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   27-MAR-2024, entry version 220.
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,
RC   Pancreas, 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; 11.
DR   ComplexPortal; CPX-5893; Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb.
DR   ComplexPortal; CPX-988; Complement C3b complex.
DR   IntAct; P01027; 5.
DR   MINT; P01027; -.
DR   STRING; 10090.ENSMUSP00000024988; -.
DR   MEROPS; I39.950; -.
DR   GlyCosmos; P01027; 2 sites, No reported glycans.
DR   GlyGen; P01027; 3 sites, 1 O-linked glycan (1 site).
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; 10090-ENSMUSP00000024988; -.
DR   PeptideAtlas; P01027; -.
DR   ProteomicsDB; 283596; -. [P01027-1]
DR   ProteomicsDB; 283597; -. [P01027-2]
DR   Pumba; P01027; -.
DR   ABCD; P01027; 3 sequenced antibodies.
DR   Antibodypedia; 692; 2194 antibodies from 44 providers.
DR   DNASU; 12266; -.
DR   Ensembl; ENSMUST00000024988.15; ENSMUSP00000024988.9; ENSMUSG00000024164.16. [P01027-1]
DR   GeneID; 12266; -.
DR   KEGG; mmu:12266; -.
DR   UCSC; uc008deg.2; mouse. [P01027-1]
DR   AGR; MGI:88227; -.
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; 4033541at2759; -.
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 64 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 167 other cell types or tissues.
DR   ExpressionAtlas; P01027; baseline and differential.
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:0032991; C:protein-containing complex; IDA:UniProtKB.
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: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:0002430; P:complement receptor mediated signaling pathway; IMP:ARUK-UCL.
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: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: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:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
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: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; cd02896; complement_C3_C4_C5; 1.
DR   CDD; cd03583; NTR_complement_C3; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 2.60.120.1540; -; 1.
DR   Gene3D; 2.60.40.1930; -; 3.
DR   Gene3D; 2.60.40.1940; -; 1.
DR   Gene3D; 6.20.50.160; -; 1.
DR   Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR   Gene3D; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR   InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
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; IPR049466; C3_CUB1.
DR   InterPro; IPR048848; C3_CUB2.
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; COMPLEMENT C3; 1.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 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; PF21406; C3_CUB1; 1.
DR   Pfam; PF21308; C3_CUB2; 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   SFLD; SFLDG01179; Complement_C3/C4_Like; 1.
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   SMART; SM01419; Thiol-ester_cl; 1.
DR   SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR   SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   SUPFAM; SSF50242; TIMP-like; 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.
DR   Genevisible; P01027; MM.
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
//