CO3_MOUSE
ID CO3_MOUSE Reviewed; 1663 AA.
AC P01027; Q61370; Q80XP1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Complement C3;
DE AltName: Full=HSE-MSF;
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=6208565; DOI=10.1098/rstb.1984.0094;
RA Fey G.H., Lundwall A., Wetsel R.A., Tack B.F., de Bruijn M.H.L., Domdey H.;
RT "Nucleotide sequence of complementary DNA and derived amino acid sequence
RT of murine complement protein C3.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:333-344(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-724 (ISOFORM LONG).
RX PubMed=6548745; DOI=10.1016/s0021-9258(18)89824-6;
RA Lundwall A., Wetsel R.A., Domdey H., Tack B.F., Fey G.H.;
RT "Structure of murine complement component C3. I. Nucleotide sequence of
RT cloned complementary and genomic DNA coding for the beta chain.";
RL J. Biol. Chem. 259:13851-13856(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX PubMed=6985486; DOI=10.1073/pnas.79.23.7077;
RA Wiebauer K., Domdey H., Diggelmann H., Fey G.;
RT "Isolation and analysis of genomic DNA clones encoding the third component
RT of mouse complement.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:7077-7081(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-1663 (ISOFORM LONG).
RX PubMed=2578664; DOI=10.1073/pnas.82.1.9;
RA Sottrup-Jensen L., Stepanik T.M., Kristensen T., Lonblad P.B., Jones C.M.,
RA Wierzbicki D.M., Magnusson S., Domdey H., Wetsel R.A., Lundwall A.,
RA Tack B.F., Fey G.H.;
RT "Common evolutionary origin of alpha 2-macroglobulin and complement
RT components C3 and C4.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:9-13(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-240 (ISOFORM LONG).
RX PubMed=6356427; DOI=10.1007/bf00205869;
RA Fey G., Domdey H., Wiebauer K., Whitehead A.S., Odink K.;
RT "Structure and expression of the C3 gene.";
RL Springer Semin. Immunopathol. 6:119-147(1983).
RN [7]
RP PROTEIN SEQUENCE OF 25-41 AND 749-760.
RX PubMed=8364938;
RA Hamada J., Cavanaugh P.G., Miki K., Nicolson G.L.;
RT "A paracrine migration-stimulating factor for metastatic tumor cells
RT secreted by mouse hepatic sinusoidal endothelial cells: identification as
RT complement component C3b.";
RL Cancer Res. 53:4418-4423(1993).
RN [8]
RP PROTEIN SEQUENCE OF 25-31 AND 671-680.
RX PubMed=2065778; DOI=10.1016/0014-5793(91)80715-f;
RA Sato T., Hong M.H., Jin C.H., Ishimi Y., Udagawa N., Shinki T., Abe E.,
RA Suda T.;
RT "The specific production of the third component of complement by
RT osteoblastic cells treated with 1 alpha,25-dihydroxyvitamin D3.";
RL FEBS Lett. 285:21-24(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 658-761.
RX PubMed=6609661; DOI=10.1111/j.1749-6632.1983.tb18118.x;
RA Fey G.H., Wiebauer K., Domdey H.;
RT "Amino acid sequences of mouse complement C3 derived from nucleotide
RT sequences of cloned cDNA.";
RL Ann. N. Y. Acad. Sci. 421:307-312(1983).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 671-1663 (ISOFORM LONG).
RX PubMed=6094532; DOI=10.1016/s0021-9258(18)89825-8;
RA Wetsel R.A., Lundwall A., Davidson F., Gibson T., Tack B.F., Fey G.H.;
RT "Structure of murine complement component C3. II. Nucleotide sequence of
RT cloned complementary DNA coding for the alpha chain.";
RL J. Biol. Chem. 259:13857-13862(1984).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 671-748.
RX PubMed=6961437; DOI=10.1073/pnas.79.24.7619;
RA Domdey H., Wiebauer K., Kazmaier M., Mueller V., Odink K., Fey G.H.;
RT "Characterization of the mRNA and cloned cDNA specifying the third
RT component of mouse complement.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:7619-7623(1982).
RN [12]
RP ALTERNATIVE INITIATION (ISOFORM SHORT).
RX PubMed=7964485; DOI=10.1084/jem.180.6.2079;
RA Cahen-Kramer Y., Martensson I.L., Melchers F.;
RT "The structure of an alternate form of complement C3 that displays
RT costimulatory growth factor activity for B lymphocytes.";
RL J. Exp. Med. 180:2079-2088(1994).
RN [13]
RP FUNCTION.
RX PubMed=12244109; DOI=10.1074/jbc.m207281200;
RA Xia Z., Sniderman A.D., Cianflone K.;
RT "Acylation-stimulating protein (ASP) deficiency induces obesity resistance
RT and increased energy expenditure in ob/ob mice.";
RL J. Biol. Chem. 277:45874-45879(2002).
RN [14]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18160458; DOI=10.1152/ajpendo.00590.2007;
RA Paglialunga S., Fisette A., Yan Y., Deshaies Y., Brouillette J.F.,
RA Pekna M., Cianflone K.;
RT "Acylation-stimulating protein deficiency and altered adipose tissue in
RT alternative complement pathway knockout mice.";
RL Am. J. Physiol. 294:E521-E529(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. The short isoform has B-cell stimulatory
CC activity. {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 -!- 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 (By similarity). The interaction
CC with Bb is dependent on Mg2+ (By similarity). C3b interacts with CR1
CC (via Sushi 8 and Sushi 9 domains). C3b interacts with CFH. C3d
CC interacts with CFH. 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 with S.aureus immunoglobulin-binding protein sbi, this
CC prevents interaction between C3dg and CR2. Interacts with S.aureus fib.
CC Interacts (both C3a and ASP) with C5AR2; the interaction occurs with
CC higher affinity for ASP, enhancing the phosphorylation and activation
CC of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of
CC GRP77. {ECO:0000250|UniProtKB:P01024}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P01027-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P01027-2; Sequence=VSP_018708;
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 dietary chylomicrons.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P01024}.
CC -!- DISRUPTION PHENOTYPE: Null mice displayed altered lipid metabolism and
CC morphological changes in adipocyte distribution. There is reduced
CC adipsin/CFD expression, increased number of smaller fat cells,
CC decreased DGAT1 expression and activity, and less triglyceride storage
CC capacity associated with delayed postprandial clearance. Mice on a
CC high-fat diet exihibited no diet-induced up-regulation of adipsin/CFD
CC expression nor adipocyte differentiation.
CC {ECO:0000269|PubMed:18160458}.
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DR EMBL; K02782; AAC42013.1; -; mRNA.
DR EMBL; BC043338; AAH43338.1; -; mRNA.
DR EMBL; M35659; AAA37339.1; -; mRNA.
DR EMBL; M33032; AAA37378.1; -; mRNA.
DR EMBL; J00369; AAA37336.1; -; Genomic_DNA.
DR EMBL; J00367; AAA37336.1; JOINED; Genomic_DNA.
DR EMBL; Z37998; CAA86099.2; -; Genomic_DNA.
DR CCDS; CCDS37670.1; -. [P01027-1]
DR PIR; A92459; C3MS.
DR PIR; I48284; I48284.
DR RefSeq; NP_033908.2; NM_009778.3. [P01027-1]
DR PDB; 6XZU; X-ray; 1.50 A; B=1517-1663.
DR PDBsum; 6XZU; -.
DR AlphaFoldDB; P01027; -.
DR SMR; P01027; -.
DR BioGRID; 198418; 10.
DR ComplexPortal; CPX-5893; Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb.
DR ComplexPortal; CPX-988; Complement C3b complex.
DR IntAct; P01027; 4.
DR MINT; P01027; -.
DR STRING; 10090.ENSMUSP00000024988; -.
DR MEROPS; I39.950; -.
DR GlyGen; P01027; 2 sites.
DR iPTMnet; P01027; -.
DR MetOSite; P01027; -.
DR PhosphoSitePlus; P01027; -.
DR SwissPalm; P01027; -.
DR CPTAC; non-CPTAC-5595; -.
DR CPTAC; non-CPTAC-5596; -.
DR EPD; P01027; -.
DR jPOST; P01027; -.
DR MaxQB; P01027; -.
DR PaxDb; P01027; -.
DR PeptideAtlas; P01027; -.
DR PRIDE; P01027; -.
DR ProteomicsDB; 283596; -. [P01027-1]
DR ProteomicsDB; 283597; -. [P01027-2]
DR ABCD; P01027; 3 sequenced antibodies.
DR Antibodypedia; 692; 1924 antibodies from 44 providers.
DR DNASU; 12266; -.
DR Ensembl; ENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164. [P01027-1]
DR GeneID; 12266; -.
DR KEGG; mmu:12266; -.
DR UCSC; uc008deg.2; mouse. [P01027-1]
DR CTD; 718; -.
DR MGI; MGI:88227; C3.
DR VEuPathDB; HostDB:ENSMUSG00000024164; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000154063; -.
DR HOGENOM; CLU_001634_4_0_1; -.
DR InParanoid; P01027; -.
DR OMA; QATNTMQ; -.
DR OrthoDB; 23785at2759; -.
DR PhylomeDB; P01027; -.
DR TreeFam; TF313285; -.
DR Reactome; R-MMU-173736; Alternative complement activation.
DR Reactome; R-MMU-174577; Activation of C3 and C5.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12266; 3 hits in 61 CRISPR screens.
DR ChiTaRS; C3; mouse.
DR PRO; PR:P01027; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P01027; protein.
DR Bgee; ENSMUSG00000024164; Expressed in left lobe of liver and 165 other tissues.
DR ExpressionAtlas; P01027; baseline and differential.
DR Genevisible; P01027; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
DR GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; ISS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
DR GO; GO:0007596; P:blood coagulation; ISO:MGI.
DR GO; GO:1905114; P:cell surface receptor signaling pathway involved in cell-cell signaling; IMP:ARUK-UCL.
DR GO; GO:0006956; P:complement activation; IDA:MGI.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0097278; P:complement-dependent cytotoxicity; IMP:MGI.
DR GO; GO:0150062; P:complement-mediated synapse pruning; IMP:ARUK-UCL.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0016322; P:neuron remodeling; IMP:ARUK-UCL.
DR GO; GO:0008228; P:opsonization; ISO:MGI.
DR GO; GO:0035846; P:oviduct epithelium development; IGI:MGI.
DR GO; GO:0001970; P:positive regulation of activation of membrane attack complex; IMP:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; ISO:MGI.
DR GO; GO:0044533; P:positive regulation of apoptotic process in another organism; IC:ComplexPortal.
DR GO; GO:0048639; P:positive regulation of developmental growth; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:ARUK-UCL.
DR GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IMP:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0030449; P:regulation of complement activation; ISO:MGI.
DR GO; GO:0030451; P:regulation of complement activation, alternative pathway; ISO:MGI.
DR GO; GO:0010866; P:regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0150064; P:vertebrate eye-specific patterning; IMP: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; Alternative initiation; Cleavage on pair of basic residues;
KW Complement alternate pathway; Complement pathway;
KW Direct protein sequencing; Disulfide bond; Fatty acid metabolism;
KW Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Secreted; Signal;
KW Thioester bond.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2065778,
FT ECO:0000269|PubMed:8364938"
FT CHAIN 25..1663
FT /note="Complement C3"
FT /id="PRO_0000005917"
FT CHAIN 25..666
FT /note="Complement C3 beta chain"
FT /id="PRO_0000005918"
FT CHAIN 569..666
FT /note="C3-beta-c"
FT /evidence="ECO:0000250"
FT /id="PRO_0000430431"
FT CHAIN 671..1663
FT /note="Complement C3 alpha chain"
FT /id="PRO_0000005919"
FT CHAIN 671..748
FT /note="C3a anaphylatoxin"
FT /id="PRO_0000005920"
FT CHAIN 671..747
FT /note="Acylation stimulating protein"
FT /id="PRO_0000419936"
FT CHAIN 749..1663
FT /note="Complement C3b alpha' chain"
FT /id="PRO_0000005921"
FT CHAIN 749..954
FT /note="Complement C3c alpha' chain fragment 1"
FT /id="PRO_0000005922"
FT CHAIN 955..1303
FT /note="Complement C3dg fragment"
FT /id="PRO_0000005923"
FT CHAIN 955..1001
FT /note="Complement C3g fragment"
FT /id="PRO_0000005924"
FT CHAIN 1002..1303
FT /note="Complement C3d fragment"
FT /id="PRO_0000005925"
FT PEPTIDE 1304..1320
FT /note="Complement C3f fragment"
FT /id="PRO_0000005927"
FT CHAIN 1321..1663
FT /note="Complement C3c alpha' chain fragment 2"
FT /id="PRO_0000273949"
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 1634..1659
FT /note="Interaction with CFP/properdin"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT SITE 747..748
FT /note="Cleavage; by carboxypeptidases"
FT /evidence="ECO:0000250"
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:0000250|UniProtKB:P01024"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 1617
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 559..816
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022,
FT ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 626..661
FT /evidence="ECO:0000250"
FT DISULFID 693..720
FT /evidence="ECO:0000250"
FT DISULFID 694..727
FT /evidence="ECO:0000250"
FT DISULFID 707..728
FT /evidence="ECO:0000250"
FT DISULFID 873..1513
FT /evidence="ECO:0000250"
FT DISULFID 1101..1158
FT /evidence="ECO:0000250"
FT DISULFID 1358..1489
FT /evidence="ECO:0000250"
FT DISULFID 1389..1458
FT /evidence="ECO:0000250"
FT DISULFID 1506..1511
FT /evidence="ECO:0000250"
FT DISULFID 1518..1590
FT /evidence="ECO:0000250"
FT DISULFID 1537..1661
FT /evidence="ECO:0000250"
FT DISULFID 1637..1646
FT /evidence="ECO:0000250"
FT CROSSLNK 1010..1013
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1128
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018708"
FT CONFLICT 137
FT /note="K -> Q (in Ref. 6; AAA37339)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="E -> Q (in Ref. 1; AAC42013)"
FT /evidence="ECO:0000305"
FT CONFLICT 1553
FT /note="E -> K (in Ref. 1; AAC42013 and 10; AAA37336)"
FT /evidence="ECO:0000305"
FT HELIX 1520..1523
FT /evidence="ECO:0007829|PDB:6XZU"
FT HELIX 1529..1535
FT /evidence="ECO:0007829|PDB:6XZU"
FT STRAND 1541..1554
FT /evidence="ECO:0007829|PDB:6XZU"
FT STRAND 1559..1570
FT /evidence="ECO:0007829|PDB:6XZU"
FT STRAND 1581..1586
FT /evidence="ECO:0007829|PDB:6XZU"
FT HELIX 1588..1590
FT /evidence="ECO:0007829|PDB:6XZU"
FT HELIX 1591..1594
FT /evidence="ECO:0007829|PDB:6XZU"
FT STRAND 1601..1607
FT /evidence="ECO:0007829|PDB:6XZU"
FT HELIX 1608..1610
FT /evidence="ECO:0007829|PDB:6XZU"
FT STRAND 1611..1613
FT /evidence="ECO:0007829|PDB:6XZU"
FT STRAND 1619..1621
FT /evidence="ECO:0007829|PDB:6XZU"
FT STRAND 1627..1631
FT /evidence="ECO:0007829|PDB:6XZU"
FT HELIX 1634..1637
FT /evidence="ECO:0007829|PDB:6XZU"
FT TURN 1640..1642
FT /evidence="ECO:0007829|PDB:6XZU"
FT HELIX 1643..1659
FT /evidence="ECO:0007829|PDB:6XZU"
SQ SEQUENCE 1663 AA; 186484 MW; 7E5546CC7C314779 CRC64;
MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD AQGDIPVTVT
VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD KEGHKYVTVV ANFGETVVEK
AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI FTVDNNLLPV GKTVVILIET PDGIPVKRDI
LSSNNQHGIL PLSWNIPELV NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT
ETFYYIDDPN GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD
AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV TSPYQIHFTK
TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL TQDDGVAKLS INTPNSRQPL
TITVRTKKDT LPESRQATKT MEAHPYSTMH NSNNYLHLSV SRMELKPGDN LNVNFHLRTD
PGHEAKIRYY TYLVMNKGKL LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA
SGQREVVADS VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG LQTEQRADLE
CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD IPMRYSCQRR ARLITQGENC
IKAFIDCCNH ITKLREQHRR DHVLGLARSE LEEDIIPEED IISRSHFPQS WLWTIEELKE
PEKNGISTKV MNIFLKDSIT TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV
RNEQVEIRAV LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI
VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE KLGQGGVQKV
DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL KHLIVTPAGC GEQNMIGMTP
TVIAVHYLDQ TEQWEKFGIE KRQEALELIK KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA
YVVKVFSLAA NLIAIDSHVL CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD
VSLTAFVLIA LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN
KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP PVVRWLNEQR
YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL PSRSSATTFR LLWENGNLLR
SEETKQNEAF SLTAKGKGRG TLSVVAVYHA KLKSKVTCKK FDLRVSIRPA PETAKKPEEA
KNTMFLEICT KYLGDVDATM SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN
KNTLIIYLEK ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG
MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT NIELLDDFDE
YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK KYLMWGLSSD LWGEKPNTSY
IIGKDTWVEH WPEAEECQDQ KYQKQCEELG AFTESMVVYG CPN
