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Entry version 183 (12 Aug 2020)
Sequence version 3 (01 Aug 1990)
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Protein

Complement C3

Gene

C3

Organism
Rattus norvegicus (Rat)
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.1 Publication
Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. In chronic inflammation, acts as a chemoattractant for neutrophils (PubMed:8352775).1 Publication
Acts as a chemoattractant for neutrophils in chronic inflammation.1 Publication
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 (By similarity).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>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

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 processChemotaxis, Complement 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-RNO-173736, Alternative complement activation
R-RNO-174577, Activation of C3 and C5
R-RNO-198933, Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-RNO-375276, Peptide ligand-binding receptors
R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-RNO-418594, G alpha (i) signalling events
R-RNO-6798695, Neutrophil degranulation
R-RNO-8957275, Post-translational protein phosphorylation
R-RNO-9660826, Purinergic signaling in leishmaniasis infection
R-RNO-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
Recommended name:
Complement C3
Cleaved into the following 12 chains:
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2232, 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 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 – 24Add 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_000000593725 – 1663Complement C3Add BLAST1639
ChainiPRO_000000593825 – 666Complement C3 beta chainAdd BLAST642
ChainiPRO_0000395292568 – 666C3-beta-cAdd BLAST99
ChainiPRO_0000005939671 – 1663Complement C3 alpha chainAdd BLAST993
ChainiPRO_0000005940671 – 748C3a anaphylatoxinAdd BLAST78
ChainiPRO_0000419937671 – 747Acylation stimulating proteinBy similarityAdd BLAST77
ChainiPRO_0000005941749 – 1663Complement C3b alpha' chainAdd BLAST915
ChainiPRO_0000273950749 – 959Complement C3c alpha' chain fragment 1Add BLAST211
ChainiPRO_0000273951960 – 1303Complement C3dg fragmentBy similarityAdd BLAST344
ChainiPRO_0000273952960 – 1001Complement C3g fragmentBy similarityAdd BLAST42
ChainiPRO_00002739531002 – 1303Complement C3d fragmentBy similarityAdd 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_00002739541304 – 1320Complement C3f fragmentBy similarityAdd BLAST17
ChainiPRO_00002739551321 – 1663Complement C3c alpha' chain fragment 2By similarityAdd 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
Modified residuei297PhosphoserineBy similarity1
Modified residuei303PhosphoserineBy 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 bondi558 ↔ 816Interchain (between beta and alpha chains)PROSITE-ProRule annotation
Disulfide bondi626 ↔ 661By similarity
Modified residuei671PhosphoserineCombined sources1
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...) asparagineCurated1
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...) asparagineCurated1

<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 (By similarity).By similarity
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
Sitei959 – 960Cleavage; by factor ISequence analysis2
Sitei1303 – 1304Cleavage; by factor IBy similarity2
Sitei1320 – 1321Cleavage; by factor IBy similarity2

Keywords - PTMi

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

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P01026

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

More...
PaxDbi
P01026

PRoteomics IDEntifications database

More...
PRIDEi
P01026

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P01026

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P01026, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P01026

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

More...
PhosphoSitePlusi
P01026

<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 binding to 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
246419, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000066885

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

Secondary structure

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

3D structure databases

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

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SMRi
P01026

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P01026

<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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P01026

KEGG Orthology (KO)

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KOi
K03990

Database of Orthologous Groups

More...
OrthoDBi
23785at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P01026

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

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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

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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

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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P01026-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGPTSGSQLL VLLLLLASSL LALGSPMYSI ITPNVLRLES EETFILEAHD
60 70 80 90 100
AQGDVPVTVT VQDFLKKQVL TSEKTVLTGA TGHLNRVFIK IPASKEFNAD
110 120 130 140 150
KGHKYVTVVA NFGATVVEKA VLVSFQSGYL FIQTDKTIYT PGSTVFYRIF
160 170 180 190 200
TVDNNLLPVG KTVVIVIETP DGVPIKRDIL SSHNQYGILP LSWNIPELVN
210 220 230 240 250
MGQWKIRAFY EHAPKQTFSA EFEVKEYVLP SFEVLVEPTE KFYYIHGPKG
260 270 280 290 300
LEVSITARFL YGKNVDGTAF VIFGVQDEDK KISLALSLTR VLIEDGSGEA
310 320 330 340 350
VLSRKVLMDG VRPSSPEALV GKSLYVSVTV ILHSGSDMVE AERSGIPIVT
360 370 380 390 400
SPYQIHFTKT PKFFKPAMPF DLMVFVTNPD GSPARRVPVV TQGSDAQALT
410 420 430 440 450
QDDGVAKLSV NTPNNRQPLT ITVSTKKEGI PDARQATRTM QAQPYSTMHN
460 470 480 490 500
SNNYLHLSVS RVELKPGDNL NVNFHLRTDA GQEAKIRYYT YLVMNKGKLL
510 520 530 540 550
KAGRQVREPG QDLVVLSLPI TPEFIPSFRL VAYYTLIGAN GQREVVADSV
560 570 580 590 600
WVDVKDSCVG TLVVKGDPRD NRQPAPGHQT TLRIEGNQGA RVGLVAVDKG
610 620 630 640 650
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLTFKTNQG
660 670 680 690 700
LQTDQREDPE CAKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD
710 720 730 740 750
IPMPYSCQRR ARLITQGESC LKAFMDCCNY ITKLREQHRR DHVLGLARSD
760 770 780 790 800
VDEDIIPEED IISRSHFPES WLWTIEELKE PEKNGISTKV MNIFLKDSIT
810 820 830 840 850
TWEILAVSLS DKKGICVADP YEITVMQDFF IDLRLPYSVV RNEQVEIRAV
860 870 880 890 900
LFNYREQEKL KVRVELLHNP AFCSMATAKK RYYQTIEIPP KSSVAVPYVI
910 920 930 940 950
VPLKIGLQEV EVKAAVFNHF ISDGVKKILK VVPEGMRVNK TVAVRTLDPE
960 970 980 990 1000
HLNQGGVQRE DVNAADLSDQ VPDTDSETRI LLQGTPVAQM AEDAVDGERL
1010 1020 1030 1040 1050
KHLIVTPSGC GEQNMIGMTP TVIAVHYLDQ TEQWEKFGLE KRQEALELIK
1060 1070 1080 1090 1100
KGYTQQLAFK QPISAYAAFN NRPPSTWLTA MWSRSFSLAA NLIAIDSQVL
1110 1120 1130 1140 1150
CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNTKEAD VSLTAFVLIA
1160 1170 1180 1190 1200
LQEARDICEG QVNSLPGSIN KAGEYLEASY LNLQRPYTVA IAGYALALMN
1210 1220 1230 1240 1250
KLEEPYLTKF LNTAKDRNRW EEPGQQLYNV EATSYALLAL LLLKDFDSVP
1260 1270 1280 1290 1300
PVVRWLNDER YYGGGYGSTQ ATFMVFQALA QYRADVPDHK DLNMDVSLHL
1310 1320 1330 1340 1350
PSRSSPTVFR LLWESGSLLR SEETKQNEGF SLTAKGKGQG TLSVVTVYHA
1360 1370 1380 1390 1400
KVKGKTTCKK FDLRVTIKPA PETAKKPQDA KSSMILDICT RYLGDVDATM
1410 1420 1430 1440 1450
SILDISMMTG FIPDTNDLEL LSSGVDRYIS KYEMDKAFSN KNTLIIYLEK
1460 1470 1480 1490 1500
ISHSEEDCLS FKVHQFFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG
1510 1520 1530 1540 1550
MLSKLCHNEM CRCAEENCFM HQSQDQVSLN ERLDKACEPG VDYVYKTKLT
1560 1570 1580 1590 1600
TIELSDDFDE YIMTIEQVIK SGSDEVQAGQ ERRFISHVKC RNALKLQKGK
1610 1620 1630 1640 1650
QYLMWGLSSD LWGEKPNTSY IIGKDTWVEH WPEAEERQDQ KNQKQCEDLG
1660
AFTETMVVFG CPN
Length:1,663
Mass (Da):186,460
Last modified:August 1, 1990 - 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:i2F87CCB143CDD4BC
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
M0RBF1M0RBF1_RAT
C3-beta-c
C3 rCG_45082
1,663Annotation 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>
M0RBJ7M0RBJ7_RAT
C3-beta-c
C3
1,662Annotation score:

Annotation score:3 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 conflicti704P → K in AAG00532 (Ref. 4) Curated1
Sequence conflicti721 – 722LK → KL AA sequence (PubMed:309768).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X52477 mRNA Translation: CAA36716.1
AF286158 mRNA Translation: AAG00532.1
M29866 mRNA Translation: AAA40837.1

Protein sequence database of the Protein Information Resource

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PIRi
S15764, C3RT

NCBI Reference Sequences

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RefSeqi
NP_058690.2, NM_016994.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
24232

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:24232

<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
X52477 mRNA Translation: CAA36716.1
AF286158 mRNA Translation: AAG00532.1
M29866 mRNA Translation: AAA40837.1
PIRiS15764, C3RT
RefSeqiNP_058690.2, NM_016994.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QQFX-ray1.45A1010-1286[»]
1QSJX-ray1.90A/B/C/D1010-1286[»]
SMRiP01026
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi246419, 3 interactors
STRINGi10116.ENSRNOP00000066885

Protein family/group databases

MEROPSiI39.950

PTM databases

CarbonylDBiP01026
GlyGeniP01026, 2 sites
iPTMnetiP01026
PhosphoSitePlusiP01026

Proteomic databases

jPOSTiP01026
PaxDbiP01026
PRIDEiP01026

Genome annotation databases

GeneIDi24232
KEGGirno:24232

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
718
RGDi2232, C3

Phylogenomic databases

eggNOGiKOG1366, Eukaryota
InParanoidiP01026
KOiK03990
OrthoDBi23785at2759
PhylomeDBiP01026

Enzyme and pathway databases

ReactomeiR-RNO-173736, Alternative complement activation
R-RNO-174577, Activation of C3 and C5
R-RNO-198933, Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-RNO-375276, Peptide ligand-binding receptors
R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-RNO-418594, G alpha (i) signalling events
R-RNO-6798695, Neutrophil degranulation
R-RNO-8957275, Post-translational protein phosphorylation
R-RNO-9660826, Purinergic signaling in leishmaniasis infection
R-RNO-977606, Regulation of Complement cascade

Miscellaneous databases

EvolutionaryTraceiP01026

Protein Ontology

More...
PROi
PR:P01026

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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_RAT
<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: P01026
Secondary accession number(s): Q9ET19, Q9QV57, Q9QV58
<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: August 1, 1990
Last modified: August 12, 2020
This is version 183 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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