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Entry version 237 (03 Jul 2019)
Sequence version 2 (12 Dec 2006)
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Protein

Complement C3

Gene

C3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.
Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.By similarity
C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation.By similarity
Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2 (PubMed:8376604, PubMed:2909530, PubMed:9059512, PubMed:10432298, PubMed:15833747, PubMed:16333141, PubMed:19615750).7 Publications

Caution

An article reported the interaction surface between C3 and CR2 (PubMed:11387479). According to a another paper, it is however an artifact and can be ascribed to the presence of zinc acetate in the buffer (PubMed:21527715).2 Publications
The difference between allele C3S (C3 slow) and allele C3F (C3 fast) was reported to be caused by a an Asn at position 1216 instead of an Asp (PubMed:2473125). The paper was however retracted (PubMed:2584723).2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processComplement alternate pathway, Complement pathway, Fatty acid metabolism, Immunity, Inflammatory response, Innate immunity, Lipid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.4.21.47 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-173736 Alternative complement activation
R-HSA-174577 Activation of C3 and C5
R-HSA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-HSA-375276 Peptide ligand-binding receptors
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-418594 G alpha (i) signalling events
R-HSA-6798695 Neutrophil degranulation
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-977606 Regulation of Complement cascade

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P01024

SIGNOR Signaling Network Open Resource

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SIGNORi
P01024

Protein family/group databases

MEROPS protease database

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MEROPSi
I39.950

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Complement C3
Alternative name(s):
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1
Cleaved into the following 12 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:C3
Synonyms:CPAMD1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:1318 C3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
120700 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P01024

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Complement component 3 deficiency (C3D)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare defect of the complement classical pathway. Patients develop recurrent, severe, pyogenic infections because of ineffective opsonization of pathogens. Some patients may also develop autoimmune disorders, such as arthralgia and vasculitic rashes, lupus-like syndrome and membranoproliferative glomerulonephritis.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_001985549D → N in C3D; impairs secretion; variant confirmed at protein level. 2 PublicationsCorresponds to variant dbSNP:rs1449441916Ensembl.1
Macular degeneration, age-related, 9 (ARMD9)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070941155K → Q in ARMD9; results in resistance to proteolytic inactivation by CFH and CFI. 1 PublicationCorresponds to variant dbSNP:rs147859257EnsemblClinVar.1
Hemolytic uremic syndrome atypical 5 (AHUS5)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
Disease descriptionAn atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063213592R → Q in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant dbSNP:rs121909583EnsemblClinVar.1
Natural variantiVAR_063214592R → W in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant dbSNP:rs771353792Ensembl.1
Natural variantiVAR_063654603F → V in AHUS5. 1 Publication1
Natural variantiVAR_063215735R → W in AHUS5. 1 PublicationCorresponds to variant dbSNP:rs117793540EnsemblClinVar.1
Natural variantiVAR_0636551042R → L in AHUS5. 1 Publication1
Natural variantiVAR_0632161094A → V in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant dbSNP:rs121909584EnsemblClinVar.1
Natural variantiVAR_0632171115D → N in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant dbSNP:rs121909585EnsemblClinVar.1
Natural variantiVAR_0632181158C → W in AHUS5. 1 Publication1
Natural variantiVAR_0632191161Q → K in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication1
Natural variantiVAR_0632201464H → D in AHUS5. 1 Publication1
Increased levels of C3 and its cleavage product ASP, are associated with obesity, diabetes and coronary heart disease. Short-term endurance training reduces baseline ASP levels and subsequently fat storage.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1029D → A: Minor effect on binding of C3d to CR2. 2 Publications1
Mutagenesisi1030E → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1032E → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1035E → A: No effect on binding of C3d to CR2. 1 Publication1
Mutagenesisi1042R → M: Impaired binding of C3d to CR2. 1 Publication1
Mutagenesisi1108 – 1109IL → RR: Impaired binding of C3d to CR2; when associated with A-1163. 1 Publication2
Mutagenesisi1110E → A: No effect on binding of C3d to CR2. 1 Publication1
Mutagenesisi1115D → A: No effect on binding of C3d to CR2. 1 Publication1
Mutagenesisi1121D → A: No effect on binding of C3d to CR2. 1 Publication1
Mutagenesisi1140D → A: No effect on binding of C3d to CR2. 2 Publications1
Mutagenesisi1153E → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1156D → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1159E → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1160E → A: Minor effect on binding of C3d to CR2. 2 Publications1
Mutagenesisi1163N → A: No effect on binding of C3d to CR2. Impaired binding of C3d to CR2; when associated with 1108-R-R-1109. 3 Publications1
Mutagenesisi1163N → R: Impaired binding of C3d to CR2. 3 Publications1
Mutagenesisi1284K → A: Impaired binding of C3d to CR2. 1 Publication1

Keywords - Diseasei

Age-related macular degeneration, Disease mutation, Hemolytic uremic syndrome

Organism-specific databases

DisGeNET

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DisGeNETi
718

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
C3

MalaCards human disease database

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MalaCardsi
C3
MIMi611378 phenotype
612925 phenotype
613779 phenotype

Open Targets

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OpenTargetsi
ENSG00000125730

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
93575 Atypical hemolytic-uremic syndrome with C3 anomaly
280133 Complement component 3 deficiency
279 NON RARE IN EUROPE: Age-related macular degeneration

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA25897

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4917

Drug and drug target database

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DrugBanki
DB00028 Immune Globulin Human
DB01915 S-Hydroxycysteine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
C3

Domain mapping of disease mutations (DMDM)

More...
DMDMi
119370332

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 221 PublicationAdd BLAST22
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000590723 – 1663Complement C3Add BLAST1641
ChainiPRO_000000590823 – 667Complement C3 beta chainAdd BLAST645
ChainiPRO_0000430430569 – 667C3-beta-cBy similarityAdd BLAST99
ChainiPRO_0000005909672 – 1663Complement C3 alpha chainAdd BLAST992
ChainiPRO_0000005910672 – 748C3a anaphylatoxinAdd BLAST77
ChainiPRO_0000419935672 – 747Acylation stimulating proteinAdd BLAST76
ChainiPRO_0000005911749 – 1663Complement C3b alpha' chainAdd BLAST915
ChainiPRO_0000005912749 – 954Complement C3c alpha' chain fragment 1Add BLAST206
ChainiPRO_0000005913955 – 1303Complement C3dg fragmentAdd BLAST349
ChainiPRO_0000005914955 – 1001Complement C3g fragmentAdd BLAST47
ChainiPRO_00000059151002 – 1303Complement C3d fragmentAdd BLAST302
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_00000059161304 – 1320Complement C3f fragment1 PublicationAdd BLAST17
ChainiPRO_00002739481321 – 1663Complement C3c alpha' chain fragment 2Add BLAST343

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei38Phosphoserine; by FAM20C1 Publication1
Modified residuei70Phosphoserine; by FAM20C1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi85N-linked (GlcNAc...) asparagine7 Publications1
Modified residuei297Phosphoserine; by FAM20C1 Publication1
Modified residuei303Phosphoserine; by FAM20C1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi559 ↔ 816Interchain (between beta and alpha chains)
Disulfide bondi627 ↔ 662
Modified residuei672Phosphoserine; by FAM20C1 Publication1
Disulfide bondi693 ↔ 7201 Publication
Disulfide bondi694 ↔ 727
Disulfide bondi707 ↔ 728
Disulfide bondi873 ↔ 1513
Glycosylationi939N-linked (GlcNAc...) asparagine3 Publications1
Modified residuei968Phosphoserine; by FAM20C1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)
Disulfide bondi1101 ↔ 1158
Modified residuei1321Phosphoserine; by FAM20C1 Publication1
Disulfide bondi1358 ↔ 1489
Disulfide bondi1389 ↔ 1458
Disulfide bondi1506 ↔ 1511
Disulfide bondi1518 ↔ 1590
Disulfide bondi1537 ↔ 1661
Modified residuei1573Phosphoserine; by FAM20C1 Publication1
Glycosylationi1617N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi1637 ↔ 1646

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by insulin and dietary chylomicrons.
(Microbial infection) C3 is cleaved by Staphylococcus aureus aureolysin; this cleavage renders C3a and C3b inactive. C3b is rapidly degraded by host factors CFH and CFI preventing its deposition on the bacterial surface while C3a is further inactivated by aureolysin.1 Publication
Phosphorylated by FAM20C in the extracellular medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei747 – 748Cleavage; by carboxypeptidases2
Sitei748 – 749Cleavage; by C3 convertase2
Sitei954 – 955Cleavage; by factor ISequence analysis2
Sitei1303 – 1304Cleavage; by factor I2
Sitei1320 – 1321Cleavage; by factor I2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Thioester bond

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P01024

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P01024

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P01024

PeptideAtlas

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PeptideAtlasi
P01024

PRoteomics IDEntifications database

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PRIDEi
P01024

ProteomicsDB human proteome resource

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ProteomicsDBi
51308

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P01024

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P01024

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P01024

GlyConnect protein glycosylation platform

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GlyConnecti
110

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P01024

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P01024

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P01024

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P01024

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Plasma. The acylation stimulating protein (ASP) is expressed in adipocytes and released into the plasma during both the fasting and postprandial periods.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000125730 Expressed in 228 organ(s), highest expression level in parietal pleura

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P01024 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P01024 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004209
HPA003563
HPA020432

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). C3b interacts with CR1 (via Sushi 8 and Sushi 9 domains) (PubMed:8175757, PubMed:2972794). C3b interacts with CFH (PubMed:21285368). C3d interacts with CFH (PubMed:21285368, PubMed:21317894). C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). During pregnancy, C3dg exists as a complex (probably a 2:2:2 heterohexamer) with AGT and the proform of PRG2.

Interacts with VSIG4.

Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77.

14 Publications

(Microbial infection) C3b interacts with herpes simplex virus 1 (HHV-1) and herpes simplex virus 2 (HHV-2) envelope glycoprotein C; this interaction inhibits the activation of the complement system.

1 Publication

(Microbial infection)

Interacts with Staphylococcus aureus immunoglobulin-binding protein Sbi; this interaction prevents the association between C3dg and CR2.

3 Publications

(Microbial infection)

Interacts with Staphylococcus aureus protein Fib.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107179, 33 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-973 Complement C3b complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P01024

Database of interacting proteins

More...
DIPi
DIP-35180N

Protein interaction database and analysis system

More...
IntActi
P01024, 23 interactors

Molecular INTeraction database

More...
MINTi
P01024

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000245907

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P01024

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P01024

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P01024

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini693 – 728Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST36
Domaini1518 – 1661NTRPROSITE-ProRule annotationAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1424 – 1456Properdin-bindingAdd BLAST33

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1366 Eukaryota
ENOG410XRED LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154063

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000286028

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P01024

KEGG Orthology (KO)

More...
KOi
K03990

Identification of Orthologs from Complete Genome Data

More...
OMAi
QDGEQRI

Database of Orthologous Groups

More...
OrthoDBi
665362at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P01024

TreeFam database of animal gene trees

More...
TreeFami
TF313285

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00017 ANATO, 1 hit
cd03583 NTR_complement_C3, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 2 hits
2.60.40.690, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009048 A-macroglobulin_rcpt-bd
IPR036595 A-macroglobulin_rcpt-bd_sf
IPR011625 A2M_N_BRD
IPR011626 Alpha-macroglobulin_TED
IPR000020 Anaphylatoxin/fibulin
IPR018081 Anaphylatoxin_comp_syst
IPR001840 Anaphylatoxn_comp_syst_dom
IPR041425 C3/4/5_MG1
IPR035711 Complement_C3-like
IPR013783 Ig-like_fold
IPR001599 Macroglobln_a2
IPR019742 MacrogloblnA2_CS
IPR002890 MG2
IPR041555 MG3
IPR040839 MG4
IPR001134 Netrin_domain
IPR018933 Netrin_module_non-TIMP
IPR035815 NTR_complement_C3
IPR008930 Terpenoid_cyclase/PrenylTrfase
IPR008993 TIMP-like_OB-fold

The PANTHER Classification System

More...
PANTHERi
PTHR11412:SF81 PTHR11412:SF81, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00207 A2M, 1 hit
PF07703 A2M_BRD, 1 hit
PF07677 A2M_recep, 1 hit
PF01821 ANATO, 1 hit
PF17790 MG1, 1 hit
PF01835 MG2, 1 hit
PF17791 MG3, 1 hit
PF17789 MG4, 1 hit
PF01759 NTR, 1 hit
PF07678 TED_complement, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00004 ANAPHYLATOXN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01360 A2M, 1 hit
SM01359 A2M_N_2, 1 hit
SM01361 A2M_recep, 1 hit
SM00104 ANATO, 1 hit
SM00643 C345C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47686 SSF47686, 1 hit
SSF48239 SSF48239, 1 hit
SSF49410 SSF49410, 1 hit
SSF50242 SSF50242, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00477 ALPHA_2_MACROGLOBULIN, 1 hit
PS01177 ANAPHYLATOXIN_1, 1 hit
PS01178 ANAPHYLATOXIN_2, 1 hit
PS50189 NTR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P01024-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGPTSGPSLL LLLLTHLPLA LGSPMYSIIT PNILRLESEE TMVLEAHDAQ
60 70 80 90 100
GDVPVTVTVH DFPGKKLVLS SEKTVLTPAT NHMGNVTFTI PANREFKSEK
110 120 130 140 150
GRNKFVTVQA TFGTQVVEKV VLVSLQSGYL FIQTDKTIYT PGSTVLYRIF
160 170 180 190 200
TVNHKLLPVG RTVMVNIENP EGIPVKQDSL SSQNQLGVLP LSWDIPELVN
210 220 230 240 250
MGQWKIRAYY ENSPQQVFST EFEVKEYVLP SFEVIVEPTE KFYYIYNEKG
260 270 280 290 300
LEVTITARFL YGKKVEGTAF VIFGIQDGEQ RISLPESLKR IPIEDGSGEV
310 320 330 340 350
VLSRKVLLDG VQNPRAEDLV GKSLYVSATV ILHSGSDMVQ AERSGIPIVT
360 370 380 390 400
SPYQIHFTKT PKYFKPGMPF DLMVFVTNPD GSPAYRVPVA VQGEDTVQSL
410 420 430 440 450
TQGDGVAKLS INTHPSQKPL SITVRTKKQE LSEAEQATRT MQALPYSTVG
460 470 480 490 500
NSNNYLHLSV LRTELRPGET LNVNFLLRMD RAHEAKIRYY TYLIMNKGRL
510 520 530 540 550
LKAGRQVREP GQDLVVLPLS ITTDFIPSFR LVAYYTLIGA SGQREVVADS
560 570 580 590 600
VWVDVKDSCV GSLVVKSGQS EDRQPVPGQQ MTLKIEGDHG ARVVLVAVDK
610 620 630 640 650
GVFVLNKKNK LTQSKIWDVV EKADIGCTPG SGKDYAGVFS DAGLTFTSSS
660 670 680 690 700
GQQTAQRAEL QCPQPAARRR RSVQLTEKRM DKVGKYPKEL RKCCEDGMRE
710 720 730 740 750
NPMRFSCQRR TRFISLGEAC KKVFLDCCNY ITELRRQHAR ASHLGLARSN
760 770 780 790 800
LDEDIIAEEN IVSRSEFPES WLWNVEDLKE PPKNGISTKL MNIFLKDSIT
810 820 830 840 850
TWEILAVSMS DKKGICVADP FEVTVMQDFF IDLRLPYSVV RNEQVEIRAV
860 870 880 890 900
LYNYRQNQEL KVRVELLHNP AFCSLATTKR RHQQTVTIPP KSSLSVPYVI
910 920 930 940 950
VPLKTGLQEV EVKAAVYHHF ISDGVRKSLK VVPEGIRMNK TVAVRTLDPE
960 970 980 990 1000
RLGREGVQKE DIPPADLSDQ VPDTESETRI LLQGTPVAQM TEDAVDAERL
1010 1020 1030 1040 1050
KHLIVTPSGC GEQNMIGMTP TVIAVHYLDE TEQWEKFGLE KRQGALELIK
1060 1070 1080 1090 1100
KGYTQQLAFR QPSSAFAAFV KRAPSTWLTA YVVKVFSLAV NLIAIDSQVL
1110 1120 1130 1140 1150
CGAVKWLILE KQKPDGVFQE DAPVIHQEMI GGLRNNNEKD MALTAFVLIS
1160 1170 1180 1190 1200
LQEAKDICEE QVNSLPGSIT KAGDFLEANY MNLQRSYTVA IAGYALAQMG
1210 1220 1230 1240 1250
RLKGPLLNKF LTTAKDKNRW EDPGKQLYNV EATSYALLAL LQLKDFDFVP
1260 1270 1280 1290 1300
PVVRWLNEQR YYGGGYGSTQ ATFMVFQALA QYQKDAPDHQ ELNLDVSLQL
1310 1320 1330 1340 1350
PSRSSKITHR IHWESASLLR SEETKENEGF TVTAEGKGQG TLSVVTMYHA
1360 1370 1380 1390 1400
KAKDQLTCNK FDLKVTIKPA PETEKRPQDA KNTMILEICT RYRGDQDATM
1410 1420 1430 1440 1450
SILDISMMTG FAPDTDDLKQ LANGVDRYIS KYELDKAFSD RNTLIIYLDK
1460 1470 1480 1490 1500
VSHSEDDCLA FKVHQYFNVE LIQPGAVKVY AYYNLEESCT RFYHPEKEDG
1510 1520 1530 1540 1550
KLNKLCRDEL CRCAEENCFI QKSDDKVTLE ERLDKACEPG VDYVYKTRLV
1560 1570 1580 1590 1600
KVQLSNDFDE YIMAIEQTIK SGSDEVQVGQ QRTFISPIKC REALKLEEKK
1610 1620 1630 1640 1650
HYLMWGLSSD FWGEKPNLSY IIGKDTWVEH WPEEDECQDE ENQKQCQDLG
1660
AFTESMVVFG CPN
Length:1,663
Mass (Da):187,148
Last modified:December 12, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i30C2832A9E75FFC4
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0QYC8M0QYC8_HUMAN
Complement C3
C3
192Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0R0Q9M0R0Q9_HUMAN
Complement C3
C3
101Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0QXZ3M0QXZ3_HUMAN
Complement C3
C3
100Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0R1Q1M0R1Q1_HUMAN
Complement C3
C3
103Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti681D → N AA sequence (PubMed:1238393).Curated1
Sequence conflicti700E → Q AA sequence (PubMed:1238393).Curated1
Sequence conflicti1026H → S AA sequence (PubMed:6175959).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

There are two alleles: C3S (C3 slow), the most common allele in all races and C3F (C3 fast), relatively frequent in Caucasians, less common in Black Americans, extremely rare in Orientals.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001983102R → G in allele C3F; associated with susceptibility to ARMD9; results in decreased binding affinity for regulator factor H; results in reduced sensitivity to cleavage by factor I. 3 PublicationsCorresponds to variant dbSNP:rs2230199EnsemblClinVar.1
Natural variantiVAR_070941155K → Q in ARMD9; results in resistance to proteolytic inactivation by CFH and CFI. 1 PublicationCorresponds to variant dbSNP:rs147859257EnsemblClinVar.1
Natural variantiVAR_001984314P → L3 PublicationsCorresponds to variant dbSNP:rs1047286EnsemblClinVar.1
Natural variantiVAR_020262469E → D. Corresponds to variant dbSNP:rs11569422EnsemblClinVar.1
Natural variantiVAR_001985549D → N in C3D; impairs secretion; variant confirmed at protein level. 2 PublicationsCorresponds to variant dbSNP:rs1449441916Ensembl.1
Natural variantiVAR_063213592R → Q in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant dbSNP:rs121909583EnsemblClinVar.1
Natural variantiVAR_063214592R → W in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant dbSNP:rs771353792Ensembl.1
Natural variantiVAR_063654603F → V in AHUS5. 1 Publication1
Natural variantiVAR_063215735R → W in AHUS5. 1 PublicationCorresponds to variant dbSNP:rs117793540EnsemblClinVar.1
Natural variantiVAR_019206863R → K1 PublicationCorresponds to variant dbSNP:rs11569472Ensembl.1
Natural variantiVAR_0636551042R → L in AHUS5. 1 Publication1
Natural variantiVAR_0632161094A → V in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant dbSNP:rs121909584EnsemblClinVar.1
Natural variantiVAR_0632171115D → N in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant dbSNP:rs121909585EnsemblClinVar.1
Natural variantiVAR_0632181158C → W in AHUS5. 1 Publication1
Natural variantiVAR_0632191161Q → K in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication1
Natural variantiVAR_0192071224G → D1 PublicationCorresponds to variant dbSNP:rs11569534EnsemblClinVar.1
Natural variantiVAR_0192081367I → T1 PublicationCorresponds to variant dbSNP:rs11569541Ensembl.1
Natural variantiVAR_0632201464H → D in AHUS5. 1 Publication1
Natural variantiVAR_0297921521Q → R. Corresponds to variant dbSNP:rs7256789Ensembl.1
Natural variantiVAR_0297931601H → N. Corresponds to variant dbSNP:rs1803225Ensembl.1
Natural variantiVAR_0293261619S → R. Corresponds to variant dbSNP:rs2230210EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K02765 mRNA Translation: AAA85332.1
AY513239 Genomic DNA Translation: AAR89906.1
CH471139 Genomic DNA Translation: EAW69071.1
BC150179 mRNA Translation: AAI50180.1
BC150200 mRNA Translation: AAI50201.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS32883.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A94065 C3HU

NCBI Reference Sequences

More...
RefSeqi
NP_000055.2, NM_000064.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000245907; ENSP00000245907; ENSG00000125730

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
718

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:718

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

C3base

C3 mutation db

Wikipedia

Complement C3 entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02765 mRNA Translation: AAA85332.1
AY513239 Genomic DNA Translation: AAR89906.1
CH471139 Genomic DNA Translation: EAW69071.1
BC150179 mRNA Translation: AAI50180.1
BC150200 mRNA Translation: AAI50201.1
CCDSiCCDS32883.1
PIRiA94065 C3HU
RefSeqiNP_000055.2, NM_000064.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C3DX-ray1.80A996-1287[»]
1GHQX-ray2.04A996-1300[»]
1W2SX-ray-A996-1299[»]
2A73X-ray3.30A23-665[»]
B673-1663[»]
2A74X-ray2.40A/D23-665[»]
B/E749-936[»]
C/F1321-1663[»]
2GOXX-ray2.20A/C996-1287[»]
2I07X-ray4.00A23-667[»]
B749-1663[»]
2ICEX-ray3.10A/D23-664[»]
B/E749-954[»]
C/F1321-1663[»]
2ICFX-ray4.10A23-664[»]
B749-1663[»]
2NOJX-ray2.70A/C/E/G996-1287[»]
2QKIX-ray2.40A/D23-665[»]
B/E749-936[»]
C/F1321-1663[»]
2WIIX-ray2.70A23-667[»]
B749-1663[»]
2WINX-ray3.90A/C/E/G23-667[»]
B/D/F/H749-1663[»]
2WY7X-ray1.70A996-1303[»]
2WY8X-ray1.70A996-1303[»]
2XQWX-ray2.31A/B996-1287[»]
2XWBX-ray3.49A/C23-664[»]
B/D752-1663[»]
2XWJX-ray4.00A/C/E/G23-667[»]
B/D/F/H749-1663[»]
3D5RX-ray2.10A/B996-1287[»]
3D5SX-ray2.30A/B996-1287[»]
3G6JX-ray3.10A/C23-666[»]
B/D749-1663[»]
3L3OX-ray3.40A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
3L5NX-ray7.54A23-667[»]
B749-1663[»]
3NMSX-ray4.10A23-667[»]
B749-954[»]
C1321-1663[»]
3OEDX-ray3.16A/B996-1303[»]
3OHXX-ray3.50A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
3OXUX-ray2.10A/B/C996-1303[»]
3RJ3X-ray2.35A/B/C996-1303[»]
3T4AX-ray3.40A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
4HW5X-ray2.25A/B672-748[»]
4HWJX-ray2.60A672-747[»]
4I6OX-ray2.14A672-748[»]
4M76X-ray2.80A994-1288[»]
4ONTX-ray2.15A/B/C996-1303[»]
4ZH1X-ray2.24A/B/C996-1303[»]
5FO7X-ray2.80A23-667[»]
B749-1663[»]
5FO8X-ray2.40A23-667[»]
B749-1663[»]
5FO9X-ray3.30A/D23-667[»]
B/E749-1663[»]
5FOAX-ray4.19A/C23-667[»]
B/D749-1663[»]
5FOBX-ray2.60A23-667[»]
B749-1663[»]
5M6WX-ray6.00A/G23-667[»]
B/H751-1663[»]
5NBQX-ray3.18A/B/C994-1287[»]
5O32X-ray4.21A/E23-667[»]
B/F749-1663[»]
5O35X-ray4.20A23-667[»]
B749-1663[»]
6EHGX-ray2.65A23-665[»]
B749-1663[»]
SMRiP01024
ModBaseiSearch...

Protein-protein interaction databases

BioGridi107179, 33 interactors
ComplexPortaliCPX-973 Complement C3b complex
CORUMiP01024
DIPiDIP-35180N
IntActiP01024, 23 interactors
MINTiP01024
STRINGi9606.ENSP00000245907

Chemistry databases

BindingDBiP01024
ChEMBLiCHEMBL4917
DrugBankiDB00028 Immune Globulin Human
DB01915 S-Hydroxycysteine

Protein family/group databases

MEROPSiI39.950

PTM databases

CarbonylDBiP01024
GlyConnecti110
iPTMnetiP01024
PhosphoSitePlusiP01024
UniCarbKBiP01024

Polymorphism and mutation databases

BioMutaiC3
DMDMi119370332

2D gel databases

DOSAC-COBS-2DPAGEiP01024
SWISS-2DPAGEiP01024

Proteomic databases

EPDiP01024
jPOSTiP01024
PaxDbiP01024
PeptideAtlasiP01024
PRIDEiP01024
ProteomicsDBi51308

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P01024
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245907; ENSP00000245907; ENSG00000125730
GeneIDi718
KEGGihsa:718

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
718
DisGeNETi718

GeneCards: human genes, protein and diseases

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GeneCardsi
C3
GeneReviewsiC3

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0020036
HGNCiHGNC:1318 C3
HPAiCAB004209
HPA003563
HPA020432
MalaCardsiC3
MIMi120700 gene
611378 phenotype
612925 phenotype
613779 phenotype
neXtProtiNX_P01024
OpenTargetsiENSG00000125730
Orphaneti93575 Atypical hemolytic-uremic syndrome with C3 anomaly
280133 Complement component 3 deficiency
279 NON RARE IN EUROPE: Age-related macular degeneration
PharmGKBiPA25897

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG1366 Eukaryota
ENOG410XRED LUCA
GeneTreeiENSGT00940000154063
HOGENOMiHOG000286028
InParanoidiP01024
KOiK03990
OMAiQDGEQRI
OrthoDBi665362at2759
PhylomeDBiP01024
TreeFamiTF313285

Enzyme and pathway databases

BRENDAi3.4.21.47 2681
ReactomeiR-HSA-173736 Alternative complement activation
R-HSA-174577 Activation of C3 and C5
R-HSA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-HSA-375276 Peptide ligand-binding receptors
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-418594 G alpha (i) signalling events
R-HSA-6798695 Neutrophil degranulation
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-977606 Regulation of Complement cascade
SABIO-RKiP01024
SIGNORiP01024

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
C3 human
EvolutionaryTraceiP01024

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Complement_component_3

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
718
PMAP-CutDBiP01024

Protein Ontology

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PROi
PR:P01024

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000125730 Expressed in 228 organ(s), highest expression level in parietal pleura
ExpressionAtlasiP01024 baseline and differential
GenevisibleiP01024 HS

Family and domain databases

CDDicd00017 ANATO, 1 hit
cd03583 NTR_complement_C3, 1 hit
Gene3Di2.60.40.10, 2 hits
2.60.40.690, 1 hit
InterProiView protein in InterPro
IPR009048 A-macroglobulin_rcpt-bd
IPR036595 A-macroglobulin_rcpt-bd_sf
IPR011625 A2M_N_BRD
IPR011626 Alpha-macroglobulin_TED
IPR000020 Anaphylatoxin/fibulin
IPR018081 Anaphylatoxin_comp_syst
IPR001840 Anaphylatoxn_comp_syst_dom
IPR041425 C3/4/5_MG1
IPR035711 Complement_C3-like
IPR013783 Ig-like_fold
IPR001599 Macroglobln_a2
IPR019742 MacrogloblnA2_CS
IPR002890 MG2
IPR041555 MG3
IPR040839 MG4
IPR001134 Netrin_domain
IPR018933 Netrin_module_non-TIMP
IPR035815 NTR_complement_C3
IPR008930 Terpenoid_cyclase/PrenylTrfase
IPR008993 TIMP-like_OB-fold
PANTHERiPTHR11412:SF81 PTHR11412:SF81, 1 hit
PfamiView protein in Pfam
PF00207 A2M, 1 hit
PF07703 A2M_BRD, 1 hit
PF07677 A2M_recep, 1 hit
PF01821 ANATO, 1 hit
PF17790 MG1, 1 hit
PF01835 MG2, 1 hit
PF17791 MG3, 1 hit
PF17789 MG4, 1 hit
PF01759 NTR, 1 hit
PF07678 TED_complement, 1 hit
PRINTSiPR00004 ANAPHYLATOXN
SMARTiView protein in SMART
SM01360 A2M, 1 hit
SM01359 A2M_N_2, 1 hit
SM01361 A2M_recep, 1 hit
SM00104 ANATO, 1 hit
SM00643 C345C, 1 hit
SUPFAMiSSF47686 SSF47686, 1 hit
SSF48239 SSF48239, 1 hit
SSF49410 SSF49410, 1 hit
SSF50242 SSF50242, 1 hit
PROSITEiView protein in PROSITE
PS00477 ALPHA_2_MACROGLOBULIN, 1 hit
PS01177 ANAPHYLATOXIN_1, 1 hit
PS01178 ANAPHYLATOXIN_2, 1 hit
PS50189 NTR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCO3_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P01024
Secondary accession number(s): A7E236
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 12, 2006
Last modified: July 3, 2019
This is version 237 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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