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UniProtKB - P01027 (CO3_MOUSE)

Entry version 207 (02 Jun 2021)
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

Acts as a chemoattractant for neutrophils in chronic inflammation.

By similarity

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.

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>Sitei1663Coordinates Mg2+ for interaction with Complement factor B Bb fragmentBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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
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

The CPTAC Assay portal

More...CPTACi		non-CPTAC-5595
non-CPTAC-5596

Encyclopedia of Proteome Dynamics

More...EPDi		P01027

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

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		283596 [P01027-1]
283597 [P01027-2]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P01027, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P01027

MetOSite database of methionine sulfoxide sites

More...MetOSitei		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

<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 uterine cervix and 217 other tissues

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%5Fsection">'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%5Fsection">'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). Forms the pro-C3-convertase enzyme complex by interacting with Complement factor B Bb fragment (Bb), which is then stabilized by binding CFP, allowing the complex to become active (By similarity). The interaction with Bb is dependent on Mg2+ (By similarity). 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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		198418, 10 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-5893, Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb
CPX-988, Complement C3b complex

Protein interaction database and analysis system

More...IntActi		P01027, 8 interactors

Molecular INTeraction database

More...MINTi		P01027

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000024988

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P01027, protein

<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

More...SMRi		P01027

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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%5Fand%5Fdomains%5Fsection">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>Regioni1634 – 1659Interaction with CFP/properdinBy similarityAdd BLAST26

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1366, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154063

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001634_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01027

Identification of Orthologs from Complete Genome Data

More...OMAi		QATNTMQ

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		2.40.50.120, 1 hit
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%5Flength">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>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
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

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]

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]

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
6XZUX-ray1.50B1517-1663[»]
SMRiP01027
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi198418, 10 interactors
ComplexPortaliCPX-5893, Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb
CPX-988, Complement C3b complex
IntActiP01027, 8 interactors
MINTiP01027
STRINGi10090.ENSMUSP00000024988

Protein family/group databases

MEROPSiI39.950

PTM databases

GlyGeniP01027, 2 sites
iPTMnetiP01027
MetOSiteiP01027
PhosphoSitePlusiP01027
SwissPalmiP01027

Proteomic databases

CPTACinon-CPTAC-5595
non-CPTAC-5596
EPDiP01027
jPOSTiP01027
MaxQBiP01027
PaxDbiP01027
PeptideAtlasiP01027
PRIDEiP01027
ProteomicsDBi283596 [P01027-1]
283597 [P01027-2]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P01027, 3 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		692, 1895 antibodies

The DNASU plasmid repository

More...DNASUi		12266

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
GeneTreeiENSGT00940000154063
HOGENOMiCLU_001634_4_0_1
InParanoidiP01027
OMAiQATNTMQ
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

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		12266, 1 hit in 47 CRISPR screens

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

More...ChiTaRSi		C3, mouse

Protein Ontology

More...PROi		PR:P01027
RNActiP01027, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000024164, Expressed in uterine cervix and 217 other tissues
ExpressionAtlasiP01027, baseline and differential
GenevisibleiP01027, MM

Family and domain databases

CDDicd00017, ANATO, 1 hit
cd03583, NTR_complement_C3, 1 hit
Gene3Di2.40.50.120, 1 hit
2.60.40.10, 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

MobiDB: a database of protein disorder and mobility annotations

More...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_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%5Fand%5Fisoforms">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: June 2, 2021
This is version 207 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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