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Database: UniProt
Entry: P01024
LinkDB: P01024
Original site: P01024 
ID   CO3_HUMAN               Reviewed;        1663 AA.
AC   P01024; A7E236;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   02-JUN-2021, entry version 251.
DE   RecName: Full=Complement C3;
DE   AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1;
DE   Contains:
DE     RecName: Full=Complement C3 beta chain;
DE   Contains:
DE     RecName: Full=C3-beta-c;
DE              Short=C3bc;
DE   Contains:
DE     RecName: Full=Complement C3 alpha chain;
DE   Contains:
DE     RecName: Full=C3a anaphylatoxin;
DE   Contains:
DE     RecName: Full=Acylation stimulating protein;
DE              Short=ASP;
DE     AltName: Full=C3adesArg;
DE   Contains:
DE     RecName: Full=Complement C3b alpha' chain;
DE   Contains:
DE     RecName: Full=Complement C3c alpha' chain fragment 1;
DE   Contains:
DE     RecName: Full=Complement C3dg fragment;
DE   Contains:
DE     RecName: Full=Complement C3g fragment;
DE   Contains:
DE     RecName: Full=Complement C3d fragment;
DE   Contains:
DE     RecName: Full=Complement C3f fragment;
DE   Contains:
DE     RecName: Full=Complement C3c alpha' chain fragment 2;
DE   Flags: Precursor;
GN   Name=C3; Synonyms=CPAMD1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-314.
RX   PubMed=2579379; DOI=10.1073/pnas.82.3.708;
RA   de Bruijn M.H.L., Fey G.H.;
RT   "Human complement component C3: cDNA coding sequence and derived primary
RT   structure.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:708-712(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-102; LEU-314; LYS-863;
RP   ASP-1224 AND THR-1367.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   FUNCTION.
RX   PubMed=8376604; DOI=10.1172/jci116733;
RA   Baldo A., Sniderman A.D., St-Luce S., Avramoglu R.K., Maslowska M.,
RA   Hoang B., Monge J.C., Bell A., Mulay S., Cianflone K.;
RT   "The adipsin-acylation stimulating protein system and regulation of
RT   intracellular triglyceride synthesis.";
RL   J. Clin. Invest. 92:1543-1547(1993).
RN   [6]
RP   PROTEIN SEQUENCE OF 672-748.
RX   PubMed=1238393;
RA   Hugli T.E.;
RT   "Human anaphylatoxin (C3a) from the third component of complement. Primary
RT   structure.";
RL   J. Biol. Chem. 250:8293-8301(1975).
RN   [7]
RP   PROTEIN SEQUENCE OF 955-966, AND SUBUNIT.
RC   TISSUE=Serum;
RX   PubMed=7539791; DOI=10.1074/jbc.270.23.13645;
RA   Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T.,
RA   Gleich G.J., Sottrup-Jensen L.;
RT   "Identification of angiotensinogen and complement C3dg as novel proteins
RT   binding the proform of eosinophil major basic protein in human pregnancy
RT   serum and plasma.";
RL   J. Biol. Chem. 270:13645-13651(1995).
RN   [8]
RP   PROTEIN SEQUENCE OF 988-1036.
RX   PubMed=6175959; DOI=10.1073/pnas.79.4.1054;
RA   Thomas M.L., Janatova J., Gray W.R., Tack B.F.;
RT   "Third component of human complement: localization of the internal
RT   thiolester bond.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:1054-1058(1982).
RN   [9]
RP   INTERACTION WITH CR1.
RX   PubMed=2972794; DOI=10.1084/jem.168.5.1699;
RA   Klickstein L.B., Bartow T.J., Miletic V., Rabson L.D., Smith J.A.,
RA   Fearon D.T.;
RT   "Identification of distinct C3b and C4b recognition sites in the human
RT   C3b/C4b receptor (CR1, CD35) by deletion mutagenesis.";
RL   J. Exp. Med. 168:1699-1717(1988).
RN   [10]
RP   PROTEIN SEQUENCE OF 1409-1563.
RX   PubMed=3279119;
RA   Daoudaki M.E., Becherer J.D., Lambris J.D.;
RT   "A 34-amino acid peptide of the third component of complement mediates
RT   properdin binding.";
RL   J. Immunol. 140:1577-1580(1988).
RN   [11]
RP   INTERACTION WITH HERPES SIMPLEX VIRUS HHV-1 AND HHV-2 GYCOPROTEIN C
RP   (MICROBIAL INFECTION).
RX   PubMed=2849025; DOI=10.1016/0882-4010(87)90012-x;
RA   Eisenberg R.J., Ponce de Leon M., Friedman H.M., Fries L.F., Frank M.M.,
RA   Hastings J.C., Cohen G.H.;
RT   "Complement component C3b binds directly to purified glycoprotein C of
RT   herpes simplex virus types 1 and 2.";
RL   Microb. Pathog. 3:423-435(1987).
RN   [12]
RP   FUNCTION.
RX   PubMed=2909530;
RA   Cianflone K.M., Sniderman A.D., Walsh M.J., Vu H.T., Gagnon J.,
RA   Rodriguez M.A.;
RT   "Purification and characterization of acylation stimulating protein.";
RL   J. Biol. Chem. 264:426-430(1989).
RN   [13]
RP   MUTAGENESIS OF THE THIOESTER BOND REGION.
RX   PubMed=1577777;
RA   Isaac L., Isenman D.E.;
RT   "Structural requirements for thioester bond formation in human complement
RT   component C3. Reassessment of the role of thioester bond integrity on the
RT   conformation of C3.";
RL   J. Biol. Chem. 267:10062-10069(1992).
RN   [14]
RP   DISULFIDE BONDS.
RX   PubMed=8416818; DOI=10.1016/0014-5793(93)81139-q;
RA   Dolmer K., Sottrup-Jensen L.;
RT   "Disulfide bridges in human complement component C3b.";
RL   FEBS Lett. 315:85-90(1993).
RN   [15]
RP   INTERACTION WITH CR1.
RX   PubMed=8175757;
RA   Krych M., Clemenza L., Howdeshell D., Hauhart R., Hourcade D.,
RA   Atkinson J.P.;
RT   "Analysis of the functional domains of complement receptor type 1 (C3b/C4b
RT   receptor; CD35) by substitution mutagenesis.";
RL   J. Biol. Chem. 269:13273-13278(1994).
RN   [16]
RP   FUNCTION.
RX   PubMed=9059512; DOI=10.1016/s0005-2760(96)00144-0;
RA   Tao Y., Cianflone K., Sniderman A.D., Colby-Germinario S.P.,
RA   Germinario R.J.;
RT   "Acylation-stimulating protein (ASP) regulates glucose transport in the rat
RT   L6 muscle cell line.";
RL   Biochim. Biophys. Acta 1344:221-229(1997).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=9555951;
RA   Saleh J., Summers L.K., Cianflone K., Fielding B.A., Sniderman A.D.,
RA   Frayn K.N.;
RT   "Coordinated release of acylation stimulating protein (ASP) and
RT   triacylglycerol clearance by human adipose tissue in vivo in the
RT   postprandial period.";
RL   J. Lipid Res. 39:884-891(1998).
RN   [18]
RP   FUNCTION.
RX   PubMed=10432298; DOI=10.1042/bj3420041;
RA   Murray I., Kohl J., Cianflone K.;
RT   "Acylation-stimulating protein (ASP): structure-function determinants of
RT   cell surface binding and triacylglycerol synthetic activity.";
RL   Biochem. J. 342:41-48(1999).
RN   [19]
RP   INTERACTION WITH C5AR2.
RX   PubMed=11773063; DOI=10.1074/jbc.c100714200;
RA   Cain S.A., Monk P.N.;
RT   "The orphan receptor C5L2 has high affinity binding sites for complement
RT   fragments C5a and C5a des Arg(74).";
RL   J. Biol. Chem. 277:7165-7169(2002).
RN   [20]
RP   INTERACTION WITH C5AR2.
RX   PubMed=12540846; DOI=10.1074/jbc.m206169200;
RA   Kalant D., Cain S.A., Maslowska M., Sniderman A.D., Cianflone K.,
RA   Monk P.N.;
RT   "The chemoattractant receptor-like protein C5L2 binds the C3a des-
RT   Arg77/acylation-stimulating protein.";
RL   J. Biol. Chem. 278:11123-11129(2003).
RN   [21]
RP   GLYCOSYLATION AT ASN-85.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [22]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-939.
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [23]
RP   EFFECTS OF EXERCISE.
RX   PubMed=15809665; DOI=10.1038/sj.ijo.0802949;
RA   Schrauwen P., Hesselink M.K., Jain M., Cianflone K.;
RT   "Acylation-stimulating protein: effect of acute exercise and endurance
RT   training.";
RL   Int. J. Obes. Relat. Metab. Disord. 29:632-638(2005).
RN   [24]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15833747; DOI=10.1074/jbc.m406921200;
RA   Kalant D., MacLaren R., Cui W., Samanta R., Monk P.N., Laporte S.A.,
RA   Cianflone K.;
RT   "C5L2 is a functional receptor for acylation-stimulating protein.";
RL   J. Biol. Chem. 280:23936-23944(2005).
RN   [25]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85; ASN-939 AND ASN-1617.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [26]
RP   ASSOCIATION WITH TYPE 2 DIABETES.
RX   PubMed=16302015; DOI=10.1038/sj.ijo.0803173;
RA   Yang Y., Lu H.L., Zhang J., Yu H.Y., Wang H.W., Zhang M.X., Cianflone K.;
RT   "Relationships among acylation stimulating protein, adiponectin and
RT   complement C3 in lean vs obese type 2 diabetes.";
RL   Int. J. Obes. Relat. Metab. Disord. 30:439-446(2006).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX   PubMed=16333141; DOI=10.1194/jlr.m500500-jlr200;
RA   Maslowska M., Legakis H., Assadi F., Cianflone K.;
RT   "Targeting the signaling pathway of acylation stimulating protein.";
RL   J. Lipid Res. 47:643-652(2006).
RN   [28]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
RC   TISSUE=Platelet;
RX   PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA   Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT   "Elucidation of N-glycosylation sites on human platelet proteins: a
RT   glycoproteomic approach.";
RL   Mol. Cell. Proteomics 5:226-233(2006).
RN   [29]
RP   ASSOCIATION WITH OBESITY.
RX   PubMed=18805911; DOI=10.1530/eje-08-0467;
RA   Wamba P.C., Mi J., Zhao X.Y., Zhang M.X., Wen Y., Cheng H., Hou D.Q.,
RA   Cianflone K.;
RT   "Acylation stimulating protein but not complement C3 associates with
RT   metabolic syndrome components in Chinese children and adolescents.";
RL   Eur. J. Endocrinol. 159:781-790(2008).
RN   [30]
RP   INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SBI (MICROBIAL INFECTION).
RX   PubMed=19112495; DOI=10.1371/journal.ppat.1000250;
RA   Haupt K., Reuter M., van den Elsen J., Burman J., Haelbich S., Richter J.,
RA   Skerka C., Zipfel P.F.;
RT   "The Staphylococcus aureus protein Sbi acts as a complement inhibitor and
RT   forms a tripartite complex with host complement Factor H and C3b.";
RL   PLoS Pathog. 4:E1000250-E1000250(2008).
RN   [31]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [32]
RP   FUNCTION.
RX   PubMed=19615750; DOI=10.1016/j.molimm.2009.06.007;
RA   Cui W., Simaan M., Laporte S., Lodge R., Cianflone K.;
RT   "C5a- and ASP-mediated C5L2 activation, endocytosis and recycling are lost
RT   in S323I-C5L2 mutation.";
RL   Mol. Immunol. 46:3086-3098(2009).
RN   [33]
RP   MUTAGENESIS OF ASP-1029; GLU-1030; GLU-1032; GLU-1035; ARG-1042; ASP-1140;
RP   GLU-1153; ASP-1156; GLU-1159; GLU-1160; ASN-1163 AND LYS-1284, AND
RP   INTERACTION WITH CR2 AND S.AUREUS SBI (MICROBIAL INFECTION).
RX   PubMed=20083651; DOI=10.4049/jimmunol.0902919;
RA   Isenman D.E., Leung E., Mackay J.D., Bagby S., van den Elsen J.M.;
RT   "Mutational analyses reveal that the staphylococcal immune evasion molecule
RT   Sbi and complement receptor 2 (CR2) share overlapping contact residues on
RT   C3d: implications for the controversy regarding the CR2/C3d cocrystal
RT   structure.";
RL   J. Immunol. 184:1946-1955(2010).
RN   [34]
RP   MUTAGENESIS OF ASP-1029; GLU-1030; GLU-1032; GLU-1110; ASP-1115; ASP-1121;
RP   ASP-1140; GLU-1153; ASP-1156; GLU-1159; GLU-1160 AND ASN-1163, AND
RP   INTERACTION WITH CR2.
RX   PubMed=20951140; DOI=10.1016/j.jmb.2010.10.005;
RA   Shaw C.D., Storek M.J., Young K.A., Kovacs J.M., Thurman J.M., Holers V.M.,
RA   Hannan J.P.;
RT   "Delineation of the complement receptor type 2-C3d complex by site-directed
RT   mutagenesis and molecular docking.";
RL   J. Mol. Biol. 404:697-710(2010).
RN   [35]
RP   ASSOCIATION WITH CORONARY HEART DISEASE.
RX   PubMed=19913840; DOI=10.1016/j.metabol.2009.09.006;
RA   Onat A., Hergenc G., Can G., Kaya Z., Yuksel H.;
RT   "Serum complement C3: a determinant of cardiometabolic risk, additive to
RT   the metabolic syndrome, in middle-aged population.";
RL   Metabolism 59:628-634(2010).
RN   [36]
RP   CLEAVAGE BY STAPHYLOCOCCUS AUREUS PROTEIN AUREOLYSIN (MICROBIAL INFECTION).
RX   PubMed=21502375; DOI=10.4049/jimmunol.1002948;
RA   Laarman A.J., Ruyken M., Malone C.L., van Strijp J.A., Horswill A.R.,
RA   Rooijakkers S.H.;
RT   "Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to
RT   mediate immune evasion.";
RL   J. Immunol. 186:6445-6453(2011).
RN   [37]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [38]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [39]
RP   PHOSPHORYLATION AT SER-38; SER-70; SER-297; SER-303; SER-672; SER-968;
RP   SER-1321 AND SER-1573.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
RN   [40]
RP   STRUCTURE BY NMR OF C3A.
RX   PubMed=3260670; DOI=10.1073/pnas.85.14.5036;
RA   Nettesheim D.G., Edalji R.P., Mollison K.W., Greer J., Zuiderweg E.R.P.;
RT   "Secondary structure of complement component C3a anaphylatoxin in solution
RT   as determined by NMR spectroscopy: differences between crystal and solution
RT   conformations.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5036-5040(1988).
RN   [41]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF C3D.
RX   PubMed=9596584; DOI=10.1126/science.280.5367.1277;
RA   Nagar B., Jones R.G., Diefenbach R.J., Isenman D.E., Rini J.M.;
RT   "X-ray crystal structure of C3d: a C3 fragment and ligand for complement
RT   receptor 2.";
RL   Science 280:1277-1281(1998).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF C3D IN COMPLEX WITH CR2, AND
RP   MUTAGENESIS OF 1108-ILE-LEU-1109 AND ASN-1163.
RX   PubMed=11387479; DOI=10.1126/science.1059118;
RA   Szakonyi G., Guthridge J.M., Li D., Young K., Holers V.M., Chen X.S.;
RT   "Structure of complement receptor 2 in complex with its C3d ligand.";
RL   Science 292:1725-1728(2001).
RN   [43]
RP   X-RAY SCATTERING SOLUTION STRUCTURE OF C3D IN COMPLEX WITH CR2.
RX   PubMed=15713468; DOI=10.1016/j.jmb.2004.12.006;
RA   Gilbert H.E., Eaton J.T., Hannan J.P., Holers V.M., Perkins S.J.;
RT   "Solution structure of the complex between CR2 SCR 1-2 and C3d of human
RT   complement: an X-ray scattering and sedimentation modelling study.";
RL   J. Mol. Biol. 346:859-873(2005).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF C3C, AND X-RAY CRYSTALLOGRAPHY
RP   (3.3 ANGSTROMS) OF C3.
RX   PubMed=16177781; DOI=10.1038/nature04005;
RA   Janssen B.J.C., Huizinga E.G., Raaijmakers H.C.A., Roos A., Daha M.R.,
RA   Nilsson-Ekdahl K., Nilsson B., Gros P.;
RT   "Structures of complement component C3 provide insights into the function
RT   and evolution of immunity.";
RL   Nature 437:505-511(2005).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF C3B.
RX   PubMed=17051160; DOI=10.1038/nature05172;
RA   Janssen B.J.C., Christodoulidou A., McCarthy A., Lambris J.D., Gros P.;
RT   "Structure of C3b reveals conformational changes that underlie complement
RT   activity.";
RL   Nature 444:213-216(2006).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF C3C IN COMPLEX WITH VSIG4, X-RAY
RP   CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF C3B IN COMPLEX WITH VSIG4, AND
RP   GLYCOSYLATION AT ASN-85 AND ASN-939.
RX   PubMed=17051150; DOI=10.1038/nature05263;
RA   Wiesmann C., Katschke K.J., Yin J., Helmy K.Y., Steffek M.,
RA   Fairbrother W.J., McCallum S.A., Embuscado L., DeForge L., Hass P.E.,
RA   van Lookeren Campagne M.;
RT   "Structure of C3b in complex with CRIg gives insights into regulation of
RT   complement activation.";
RL   Nature 444:217-220(2006).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-936 AND 1321-1663 IN COMPLEX
RP   WITH INHIBITOR COMPSTATIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-85.
RX   PubMed=17684013; DOI=10.1074/jbc.m704587200;
RA   Janssen B.J., Halff E.F., Lambris J.D., Gros P.;
RT   "Structure of compstatin in complex with complement component C3c reveals a
RT   new mechanism of complement inhibition.";
RL   J. Biol. Chem. 282:29241-29247(2007).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 996-1287 IN COMPLEX WITH
RP   STAPHYLOCOCCUS AUREUS PROTEIN FIB (MICROBIAL INFECTION).
RX   PubMed=17351618; DOI=10.1038/ni1450;
RA   Hammel M., Sfyroera G., Ricklin D., Magotti P., Lambris J.D.,
RA   Geisbrecht B.V.;
RT   "A structural basis for complement inhibition by Staphylococcus aureus.";
RL   Nat. Immunol. 8:430-437(2007).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 996-1303 IN COMPLEX WITH
RP   STAPHYLOCOCCUS AUREUS SBI (MICROBIAL INFECTION), AND SUBUNIT.
RX   PubMed=21055811; DOI=10.1016/j.molimm.2010.09.017;
RA   Clark E.A., Crennell S., Upadhyay A., Zozulya A.V., Mackay J.D.,
RA   Svergun D.I., Bagby S., van den Elsen J.M.;
RT   "A structural basis for Staphylococcal complement subversion: X-ray
RT   structure of the complement-binding domain of Staphylococcus aureus protein
RT   Sbi in complex with ligand C3d.";
RL   Mol. Immunol. 48:452-462(2011).
RN   [50]
RP   X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 996-1303 IN COMPLEX WITH CR2, AND
RP   INTERACTION WITH CR2.
RX   PubMed=21527715; DOI=10.1126/science.1201954;
RA   van den Elsen J.M., Isenman D.E.;
RT   "A crystal structure of the complex between human complement receptor 2 and
RT   its ligand C3d.";
RL   Science 332:608-611(2011).
RN   [51] {ECO:0007744|PDB:6RUR}
RP   X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS) OF 23-667 AND 749-1663 IN COMPLEX
RP   WITH CFP; COMPLEMENT FACTOR B BB FRAGMENT AND STAPHYLOCOCCUS AUREUS PROTEIN
RP   SCN, AND INTERACTION WITH COMPLEMENT FACTOR B BB FRAGMENT AND CFP.
RX   PubMed=28264884; DOI=10.15252/embj.201696173;
RA   Pedersen D.V., Roumenina L., Jensen R.K., Gadeberg T.A., Marinozzi C.,
RA   Picard C., Rybkine T., Thiel S., Soerensen U.B., Stover C.,
RA   Fremeaux-Bacchi V., Andersen G.R.;
RT   "Functional and structural insight into properdin control of complement
RT   alternative pathway amplification.";
RL   EMBO J. 36:1084-1099(2017).
RN   [52] {ECO:0007744|PDB:6RUV}
RP   X-RAY CRYSTALLOGRAPHY (6.15 ANGSTROMS) OF 23-667 AND 749-1663 IN COMPLEX
RP   WITH COMPLEMENT FACTOR B BB FRAGMENT; CFP AND STAPHYLOCOCCUS AUREUS PROTEIN
RP   SCN, AND INTERACTION WITH COMPLEMENT FACTOR B BB FRAGMENT AND CFP.
RX   PubMed=31507604; DOI=10.3389/fimmu.2019.02007;
RA   Pedersen D.V., Gadeberg T.A.F., Thomas C., Wang Y., Joram N., Jensen R.K.,
RA   Mazarakis S.M.M., Revel M., El Sissy C., Petersen S.V., Lindorff-Larsen K.,
RA   Thiel S., Laursen N.S., Fremeaux-Bacchi V., Andersen G.R.;
RT   "Structural Basis for Properdin Oligomerization and Convertase Stimulation
RT   in the Human Complement System.";
RL   Front. Immunol. 10:2007-2007(2019).
RN   [53]
RP   RETRACTED PAPER.
RX   PubMed=2473125;
RA   Poznansky M.C., Clissold P.M., Lachmann P.J.;
RT   "The difference between human C3F and C3S results from a single amino acid
RT   change from an asparagine to an aspartate residue at position 1216 on the
RT   alpha-chain of the complement component, C3.";
RL   J. Immunol. 143:1254-1258(1989).
RN   [54]
RP   RETRACTION NOTICE OF PUBMED:2473125.
RX   PubMed=2584723;
RA   Poznansky M.C., Clissold P.M., Lachmann P.J.;
RL   J. Immunol. 143:3860-3862(1989).
RN   [55]
RP   VARIANTS GLY-102 AND LEU-314.
RX   PubMed=1976733; DOI=10.1084/jem.172.4.1011;
RA   Botto M., Yong Fong K., So A.K., Koch C., Walport M.J.;
RT   "Molecular basis of polymorphisms of human complement component C3.";
RL   J. Exp. Med. 172:1011-1017(1990).
RN   [56]
RP   VARIANT C3D ASN-549.
RX   PubMed=7961791;
RA   Singer L., Whitehead W.T., Akama H., Katz Y., Fishelson Z., Wetsel R.A.;
RT   "Inherited human complement C3 deficiency. An amino acid substitution in
RT   the beta-chain (Asp549 to Asn) impairs C3 secretion.";
RL   J. Biol. Chem. 269:28494-28499(1994).
RN   [57]
RP   ASSOCIATION OF VARIANT GLY-102 WITH ARMD9.
RX   PubMed=17634448; DOI=10.1056/nejmoa072618;
RA   Yates J.R.W., Sepp T., Matharu B.K., Khan J.C., Thurlby D.A., Shahid H.,
RA   Clayton D.G., Hayward C., Morgan J., Wright A.F., Armbrecht A.M.,
RA   Dhillon B., Deary I.J., Redmond E., Bird A.C., Moore A.T.;
RT   "Complement C3 variant and the risk of age-related macular degeneration.";
RL   N. Engl. J. Med. 357:553-561(2007).
RN   [58]
RP   VARIANTS AHUS5 GLN-592; TRP-592; TRP-735; VAL-1094; ASN-1115; TRP-1158;
RP   LYS-1161 AND ASP-1464, AND CHARACTERIZATION OF VARIANTS AHUS5 GLN-592;
RP   TRP-592; VAL-1094; ASN-1115 AND LYS-1161.
RX   PubMed=18796626; DOI=10.1182/blood-2008-01-133702;
RA   Fremeaux-Bacchi V., Miller E.C., Liszewski M.K., Strain L., Blouin J.,
RA   Brown A.L., Moghal N., Kaplan B.S., Weiss R.A., Lhotta K., Kapur G.,
RA   Mattoo T., Nivet H., Wong W., Gie S., Hurault de Ligny B., Fischbach M.,
RA   Gupta R., Hauhart R., Meunier V., Loirat C., Dragon-Durey M.A.,
RA   Fridman W.H., Janssen B.J., Goodship T.H., Atkinson J.P.;
RT   "Mutations in complement C3 predispose to development of atypical hemolytic
RT   uremic syndrome.";
RL   Blood 112:4948-4952(2008).
RN   [59]
RP   VARIANTS AHUS5 VAL-603 AND LEU-1042.
RX   PubMed=20513133; DOI=10.1002/humu.21256;
RA   Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.;
RT   "Mutations in alternative pathway complement proteins in American patients
RT   with atypical hemolytic uremic syndrome.";
RL   Hum. Mutat. 31:E1445-E1460(2010).
RN   [60]
RP   VARIANT ASN-549, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22028381; DOI=10.1093/jmcb/mjr024;
RA   Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X.,
RA   Zeng R., Wu J.R.;
RT   "Quantitative detection of single amino acid polymorphisms by targeted
RT   proteomics.";
RL   J. Mol. Cell Biol. 3:309-315(2011).
RN   [61]
RP   CHARACTERIZATION OF VARIANT GLY-102.
RX   PubMed=21555552; DOI=10.1073/pnas.1019338108;
RA   Heurich M., Martinez-Barricarte R., Francis N.J., Roberts D.L.,
RA   Rodriguez de Cordoba S., Morgan B.P., Harris C.L.;
RT   "Common polymorphisms in C3, factor B, and factor H collaborate to
RT   determine systemic complement activity and disease risk.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:8761-8766(2011).
RN   [62]
RP   X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 996-1287, AND INTERACTION WITH
RP   CFH.
RX   PubMed=21285368; DOI=10.1073/pnas.1017087108;
RA   Kajander T., Lehtinen M.J., Hyvaerinen S., Bhattacharjee A., Leung E.,
RA   Isenman D.E., Meri S., Goldman A., Jokiranta T.S.;
RT   "Dual interaction of factor H with C3d and glycosaminoglycans in host-
RT   nonhost discrimination by complement.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2897-2902(2011).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 996-1303, AND INTERACTION WITH
RP   CFH.
RX   PubMed=21317894; DOI=10.1038/nsmb.2018;
RA   Morgan H.P., Schmidt C.Q., Guariento M., Blaum B.S., Gillespie D.,
RA   Herbert A.P., Kavanagh D., Mertens H.D., Svergun D.I., Johansson C.M.,
RA   Uhrin D., Barlow P.N., Hannan J.P.;
RT   "Structural basis for engagement by complement factor H of C3b on a self
RT   surface.";
RL   Nat. Struct. Mol. Biol. 18:463-470(2011).
RN   [64]
RP   VARIANT ARMD9 GLN-155, AND CHARACTERIZATION OF VARIANT ARMD9 GLN-155.
RX   PubMed=24036952; DOI=10.1038/ng.2741;
RA   Seddon J.M., Yu Y., Miller E.C., Reynolds R., Tan P.L., Gowrisankar S.,
RA   Goldstein J.I., Triebwasser M., Anderson H.E., Zerbib J., Kavanagh D.,
RA   Souied E., Katsanis N., Daly M.J., Atkinson J.P., Raychaudhuri S.;
RT   "Rare variants in CFI, C3 and C9 are associated with high risk of advanced
RT   age-related macular degeneration.";
RL   Nat. Genet. 45:1366-1370(2013).
CC   -!- FUNCTION: C3 plays a central role in the activation of the complement
CC       system. Its processing by C3 convertase is the central reaction in both
CC       classical and alternative complement pathways. After activation C3b can
CC       bind covalently, via its reactive thioester, to cell surface
CC       carbohydrates or immune aggregates.
CC   -!- FUNCTION: Derived from proteolytic degradation of complement C3, C3a
CC       anaphylatoxin is a mediator of local inflammatory process. In chronic
CC       inflammation, acts as a chemoattractant for neutrophils (By
CC       similarity). It induces the contraction of smooth muscle, increases
CC       vascular permeability and causes histamine release from mast cells and
CC       basophilic leukocytes. {ECO:0000250}.
CC   -!- FUNCTION: [C3-beta-c]: Acts as a chemoattractant for neutrophils in
CC       chronic inflammation. {ECO:0000250}.
CC   -!- FUNCTION: [Acylation stimulating protein]: adipogenic hormone that
CC       stimulates triglyceride (TG) synthesis and glucose transport in
CC       adipocytes, regulating fat storage and playing a role in postprandial
CC       TG clearance. Appears to stimulate TG synthesis via activation of the
CC       PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the
CC       phosphorylation, ARRB2-mediated internalization and recycling of C5AR2
CC       (PubMed:8376604, PubMed:2909530, PubMed:9059512, PubMed:10432298,
CC       PubMed:15833747, PubMed:16333141, PubMed:19615750).
CC       {ECO:0000269|PubMed:10432298, ECO:0000269|PubMed:15833747,
CC       ECO:0000269|PubMed:16333141, ECO:0000269|PubMed:19615750,
CC       ECO:0000269|PubMed:2909530, ECO:0000269|PubMed:8376604,
CC       ECO:0000269|PubMed:9059512}.
CC   -!- SUBUNIT: C3 precursor is first processed by the removal of 4 Arg
CC       residues, forming two chains, beta and alpha, linked by a disulfide
CC       bond. C3 convertase activates C3 by cleaving the alpha chain, releasing
CC       C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). Forms
CC       the pro-C3-convertase enzyme complex by interacting with Complement
CC       factor B Bb fragment (Bb), which is then stabilized by binding CFP,
CC       allowing the complex to become active (PubMed:28264884,
CC       PubMed:31507604). The interaction with Bb is dependent on Mg2+
CC       (PubMed:31507604). C3b interacts with CR1 (via Sushi 8 and Sushi 9
CC       domains) (PubMed:8175757, PubMed:2972794). C3b interacts with CFH
CC       (PubMed:21285368). C3d interacts with CFH (PubMed:21285368,
CC       PubMed:21317894). C3dg interacts with CR2 (via the N-terminal Sushi
CC       domains 1 and 2). During pregnancy, C3dg exists as a complex (probably
CC       a 2:2:2 heterohexamer) with AGT and the proform of PRG2. Interacts with
CC       VSIG4. Interacts (both C3a and ASP) with C5AR2; the interaction occurs
CC       with higher affinity for ASP, enhancing the phosphorylation and
CC       activation of C5AR2, recruitment of ARRB2 to the cell surface and
CC       endocytosis of GRP77. {ECO:0000269|PubMed:11387479,
CC       ECO:0000269|PubMed:11773063, ECO:0000269|PubMed:12540846,
CC       ECO:0000269|PubMed:17051150, ECO:0000269|PubMed:17684013,
CC       ECO:0000269|PubMed:20083651, ECO:0000269|PubMed:20951140,
CC       ECO:0000269|PubMed:21285368, ECO:0000269|PubMed:21317894,
CC       ECO:0000269|PubMed:21527715, ECO:0000269|PubMed:28264884,
CC       ECO:0000269|PubMed:2849025, ECO:0000269|PubMed:2972794,
CC       ECO:0000269|PubMed:31507604, ECO:0000269|PubMed:7539791,
CC       ECO:0000269|PubMed:8175757}.
CC   -!- SUBUNIT: (Microbial infection) C3b interacts with herpes simplex virus
CC       1 (HHV-1) and herpes simplex virus 2 (HHV-2) envelope glycoprotein C;
CC       this interaction inhibits the activation of the complement system.
CC       {ECO:0000269|PubMed:2849025}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC       immunoglobulin-binding protein Sbi; this interaction prevents the
CC       association between C3dg and CR2. {ECO:0000269|PubMed:19112495,
CC       ECO:0000269|PubMed:20083651, ECO:0000269|PubMed:21055811}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC       protein Fib. {ECO:0000269|PubMed:17351618}.
CC   -!- INTERACTION:
CC       P01024; O95994: AGR2; NbExp=3; IntAct=EBI-905851, EBI-712648;
CC       P01024; P15529: CD46; NbExp=2; IntAct=EBI-905851, EBI-2623451;
CC       P01024; P00751: CFB; NbExp=3; IntAct=EBI-905851, EBI-1223668;
CC       P01024; P08603: CFH; NbExp=6; IntAct=EBI-905851, EBI-1223708;
CC       P01024; PRO_0000005896 [Q03591]: CFHR1; NbExp=2; IntAct=EBI-905851, EBI-22118464;
CC       P01024; Q92496-1: CFHR4; NbExp=5; IntAct=EBI-905851, EBI-22033617;
CC       P01024; O95967: EFEMP2; NbExp=3; IntAct=EBI-905851, EBI-743414;
CC       P01024; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-905851, EBI-5916454;
CC       P01024; Q15323: KRT31; NbExp=3; IntAct=EBI-905851, EBI-948001;
CC       P01024; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-905851, EBI-10171774;
CC       P01024; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-905851, EBI-742388;
CC       P01024; Q9Y279-1: VSIG4; NbExp=5; IntAct=EBI-905851, EBI-903144;
CC       P01024; Q9Y279-2: VSIG4; NbExp=2; IntAct=EBI-905851, EBI-903148;
CC       PRO_0000005908; P08603: CFH; NbExp=4; IntAct=EBI-6863145, EBI-1223708;
CC       PRO_0000005911; PRO_0000005908 [P01024]: C3; NbExp=9; IntAct=EBI-12735725, EBI-6863145;
CC       PRO_0000005911; Q92496-3: CFHR4; NbExp=3; IntAct=EBI-12735725, EBI-22033638;
CC       PRO_0000005913; PRO_0000005897 [P36980]: CFHR2; NbExp=2; IntAct=EBI-21988425, EBI-21988278;
CC       PRO_0000005915; P08603: CFH; NbExp=2; IntAct=EBI-6863106, EBI-1223708;
CC       PRO_0000005915; PRO_0000005897 [P36980]: CFHR2; NbExp=3; IntAct=EBI-6863106, EBI-21988278;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma. The acylation stimulating protein (ASP) is
CC       expressed in adipocytes and released into the plasma during both the
CC       fasting and postprandial periods. {ECO:0000269|PubMed:15833747,
CC       ECO:0000269|PubMed:9555951}.
CC   -!- PTM: C3b is rapidly split in two positions by factor I and a cofactor
CC       to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is
CC       slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha'
CC       chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other
CC       proteases produce other fragments such as C3d or C3g. C3a is further
CC       processed by carboxypeptidases to release the C-terminal arginine
CC       residue generating the acylation stimulating protein (ASP). Levels of
CC       ASP are increased in adipocytes in the postprandial period and by
CC       insulin and dietary chylomicrons.
CC   -!- PTM: (Microbial infection) C3 is cleaved by Staphylococcus aureus
CC       aureolysin; this cleavage renders C3a and C3b inactive. C3b is rapidly
CC       degraded by host factors CFH and CFI preventing its deposition on the
CC       bacterial surface while C3a is further inactivated by aureolysin.
CC       {ECO:0000269|PubMed:21502375}.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000269|PubMed:26091039}.
CC   -!- POLYMORPHISM: There are two alleles: C3S (C3 slow), the most common
CC       allele in all races and C3F (C3 fast), relatively frequent in
CC       Caucasians, less common in Black Americans, extremely rare in
CC       Orientals.
CC   -!- DISEASE: Complement component 3 deficiency (C3D) [MIM:613779]: A rare
CC       defect of the complement classical pathway. Patients develop recurrent,
CC       severe, pyogenic infections because of ineffective opsonization of
CC       pathogens. Some patients may also develop autoimmune disorders, such as
CC       arthralgia and vasculitic rashes, lupus-like syndrome and
CC       membranoproliferative glomerulonephritis. {ECO:0000269|PubMed:7961791}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- DISEASE: Macular degeneration, age-related, 9 (ARMD9) [MIM:611378]: A
CC       form of age-related macular degeneration, a multifactorial eye disease
CC       and the most common cause of irreversible vision loss in the developed
CC       world. In most patients, the disease is manifest as ophthalmoscopically
CC       visible yellowish accumulations of protein and lipid that lie beneath
CC       the retinal pigment epithelium and within an elastin-containing
CC       structure known as Bruch membrane. {ECO:0000269|PubMed:17634448,
CC       ECO:0000269|PubMed:24036952}. Note=Disease susceptibility is associated
CC       with variants affecting the gene represented in this entry.
CC   -!- DISEASE: Hemolytic uremic syndrome atypical 5 (AHUS5) [MIM:612925]: An
CC       atypical form of hemolytic uremic syndrome. It is a complex genetic
CC       disease characterized by microangiopathic hemolytic anemia,
CC       thrombocytopenia, renal failure and absence of episodes of
CC       enterocolitis and diarrhea. In contrast to typical hemolytic uremic
CC       syndrome, atypical forms have a poorer prognosis, with higher death
CC       rates and frequent progression to end-stage renal disease.
CC       {ECO:0000269|PubMed:18796626, ECO:0000269|PubMed:20513133}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       gene represented in this entry. Other genes may play a role in
CC       modifying the phenotype.
CC   -!- DISEASE: Note=Increased levels of C3 and its cleavage product ASP, are
CC       associated with obesity, diabetes and coronary heart disease. Short-
CC       term endurance training reduces baseline ASP levels and subsequently
CC       fat storage.
CC   -!- CAUTION: An article reported the interaction surface between C3 and CR2
CC       (PubMed:11387479). According to a another paper, it is however an
CC       artifact and can be ascribed to the presence of zinc acetate in the
CC       buffer (PubMed:21527715). {ECO:0000269|PubMed:11387479,
CC       ECO:0000269|PubMed:21527715}.
CC   -!- CAUTION: The difference between allele C3S (C3 slow) and allele C3F (C3
CC       fast) was reported to be caused by a an Asn at position 1216 instead of
CC       an Asp (PubMed:2473125). The paper was however retracted
CC       (PubMed:2584723). {ECO:0000269|PubMed:2473125,
CC       ECO:0000269|PubMed:2584723}.
CC   -!- WEB RESOURCE: Name=C3base; Note=C3 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/C3base/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Complement C3 entry;
CC       URL="https://en.wikipedia.org/wiki/Complement_c3";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/c3/";
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DR   EMBL; K02765; AAA85332.1; -; mRNA.
DR   EMBL; AY513239; AAR89906.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69071.1; -; Genomic_DNA.
DR   EMBL; BC150179; AAI50180.1; -; mRNA.
DR   EMBL; BC150200; AAI50201.1; -; mRNA.
DR   CCDS; CCDS32883.1; -.
DR   PIR; A94065; C3HU.
DR   RefSeq; NP_000055.2; NM_000064.3.
DR   PDB; 1C3D; X-ray; 1.80 A; A=996-1287.
DR   PDB; 1GHQ; X-ray; 2.04 A; A=996-1300.
DR   PDB; 1W2S; X-ray; -; A=996-1299.
DR   PDB; 2A73; X-ray; 3.30 A; A=23-665, B=673-1663.
DR   PDB; 2A74; X-ray; 2.40 A; A/D=23-665, B/E=749-936, C/F=1321-1663.
DR   PDB; 2GOX; X-ray; 2.20 A; A/C=996-1287.
DR   PDB; 2I07; X-ray; 4.00 A; A=23-667, B=749-1663.
DR   PDB; 2ICE; X-ray; 3.10 A; A/D=23-664, B/E=749-954, C/F=1321-1663.
DR   PDB; 2ICF; X-ray; 4.10 A; A=23-664, B=749-1663.
DR   PDB; 2NOJ; X-ray; 2.70 A; A/C/E/G=996-1287.
DR   PDB; 2QKI; X-ray; 2.40 A; A/D=23-665, B/E=749-936, C/F=1321-1663.
DR   PDB; 2WII; X-ray; 2.70 A; A=23-667, B=749-1663.
DR   PDB; 2WIN; X-ray; 3.90 A; A/C/E/G=23-667, B/D/F/H=749-1663.
DR   PDB; 2WY7; X-ray; 1.70 A; A=996-1303.
DR   PDB; 2WY8; X-ray; 1.70 A; A=996-1303.
DR   PDB; 2XQW; X-ray; 2.31 A; A/B=996-1287.
DR   PDB; 2XWB; X-ray; 3.49 A; A/C=23-664, B/D=752-1663.
DR   PDB; 2XWJ; X-ray; 4.00 A; A/C/E/G=23-667, B/D/F/H=749-1663.
DR   PDB; 3D5R; X-ray; 2.10 A; A/B=996-1287.
DR   PDB; 3D5S; X-ray; 2.30 A; A/B=996-1287.
DR   PDB; 3G6J; X-ray; 3.10 A; A/C=23-666, B/D=749-1663.
DR   PDB; 3L3O; X-ray; 3.40 A; A/D=23-667, B/E=749-954, C/F=1321-1663.
DR   PDB; 3L5N; X-ray; 7.54 A; A=23-667, B=749-1663.
DR   PDB; 3NMS; X-ray; 4.10 A; A=23-667, B=749-954, C=1321-1663.
DR   PDB; 3OED; X-ray; 3.16 A; A/B=996-1303.
DR   PDB; 3OHX; X-ray; 3.50 A; A/D=23-667, B/E=749-954, C/F=1321-1663.
DR   PDB; 3OXU; X-ray; 2.10 A; A/B/C=996-1303.
DR   PDB; 3RJ3; X-ray; 2.35 A; A/B/C=996-1303.
DR   PDB; 3T4A; X-ray; 3.40 A; A/D=23-667, B/E=749-954, C/F=1321-1663.
DR   PDB; 4HW5; X-ray; 2.25 A; A/B=672-748.
DR   PDB; 4HWJ; X-ray; 2.60 A; A=672-747.
DR   PDB; 4I6O; X-ray; 2.14 A; A=672-748.
DR   PDB; 4M76; X-ray; 2.80 A; A=994-1288.
DR   PDB; 4ONT; X-ray; 2.15 A; A/B/C=996-1303.
DR   PDB; 4ZH1; X-ray; 2.24 A; A/B/C=996-1303.
DR   PDB; 5FO7; X-ray; 2.80 A; A=23-667, B=749-1663.
DR   PDB; 5FO8; X-ray; 2.40 A; A=23-667, B=749-1663.
DR   PDB; 5FO9; X-ray; 3.30 A; A/D=23-667, B/E=749-1663.
DR   PDB; 5FOA; X-ray; 4.19 A; A/C=23-667, B/D=749-1663.
DR   PDB; 5FOB; X-ray; 2.60 A; A=23-667, B=749-1663.
DR   PDB; 5NBQ; X-ray; 3.18 A; A/B/C=994-1287.
DR   PDB; 5O32; X-ray; 4.21 A; A/E=23-667, B/F=749-1663.
DR   PDB; 5O35; X-ray; 4.20 A; A=23-667, B=749-1663.
DR   PDB; 6EHG; X-ray; 2.65 A; A=23-665, B=749-1663.
DR   PDB; 6RMT; X-ray; 2.00 A; A/B=996-1303.
DR   PDB; 6RMU; X-ray; 2.40 A; A/B=996-1303.
DR   PDB; 6RUR; X-ray; 6.00 A; A/G=23-667, B/H=749-1663.
DR   PDB; 6RUV; X-ray; 6.15 A; A/G=23-667, B/H=749-1663.
DR   PDB; 6S0B; X-ray; 2.31 A; C=1517-1663.
DR   PDBsum; 1C3D; -.
DR   PDBsum; 1GHQ; -.
DR   PDBsum; 1W2S; -.
DR   PDBsum; 2A73; -.
DR   PDBsum; 2A74; -.
DR   PDBsum; 2GOX; -.
DR   PDBsum; 2I07; -.
DR   PDBsum; 2ICE; -.
DR   PDBsum; 2ICF; -.
DR   PDBsum; 2NOJ; -.
DR   PDBsum; 2QKI; -.
DR   PDBsum; 2WII; -.
DR   PDBsum; 2WIN; -.
DR   PDBsum; 2WY7; -.
DR   PDBsum; 2WY8; -.
DR   PDBsum; 2XQW; -.
DR   PDBsum; 2XWB; -.
DR   PDBsum; 2XWJ; -.
DR   PDBsum; 3D5R; -.
DR   PDBsum; 3D5S; -.
DR   PDBsum; 3G6J; -.
DR   PDBsum; 3L3O; -.
DR   PDBsum; 3L5N; -.
DR   PDBsum; 3NMS; -.
DR   PDBsum; 3OED; -.
DR   PDBsum; 3OHX; -.
DR   PDBsum; 3OXU; -.
DR   PDBsum; 3RJ3; -.
DR   PDBsum; 3T4A; -.
DR   PDBsum; 4HW5; -.
DR   PDBsum; 4HWJ; -.
DR   PDBsum; 4I6O; -.
DR   PDBsum; 4M76; -.
DR   PDBsum; 4ONT; -.
DR   PDBsum; 4ZH1; -.
DR   PDBsum; 5FO7; -.
DR   PDBsum; 5FO8; -.
DR   PDBsum; 5FO9; -.
DR   PDBsum; 5FOA; -.
DR   PDBsum; 5FOB; -.
DR   PDBsum; 5NBQ; -.
DR   PDBsum; 5O32; -.
DR   PDBsum; 5O35; -.
DR   PDBsum; 6EHG; -.
DR   PDBsum; 6RMT; -.
DR   PDBsum; 6RMU; -.
DR   PDBsum; 6RUR; -.
DR   PDBsum; 6RUV; -.
DR   PDBsum; 6S0B; -.
DR   SMR; P01024; -.
DR   BioGRID; 107179; 49.
DR   ComplexPortal; CPX-5381; Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb.
DR   ComplexPortal; CPX-973; Complement C3b complex.
DR   CORUM; P01024; -.
DR   DIP; DIP-35180N; -.
DR   IntAct; P01024; 52.
DR   MINT; P01024; -.
DR   STRING; 9606.ENSP00000245907; -.
DR   BindingDB; P01024; -.
DR   ChEMBL; CHEMBL4917; -.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB00028; Human immunoglobulin G.
DR   DrugBank; DB06492; Mirococept.
DR   DrugBank; DB01915; S-Hydroxycysteine.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   MEROPS; I39.950; -.
DR   CarbonylDB; P01024; -.
DR   GlyConnect; 110; 35 N-Linked glycans (3 sites), 1 O-Linked glycan (1 site).
DR   GlyGen; P01024; 5 sites, 20 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P01024; -.
DR   MetOSite; P01024; -.
DR   PhosphoSitePlus; P01024; -.
DR   BioMuta; C3; -.
DR   DMDM; 119370332; -.
DR   DOSAC-COBS-2DPAGE; P01024; -.
DR   SWISS-2DPAGE; P01024; -.
DR   CPTAC; CPTAC-1239; -.
DR   CPTAC; non-CPTAC-1105; -.
DR   CPTAC; non-CPTAC-1106; -.
DR   CPTAC; non-CPTAC-2653; -.
DR   EPD; P01024; -.
DR   jPOST; P01024; -.
DR   MassIVE; P01024; -.
DR   PaxDb; P01024; -.
DR   PeptideAtlas; P01024; -.
DR   PRIDE; P01024; -.
DR   ProteomicsDB; 51308; -.
DR   ABCD; P01024; 22 sequenced antibodies.
DR   Antibodypedia; 692; 1895 antibodies.
DR   DNASU; 718; -.
DR   Ensembl; ENST00000245907; ENSP00000245907; ENSG00000125730.
DR   GeneID; 718; -.
DR   KEGG; hsa:718; -.
DR   CTD; 718; -.
DR   DisGeNET; 718; -.
DR   GeneCards; C3; -.
DR   GeneReviews; C3; -.
DR   HGNC; HGNC:1318; C3.
DR   HPA; ENSG00000125730; Tissue enriched (liver).
DR   MalaCards; C3; -.
DR   MIM; 120700; gene.
DR   MIM; 611378; phenotype.
DR   MIM; 612925; phenotype.
DR   MIM; 613779; phenotype.
DR   neXtProt; NX_P01024; -.
DR   OpenTargets; ENSG00000125730; -.
DR   Orphanet; 544472; Atypical hemolytic uremic syndrome with complement gene abnormality.
DR   Orphanet; 280133; Complement component 3 deficiency.
DR   Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
DR   PharmGKB; PA25897; -.
DR   VEuPathDB; HostDB:ENSG00000125730.16; -.
DR   eggNOG; KOG1366; Eukaryota.
DR   GeneTree; ENSGT00940000154063; -.
DR   HOGENOM; CLU_001634_4_0_1; -.
DR   InParanoid; P01024; -.
DR   OMA; QATNTMQ; -.
DR   OrthoDB; 23785at2759; -.
DR   PhylomeDB; P01024; -.
DR   TreeFam; TF313285; -.
DR   BRENDA; 3.4.21.47; 2681.
DR   PathwayCommons; P01024; -.
DR   Reactome; R-HSA-173736; Alternative complement activation.
DR   Reactome; R-HSA-174577; Activation of C3 and C5.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SABIO-RK; P01024; -.
DR   SIGNOR; P01024; -.
DR   BioGRID-ORCS; 718; 7 hits in 988 CRISPR screens.
DR   ChiTaRS; C3; human.
DR   EvolutionaryTrace; P01024; -.
DR   GeneWiki; Complement_component_3; -.
DR   GenomeRNAi; 718; -.
DR   Pharos; P01024; Tbio.
DR   PRO; PR:P01024; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P01024; protein.
DR   Bgee; ENSG00000125730; Expressed in parietal pleura and 238 other tissues.
DR   ExpressionAtlas; P01024; baseline and differential.
DR   Genevisible; P01024; HS.
DR   GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; IDA:UniProtKB.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR   GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
DR   GO; GO:1905114; P:cell surface receptor signaling pathway involved in cell-cell signaling; IEA:Ensembl.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0006956; P:complement activation; IMP:BHF-UCL.
DR   GO; GO:0006957; P:complement activation, alternative pathway; TAS:Reactome.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0097278; P:complement-dependent cytotoxicity; IEA:Ensembl.
DR   GO; GO:0150062; P:complement-mediated synapse pruning; ISS:ARUK-UCL.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0016322; P:neuron remodeling; ISS:ARUK-UCL.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0035846; P:oviduct epithelium development; IEA:Ensembl.
DR   GO; GO:0001970; P:positive regulation of activation of membrane attack complex; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IMP:BHF-UCL.
DR   GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0010884; P:positive regulation of lipid storage; IDA:UniProtKB.
DR   GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:ARUK-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:ARUK-UCL.
DR   GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IEA:Ensembl.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   GO; GO:0010866; P:regulation of triglyceride biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0150064; P:vertebrate eye-specific patterning; ISS:ARUK-UCL.
DR   CDD; cd00017; ANATO; 1.
DR   CDD; cd03583; NTR_complement_C3; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.60.40.690; -; 1.
DR   InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR   InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR000020; Anaphylatoxin/fibulin.
DR   InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR   InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR   InterPro; IPR041425; C3/4/5_MG1.
DR   InterPro; IPR035711; Complement_C3-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR019742; MacrogloblnA2_CS.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR041555; MG3.
DR   InterPro; IPR040839; MG4.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR018933; Netrin_module_non-TIMP.
DR   InterPro; IPR035815; NTR_complement_C3.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF07677; A2M_recep; 1.
DR   Pfam; PF01821; ANATO; 1.
DR   Pfam; PF17790; MG1; 1.
DR   Pfam; PF01835; MG2; 1.
DR   Pfam; PF17791; MG3; 1.
DR   Pfam; PF17789; MG4; 1.
DR   Pfam; PF01759; NTR; 1.
DR   Pfam; PF07678; TED_complement; 1.
DR   PRINTS; PR00004; ANAPHYLATOXN.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SMART; SM01361; A2M_recep; 1.
DR   SMART; SM00104; ANATO; 1.
DR   SMART; SM00643; C345C; 1.
DR   SUPFAM; SSF47686; SSF47686; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF49410; SSF49410; 1.
DR   SUPFAM; SSF50242; SSF50242; 1.
DR   PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR   PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR   PROSITE; PS50189; NTR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Age-related macular degeneration;
KW   Cleavage on pair of basic residues; Complement alternate pathway;
KW   Complement pathway; Direct protein sequencing; Disease variant;
KW   Disulfide bond; Fatty acid metabolism; Glycoprotein;
KW   Hemolytic uremic syndrome; Immunity; Inflammatory response;
KW   Innate immunity; Lipid metabolism; Phosphoprotein; Reference proteome;
KW   Secreted; Signal; Thioester bond.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:8376604"
FT   CHAIN           23..1663
FT                   /note="Complement C3"
FT                   /id="PRO_0000005907"
FT   CHAIN           23..667
FT                   /note="Complement C3 beta chain"
FT                   /id="PRO_0000005908"
FT   CHAIN           569..667
FT                   /note="C3-beta-c"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000430430"
FT   CHAIN           672..1663
FT                   /note="Complement C3 alpha chain"
FT                   /id="PRO_0000005909"
FT   CHAIN           672..748
FT                   /note="C3a anaphylatoxin"
FT                   /id="PRO_0000005910"
FT   CHAIN           672..747
FT                   /note="Acylation stimulating protein"
FT                   /id="PRO_0000419935"
FT   CHAIN           749..1663
FT                   /note="Complement C3b alpha' chain"
FT                   /id="PRO_0000005911"
FT   CHAIN           749..954
FT                   /note="Complement C3c alpha' chain fragment 1"
FT                   /id="PRO_0000005912"
FT   CHAIN           955..1303
FT                   /note="Complement C3dg fragment"
FT                   /id="PRO_0000005913"
FT   CHAIN           955..1001
FT                   /note="Complement C3g fragment"
FT                   /id="PRO_0000005914"
FT   CHAIN           1002..1303
FT                   /note="Complement C3d fragment"
FT                   /id="PRO_0000005915"
FT   PEPTIDE         1304..1320
FT                   /note="Complement C3f fragment"
FT                   /evidence="ECO:0000269|PubMed:8376604"
FT                   /id="PRO_0000005916"
FT   CHAIN           1321..1663
FT                   /note="Complement C3c alpha' chain fragment 2"
FT                   /id="PRO_0000273948"
FT   DOMAIN          693..728
FT                   /note="Anaphylatoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   DOMAIN          1518..1661
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          954..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1634..1659
FT                   /note="Interaction with CFP/properdin"
FT                   /evidence="ECO:0000269|PubMed:28264884,
FT                   ECO:0000269|PubMed:31507604"
FT   SITE            747..748
FT                   /note="Cleavage; by carboxypeptidases"
FT   SITE            748..749
FT                   /note="Cleavage; by C3 convertase"
FT   SITE            954..955
FT                   /note="Cleavage; by factor I"
FT                   /evidence="ECO:0000255"
FT   SITE            1303..1304
FT                   /note="Cleavage; by factor I"
FT   SITE            1320..1321
FT                   /note="Cleavage; by factor I"
FT   SITE            1663
FT                   /note="Coordinates Mg2+ for interaction with Complement
FT                   factor B Bb fragment"
FT                   /evidence="ECO:0000269|PubMed:28264884,
FT                   ECO:0000269|PubMed:31507604"
FT   MOD_RES         38
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         70
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         297
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         303
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         672
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         968
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         1321
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         1573
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519,
FT                   ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:17051150, ECO:0000269|PubMed:17684013,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2579379"
FT   CARBOHYD        939
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17051150"
FT   CARBOHYD        1617
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   DISULFID        559..816
FT                   /note="Interchain (between beta and alpha chains)"
FT   DISULFID        627..662
FT   DISULFID        693..720
FT                   /evidence="ECO:0000269|PubMed:8416818"
FT   DISULFID        694..727
FT   DISULFID        707..728
FT   DISULFID        873..1513
FT   DISULFID        1101..1158
FT   DISULFID        1358..1489
FT   DISULFID        1389..1458
FT   DISULFID        1506..1511
FT   DISULFID        1518..1590
FT   DISULFID        1537..1661
FT   DISULFID        1637..1646
FT   CROSSLNK        1010..1013
FT                   /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT   VARIANT         102
FT                   /note="R -> G (in allele C3F; associated with
FT                   susceptibility to ARMD9; results in decreased binding
FT                   affinity for regulator factor H; results in reduced
FT                   sensitivity to cleavage by factor I; dbSNP:rs2230199)"
FT                   /evidence="ECO:0000269|PubMed:1976733,
FT                   ECO:0000269|PubMed:21555552, ECO:0000269|Ref.2"
FT                   /id="VAR_001983"
FT   VARIANT         155
FT                   /note="K -> Q (in ARMD9; results in resistance to
FT                   proteolytic inactivation by CFH and CFI;
FT                   dbSNP:rs147859257)"
FT                   /evidence="ECO:0000269|PubMed:24036952"
FT                   /id="VAR_070941"
FT   VARIANT         314
FT                   /note="P -> L (in dbSNP:rs1047286)"
FT                   /evidence="ECO:0000269|PubMed:1976733,
FT                   ECO:0000269|PubMed:2579379, ECO:0000269|Ref.2"
FT                   /id="VAR_001984"
FT   VARIANT         469
FT                   /note="E -> D (in dbSNP:rs11569422)"
FT                   /id="VAR_020262"
FT   VARIANT         549
FT                   /note="D -> N (in C3D; impairs secretion; variant confirmed
FT                   at protein level; dbSNP:rs1449441916)"
FT                   /evidence="ECO:0000269|PubMed:22028381,
FT                   ECO:0000269|PubMed:7961791"
FT                   /id="VAR_001985"
FT   VARIANT         592
FT                   /note="R -> Q (in AHUS5; leads to impaired binding to the
FT                   regulator CD46/MCP and resistance to cleavage by factor I;
FT                   dbSNP:rs121909583)"
FT                   /evidence="ECO:0000269|PubMed:18796626"
FT                   /id="VAR_063213"
FT   VARIANT         592
FT                   /note="R -> W (in AHUS5; leads to impaired binding to the
FT                   regulator CD46/MCP and resistance to cleavage by factor I;
FT                   dbSNP:rs771353792)"
FT                   /evidence="ECO:0000269|PubMed:18796626"
FT                   /id="VAR_063214"
FT   VARIANT         603
FT                   /note="F -> V (in AHUS5)"
FT                   /evidence="ECO:0000269|PubMed:20513133"
FT                   /id="VAR_063654"
FT   VARIANT         735
FT                   /note="R -> W (in AHUS5; dbSNP:rs117793540)"
FT                   /evidence="ECO:0000269|PubMed:18796626"
FT                   /id="VAR_063215"
FT   VARIANT         863
FT                   /note="R -> K (in dbSNP:rs11569472)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019206"
FT   VARIANT         1042
FT                   /note="R -> L (in AHUS5)"
FT                   /evidence="ECO:0000269|PubMed:20513133"
FT                   /id="VAR_063655"
FT   VARIANT         1094
FT                   /note="A -> V (in AHUS5; leads to impaired binding to the
FT                   regulator CD46/MCP and resistance to cleavage by factor I;
FT                   dbSNP:rs121909584)"
FT                   /evidence="ECO:0000269|PubMed:18796626"
FT                   /id="VAR_063216"
FT   VARIANT         1115
FT                   /note="D -> N (in AHUS5; leads to impaired binding to the
FT                   regulator CD46/MCP and resistance to cleavage by factor I;
FT                   dbSNP:rs121909585)"
FT                   /evidence="ECO:0000269|PubMed:18796626"
FT                   /id="VAR_063217"
FT   VARIANT         1158
FT                   /note="C -> W (in AHUS5)"
FT                   /evidence="ECO:0000269|PubMed:18796626"
FT                   /id="VAR_063218"
FT   VARIANT         1161
FT                   /note="Q -> K (in AHUS5; leads to impaired binding to the
FT                   regulator CD46/MCP and resistance to cleavage by factor I)"
FT                   /evidence="ECO:0000269|PubMed:18796626"
FT                   /id="VAR_063219"
FT   VARIANT         1224
FT                   /note="G -> D (in dbSNP:rs11569534)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019207"
FT   VARIANT         1367
FT                   /note="I -> T (in dbSNP:rs11569541)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019208"
FT   VARIANT         1464
FT                   /note="H -> D (in AHUS5)"
FT                   /evidence="ECO:0000269|PubMed:18796626"
FT                   /id="VAR_063220"
FT   VARIANT         1521
FT                   /note="Q -> R (in dbSNP:rs7256789)"
FT                   /id="VAR_029792"
FT   VARIANT         1601
FT                   /note="H -> N (in dbSNP:rs1803225)"
FT                   /id="VAR_029793"
FT   VARIANT         1619
FT                   /note="S -> R (in dbSNP:rs2230210)"
FT                   /id="VAR_029326"
FT   MUTAGEN         1029
FT                   /note="D->A: Minor effect on binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651,
FT                   ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1030
FT                   /note="E->A: Impaired binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651,
FT                   ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1032
FT                   /note="E->A: Impaired binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651,
FT                   ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1035
FT                   /note="E->A: No effect on binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651"
FT   MUTAGEN         1042
FT                   /note="R->M: Impaired binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651"
FT   MUTAGEN         1108..1109
FT                   /note="IL->RR: Impaired binding of C3d to CR2; when
FT                   associated with A-1163."
FT                   /evidence="ECO:0000269|PubMed:11387479"
FT   MUTAGEN         1110
FT                   /note="E->A: No effect on binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1115
FT                   /note="D->A: No effect on binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1121
FT                   /note="D->A: No effect on binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1140
FT                   /note="D->A: No effect on binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651,
FT                   ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1153
FT                   /note="E->A: Impaired binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651,
FT                   ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1156
FT                   /note="D->A: Impaired binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651,
FT                   ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1159
FT                   /note="E->A: Impaired binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651,
FT                   ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1160
FT                   /note="E->A: Minor effect on binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651,
FT                   ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1163
FT                   /note="N->A: No effect on binding of C3d to CR2. Impaired
FT                   binding of C3d to CR2; when associated with 1108-R-R-1109."
FT                   /evidence="ECO:0000269|PubMed:11387479,
FT                   ECO:0000269|PubMed:20083651, ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1163
FT                   /note="N->R: Impaired binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:11387479,
FT                   ECO:0000269|PubMed:20083651, ECO:0000269|PubMed:20951140"
FT   MUTAGEN         1284
FT                   /note="K->A: Impaired binding of C3d to CR2."
FT                   /evidence="ECO:0000269|PubMed:20083651"
FT   CONFLICT        681
FT                   /note="D -> N (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        700
FT                   /note="E -> Q (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1026
FT                   /note="H -> S (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          53..64
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:2ICE"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:2ICE"
FT   STRAND          105..112
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          115..123
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          144..152
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          162..168
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            183..187
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          202..210
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          214..216
FT                   /evidence="ECO:0007829|PDB:2XWB"
FT   STRAND          218..224
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          231..244
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          251..259
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          267..277
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          280..294
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          297..302
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           304..309
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          311..313
FT                   /evidence="ECO:0007829|PDB:5FO9"
FT   HELIX           316..319
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          323..332
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          338..352
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          358..360
FT                   /evidence="ECO:0007829|PDB:2A73"
FT   STRAND          362..364
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          370..377
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:3T4A"
FT   STRAND          388..393
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           395..397
FT                   /evidence="ECO:0007829|PDB:2QKI"
FT   STRAND          398..400
FT                   /evidence="ECO:0007829|PDB:6EHG"
FT   STRAND          405..411
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          420..426
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            429..431
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           433..435
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          439..445
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           449..451
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          455..459
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          470..478
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            481..483
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           484..486
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          489..496
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          499..507
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          513..520
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           523..525
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          527..538
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          540..542
FT                   /evidence="ECO:0007829|PDB:2QKI"
FT   STRAND          544..554
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          563..567
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            568..570
FT                   /evidence="ECO:0007829|PDB:2ICE"
FT   STRAND          571..573
FT                   /evidence="ECO:0007829|PDB:3G6J"
FT   STRAND          580..588
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          592..599
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           602..605
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           613..622
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          628..630
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           635..641
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          644..648
FT                   /evidence="ECO:0007829|PDB:2QKI"
FT   HELIX           675..684
FT                   /evidence="ECO:0007829|PDB:4HW5"
FT   HELIX           688..697
FT                   /evidence="ECO:0007829|PDB:4I6O"
FT   HELIX           707..710
FT                   /evidence="ECO:0007829|PDB:4I6O"
FT   TURN            712..714
FT                   /evidence="ECO:0007829|PDB:4HW5"
FT   HELIX           718..743
FT                   /evidence="ECO:0007829|PDB:4I6O"
FT   STRAND          753..755
FT                   /evidence="ECO:0007829|PDB:3L3O"
FT   HELIX           758..760
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          769..771
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          775..777
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          786..794
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          800..810
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            811..813
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          814..817
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          821..825
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          828..834
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          837..840
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          845..853
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          860..866
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          872..875
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          878..880
FT                   /evidence="ECO:0007829|PDB:5FOB"
FT   STRAND          882..888
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          892..902
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          906..916
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            917..920
FT                   /evidence="ECO:0007829|PDB:3G6J"
FT   STRAND          922..932
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          934..947
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   HELIX           949..952
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          954..956
FT                   /evidence="ECO:0007829|PDB:2A73"
FT   STRAND          957..962
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          968..970
FT                   /evidence="ECO:0007829|PDB:5FOB"
FT   STRAND          977..984
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   TURN            988..990
FT                   /evidence="ECO:0007829|PDB:3G6J"
FT   HELIX           997..999
FT                   /evidence="ECO:0007829|PDB:2WY8"
FT   HELIX           1001..1003
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   STRAND          1009..1012
FT                   /evidence="ECO:0007829|PDB:3G6J"
FT   HELIX           1013..1031
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1034..1037
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1041..1057
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   TURN            1062..1064
FT                   /evidence="ECO:0007829|PDB:5FO7"
FT   STRAND          1068..1072
FT                   /evidence="ECO:0007829|PDB:5FOB"
FT   HELIX           1076..1089
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   TURN            1090..1092
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1097..1111
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   TURN            1114..1116
FT                   /evidence="ECO:0007829|PDB:2NOJ"
FT   HELIX           1127..1133
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1139..1158
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   TURN            1159..1161
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1165..1179
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1180..1182
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1186..1198
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1204..1213
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   TURN            1216..1218
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   STRAND          1223..1225
FT                   /evidence="ECO:0007829|PDB:1GHQ"
FT   HELIX           1226..1243
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   TURN            1246..1248
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1249..1258
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   STRAND          1265..1267
FT                   /evidence="ECO:0007829|PDB:3G6J"
FT   HELIX           1269..1285
FT                   /evidence="ECO:0007829|PDB:2WY7"
FT   HELIX           1286..1288
FT                   /evidence="ECO:0007829|PDB:6RMU"
FT   TURN            1297..1299
FT                   /evidence="ECO:0007829|PDB:3OXU"
FT   STRAND          1303..1305
FT                   /evidence="ECO:0007829|PDB:2WII"
FT   STRAND          1307..1313
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   TURN            1314..1317
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          1320..1326
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          1330..1338
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          1340..1350
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          1359..1369
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1384..1392
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1394..1396
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1400..1406
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1411..1413
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           1415..1422
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1424..1428
FT                   /evidence="ECO:0007829|PDB:6EHG"
FT   HELIX           1431..1434
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            1438..1440
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1442..1449
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1453..1455
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1457..1467
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1469..1471
FT                   /evidence="ECO:0007829|PDB:2A73"
FT   STRAND          1475..1481
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1485..1493
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1495..1497
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   HELIX           1498..1500
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1504..1507
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1510..1513
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            1515..1517
FT                   /evidence="ECO:0007829|PDB:2WII"
FT   STRAND          1518..1520
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   TURN            1524..1526
FT                   /evidence="ECO:0007829|PDB:6EHG"
FT   HELIX           1529..1535
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   STRAND          1537..1540
FT                   /evidence="ECO:0007829|PDB:2ICE"
FT   STRAND          1541..1551
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   STRAND          1559..1570
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   TURN            1577..1579
FT                   /evidence="ECO:0007829|PDB:5FOB"
FT   STRAND          1581..1586
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   HELIX           1588..1590
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   HELIX           1591..1594
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   STRAND          1601..1607
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   HELIX           1608..1610
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   STRAND          1611..1613
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1615..1617
FT                   /evidence="ECO:0007829|PDB:5FOB"
FT   STRAND          1619..1621
FT                   /evidence="ECO:0007829|PDB:2A74"
FT   STRAND          1627..1631
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   HELIX           1636..1638
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   TURN            1640..1642
FT                   /evidence="ECO:0007829|PDB:6S0B"
FT   HELIX           1643..1659
FT                   /evidence="ECO:0007829|PDB:6S0B"
SQ   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
//
DBGET integrated database retrieval system