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UniProtKB - P01027 (CO3_MOUSE)

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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; 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

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P01027

MaxQB - The MaxQuant DataBase

More...MaxQBi		P01027

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

More...PaxDbi		P01027

PeptideAtlas

More...PeptideAtlasi		P01027

PRoteomics IDEntifications database

More...PRIDEi		P01027

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P01027

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

More...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

CleanEx database of gene expression profiles

More...CleanExi		MM_C3

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P01027 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		198418, 2 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-988 Complement C3b complex

Protein interaction database and analysis system

More...IntActi		P01027, 7 interactors

Molecular INTeraction database

More...MINTi		P01027

STRING: functional protein association networks

More...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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P01027

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

More...SMRi		P01027

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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

More...eggNOGi		KOG1366 Eukaryota
ENOG410XRED LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154063

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000286028

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG005110

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01027

KEGG Orthology (KO)

More...KOi		K03990

Identification of Orthologs from Complete Genome Data

More...OMAi		QDGEQRI

Database of Orthologous Groups

More...OrthoDBi		23785at2759

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
IPR035711 Complement_C3-like
IPR013783 Ig-like_fold
IPR001599 Macroglobln_a2
IPR019742 MacrogloblnA2_CS
IPR002890 MG2
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
PF01835 MG2, 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>.<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:2 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:2 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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<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

More...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

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

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.19131

Genome annotation databases

Ensembl eukaryotic genome annotation project

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

Database of genes from NCBI RefSeq genomes

More...GeneIDi		12266

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:12266

UCSC genome browser

More...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]
UniGeneiMm.19131

3D structure databases

ProteinModelPortaliP01027
SMRiP01027
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198418, 2 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

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
HOVERGENiHBG005110
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
CleanExiMM_C3
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
IPR035711 Complement_C3-like
IPR013783 Ig-like_fold
IPR001599 Macroglobln_a2
IPR019742 MacrogloblnA2_CS
IPR002890 MG2
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
PF01835 MG2, 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: January 16, 2019
This is version 191 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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