TURN 481 483 {ECO:0000244|PDB:2A74}.
HELIX 484 486 {ECO:0000244|PDB:2A74}.
STRAND 489 496 {ECO:0000244|PDB:2A74}.
STRAND 499 507 {ECO:0000244|PDB:2A74}.
STRAND 513 520 {ECO:0000244|PDB:2A74}.
HELIX 523 525 {ECO:0000244|PDB:2A74}.
STRAND 527 538 {ECO:0000244|PDB:2A74}.
STRAND 540 542 {ECO:0000244|PDB:2QKI}.
STRAND 544 554 {ECO:0000244|PDB:2A74}.
STRAND 563 567 {ECO:0000244|PDB:2A74}.
TURN 568 570 {ECO:0000244|PDB:2ICE}.
STRAND 571 573 {ECO:0000244|PDB:3G6J}.
STRAND 580 588 {ECO:0000244|PDB:2A74}.
STRAND 592 599 {ECO:0000244|PDB:2A74}.
HELIX 602 605 {ECO:0000244|PDB:2A74}.
HELIX 613 622 {ECO:0000244|PDB:2A74}.
STRAND 628 630 {ECO:0000244|PDB:2A74}.
HELIX 635 641 {ECO:0000244|PDB:2A74}.
STRAND 644 648 {ECO:0000244|PDB:2QKI}.
HELIX 675 684 {ECO:0000244|PDB:4HW5}.
HELIX 688 697 {ECO:0000244|PDB:4I6O}.
HELIX 707 710 {ECO:0000244|PDB:4I6O}.
TURN 712 714 {ECO:0000244|PDB:4HW5}.
HELIX 718 743 {ECO:0000244|PDB:4I6O}.
STRAND 753 755 {ECO:0000244|PDB:3L3O}.
HELIX 758 760 {ECO:0000244|PDB:2A74}.
STRAND 769 771 {ECO:0000244|PDB:2A74}.
STRAND 775 777 {ECO:0000244|PDB:2A74}.
STRAND 786 794 {ECO:0000244|PDB:2A74}.
STRAND 800 810 {ECO:0000244|PDB:2A74}.
TURN 811 813 {ECO:0000244|PDB:2A74}.
STRAND 814 817 {ECO:0000244|PDB:2A74}.
STRAND 821 825 {ECO:0000244|PDB:2A74}.
STRAND 828 834 {ECO:0000244|PDB:2A74}.
STRAND 837 840 {ECO:0000244|PDB:2A74}.
STRAND 845 853 {ECO:0000244|PDB:2A74}.
STRAND 860 866 {ECO:0000244|PDB:2A74}.
STRAND 872 875 {ECO:0000244|PDB:2A74}.
STRAND 878 880 {ECO:0000244|PDB:5FOB}.
STRAND 882 888 {ECO:0000244|PDB:2A74}.
STRAND 892 902 {ECO:0000244|PDB:2A74}.
STRAND 906 916 {ECO:0000244|PDB:2A74}.
TURN 917 920 {ECO:0000244|PDB:3G6J}.
STRAND 922 932 {ECO:0000244|PDB:2A74}.
STRAND 934 947 {ECO:0000244|PDB:5FO8}.
HELIX 949 952 {ECO:0000244|PDB:5FO8}.
STRAND 954 956 {ECO:0000244|PDB:2A73}.
STRAND 957 962 {ECO:0000244|PDB:5FO8}.
STRAND 968 970 {ECO:0000244|PDB:5FOB}.
STRAND 977 984 {ECO:0000244|PDB:5FO8}.
TURN 988 990 {ECO:0000244|PDB:3G6J}.
HELIX 997 999 {ECO:0000244|PDB:2WY8}.
HELIX 1001 1003 {ECO:0000244|PDB:2WY7}.
STRAND 1009 1012 {ECO:0000244|PDB:3G6J}.
HELIX 1013 1031 {ECO:0000244|PDB:2WY7}.
HELIX 1034 1037 {ECO:0000244|PDB:2WY7}.
HELIX 1041 1057 {ECO:0000244|PDB:2WY7}.
TURN 1062 1064 {ECO:0000244|PDB:5FO7}.
STRAND 1068 1072 {ECO:0000244|PDB:5FOB}.
HELIX 1076 1089 {ECO:0000244|PDB:2WY7}.
TURN 1090 1092 {ECO:0000244|PDB:2WY7}.
HELIX 1097 1111 {ECO:0000244|PDB:2WY7}.
TURN 1114 1116 {ECO:0000244|PDB:2NOJ}.
HELIX 1127 1133 {ECO:0000244|PDB:2WY7}.
HELIX 1139 1158 {ECO:0000244|PDB:2WY7}.
TURN 1159 1161 {ECO:0000244|PDB:2WY7}.
HELIX 1165 1179 {ECO:0000244|PDB:2WY7}.
HELIX 1180 1182 {ECO:0000244|PDB:2WY7}.
HELIX 1186 1198 {ECO:0000244|PDB:2WY7}.
HELIX 1204 1213 {ECO:0000244|PDB:2WY7}.
TURN 1216 1218 {ECO:0000244|PDB:2WY7}.
STRAND 1223 1225 {ECO:0000244|PDB:1GHQ}.
HELIX 1226 1243 {ECO:0000244|PDB:2WY7}.
TURN 1246 1248 {ECO:0000244|PDB:2WY7}.
HELIX 1249 1258 {ECO:0000244|PDB:2WY7}.
STRAND 1265 1267 {ECO:0000244|PDB:3G6J}.
HELIX 1269 1285 {ECO:0000244|PDB:2WY7}.
TURN 1297 1299 {ECO:0000244|PDB:3OXU}.
STRAND 1303 1305 {ECO:0000244|PDB:2WII}.
STRAND 1307 1313 {ECO:0000244|PDB:5FO8}.
TURN 1314 1317 {ECO:0000244|PDB:5FO8}.
STRAND 1320 1326 {ECO:0000244|PDB:5FO8}.
STRAND 1330 1338 {ECO:0000244|PDB:5FO8}.
STRAND 1340 1350 {ECO:0000244|PDB:5FO8}.
STRAND 1359 1369 {ECO:0000244|PDB:2A74}.
STRAND 1384 1392 {ECO:0000244|PDB:2A74}.
STRAND 1394 1396 {ECO:0000244|PDB:2A74}.
STRAND 1400 1406 {ECO:0000244|PDB:2A74}.
STRAND 1411 1413 {ECO:0000244|PDB:2A74}.
HELIX 1415 1422 {ECO:0000244|PDB:2A74}.
STRAND 1424 1426 {ECO:0000244|PDB:2A73}.
HELIX 1431 1434 {ECO:0000244|PDB:2A74}.
TURN 1438 1440 {ECO:0000244|PDB:2A74}.
STRAND 1442 1449 {ECO:0000244|PDB:2A74}.
STRAND 1453 1455 {ECO:0000244|PDB:2A74}.
STRAND 1457 1467 {ECO:0000244|PDB:2A74}.
STRAND 1469 1471 {ECO:0000244|PDB:2A73}.
STRAND 1475 1481 {ECO:0000244|PDB:2A74}.
STRAND 1485 1493 {ECO:0000244|PDB:2A74}.
STRAND 1495 1497 {ECO:0000244|PDB:2A74}.
HELIX 1498 1500 {ECO:0000244|PDB:2A74}.
STRAND 1504 1507 {ECO:0000244|PDB:2A74}.
STRAND 1510 1513 {ECO:0000244|PDB:2A74}.
TURN 1515 1517 {ECO:0000244|PDB:2WII}.
STRAND 1518 1520 {ECO:0000244|PDB:2A74}.
TURN 1524 1526 {ECO:0000244|PDB:2WII}.
HELIX 1529 1536 {ECO:0000244|PDB:2A74}.
STRAND 1537 1540 {ECO:0000244|PDB:2ICE}.
STRAND 1541 1553 {ECO:0000244|PDB:2A74}.
STRAND 1556 1570 {ECO:0000244|PDB:2A74}.
TURN 1577 1579 {ECO:0000244|PDB:5FOB}.
STRAND 1581 1587 {ECO:0000244|PDB:2A74}.
HELIX 1588 1590 {ECO:0000244|PDB:2A74}.
HELIX 1591 1594 {ECO:0000244|PDB:2A74}.
STRAND 1601 1607 {ECO:0000244|PDB:2A74}.
HELIX 1608 1610 {ECO:0000244|PDB:2A74}.
STRAND 1611 1613 {ECO:0000244|PDB:2A74}.
STRAND 1615 1617 {ECO:0000244|PDB:5FOB}.
STRAND 1619 1621 {ECO:0000244|PDB:2A74}.
STRAND 1627 1631 {ECO:0000244|PDB:2A74}.
TURN 1634 1636 {ECO:0000244|PDB:2A74}.
STRAND 1637 1639 {ECO:0000244|PDB:2A74}.
TURN 1640 1642 {ECO:0000244|PDB:2QKI}.
HELIX 1643 1659 {ECO:0000244|PDB:2A74}.
SEQUENCE 1663 AA; 187148 MW; 30C2832A9E75FFC4 CRC64;
MGPTSGPSLL LLLLTHLPLA LGSPMYSIIT PNILRLESEE TMVLEAHDAQ GDVPVTVTVH
DFPGKKLVLS SEKTVLTPAT NHMGNVTFTI PANREFKSEK GRNKFVTVQA TFGTQVVEKV
VLVSLQSGYL FIQTDKTIYT PGSTVLYRIF TVNHKLLPVG RTVMVNIENP EGIPVKQDSL
SSQNQLGVLP LSWDIPELVN MGQWKIRAYY ENSPQQVFST EFEVKEYVLP SFEVIVEPTE
KFYYIYNEKG LEVTITARFL YGKKVEGTAF VIFGIQDGEQ RISLPESLKR IPIEDGSGEV
VLSRKVLLDG VQNPRAEDLV GKSLYVSATV ILHSGSDMVQ AERSGIPIVT SPYQIHFTKT
PKYFKPGMPF DLMVFVTNPD GSPAYRVPVA VQGEDTVQSL TQGDGVAKLS INTHPSQKPL
SITVRTKKQE LSEAEQATRT MQALPYSTVG NSNNYLHLSV LRTELRPGET LNVNFLLRMD
RAHEAKIRYY TYLIMNKGRL LKAGRQVREP GQDLVVLPLS ITTDFIPSFR LVAYYTLIGA
SGQREVVADS VWVDVKDSCV GSLVVKSGQS EDRQPVPGQQ MTLKIEGDHG ARVVLVAVDK
GVFVLNKKNK LTQSKIWDVV EKADIGCTPG SGKDYAGVFS DAGLTFTSSS GQQTAQRAEL
QCPQPAARRR RSVQLTEKRM DKVGKYPKEL RKCCEDGMRE NPMRFSCQRR TRFISLGEAC
KKVFLDCCNY ITELRRQHAR ASHLGLARSN LDEDIIAEEN IVSRSEFPES WLWNVEDLKE
PPKNGISTKL MNIFLKDSIT TWEILAVSMS DKKGICVADP FEVTVMQDFF IDLRLPYSVV
RNEQVEIRAV LYNYRQNQEL KVRVELLHNP AFCSLATTKR RHQQTVTIPP KSSLSVPYVI
VPLKTGLQEV EVKAAVYHHF ISDGVRKSLK VVPEGIRMNK TVAVRTLDPE RLGREGVQKE
DIPPADLSDQ VPDTESETRI LLQGTPVAQM TEDAVDAERL KHLIVTPSGC GEQNMIGMTP
TVIAVHYLDE TEQWEKFGLE KRQGALELIK KGYTQQLAFR QPSSAFAAFV KRAPSTWLTA
YVVKVFSLAV NLIAIDSQVL CGAVKWLILE KQKPDGVFQE DAPVIHQEMI GGLRNNNEKD
MALTAFVLIS LQEAKDICEE QVNSLPGSIT KAGDFLEANY MNLQRSYTVA IAGYALAQMG
RLKGPLLNKF LTTAKDKNRW EDPGKQLYNV EATSYALLAL LQLKDFDFVP PVVRWLNEQR
YYGGGYGSTQ ATFMVFQALA QYQKDAPDHQ ELNLDVSLQL PSRSSKITHR IHWESASLLR
SEETKENEGF TVTAEGKGQG TLSVVTMYHA KAKDQLTCNK FDLKVTIKPA PETEKRPQDA
KNTMILEICT RYRGDQDATM SILDISMMTG FAPDTDDLKQ LANGVDRYIS KYELDKAFSD
RNTLIIYLDK VSHSEDDCLA FKVHQYFNVE LIQPGAVKVY AYYNLEESCT RFYHPEKEDG
KLNKLCRDEL CRCAEENCFI QKSDDKVTLE ERLDKACEPG VDYVYKTRLV KVQLSNDFDE
YIMAIEQTIK SGSDEVQVGQ QRTFISPIKC REALKLEEKK HYLMWGLSSD FWGEKPNLSY
IIGKDTWVEH WPEEDECQDE ENQKQCQDLG AFTESMVVFG CPN


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bs-4874R-Cy3 Rabbit Anti-Complement C3c alpha' chain fragment 1 Polyclonal Antibody, Cy3 Conjugated 100ul
bs-4878R-Cy5 Rabbit Anti-Complement C3c alpha' chain fragment 2 Polyclonal Antibody, Cy5 Conjugated 100ul
bs-4878R-A488 Rabbit Anti-Complement C3c alpha' chain fragment 2 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-4874R-A647 Rabbit Anti-Complement C3c alpha' chain fragment 1 Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-4874R-A488 Rabbit Anti-Complement C3c alpha' chain fragment 1 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-4878R-A647 Rabbit Anti-Complement C3c alpha' chain fragment 2 Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-4878R-A350 Rabbit Anti-Complement C3c alpha' chain fragment 2 Polyclonal Antibody, ALEXA FLUOR 350 Conjugated 100ul
bs-4874R-A350 Rabbit Anti-Complement C3c alpha' chain fragment 1 Polyclonal Antibody, ALEXA FLUOR 350 Conjugated 100ul
bs-4874R-A555 Rabbit Anti-Complement C3c alpha' chain fragment 1 Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-4878R-A555 Rabbit Anti-Complement C3c alpha' chain fragment 2 Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-4878R-Biotin Rabbit Anti-Complement C3c alpha' chain fragment 2 Polyclonal Antibody, Biotin Conjugated 100ul
bs-4874R-Biotin Rabbit Anti-Complement C3c alpha' chain fragment 1 Polyclonal Antibody, Biotin Conjugated 100ul
bs-4874R-FITC Rabbit Anti-Complement C3c alpha' chain fragment 1 Polyclonal Antibody, FITC Conjugated 100ul
bs-4878R-FITC Rabbit Anti-Complement C3c alpha' chain fragment 2 Polyclonal Antibody, FITC Conjugated 100ul
E1970Rb ELISA C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Oryctolagus cuniculus,Rabbit 96T
E1970h ELISA kit C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Homo sapiens,Human 96T
E1970Rb ELISA kit C8A,Complement component 8 subunit alpha,Complement component C8 alpha chain,Oryctolagus cuniculus,Rabbit 96T


 

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