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Entry version 193 (08 May 2019)
Sequence version 3 (27 Jul 2011)
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Protein

Complement C3

Gene

C3

Organism
Mus musculus (Mouse)
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. The short isoform has B-cell stimulatory activity.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.

<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

Reactome - a knowledgebase of biological pathways and processes

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

Protein family/group databases

MEROPS protease database

More...
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
<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 17

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:88227 C3

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Null mice displayed altered lipid metabolism and morphological changes in adipocyte distribution. There is reduced adipsin/CFD expression, increased number of smaller fat cells, decreased DGAT1 expression and activity, and less triglyceride storage capacity associated with delayed postprandial clearance. Mice on a high-fat diet exihibited no diet-induced up-regulation of adipsin/CFD expression nor adipocyte differentiation.1 Publication

<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 – 242 PublicationsAdd BLAST24
<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_000000591725 – 1663Complement C3Add BLAST1639
ChainiPRO_000000591825 – 666Complement C3 beta chainAdd BLAST642
ChainiPRO_0000430431569 – 666C3-beta-cBy similarityAdd BLAST98
ChainiPRO_0000005919671 – 1663Complement C3 alpha chainAdd BLAST993
ChainiPRO_0000005920671 – 748C3a anaphylatoxinAdd BLAST78
ChainiPRO_0000419936671 – 747Acylation stimulating proteinAdd BLAST77
ChainiPRO_0000005921749 – 1663Complement C3b alpha' chainAdd BLAST915
ChainiPRO_0000005922749 – 954Complement C3c alpha' chain fragment 1Add BLAST206
ChainiPRO_0000005923955 – 1303Complement C3dg fragmentAdd BLAST349
ChainiPRO_0000005924955 – 1001Complement C3g fragmentAdd BLAST47
ChainiPRO_00000059251002 – 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_00000059271304 – 1320Complement C3f fragmentAdd BLAST17
ChainiPRO_00002739491321 – 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 residuei40PhosphoserineBy similarity1
<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)PROSITE-ProRule annotation
Disulfide bondi626 ↔ 661By similarity
Modified residuei671PhosphoserineBy similarity1
Disulfide bondi693 ↔ 720By similarity
Disulfide bondi694 ↔ 727By similarity
Disulfide bondi707 ↔ 728By similarity
Disulfide bondi873 ↔ 1513By similarity
<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>Glycosylationi939N-linked (GlcNAc...) asparagine1
Modified residuei968PhosphoserineBy similarity1
<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)By similarity
Disulfide bondi1101 ↔ 1158By similarity
Modified residuei1321PhosphoserineBy similarity1
Disulfide bondi1358 ↔ 1489By similarity
Disulfide bondi1389 ↔ 1458By similarity
Disulfide bondi1506 ↔ 1511By similarity
Disulfide bondi1518 ↔ 1590By similarity
Disulfide bondi1537 ↔ 1661By similarity
Modified residuei1573PhosphoserineBy similarity1
Glycosylationi1617N-linked (GlcNAc...) asparagine1
Disulfide bondi1637 ↔ 1646By similarity

<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 dietary chylomicrons.
Phosphorylated by FAM20C in the extracellular medium.By similarity

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 carboxypeptidasesBy similarity2
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
P01027

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P01027

MaxQB - The MaxQuant DataBase

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MaxQBi
P01027

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

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PaxDbi
P01027

PeptideAtlas

More...
PeptideAtlasi
P01027

PRoteomics IDEntifications database

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PRIDEi
P01027

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P01027

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

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PhosphoSitePlusi
P01027

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P01027

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P01027

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000024164 Expressed in 182 organ(s), highest expression level in uterine cervix

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P01027 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P01027 MM

<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). C3b interacts with CFH. C3d interacts with CFH. 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 with S.aureus immunoglobulin-binding protein sbi, this prevents interaction between C3dg and CR2. Interacts with S.aureus fib. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77.By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
198418, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-988 Complement C3b complex

Protein interaction database and analysis system

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IntActi
P01027, 7 interactors

Molecular INTeraction database

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MINTi
P01027

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000024988

<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

3D structure databases

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

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SMRi
P01027

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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-bindingBy similarityAdd BLAST33

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1366 Eukaryota
ENOG410XRED LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154063

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000286028

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P01027

KEGG Orthology (KO)

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KOi
K03990

Identification of Orthologs from Complete Genome Data

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OMAi
QDGEQRI

Database of Orthologous Groups

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OrthoDBi
23785at2759

TreeFam database of animal gene trees

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TreeFami
TF313285

Family and domain databases

Conserved Domains Database

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CDDi
cd00017 ANATO, 1 hit
cd03583 NTR_complement_C3, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 2 hits
2.60.40.690, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR11412:SF81 PTHR11412:SF81, 1 hit

Pfam protein domain database

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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

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PRINTSi
PR00004 ANAPHYLATOXN

Simple Modular Architecture Research Tool; a protein domain database

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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

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

PROSITE; a protein domain and family database

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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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform Long (identifier: P01027-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD
60 70 80 90 100
AQGDIPVTVT VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD
110 120 130 140 150
KEGHKYVTVV ANFGETVVEK AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI
160 170 180 190 200
FTVDNNLLPV GKTVVILIET PDGIPVKRDI LSSNNQHGIL PLSWNIPELV
210 220 230 240 250
NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT ETFYYIDDPN
260 270 280 290 300
GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD
310 320 330 340 350
AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV
360 370 380 390 400
TSPYQIHFTK TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL
410 420 430 440 450
TQDDGVAKLS INTPNSRQPL TITVRTKKDT LPESRQATKT MEAHPYSTMH
460 470 480 490 500
NSNNYLHLSV SRMELKPGDN LNVNFHLRTD PGHEAKIRYY TYLVMNKGKL
510 520 530 540 550
LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA SGQREVVADS
560 570 580 590 600
VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG
610 620 630 640 650
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG
660 670 680 690 700
LQTEQRADLE CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD
710 720 730 740 750
IPMRYSCQRR ARLITQGENC IKAFIDCCNH ITKLREQHRR DHVLGLARSE
760 770 780 790 800
LEEDIIPEED IISRSHFPQS WLWTIEELKE PEKNGISTKV MNIFLKDSIT
810 820 830 840 850
TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV RNEQVEIRAV
860 870 880 890 900
LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI
910 920 930 940 950
VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE
960 970 980 990 1000
KLGQGGVQKV DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL
1010 1020 1030 1040 1050
KHLIVTPAGC GEQNMIGMTP TVIAVHYLDQ TEQWEKFGIE KRQEALELIK
1060 1070 1080 1090 1100
KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA YVVKVFSLAA NLIAIDSHVL
1110 1120 1130 1140 1150
CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD VSLTAFVLIA
1160 1170 1180 1190 1200
LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN
1210 1220 1230 1240 1250
KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP
1260 1270 1280 1290 1300
PVVRWLNEQR YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL
1310 1320 1330 1340 1350
PSRSSATTFR LLWENGNLLR SEETKQNEAF SLTAKGKGRG TLSVVAVYHA
1360 1370 1380 1390 1400
KLKSKVTCKK FDLRVSIRPA PETAKKPEEA KNTMFLEICT KYLGDVDATM
1410 1420 1430 1440 1450
SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN KNTLIIYLEK
1460 1470 1480 1490 1500
ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG
1510 1520 1530 1540 1550
MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT
1560 1570 1580 1590 1600
NIELLDDFDE YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK
1610 1620 1630 1640 1650
KYLMWGLSSD LWGEKPNTSY IIGKDTWVEH WPEAEECQDQ KYQKQCEELG
1660
AFTESMVVYG CPN
Length:1,663
Mass (Da):186,484
Last modified:July 27, 2011 - v3
<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:i7E5546CC7C314779
GO
Isoform Short (identifier: P01027-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1128: Missing.

Show »
Length:535
Mass (Da):60,952
Checksum:i6F6187342DC868CD
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BKW9H3BKW9_MOUSE
Complement C3
C3
185Annotation 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>
H3BL60H3BL60_MOUSE
Complement C3
C3 mCG_140909
102Annotation 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 conflicti137K → Q in AAA37339 (PubMed:6356427).Curated1
Sequence conflicti858E → Q in AAC42013 (PubMed:6208565).Curated1
Sequence conflicti1553E → K in AAC42013 (PubMed:6208565).Curated1
Sequence conflicti1553E → K in AAA37336 (PubMed:6094532).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0187081 – 1128Missing in isoform Short. CuratedAdd BLAST1128

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K02782 mRNA Translation: AAC42013.1
BC043338 mRNA Translation: AAH43338.1
M35659 mRNA Translation: AAA37339.1
M33032 mRNA Translation: AAA37378.1
J00369, J00367 Genomic DNA Translation: AAA37336.1
Z37998 Genomic DNA Translation: CAA86099.2

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS37670.1 [P01027-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A92459 C3MS
I48284

NCBI Reference Sequences

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RefSeqi
NP_033908.2, NM_009778.3 [P01027-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164 [P01027-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
12266

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:12266

UCSC genome browser

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UCSCi
uc008deg.2 mouse [P01027-1]

Keywords - Coding sequence diversityi

Alternative initiation

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02782 mRNA Translation: AAC42013.1
BC043338 mRNA Translation: AAH43338.1
M35659 mRNA Translation: AAA37339.1
M33032 mRNA Translation: AAA37378.1
J00369, J00367 Genomic DNA Translation: AAA37336.1
Z37998 Genomic DNA Translation: CAA86099.2
CCDSiCCDS37670.1 [P01027-1]
PIRiA92459 C3MS
I48284
RefSeqiNP_033908.2, NM_009778.3 [P01027-1]

3D structure databases

SMRiP01027
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198418, 3 interactors
ComplexPortaliCPX-988 Complement C3b complex
IntActiP01027, 7 interactors
MINTiP01027
STRINGi10090.ENSMUSP00000024988

Protein family/group databases

MEROPSiI39.950

PTM databases

iPTMnetiP01027
PhosphoSitePlusiP01027
SwissPalmiP01027

Proteomic databases

EPDiP01027
jPOSTiP01027
MaxQBiP01027
PaxDbiP01027
PeptideAtlasiP01027
PRIDEiP01027

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164 [P01027-1]
GeneIDi12266
KEGGimmu:12266
UCSCiuc008deg.2 mouse [P01027-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
718
MGIiMGI:88227 C3

Phylogenomic databases

eggNOGiKOG1366 Eukaryota
ENOG410XRED LUCA
GeneTreeiENSGT00940000154063
HOGENOMiHOG000286028
InParanoidiP01027
KOiK03990
OMAiQDGEQRI
OrthoDBi23785at2759
TreeFamiTF313285

Enzyme and pathway databases

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

Miscellaneous databases

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

More...
ChiTaRSi
C3 mouse
PMAP-CutDBiP01027

Protein Ontology

More...
PROi
PR:P01027

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000024164 Expressed in 182 organ(s), highest expression level in uterine cervix
ExpressionAtlasiP01027 baseline and differential
GenevisibleiP01027 MM

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

More...
ProtoNeti
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_MOUSE
<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: P01027
Secondary accession number(s): Q61370, Q80XP1
<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: July 27, 2011
Last modified: May 8, 2019
This is version 193 of the entry and version 3 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

<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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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