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Protein

Complement C3

Gene

C3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
  • endopeptidase inhibitor activity Source: InterPro
  • receptor binding Source: ProtInc
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

  • complement activation Source: BHF-UCL
  • complement activation, alternative pathway Source: Reactome
  • complement activation, classical pathway Source: UniProtKB-KW
  • fatty acid metabolic process Source: UniProtKB-KW
  • G-protein coupled receptor signaling pathway Source: ProtInc
  • immune response Source: ProtInc
  • inflammatory response Source: UniProtKB-KW
  • positive regulation of activation of membrane attack complex Source: Ensembl
  • positive regulation of angiogenesis Source: Ensembl
  • positive regulation of apoptotic cell clearance Source: BHF-UCL
  • positive regulation of glucose transport Source: UniProtKB
  • positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  • positive regulation of lipid storage Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of type IIa hypersensitivity Source: Ensembl
  • positive regulation of vascular endothelial growth factor production Source: BHF-UCL
  • regulation of complement activation Source: Reactome
  • regulation of immune response Source: Reactome
  • regulation of triglyceride biosynthetic process Source: UniProtKB
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125730-MONOMER.
BRENDAi3.4.21.47. 2681.
ReactomeiR-HSA-173736. Alternative complement activation.
R-HSA-174577. Activation of C3 and C5.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-977606. Regulation of Complement cascade.

Protein family/group databases

MEROPSiI39.950.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C3
Alternative name(s):
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1
Cleaved into the following 12 chains:
Gene namesi
Name:C3
Synonyms:CPAMD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1318. C3.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Complement component 3 deficiency (C3D)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare defect of the complement classical pathway. Patients develop recurrent, severe, pyogenic infections because of ineffective opsonization of pathogens. Some patients may also develop autoimmune disorders, such as arthralgia and vasculitic rashes, lupus-like syndrome and membranoproliferative glomerulonephritis.
See also OMIM:613779
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001985549D → N in C3D; impairs secretion; variant confirmed at protein level. 2 Publications1
Macular degeneration, age-related, 9 (ARMD9)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
See also OMIM:611378
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001983102R → G in allele C3F; associated with susceptibility to ARMD9; results in decreased binding affinity for regulator factor H; results in reduced sensitivity to cleavage by factor I. 3 PublicationsCorresponds to variant rs2230199dbSNPEnsembl.1
Natural variantiVAR_070941155K → Q in ARMD9; results in resistance to proteolytic inactivation by CFH and CFI. 1 PublicationCorresponds to variant rs147859257dbSNPEnsembl.1
Hemolytic uremic syndrome atypical 5 (AHUS5)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
Disease descriptionAn atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease.
See also OMIM:612925
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063213592R → Q in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant rs121909583dbSNPEnsembl.1
Natural variantiVAR_063214592R → W in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant rs771353792dbSNPEnsembl.1
Natural variantiVAR_063654603F → V in AHUS5. 1 Publication1
Natural variantiVAR_063215735R → W in AHUS5. 1 PublicationCorresponds to variant rs117793540dbSNPEnsembl.1
Natural variantiVAR_0636551042R → L in AHUS5. 1 Publication1
Natural variantiVAR_0632161094A → V in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant rs121909584dbSNPEnsembl.1
Natural variantiVAR_0632171115D → N in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant rs121909585dbSNPEnsembl.1
Natural variantiVAR_0632181158C → W in AHUS5. 1 Publication1
Natural variantiVAR_0632191161Q → K in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication1
Natural variantiVAR_0632201464H → D in AHUS5. 1 Publication1

Increased levels of C3 and its cleavage product ASP, are associated with obesity, diabetes and coronary heart disease. Short-term endurance training reduces baseline ASP levels and subsequently fat storage.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1029D → A: Minor effect on binding of C3d to CR2. 2 Publications1
Mutagenesisi1030E → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1032E → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1035E → A: No effect on binding of C3d to CR2. 1 Publication1
Mutagenesisi1042R → M: Impaired binding of C3d to CR2. 1 Publication1
Mutagenesisi1108 – 1109IL → RR: Impaired binding of C3d to CR2; when associated with A-1163. 1 Publication2
Mutagenesisi1110E → A: No effect on binding of C3d to CR2. 1 Publication1
Mutagenesisi1115D → A: No effect on binding of C3d to CR2. 1 Publication1
Mutagenesisi1121D → A: No effect on binding of C3d to CR2. 1 Publication1
Mutagenesisi1140D → A: No effect on binding of C3d to CR2. 2 Publications1
Mutagenesisi1153E → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1156D → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1159E → A: Impaired binding of C3d to CR2. 2 Publications1
Mutagenesisi1160E → A: Minor effect on binding of C3d to CR2. 2 Publications1
Mutagenesisi1163N → A: No effect on binding of C3d to CR2. Impaired binding of C3d to CR2; when associated with 1108-R-R-1109. 3 Publications1
Mutagenesisi1163N → R: Impaired binding of C3d to CR2. 3 Publications1
Mutagenesisi1284K → A: Impaired binding of C3d to CR2. 1 Publication1

Keywords - Diseasei

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

Organism-specific databases

DisGeNETi718.
MalaCardsiC3.
MIMi611378. phenotype.
612925. phenotype.
613779. phenotype.
OpenTargetsiENSG00000125730.
Orphaneti279. Age-related macular degeneration.
93575. Atypical hemolytic-uremic syndrome with C3 anomaly.
280133. Complement component 3 deficiency.
PharmGKBiPA25897.

Chemistry databases

ChEMBLiCHEMBL4917.
DrugBankiDB00028. Intravenous Immunoglobulin.

Polymorphism and mutation databases

BioMutaiC3.
DMDMi119370332.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000000590723 – 1663Complement C3Add BLAST1641
ChainiPRO_000000590823 – 667Complement C3 beta chainAdd BLAST645
ChainiPRO_0000430430569 – 667C3-beta-cBy similarityAdd BLAST99
ChainiPRO_0000005909672 – 1663Complement C3 alpha chainAdd BLAST992
ChainiPRO_0000005910672 – 748C3a anaphylatoxinAdd BLAST77
ChainiPRO_0000419935672 – 747Acylation stimulating proteinAdd BLAST76
ChainiPRO_0000005911749 – 1663Complement C3b alpha' chainAdd BLAST915
ChainiPRO_0000005912749 – 954Complement C3c alpha' chain fragment 1Add BLAST206
ChainiPRO_0000005913955 – 1303Complement C3dg fragmentAdd BLAST349
ChainiPRO_0000005914955 – 1001Complement C3g fragmentAdd BLAST47
ChainiPRO_00000059151002 – 1303Complement C3d fragmentAdd BLAST302
PeptideiPRO_00000059161304 – 1320Complement C3f fragment1 PublicationAdd BLAST17
ChainiPRO_00002739481321 – 1663Complement C3c alpha' chain fragment 2Add BLAST343

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38Phosphoserine; by FAM20C1 Publication1
Modified residuei70Phosphoserine; by FAM20C1 Publication1
Glycosylationi85N-linked (GlcNAc...)7 Publications1
Modified residuei297Phosphoserine; by FAM20C1 Publication1
Modified residuei303Phosphoserine; by FAM20C1 Publication1
Disulfide bondi559 ↔ 816Interchain (between beta and alpha chains)
Disulfide bondi627 ↔ 662
Modified residuei672Phosphoserine; by FAM20C1 Publication1
Disulfide bondi693 ↔ 7201 Publication
Disulfide bondi694 ↔ 727
Disulfide bondi707 ↔ 728
Disulfide bondi873 ↔ 1513
Glycosylationi939N-linked (GlcNAc...)3 Publications1
Modified residuei968Phosphoserine; by FAM20C1 Publication1
Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)
Disulfide bondi1101 ↔ 1158
Modified residuei1321Phosphoserine; by FAM20C1 Publication1
Disulfide bondi1358 ↔ 1489
Disulfide bondi1389 ↔ 1458
Disulfide bondi1506 ↔ 1511
Disulfide bondi1518 ↔ 1590
Disulfide bondi1537 ↔ 1661
Modified residuei1573Phosphoserine; by FAM20C1 Publication1
Glycosylationi1617N-linked (GlcNAc...)1 Publication1
Disulfide bondi1637 ↔ 1646

Post-translational modificationi

C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by insulin and dietary chylomicrons.
Phosphorylated by FAM20C in the extracellular medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei747 – 748Cleavage; by carboxypeptidases2
Sitei748 – 749Cleavage; by C3 convertase2
Sitei954 – 955Cleavage; by factor ISequence analysis2
Sitei1303 – 1304Cleavage; by factor I2
Sitei1320 – 1321Cleavage; by factor I2

Keywords - PTMi

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

Proteomic databases

EPDiP01024.
PaxDbiP01024.
PeptideAtlasiP01024.
PRIDEiP01024.

2D gel databases

DOSAC-COBS-2DPAGEP01024.
SWISS-2DPAGEP01024.

PTM databases

iPTMnetiP01024.
PhosphoSitePlusiP01024.
UniCarbKBiP01024.

Miscellaneous databases

PMAP-CutDBP01024.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000125730.
CleanExiHS_C3.
ExpressionAtlasiP01024. baseline and differential.
GenevisibleiP01024. HS.

Organism-specific databases

HPAiCAB004209.
HPA003563.
HPA020432.

Interactioni

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). 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. C3b interacts with herpes simplex virus 1 (HHV-1) and herpes simplex virus 2 (HHV-2) envelope glycoprotein C; this interaction inhibits the activation of the complement system. 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 GRP77.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CFHP086032EBI-6863145,EBI-1223708
VSIG4Q9Y279-15EBI-905851,EBI-903144
VSIG4Q9Y279-22EBI-905851,EBI-903148

GO - Molecular functioni

  • C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
  • receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi107179. 28 interactors.
DIPiDIP-35180N.
IntActiP01024. 17 interactors.
MINTiMINT-5003988.
STRINGi9606.ENSP00000245907.

Chemistry databases

BindingDBiP01024.

Structurei

Secondary structure

11663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 29Combined sources5
Beta strandi31 – 34Combined sources4
Beta strandi36 – 41Combined sources6
Beta strandi43 – 47Combined sources5
Beta strandi53 – 64Combined sources12
Beta strandi67 – 69Combined sources3
Beta strandi73 – 76Combined sources4
Helixi78 – 80Combined sources3
Beta strandi87 – 89Combined sources3
Helixi94 – 97Combined sources4
Beta strandi105 – 112Combined sources8
Beta strandi115 – 123Combined sources9
Beta strandi129 – 135Combined sources7
Beta strandi137 – 139Combined sources3
Beta strandi144 – 152Combined sources9
Beta strandi162 – 168Combined sources7
Beta strandi174 – 176Combined sources3
Beta strandi179 – 181Combined sources3
Turni183 – 187Combined sources5
Beta strandi188 – 194Combined sources7
Beta strandi202 – 210Combined sources9
Beta strandi214 – 216Combined sources3
Beta strandi218 – 224Combined sources7
Beta strandi231 – 244Combined sources14
Beta strandi251 – 259Combined sources9
Beta strandi267 – 277Combined sources11
Beta strandi280 – 294Combined sources15
Beta strandi297 – 302Combined sources6
Helixi304 – 309Combined sources6
Beta strandi311 – 313Combined sources3
Helixi316 – 319Combined sources4
Beta strandi323 – 332Combined sources10
Beta strandi338 – 352Combined sources15
Beta strandi354 – 356Combined sources3
Beta strandi358 – 360Combined sources3
Beta strandi362 – 364Combined sources3
Beta strandi370 – 377Combined sources8
Beta strandi379 – 381Combined sources3
Beta strandi388 – 393Combined sources6
Helixi395 – 397Combined sources3
Beta strandi398 – 400Combined sources3
Beta strandi405 – 411Combined sources7
Beta strandi415 – 417Combined sources3
Beta strandi420 – 426Combined sources7
Turni429 – 431Combined sources3
Helixi433 – 435Combined sources3
Beta strandi439 – 445Combined sources7
Helixi449 – 451Combined sources3
Beta strandi455 – 459Combined sources5
Beta strandi470 – 478Combined sources9
Turni481 – 483Combined sources3
Helixi484 – 486Combined sources3
Beta strandi489 – 496Combined sources8
Beta strandi499 – 507Combined sources9
Beta strandi513 – 520Combined sources8
Helixi523 – 525Combined sources3
Beta strandi527 – 538Combined sources12
Beta strandi540 – 542Combined sources3
Beta strandi544 – 554Combined sources11
Beta strandi563 – 567Combined sources5
Turni568 – 570Combined sources3
Beta strandi571 – 573Combined sources3
Beta strandi580 – 588Combined sources9
Beta strandi592 – 599Combined sources8
Helixi602 – 605Combined sources4
Helixi613 – 622Combined sources10
Beta strandi628 – 630Combined sources3
Helixi635 – 641Combined sources7
Beta strandi644 – 648Combined sources5
Helixi675 – 684Combined sources10
Helixi688 – 697Combined sources10
Helixi707 – 710Combined sources4
Turni712 – 714Combined sources3
Helixi718 – 743Combined sources26
Beta strandi753 – 755Combined sources3
Helixi758 – 760Combined sources3
Beta strandi769 – 771Combined sources3
Beta strandi775 – 777Combined sources3
Beta strandi786 – 794Combined sources9
Beta strandi800 – 810Combined sources11
Turni811 – 813Combined sources3
Beta strandi814 – 817Combined sources4
Beta strandi821 – 825Combined sources5
Beta strandi828 – 834Combined sources7
Beta strandi837 – 840Combined sources4
Beta strandi845 – 853Combined sources9
Beta strandi860 – 866Combined sources7
Beta strandi872 – 875Combined sources4
Beta strandi878 – 880Combined sources3
Beta strandi882 – 888Combined sources7
Beta strandi892 – 902Combined sources11
Beta strandi906 – 916Combined sources11
Turni917 – 920Combined sources4
Beta strandi922 – 932Combined sources11
Beta strandi934 – 947Combined sources14
Helixi949 – 952Combined sources4
Beta strandi954 – 956Combined sources3
Beta strandi957 – 962Combined sources6
Beta strandi968 – 970Combined sources3
Beta strandi977 – 984Combined sources8
Turni988 – 990Combined sources3
Helixi997 – 999Combined sources3
Helixi1001 – 1003Combined sources3
Beta strandi1009 – 1012Combined sources4
Helixi1013 – 1031Combined sources19
Helixi1034 – 1037Combined sources4
Helixi1041 – 1057Combined sources17
Turni1062 – 1064Combined sources3
Beta strandi1068 – 1072Combined sources5
Helixi1076 – 1089Combined sources14
Turni1090 – 1092Combined sources3
Helixi1097 – 1111Combined sources15
Turni1114 – 1116Combined sources3
Helixi1127 – 1133Combined sources7
Helixi1139 – 1158Combined sources20
Turni1159 – 1161Combined sources3
Helixi1165 – 1179Combined sources15
Helixi1180 – 1182Combined sources3
Helixi1186 – 1198Combined sources13
Helixi1204 – 1213Combined sources10
Turni1216 – 1218Combined sources3
Beta strandi1223 – 1225Combined sources3
Helixi1226 – 1243Combined sources18
Turni1246 – 1248Combined sources3
Helixi1249 – 1258Combined sources10
Beta strandi1265 – 1267Combined sources3
Helixi1269 – 1285Combined sources17
Turni1297 – 1299Combined sources3
Beta strandi1303 – 1305Combined sources3
Beta strandi1307 – 1313Combined sources7
Turni1314 – 1317Combined sources4
Beta strandi1320 – 1326Combined sources7
Beta strandi1330 – 1338Combined sources9
Beta strandi1340 – 1350Combined sources11
Beta strandi1359 – 1369Combined sources11
Beta strandi1384 – 1392Combined sources9
Beta strandi1394 – 1396Combined sources3
Beta strandi1400 – 1406Combined sources7
Beta strandi1411 – 1413Combined sources3
Helixi1415 – 1422Combined sources8
Beta strandi1424 – 1426Combined sources3
Helixi1431 – 1434Combined sources4
Turni1438 – 1440Combined sources3
Beta strandi1442 – 1449Combined sources8
Beta strandi1453 – 1455Combined sources3
Beta strandi1457 – 1467Combined sources11
Beta strandi1469 – 1471Combined sources3
Beta strandi1475 – 1481Combined sources7
Beta strandi1485 – 1493Combined sources9
Beta strandi1495 – 1497Combined sources3
Helixi1498 – 1500Combined sources3
Beta strandi1504 – 1507Combined sources4
Beta strandi1510 – 1513Combined sources4
Turni1515 – 1517Combined sources3
Beta strandi1518 – 1520Combined sources3
Turni1524 – 1526Combined sources3
Helixi1529 – 1536Combined sources8
Beta strandi1537 – 1540Combined sources4
Beta strandi1541 – 1553Combined sources13
Beta strandi1556 – 1570Combined sources15
Turni1577 – 1579Combined sources3
Beta strandi1581 – 1587Combined sources7
Helixi1588 – 1590Combined sources3
Helixi1591 – 1594Combined sources4
Beta strandi1601 – 1607Combined sources7
Helixi1608 – 1610Combined sources3
Beta strandi1611 – 1613Combined sources3
Beta strandi1615 – 1617Combined sources3
Beta strandi1619 – 1621Combined sources3
Beta strandi1627 – 1631Combined sources5
Turni1634 – 1636Combined sources3
Beta strandi1637 – 1639Combined sources3
Turni1640 – 1642Combined sources3
Helixi1643 – 1659Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C3DX-ray1.80A996-1287[»]
1GHQX-ray2.04A996-1300[»]
1W2SX-ray-A996-1299[»]
2A73X-ray3.30A23-665[»]
B673-1663[»]
2A74X-ray2.40A/D23-665[»]
B/E749-936[»]
C/F1321-1663[»]
2GOXX-ray2.20A/C996-1287[»]
2I07X-ray4.00A23-667[»]
B749-1663[»]
2ICEX-ray3.10A/D23-664[»]
B/E749-954[»]
C/F1321-1663[»]
2ICFX-ray4.10A23-664[»]
B749-1663[»]
2NOJX-ray2.70A/C/E/G996-1287[»]
2QKIX-ray2.40A/D23-665[»]
B/E749-936[»]
C/F1321-1663[»]
2WIIX-ray2.70A23-667[»]
B749-1663[»]
2WINX-ray3.90A/C/E/G23-667[»]
B/D/F/H749-1663[»]
2WY7X-ray1.70A996-1303[»]
2WY8X-ray1.70A996-1303[»]
2XQWX-ray2.31A/B996-1287[»]
2XWBX-ray3.49A/C23-664[»]
B/D752-1663[»]
2XWJX-ray4.00A/C/E/G23-667[»]
B/D/F/H749-1663[»]
3D5RX-ray2.10A/B996-1287[»]
3D5SX-ray2.30A/B996-1287[»]
3G6JX-ray3.10A/C23-666[»]
B/D749-1663[»]
3L3OX-ray3.40A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
3L5NX-ray7.54A23-667[»]
B749-1663[»]
3NMSX-ray4.10A23-667[»]
B749-954[»]
C1321-1663[»]
3OEDX-ray3.16A/B996-1303[»]
3OHXX-ray3.50A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
3OXUX-ray2.10A/B/C996-1303[»]
3RJ3X-ray2.35A/B/C996-1303[»]
3T4AX-ray3.40A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
4HW5X-ray2.25A/B672-748[»]
4HWJX-ray2.60A672-747[»]
4I6OX-ray2.14A672-748[»]
4M76X-ray2.80A994-1288[»]
4ONTX-ray2.15A/B/C996-1303[»]
4ZH1X-ray2.24A/B/C996-1303[»]
5FO7X-ray2.80A23-667[»]
B749-1663[»]
5FO8X-ray2.40A23-667[»]
B749-1663[»]
5FO9X-ray3.30A/D23-667[»]
B/E749-1663[»]
5FOAX-ray4.19A/C23-667[»]
B/D749-1663[»]
5FOBX-ray2.60A23-667[»]
B749-1663[»]
ProteinModelPortaliP01024.
SMRiP01024.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01024.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini693 – 728Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST36
Domaini1518 – 1661NTRPROSITE-ProRule annotationAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1424 – 1456Properdin-bindingAdd BLAST33

Sequence similaritiesi

Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000286028.
HOVERGENiHBG005110.
InParanoidiP01024.
KOiK03990.
OMAiDETEQWE.
OrthoDBiEOG091G00FJ.
PhylomeDBiP01024.
TreeFamiTF313285.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPTSGPSLL LLLLTHLPLA LGSPMYSIIT PNILRLESEE TMVLEAHDAQ
60 70 80 90 100
GDVPVTVTVH DFPGKKLVLS SEKTVLTPAT NHMGNVTFTI PANREFKSEK
110 120 130 140 150
GRNKFVTVQA TFGTQVVEKV VLVSLQSGYL FIQTDKTIYT PGSTVLYRIF
160 170 180 190 200
TVNHKLLPVG RTVMVNIENP EGIPVKQDSL SSQNQLGVLP LSWDIPELVN
210 220 230 240 250
MGQWKIRAYY ENSPQQVFST EFEVKEYVLP SFEVIVEPTE KFYYIYNEKG
260 270 280 290 300
LEVTITARFL YGKKVEGTAF VIFGIQDGEQ RISLPESLKR IPIEDGSGEV
310 320 330 340 350
VLSRKVLLDG VQNPRAEDLV GKSLYVSATV ILHSGSDMVQ AERSGIPIVT
360 370 380 390 400
SPYQIHFTKT PKYFKPGMPF DLMVFVTNPD GSPAYRVPVA VQGEDTVQSL
410 420 430 440 450
TQGDGVAKLS INTHPSQKPL SITVRTKKQE LSEAEQATRT MQALPYSTVG
460 470 480 490 500
NSNNYLHLSV LRTELRPGET LNVNFLLRMD RAHEAKIRYY TYLIMNKGRL
510 520 530 540 550
LKAGRQVREP GQDLVVLPLS ITTDFIPSFR LVAYYTLIGA SGQREVVADS
560 570 580 590 600
VWVDVKDSCV GSLVVKSGQS EDRQPVPGQQ MTLKIEGDHG ARVVLVAVDK
610 620 630 640 650
GVFVLNKKNK LTQSKIWDVV EKADIGCTPG SGKDYAGVFS DAGLTFTSSS
660 670 680 690 700
GQQTAQRAEL QCPQPAARRR RSVQLTEKRM DKVGKYPKEL RKCCEDGMRE
710 720 730 740 750
NPMRFSCQRR TRFISLGEAC KKVFLDCCNY ITELRRQHAR ASHLGLARSN
760 770 780 790 800
LDEDIIAEEN IVSRSEFPES WLWNVEDLKE PPKNGISTKL MNIFLKDSIT
810 820 830 840 850
TWEILAVSMS DKKGICVADP FEVTVMQDFF IDLRLPYSVV RNEQVEIRAV
860 870 880 890 900
LYNYRQNQEL KVRVELLHNP AFCSLATTKR RHQQTVTIPP KSSLSVPYVI
910 920 930 940 950
VPLKTGLQEV EVKAAVYHHF ISDGVRKSLK VVPEGIRMNK TVAVRTLDPE
960 970 980 990 1000
RLGREGVQKE DIPPADLSDQ VPDTESETRI LLQGTPVAQM TEDAVDAERL
1010 1020 1030 1040 1050
KHLIVTPSGC GEQNMIGMTP TVIAVHYLDE TEQWEKFGLE KRQGALELIK
1060 1070 1080 1090 1100
KGYTQQLAFR QPSSAFAAFV KRAPSTWLTA YVVKVFSLAV NLIAIDSQVL
1110 1120 1130 1140 1150
CGAVKWLILE KQKPDGVFQE DAPVIHQEMI GGLRNNNEKD MALTAFVLIS
1160 1170 1180 1190 1200
LQEAKDICEE QVNSLPGSIT KAGDFLEANY MNLQRSYTVA IAGYALAQMG
1210 1220 1230 1240 1250
RLKGPLLNKF LTTAKDKNRW EDPGKQLYNV EATSYALLAL LQLKDFDFVP
1260 1270 1280 1290 1300
PVVRWLNEQR YYGGGYGSTQ ATFMVFQALA QYQKDAPDHQ ELNLDVSLQL
1310 1320 1330 1340 1350
PSRSSKITHR IHWESASLLR SEETKENEGF TVTAEGKGQG TLSVVTMYHA
1360 1370 1380 1390 1400
KAKDQLTCNK FDLKVTIKPA PETEKRPQDA KNTMILEICT RYRGDQDATM
1410 1420 1430 1440 1450
SILDISMMTG FAPDTDDLKQ LANGVDRYIS KYELDKAFSD RNTLIIYLDK
1460 1470 1480 1490 1500
VSHSEDDCLA FKVHQYFNVE LIQPGAVKVY AYYNLEESCT RFYHPEKEDG
1510 1520 1530 1540 1550
KLNKLCRDEL CRCAEENCFI QKSDDKVTLE ERLDKACEPG VDYVYKTRLV
1560 1570 1580 1590 1600
KVQLSNDFDE YIMAIEQTIK SGSDEVQVGQ QRTFISPIKC REALKLEEKK
1610 1620 1630 1640 1650
HYLMWGLSSD FWGEKPNLSY IIGKDTWVEH WPEEDECQDE ENQKQCQDLG
1660
AFTESMVVFG CPN
Length:1,663
Mass (Da):187,148
Last modified:December 12, 2006 - v2
Checksum:i30C2832A9E75FFC4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti681D → N AA sequence (PubMed:1238393).Curated1
Sequence conflicti700E → Q AA sequence (PubMed:1238393).Curated1
Sequence conflicti1026H → S AA sequence (PubMed:6175959).Curated1

Polymorphismi

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001983102R → G in allele C3F; associated with susceptibility to ARMD9; results in decreased binding affinity for regulator factor H; results in reduced sensitivity to cleavage by factor I. 3 PublicationsCorresponds to variant rs2230199dbSNPEnsembl.1
Natural variantiVAR_070941155K → Q in ARMD9; results in resistance to proteolytic inactivation by CFH and CFI. 1 PublicationCorresponds to variant rs147859257dbSNPEnsembl.1
Natural variantiVAR_001984314P → L.3 PublicationsCorresponds to variant rs1047286dbSNPEnsembl.1
Natural variantiVAR_020262469E → D.Corresponds to variant rs11569422dbSNPEnsembl.1
Natural variantiVAR_001985549D → N in C3D; impairs secretion; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_063213592R → Q in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant rs121909583dbSNPEnsembl.1
Natural variantiVAR_063214592R → W in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant rs771353792dbSNPEnsembl.1
Natural variantiVAR_063654603F → V in AHUS5. 1 Publication1
Natural variantiVAR_063215735R → W in AHUS5. 1 PublicationCorresponds to variant rs117793540dbSNPEnsembl.1
Natural variantiVAR_019206863R → K.1 PublicationCorresponds to variant rs11569472dbSNPEnsembl.1
Natural variantiVAR_0636551042R → L in AHUS5. 1 Publication1
Natural variantiVAR_0632161094A → V in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant rs121909584dbSNPEnsembl.1
Natural variantiVAR_0632171115D → N in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 PublicationCorresponds to variant rs121909585dbSNPEnsembl.1
Natural variantiVAR_0632181158C → W in AHUS5. 1 Publication1
Natural variantiVAR_0632191161Q → K in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication1
Natural variantiVAR_0227611216D → N in C3S. 1 Publication1
Natural variantiVAR_0192071224G → D.1 PublicationCorresponds to variant rs11569534dbSNPEnsembl.1
Natural variantiVAR_0192081367I → T.1 PublicationCorresponds to variant rs11569541dbSNPEnsembl.1
Natural variantiVAR_0632201464H → D in AHUS5. 1 Publication1
Natural variantiVAR_0297921521Q → R.Corresponds to variant rs7256789dbSNPEnsembl.1
Natural variantiVAR_0297931601H → N.Corresponds to variant rs1803225dbSNPEnsembl.1
Natural variantiVAR_0293261619S → R.Corresponds to variant rs2230210dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02765 mRNA. Translation: AAA85332.1.
AY513239 Genomic DNA. Translation: AAR89906.1.
CH471139 Genomic DNA. Translation: EAW69071.1.
BC150179 mRNA. Translation: AAI50180.1.
BC150200 mRNA. Translation: AAI50201.1.
CCDSiCCDS32883.1.
PIRiA94065. C3HU.
RefSeqiNP_000055.2. NM_000064.3.
UniGeneiHs.529053.

Genome annotation databases

EnsembliENST00000245907; ENSP00000245907; ENSG00000125730.
GeneIDi718.
KEGGihsa:718.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

C3base

C3 mutation db

Wikipedia

Complement C3 entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02765 mRNA. Translation: AAA85332.1.
AY513239 Genomic DNA. Translation: AAR89906.1.
CH471139 Genomic DNA. Translation: EAW69071.1.
BC150179 mRNA. Translation: AAI50180.1.
BC150200 mRNA. Translation: AAI50201.1.
CCDSiCCDS32883.1.
PIRiA94065. C3HU.
RefSeqiNP_000055.2. NM_000064.3.
UniGeneiHs.529053.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C3DX-ray1.80A996-1287[»]
1GHQX-ray2.04A996-1300[»]
1W2SX-ray-A996-1299[»]
2A73X-ray3.30A23-665[»]
B673-1663[»]
2A74X-ray2.40A/D23-665[»]
B/E749-936[»]
C/F1321-1663[»]
2GOXX-ray2.20A/C996-1287[»]
2I07X-ray4.00A23-667[»]
B749-1663[»]
2ICEX-ray3.10A/D23-664[»]
B/E749-954[»]
C/F1321-1663[»]
2ICFX-ray4.10A23-664[»]
B749-1663[»]
2NOJX-ray2.70A/C/E/G996-1287[»]
2QKIX-ray2.40A/D23-665[»]
B/E749-936[»]
C/F1321-1663[»]
2WIIX-ray2.70A23-667[»]
B749-1663[»]
2WINX-ray3.90A/C/E/G23-667[»]
B/D/F/H749-1663[»]
2WY7X-ray1.70A996-1303[»]
2WY8X-ray1.70A996-1303[»]
2XQWX-ray2.31A/B996-1287[»]
2XWBX-ray3.49A/C23-664[»]
B/D752-1663[»]
2XWJX-ray4.00A/C/E/G23-667[»]
B/D/F/H749-1663[»]
3D5RX-ray2.10A/B996-1287[»]
3D5SX-ray2.30A/B996-1287[»]
3G6JX-ray3.10A/C23-666[»]
B/D749-1663[»]
3L3OX-ray3.40A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
3L5NX-ray7.54A23-667[»]
B749-1663[»]
3NMSX-ray4.10A23-667[»]
B749-954[»]
C1321-1663[»]
3OEDX-ray3.16A/B996-1303[»]
3OHXX-ray3.50A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
3OXUX-ray2.10A/B/C996-1303[»]
3RJ3X-ray2.35A/B/C996-1303[»]
3T4AX-ray3.40A/D23-667[»]
B/E749-954[»]
C/F1321-1663[»]
4HW5X-ray2.25A/B672-748[»]
4HWJX-ray2.60A672-747[»]
4I6OX-ray2.14A672-748[»]
4M76X-ray2.80A994-1288[»]
4ONTX-ray2.15A/B/C996-1303[»]
4ZH1X-ray2.24A/B/C996-1303[»]
5FO7X-ray2.80A23-667[»]
B749-1663[»]
5FO8X-ray2.40A23-667[»]
B749-1663[»]
5FO9X-ray3.30A/D23-667[»]
B/E749-1663[»]
5FOAX-ray4.19A/C23-667[»]
B/D749-1663[»]
5FOBX-ray2.60A23-667[»]
B749-1663[»]
ProteinModelPortaliP01024.
SMRiP01024.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107179. 28 interactors.
DIPiDIP-35180N.
IntActiP01024. 17 interactors.
MINTiMINT-5003988.
STRINGi9606.ENSP00000245907.

Chemistry databases

BindingDBiP01024.
ChEMBLiCHEMBL4917.
DrugBankiDB00028. Intravenous Immunoglobulin.

Protein family/group databases

MEROPSiI39.950.

PTM databases

iPTMnetiP01024.
PhosphoSitePlusiP01024.
UniCarbKBiP01024.

Polymorphism and mutation databases

BioMutaiC3.
DMDMi119370332.

2D gel databases

DOSAC-COBS-2DPAGEP01024.
SWISS-2DPAGEP01024.

Proteomic databases

EPDiP01024.
PaxDbiP01024.
PeptideAtlasiP01024.
PRIDEiP01024.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245907; ENSP00000245907; ENSG00000125730.
GeneIDi718.
KEGGihsa:718.

Organism-specific databases

CTDi718.
DisGeNETi718.
GeneCardsiC3.
GeneReviewsiC3.
H-InvDBHIX0020036.
HGNCiHGNC:1318. C3.
HPAiCAB004209.
HPA003563.
HPA020432.
MalaCardsiC3.
MIMi120700. gene.
611378. phenotype.
612925. phenotype.
613779. phenotype.
neXtProtiNX_P01024.
OpenTargetsiENSG00000125730.
Orphaneti279. Age-related macular degeneration.
93575. Atypical hemolytic-uremic syndrome with C3 anomaly.
280133. Complement component 3 deficiency.
PharmGKBiPA25897.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000286028.
HOVERGENiHBG005110.
InParanoidiP01024.
KOiK03990.
OMAiDETEQWE.
OrthoDBiEOG091G00FJ.
PhylomeDBiP01024.
TreeFamiTF313285.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125730-MONOMER.
BRENDAi3.4.21.47. 2681.
ReactomeiR-HSA-173736. Alternative complement activation.
R-HSA-174577. Activation of C3 and C5.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-977606. Regulation of Complement cascade.

Miscellaneous databases

ChiTaRSiC3. human.
EvolutionaryTraceiP01024.
GeneWikiiComplement_component_3.
GenomeRNAii718.
PMAP-CutDBP01024.
PROiP01024.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000125730.
CleanExiHS_C3.
ExpressionAtlasiP01024. baseline and differential.
GenevisibleiP01024. HS.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO3_HUMAN
AccessioniPrimary (citable) accession number: P01024
Secondary accession number(s): A7E236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 12, 2006
Last modified: November 30, 2016
This is version 211 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

According to PubMed:21527715, the interaction surface between C3 and CR2 reported in PubMed:11387479 is artifactual and can be ascribed to the presence of zinc acetate in the buffer.Curated

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.