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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
  • cofactor binding Source: Ensembl
  • endopeptidase inhibitor activity Source: InterPro
  • lipid binding Source: Ensembl
  • receptor binding Source: ProtInc
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

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

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-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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti549 – 5491D → N in C3D; impairs secretion; variant confirmed at protein level. 2 Publications
VAR_001985
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021R → 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 Publications
Corresponds to variant rs2230199 [ dbSNP | Ensembl ].
VAR_001983
Natural varianti155 – 1551K → Q in ARMD9; results in resistance to proteolytic inactivation by CFH and CFI. 1 Publication
Corresponds to variant rs147859257 [ dbSNP | Ensembl ].
VAR_070941
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti592 – 5921R → Q in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
Corresponds to variant rs121909583 [ dbSNP | Ensembl ].
VAR_063213
Natural varianti592 – 5921R → W in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
Corresponds to variant rs771353792 [ dbSNP | Ensembl ].
VAR_063214
Natural varianti603 – 6031F → V in AHUS5. 1 Publication
VAR_063654
Natural varianti735 – 7351R → W in AHUS5. 1 Publication
Corresponds to variant rs117793540 [ dbSNP | Ensembl ].
VAR_063215
Natural varianti1042 – 10421R → L in AHUS5. 1 Publication
VAR_063655
Natural varianti1094 – 10941A → V in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
Corresponds to variant rs121909584 [ dbSNP | Ensembl ].
VAR_063216
Natural varianti1115 – 11151D → N in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
Corresponds to variant rs121909585 [ dbSNP | Ensembl ].
VAR_063217
Natural varianti1158 – 11581C → W in AHUS5. 1 Publication
VAR_063218
Natural varianti1161 – 11611Q → K in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
VAR_063219
Natural varianti1464 – 14641H → D in AHUS5. 1 Publication
VAR_063220

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1029 – 10291D → A: Minor effect on binding of C3d to CR2. 2 Publications
Mutagenesisi1030 – 10301E → A: Impaired binding of C3d to CR2. 2 Publications
Mutagenesisi1032 – 10321E → A: Impaired binding of C3d to CR2. 2 Publications
Mutagenesisi1035 – 10351E → A: No effect on binding of C3d to CR2. 1 Publication
Mutagenesisi1042 – 10421R → M: Impaired binding of C3d to CR2. 1 Publication
Mutagenesisi1108 – 11092IL → RR: Impaired binding of C3d to CR2; when associated with A-1163. 1 Publication
Mutagenesisi1110 – 11101E → A: No effect on binding of C3d to CR2. 1 Publication
Mutagenesisi1115 – 11151D → A: No effect on binding of C3d to CR2. 1 Publication
Mutagenesisi1121 – 11211D → A: No effect on binding of C3d to CR2. 1 Publication
Mutagenesisi1140 – 11401D → A: No effect on binding of C3d to CR2. 2 Publications
Mutagenesisi1153 – 11531E → A: Impaired binding of C3d to CR2. 2 Publications
Mutagenesisi1156 – 11561D → A: Impaired binding of C3d to CR2. 2 Publications
Mutagenesisi1159 – 11591E → A: Impaired binding of C3d to CR2. 2 Publications
Mutagenesisi1160 – 11601E → A: Minor effect on binding of C3d to CR2. 2 Publications
Mutagenesisi1163 – 11631N → A: No effect on binding of C3d to CR2. Impaired binding of C3d to CR2; when associated with 1108-R-R-1109. 3 Publications
Mutagenesisi1163 – 11631N → R: Impaired binding of C3d to CR2. 3 Publications
Mutagenesisi1284 – 12841K → A: Impaired binding of C3d to CR2. 1 Publication

Keywords - Diseasei

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

Organism-specific databases

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

Chemistry

ChEMBLiCHEMBL4917.
DrugBankiDB00028. Intravenous Immunoglobulin.

Polymorphism and mutation databases

BioMutaiC3.
DMDMi119370332.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 16631641Complement C3PRO_0000005907Add
BLAST
Chaini23 – 667645Complement C3 beta chainPRO_0000005908Add
BLAST
Chaini569 – 66799C3-beta-cBy similarityPRO_0000430430Add
BLAST
Chaini672 – 1663992Complement C3 alpha chainPRO_0000005909Add
BLAST
Chaini672 – 74877C3a anaphylatoxinPRO_0000005910Add
BLAST
Chaini672 – 74776Acylation stimulating proteinPRO_0000419935Add
BLAST
Chaini749 – 1663915Complement C3b alpha' chainPRO_0000005911Add
BLAST
Chaini749 – 954206Complement C3c alpha' chain fragment 1PRO_0000005912Add
BLAST
Chaini955 – 1303349Complement C3dg fragmentPRO_0000005913Add
BLAST
Chaini955 – 100147Complement C3g fragmentPRO_0000005914Add
BLAST
Chaini1002 – 1303302Complement C3d fragmentPRO_0000005915Add
BLAST
Peptidei1304 – 132017Complement C3f fragment1 PublicationPRO_0000005916Add
BLAST
Chaini1321 – 1663343Complement C3c alpha' chain fragment 2PRO_0000273948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Phosphoserine; by FAM20C1 Publication
Modified residuei70 – 701Phosphoserine; by FAM20C1 Publication
Glycosylationi85 – 851N-linked (GlcNAc...)7 Publications
Modified residuei297 – 2971Phosphoserine; by FAM20C1 Publication
Modified residuei303 – 3031Phosphoserine; by FAM20C1 Publication
Disulfide bondi559 ↔ 816Interchain (between beta and alpha chains)
Disulfide bondi627 ↔ 662
Modified residuei672 – 6721Phosphoserine; by FAM20C1 Publication
Disulfide bondi693 ↔ 7201 Publication
Disulfide bondi694 ↔ 727
Disulfide bondi707 ↔ 728
Disulfide bondi873 ↔ 1513
Glycosylationi939 – 9391N-linked (GlcNAc...)3 Publications
Modified residuei968 – 9681Phosphoserine; by FAM20C1 Publication
Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)
Disulfide bondi1101 ↔ 1158
Modified residuei1321 – 13211Phosphoserine; by FAM20C1 Publication
Disulfide bondi1358 ↔ 1489
Disulfide bondi1389 ↔ 1458
Disulfide bondi1506 ↔ 1511
Disulfide bondi1518 ↔ 1590
Disulfide bondi1537 ↔ 1661
Modified residuei1573 – 15731Phosphoserine; by FAM20C1 Publication
Glycosylationi1617 – 16171N-linked (GlcNAc...)1 Publication
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei747 – 7482Cleavage; by carboxypeptidases
Sitei748 – 7492Cleavage; by C3 convertase
Sitei954 – 9552Cleavage; by factor ISequence analysis
Sitei1303 – 13042Cleavage; by factor I
Sitei1320 – 13212Cleavage; by factor I

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.
PhosphoSiteiP01024.
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-6863106,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 interactions.
DIPiDIP-35180N.
IntActiP01024. 13 interactions.
MINTiMINT-5003988.
STRINGi9606.ENSP00000245907.

Chemistry

BindingDBiP01024.

Structurei

Secondary structure

1
1663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 295Combined sources
Beta strandi31 – 344Combined sources
Beta strandi36 – 416Combined sources
Beta strandi43 – 475Combined sources
Beta strandi53 – 6412Combined sources
Beta strandi67 – 693Combined sources
Beta strandi73 – 764Combined sources
Helixi78 – 803Combined sources
Beta strandi87 – 893Combined sources
Helixi94 – 974Combined sources
Beta strandi105 – 1128Combined sources
Beta strandi115 – 1239Combined sources
Beta strandi129 – 1357Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi144 – 1529Combined sources
Beta strandi162 – 1687Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi179 – 1813Combined sources
Turni183 – 1875Combined sources
Beta strandi188 – 1947Combined sources
Beta strandi202 – 2109Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi218 – 2247Combined sources
Beta strandi231 – 24414Combined sources
Beta strandi251 – 2599Combined sources
Beta strandi267 – 27711Combined sources
Beta strandi280 – 29415Combined sources
Beta strandi297 – 3026Combined sources
Helixi304 – 3096Combined sources
Beta strandi311 – 3133Combined sources
Helixi316 – 3194Combined sources
Beta strandi323 – 33210Combined sources
Beta strandi338 – 35215Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi370 – 3778Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi388 – 3936Combined sources
Helixi395 – 3973Combined sources
Beta strandi398 – 4003Combined sources
Beta strandi405 – 4117Combined sources
Beta strandi415 – 4173Combined sources
Beta strandi420 – 4267Combined sources
Turni429 – 4313Combined sources
Helixi433 – 4353Combined sources
Beta strandi439 – 4457Combined sources
Helixi449 – 4513Combined sources
Beta strandi455 – 4595Combined sources
Beta strandi470 – 4789Combined sources
Turni481 – 4833Combined sources
Helixi484 – 4863Combined sources
Beta strandi489 – 4968Combined sources
Beta strandi499 – 5079Combined sources
Beta strandi513 – 5208Combined sources
Helixi523 – 5253Combined sources
Beta strandi527 – 53812Combined sources
Beta strandi540 – 5423Combined sources
Beta strandi544 – 55411Combined sources
Beta strandi563 – 5675Combined sources
Turni568 – 5703Combined sources
Beta strandi571 – 5733Combined sources
Beta strandi580 – 5889Combined sources
Beta strandi592 – 5998Combined sources
Helixi602 – 6054Combined sources
Helixi613 – 62210Combined sources
Beta strandi628 – 6303Combined sources
Helixi635 – 6417Combined sources
Beta strandi644 – 6485Combined sources
Helixi675 – 68410Combined sources
Helixi688 – 69710Combined sources
Helixi707 – 7104Combined sources
Turni712 – 7143Combined sources
Helixi718 – 74326Combined sources
Beta strandi753 – 7553Combined sources
Helixi758 – 7603Combined sources
Beta strandi769 – 7713Combined sources
Beta strandi775 – 7773Combined sources
Beta strandi786 – 7949Combined sources
Beta strandi800 – 81011Combined sources
Turni811 – 8133Combined sources
Beta strandi814 – 8174Combined sources
Beta strandi821 – 8255Combined sources
Beta strandi828 – 8347Combined sources
Beta strandi837 – 8404Combined sources
Beta strandi845 – 8539Combined sources
Beta strandi860 – 8667Combined sources
Beta strandi872 – 8754Combined sources
Beta strandi878 – 8803Combined sources
Beta strandi882 – 8887Combined sources
Beta strandi892 – 90211Combined sources
Beta strandi906 – 91611Combined sources
Turni917 – 9204Combined sources
Beta strandi922 – 93211Combined sources
Beta strandi934 – 94714Combined sources
Helixi949 – 9524Combined sources
Beta strandi954 – 9563Combined sources
Beta strandi957 – 9626Combined sources
Beta strandi968 – 9703Combined sources
Beta strandi977 – 9848Combined sources
Turni988 – 9903Combined sources
Helixi997 – 9993Combined sources
Helixi1001 – 10033Combined sources
Beta strandi1009 – 10124Combined sources
Helixi1013 – 103119Combined sources
Helixi1034 – 10374Combined sources
Helixi1041 – 105717Combined sources
Turni1062 – 10643Combined sources
Beta strandi1068 – 10725Combined sources
Helixi1076 – 108914Combined sources
Turni1090 – 10923Combined sources
Helixi1097 – 111115Combined sources
Turni1114 – 11163Combined sources
Helixi1127 – 11337Combined sources
Helixi1139 – 115820Combined sources
Turni1159 – 11613Combined sources
Helixi1165 – 117915Combined sources
Helixi1180 – 11823Combined sources
Helixi1186 – 119813Combined sources
Helixi1204 – 121310Combined sources
Turni1216 – 12183Combined sources
Beta strandi1223 – 12253Combined sources
Helixi1226 – 124318Combined sources
Turni1246 – 12483Combined sources
Helixi1249 – 125810Combined sources
Beta strandi1265 – 12673Combined sources
Helixi1269 – 128517Combined sources
Turni1297 – 12993Combined sources
Beta strandi1303 – 13053Combined sources
Beta strandi1307 – 13137Combined sources
Turni1314 – 13174Combined sources
Beta strandi1320 – 13267Combined sources
Beta strandi1330 – 13389Combined sources
Beta strandi1340 – 135011Combined sources
Beta strandi1359 – 136911Combined sources
Beta strandi1384 – 13929Combined sources
Beta strandi1394 – 13963Combined sources
Beta strandi1400 – 14067Combined sources
Beta strandi1411 – 14133Combined sources
Helixi1415 – 14228Combined sources
Beta strandi1424 – 14263Combined sources
Helixi1431 – 14344Combined sources
Turni1438 – 14403Combined sources
Beta strandi1442 – 14498Combined sources
Beta strandi1453 – 14553Combined sources
Beta strandi1457 – 146711Combined sources
Beta strandi1469 – 14713Combined sources
Beta strandi1475 – 14817Combined sources
Beta strandi1485 – 14939Combined sources
Beta strandi1495 – 14973Combined sources
Helixi1498 – 15003Combined sources
Beta strandi1504 – 15074Combined sources
Beta strandi1510 – 15134Combined sources
Turni1515 – 15173Combined sources
Beta strandi1518 – 15203Combined sources
Turni1524 – 15263Combined sources
Helixi1529 – 15368Combined sources
Beta strandi1537 – 15404Combined sources
Beta strandi1541 – 155313Combined sources
Beta strandi1556 – 157015Combined sources
Turni1577 – 15793Combined sources
Beta strandi1581 – 15877Combined sources
Helixi1588 – 15903Combined sources
Helixi1591 – 15944Combined sources
Beta strandi1601 – 16077Combined sources
Helixi1608 – 16103Combined sources
Beta strandi1611 – 16133Combined sources
Beta strandi1615 – 16173Combined sources
Beta strandi1619 – 16213Combined sources
Beta strandi1627 – 16315Combined sources
Turni1634 – 16363Combined sources
Beta strandi1637 – 16393Combined sources
Turni1640 – 16423Combined sources
Helixi1643 – 165917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 23-664, 673-1663.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01024.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini693 – 72836Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini1518 – 1661144NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1424 – 145633Properdin-bindingAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti681 – 6811D → N AA sequence (PubMed:1238393).Curated
Sequence conflicti700 – 7001E → Q AA sequence (PubMed:1238393).Curated
Sequence conflicti1026 – 10261H → S AA sequence (PubMed:6175959).Curated

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021R → 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 Publications
Corresponds to variant rs2230199 [ dbSNP | Ensembl ].
VAR_001983
Natural varianti155 – 1551K → Q in ARMD9; results in resistance to proteolytic inactivation by CFH and CFI. 1 Publication
Corresponds to variant rs147859257 [ dbSNP | Ensembl ].
VAR_070941
Natural varianti314 – 3141P → L.3 Publications
Corresponds to variant rs1047286 [ dbSNP | Ensembl ].
VAR_001984
Natural varianti469 – 4691E → D.
Corresponds to variant rs11569422 [ dbSNP | Ensembl ].
VAR_020262
Natural varianti549 – 5491D → N in C3D; impairs secretion; variant confirmed at protein level. 2 Publications
VAR_001985
Natural varianti592 – 5921R → Q in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
Corresponds to variant rs121909583 [ dbSNP | Ensembl ].
VAR_063213
Natural varianti592 – 5921R → W in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
Corresponds to variant rs771353792 [ dbSNP | Ensembl ].
VAR_063214
Natural varianti603 – 6031F → V in AHUS5. 1 Publication
VAR_063654
Natural varianti735 – 7351R → W in AHUS5. 1 Publication
Corresponds to variant rs117793540 [ dbSNP | Ensembl ].
VAR_063215
Natural varianti863 – 8631R → K.1 Publication
Corresponds to variant rs11569472 [ dbSNP | Ensembl ].
VAR_019206
Natural varianti1042 – 10421R → L in AHUS5. 1 Publication
VAR_063655
Natural varianti1094 – 10941A → V in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
Corresponds to variant rs121909584 [ dbSNP | Ensembl ].
VAR_063216
Natural varianti1115 – 11151D → N in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
Corresponds to variant rs121909585 [ dbSNP | Ensembl ].
VAR_063217
Natural varianti1158 – 11581C → W in AHUS5. 1 Publication
VAR_063218
Natural varianti1161 – 11611Q → K in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. 1 Publication
VAR_063219
Natural varianti1216 – 12161D → N in C3S. 1 Publication
VAR_022761
Natural varianti1224 – 12241G → D.1 Publication
Corresponds to variant rs11569534 [ dbSNP | Ensembl ].
VAR_019207
Natural varianti1367 – 13671I → T.1 Publication
Corresponds to variant rs11569541 [ dbSNP | Ensembl ].
VAR_019208
Natural varianti1464 – 14641H → D in AHUS5. 1 Publication
VAR_063220
Natural varianti1521 – 15211Q → R.
Corresponds to variant rs7256789 [ dbSNP | Ensembl ].
VAR_029792
Natural varianti1601 – 16011H → N.
Corresponds to variant rs1803225 [ dbSNP | Ensembl ].
VAR_029793
Natural varianti1619 – 16191S → R.
Corresponds to variant rs2230210 [ dbSNP | Ensembl ].
VAR_029326

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
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. Positions 23-664, 673-1663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107179. 28 interactions.
DIPiDIP-35180N.
IntActiP01024. 13 interactions.
MINTiMINT-5003988.
STRINGi9606.ENSP00000245907.

Chemistry

BindingDBiP01024.
ChEMBLiCHEMBL4917.
DrugBankiDB00028. Intravenous Immunoglobulin.

Protein family/group databases

MEROPSiI39.950.

PTM databases

iPTMnetiP01024.
PhosphoSiteiP01024.
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.
GeneCardsiC3.
GeneReviewsiC3.
H-InvDBHIX0020036.
HGNCiHGNC:1318. C3.
HPAiCAB004209.
HPA003563.
HPA020432.
MalaCardsiC3.
MIMi120700. gene.
611378. phenotype.
612925. phenotype.
613779. phenotype.
neXtProtiNX_P01024.
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

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-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: September 7, 2016
This is version 208 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.