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P01024

- CO3_HUMAN

UniProt

P01024 - CO3_HUMAN

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Protein

Complement C3

Gene

C3

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

GO - Molecular functioni

  1. C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
  2. endopeptidase inhibitor activity Source: InterPro
  3. receptor binding Source: ProtInc

GO - Biological processi

  1. complement activation Source: BHF-UCL
  2. complement activation, alternative pathway Source: Reactome
  3. complement activation, classical pathway Source: UniProtKB-KW
  4. fatty acid metabolic process Source: UniProtKB-KW
  5. G-protein coupled receptor signaling pathway Source: ProtInc
  6. immune response Source: ProtInc
  7. inflammatory response Source: UniProtKB-KW
  8. innate immune response Source: Reactome
  9. positive regulation of activation of membrane attack complex Source: Ensembl
  10. positive regulation of angiogenesis Source: Ensembl
  11. positive regulation of apoptotic cell clearance Source: BHF-UCL
  12. positive regulation of glucose transport Source: UniProtKB
  13. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  14. positive regulation of lipid storage Source: UniProtKB
  15. positive regulation of protein phosphorylation Source: UniProtKB
  16. positive regulation of type IIa hypersensitivity Source: Ensembl
  17. positive regulation vascular endothelial growth factor production Source: BHF-UCL
  18. regulation of complement activation Source: Reactome
  19. regulation of immune response Source: Reactome
  20. regulation of triglyceride biosynthetic process Source: UniProtKB
  21. 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

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_118707. Regulation of Complement cascade.
REACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.
REACT_7972. Activation of C3 and C5.
REACT_8001. Alternative complement activation.

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
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1318. C3.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Complement component 3 deficiency (C3D) [MIM:613779]: A 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti549 – 5491D → N in C3D; impairs secretion; variant confirmed at protein level. 2 Publications
VAR_001985
Natural varianti1320 – 13201R → Q in C3D; allotype C3'F02'; may inhibit IC3B synthesis. 1 Publication
VAR_001986
Macular degeneration, age-related, 9 (ARMD9) [MIM:611378]: A 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.2 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
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. 2 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
VAR_070941
Hemolytic uremic syndrome atypical 5 (AHUS5) [MIM:612925]: An 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.2 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
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
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
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
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
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

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.

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
Glycosylationi85 – 851N-linked (GlcNAc...)7 Publications
Disulfide bondi559 ↔ 816Interchain (between beta and alpha chains)
Disulfide bondi627 ↔ 662
Disulfide bondi693 ↔ 7201 Publication
Disulfide bondi694 ↔ 727
Disulfide bondi707 ↔ 728
Disulfide bondi873 ↔ 1513
Glycosylationi939 – 9391N-linked (GlcNAc...)3 Publications
Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)
Disulfide bondi1101 ↔ 1158
Disulfide bondi1358 ↔ 1489
Disulfide bondi1389 ↔ 1458
Disulfide bondi1506 ↔ 1511
Disulfide bondi1518 ↔ 1590
Disulfide bondi1537 ↔ 1661
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.
Phosphorylation sites are present in the extracellular medium.

Keywords - PTMi

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

Proteomic databases

MaxQBiP01024.
PaxDbiP01024.
PeptideAtlasiP01024.
PRIDEiP01024.

2D gel databases

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

PTM databases

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

BgeeiP01024.
CleanExiHS_C3.
ExpressionAtlasiP01024. baseline and differential.
GenevestigatoriP01024.

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

Protein-protein interaction databases

BioGridi107179. 17 interactions.
DIPiDIP-35180N.
IntActiP01024. 10 interactions.
MINTiMINT-5003988.
STRINGi9606.ENSP00000245907.

Structurei

Secondary structure

1
1663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 358
Beta strandi36 – 416
Beta strandi43 – 475
Beta strandi54 – 563
Beta strandi59 – 613
Turni62 – 643
Beta strandi67 – 693
Beta strandi73 – 753
Helixi78 – 803
Beta strandi87 – 893
Helixi94 – 974
Beta strandi105 – 1128
Beta strandi115 – 12410
Beta strandi129 – 1357
Beta strandi137 – 1393
Beta strandi143 – 15210
Beta strandi162 – 1687
Beta strandi174 – 1818
Turni183 – 1875
Beta strandi188 – 1947
Beta strandi202 – 2109
Beta strandi216 – 2238
Beta strandi233 – 24412
Beta strandi251 – 2588
Beta strandi267 – 27711
Beta strandi280 – 2834
Helixi285 – 2873
Beta strandi289 – 2946
Beta strandi297 – 3026
Helixi304 – 3085
Turni310 – 3123
Helixi316 – 3194
Beta strandi323 – 33614
Beta strandi338 – 35013
Beta strandi354 – 3563
Beta strandi358 – 3603
Beta strandi362 – 3643
Beta strandi368 – 37710
Beta strandi379 – 3835
Beta strandi389 – 3946
Helixi395 – 3973
Beta strandi398 – 4003
Beta strandi405 – 4128
Beta strandi420 – 4267
Turni429 – 4313
Turni433 – 4353
Beta strandi438 – 4447
Helixi449 – 4513
Beta strandi455 – 4606
Beta strandi469 – 47810
Turni481 – 4833
Turni484 – 4863
Beta strandi489 – 4968
Beta strandi499 – 5079
Beta strandi513 – 5208
Helixi523 – 5253
Beta strandi527 – 53812
Beta strandi540 – 55415
Beta strandi564 – 5674
Turni568 – 5703
Beta strandi571 – 5733
Beta strandi580 – 5889
Beta strandi592 – 5987
Helixi600 – 6034
Helixi613 – 6219
Beta strandi628 – 6303
Beta strandi633 – 6364
Helixi637 – 6404
Turni641 – 6433
Beta strandi644 – 6474
Beta strandi649 – 6513
Helixi675 – 68410
Helixi688 – 69710
Helixi707 – 7104
Turni712 – 7143
Helixi718 – 74326
Beta strandi753 – 7553
Helixi758 – 7603
Beta strandi769 – 7713
Beta strandi775 – 7773
Beta strandi786 – 7949
Beta strandi800 – 81011
Turni811 – 8133
Beta strandi814 – 8174
Beta strandi821 – 8255
Beta strandi828 – 8347
Beta strandi837 – 8404
Beta strandi845 – 8539
Beta strandi860 – 8667
Beta strandi872 – 8754
Beta strandi878 – 8803
Beta strandi882 – 8887
Beta strandi892 – 90211
Beta strandi906 – 91914
Beta strandi922 – 93211
Helixi942 – 9476
Helixi949 – 9524
Beta strandi956 – 9627
Beta strandi968 – 9703
Beta strandi983 – 9886
Helixi989 – 9957
Helixi997 – 9993
Helixi1001 – 10033
Beta strandi1009 – 10124
Helixi1013 – 103119
Helixi1034 – 10374
Helixi1041 – 105717
Turni1062 – 10643
Beta strandi1067 – 10726
Helixi1076 – 108914
Turni1090 – 10923
Helixi1097 – 111115
Turni1114 – 11163
Helixi1127 – 11337
Helixi1139 – 115820
Turni1159 – 11613
Helixi1165 – 117915
Helixi1180 – 11823
Helixi1186 – 119813
Helixi1204 – 121310
Turni1216 – 12183
Beta strandi1223 – 12253
Helixi1226 – 124318
Turni1246 – 12483
Helixi1249 – 125810
Beta strandi1262 – 12654
Helixi1269 – 128517
Beta strandi1293 – 12997
Beta strandi1303 – 13053
Beta strandi1307 – 13126
Beta strandi1313 – 13164
Beta strandi1320 – 13267
Beta strandi1331 – 13333
Beta strandi1337 – 13393
Beta strandi1340 – 135011
Beta strandi1359 – 136911
Beta strandi1381 – 139212
Beta strandi1394 – 13963
Beta strandi1400 – 14067
Beta strandi1409 – 14135
Helixi1415 – 14239
Beta strandi1424 – 14263
Beta strandi1430 – 14323
Turni1438 – 14403
Beta strandi1443 – 14497
Beta strandi1453 – 14553
Beta strandi1459 – 14679
Beta strandi1469 – 14713
Beta strandi1475 – 14817
Beta strandi1484 – 149310
Turni1495 – 14984
Beta strandi1504 – 15074
Beta strandi1510 – 15134
Turni1515 – 15173
Beta strandi1518 – 15203
Turni1524 – 15263
Helixi1529 – 15357
Beta strandi1537 – 15404
Beta strandi1541 – 155414
Beta strandi1556 – 157015
Beta strandi1581 – 15877
Helixi1588 – 15903
Helixi1591 – 15944
Beta strandi1601 – 16077
Helixi1608 – 16103
Beta strandi1611 – 16133
Beta strandi1615 – 16173
Beta strandi1619 – 16213
Beta strandi1627 – 16315
Helixi1634 – 16363
Beta strandi1637 – 16393
Turni1640 – 16423
Helixi1643 – 165715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
2HR0X-ray2.26A23-667[»]
B749-1663[»]
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[»]
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

eggNOGiNOG241555.
HOGENOMiHOG000286028.
HOVERGENiHBG005110.
InParanoidiP01024.
KOiK03990.
OMAiPGMPFDL.
OrthoDBiEOG77HDCX.
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.
SMARTiSM00104. 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. 2 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
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
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
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
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
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 varianti1320 – 13201R → Q in C3D; allotype C3'F02'; may inhibit IC3B synthesis. 1 Publication
VAR_001986
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:
EMBL
GenBank
DDBJ
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_000064.2.
UniGeneiHs.529053.

Genome annotation databases

EnsembliENST00000245907; ENSP00000245907; ENSG00000125730.
GeneIDi718.
KEGGihsa:718.
UCSCiuc002mfm.3. human.

Polymorphism databases

DMDMi119370332.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

C3base

C3 mutation db

Wikipedia

Complement C3 entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS32883.1.
PIRi A94065. C3HU.
RefSeqi NP_000055.2. NM_000064.2.
UniGenei Hs.529053.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C3D X-ray 1.80 A 996-1287 [» ]
1GHQ X-ray 2.04 A 996-1300 [» ]
1W2S X-ray - A 996-1299 [» ]
2A73 X-ray 3.30 A 23-665 [» ]
B 673-1663 [» ]
2A74 X-ray 2.40 A/D 23-665 [» ]
B/E 749-936 [» ]
C/F 1321-1663 [» ]
2GOX X-ray 2.20 A/C 996-1287 [» ]
2HR0 X-ray 2.26 A 23-667 [» ]
B 749-1663 [» ]
2I07 X-ray 4.00 A 23-667 [» ]
B 749-1663 [» ]
2ICE X-ray 3.10 A/D 23-664 [» ]
B/E 749-954 [» ]
C/F 1321-1663 [» ]
2ICF X-ray 4.10 A 23-664 [» ]
B 749-1663 [» ]
2NOJ X-ray 2.70 A/C/E/G 996-1287 [» ]
2QKI X-ray 2.40 A/D 23-665 [» ]
B/E 749-936 [» ]
C/F 1321-1663 [» ]
2WII X-ray 2.70 A 23-667 [» ]
B 749-1663 [» ]
2WIN X-ray 3.90 A/C/E/G 23-667 [» ]
B/D/F/H 749-1663 [» ]
2WY7 X-ray 1.70 A 996-1303 [» ]
2WY8 X-ray 1.70 A 996-1303 [» ]
2XQW X-ray 2.31 A/B 996-1287 [» ]
2XWB X-ray 3.49 A/C 23-664 [» ]
B/D 752-1663 [» ]
2XWJ X-ray 4.00 A/C/E/G 23-667 [» ]
B/D/F/H 749-1663 [» ]
3D5R X-ray 2.10 A/B 996-1287 [» ]
3D5S X-ray 2.30 A/B 996-1287 [» ]
3G6J X-ray 3.10 A/C 23-666 [» ]
B/D 749-1663 [» ]
3L3O X-ray 3.40 A/D 23-667 [» ]
B/E 749-954 [» ]
C/F 1321-1663 [» ]
3L5N X-ray 7.54 A 23-667 [» ]
B 749-1663 [» ]
3NMS X-ray 4.10 A 23-667 [» ]
B 749-954 [» ]
C 1321-1663 [» ]
3OED X-ray 3.16 A/B 996-1303 [» ]
3OHX X-ray 3.50 A/D 23-667 [» ]
B/E 749-954 [» ]
C/F 1321-1663 [» ]
3OXU X-ray 2.10 A/B/C 996-1303 [» ]
3RJ3 X-ray 2.35 A/B/C 996-1303 [» ]
3T4A X-ray 3.40 A/D 23-667 [» ]
B/E 749-954 [» ]
C/F 1321-1663 [» ]
4HW5 X-ray 2.25 A/B 672-748 [» ]
4HWJ X-ray 2.60 A 672-747 [» ]
4I6O X-ray 2.14 A 672-748 [» ]
4M76 X-ray 2.80 A 994-1288 [» ]
ProteinModelPortali P01024.
SMRi P01024. Positions 23-664, 673-1663.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107179. 17 interactions.
DIPi DIP-35180N.
IntActi P01024. 10 interactions.
MINTi MINT-5003988.
STRINGi 9606.ENSP00000245907.

Chemistry

BindingDBi P01024.
ChEMBLi CHEMBL4917.
DrugBanki DB00028. Intravenous Immunoglobulin.

Protein family/group databases

MEROPSi I39.950.

PTM databases

PhosphoSitei P01024.
UniCarbKBi P01024.

Polymorphism databases

DMDMi 119370332.

2D gel databases

DOSAC-COBS-2DPAGE P01024.
SWISS-2DPAGE P01024.

Proteomic databases

MaxQBi P01024.
PaxDbi P01024.
PeptideAtlasi P01024.
PRIDEi P01024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000245907 ; ENSP00000245907 ; ENSG00000125730 .
GeneIDi 718.
KEGGi hsa:718.
UCSCi uc002mfm.3. human.

Organism-specific databases

CTDi 718.
GeneCardsi GC19M006677.
GeneReviewsi C3.
H-InvDB HIX0020036.
HGNCi HGNC:1318. C3.
HPAi CAB004209.
HPA003563.
HPA020432.
MIMi 120700. gene.
611378. phenotype.
612925. phenotype.
613779. phenotype.
neXtProti NX_P01024.
Orphaneti 279. Age-related macular degeneration.
93575. Atypical hemolytic-uremic syndrome with C3 anomaly.
280133. Complement component 3 deficiency.
PharmGKBi PA25897.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG241555.
HOGENOMi HOG000286028.
HOVERGENi HBG005110.
InParanoidi P01024.
KOi K03990.
OMAi PGMPFDL.
OrthoDBi EOG77HDCX.
PhylomeDBi P01024.
TreeFami TF313285.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_118707. Regulation of Complement cascade.
REACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.
REACT_7972. Activation of C3 and C5.
REACT_8001. Alternative complement activation.

Miscellaneous databases

ChiTaRSi C3. human.
EvolutionaryTracei P01024.
GeneWikii Complement_component_3.
GenomeRNAii 718.
NextBioi 2922.
PMAP-CutDB P01024.
PROi P01024.
SOURCEi Search...

Gene expression databases

Bgeei P01024.
CleanExi HS_C3.
ExpressionAtlasi P01024. baseline and differential.
Genevestigatori P01024.

Family and domain databases

Gene3Di 1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProi IPR009048. 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 ]
Pfami PF00207. 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 ]
PRINTSi PR00004. ANAPHYLATOXN.
SMARTi SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view ]
SUPFAMi SSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human complement component C3: cDNA coding sequence and derived primary structure."
    de Bruijn M.H.L., Fey G.H.
    Proc. Natl. Acad. Sci. U.S.A. 82:708-712(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-314.
  2. SeattleSNPs variation discovery resource
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-102; LEU-314; LYS-863; ASP-1224 AND THR-1367.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The adipsin-acylation stimulating protein system and regulation of intracellular triglyceride synthesis."
    Baldo A., Sniderman A.D., St-Luce S., Avramoglu R.K., Maslowska M., Hoang B., Monge J.C., Bell A., Mulay S., Cianflone K.
    J. Clin. Invest. 92:1543-1547(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  6. "Human anaphylatoxin (C3a) from the third component of complement. Primary structure."
    Hugli T.E.
    J. Biol. Chem. 250:8293-8301(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 672-748.
  7. "Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma."
    Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L.
    J. Biol. Chem. 270:13645-13651(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 955-966, SUBUNIT.
    Tissue: Serum.
  8. "Third component of human complement: localization of the internal thiolester bond."
    Thomas M.L., Janatova J., Gray W.R., Tack B.F.
    Proc. Natl. Acad. Sci. U.S.A. 79:1054-1058(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 988-1036.
  9. "A 34-amino acid peptide of the third component of complement mediates properdin binding."
    Daoudaki M.E., Becherer J.D., Lambris J.D.
    J. Immunol. 140:1577-1580(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1409-1563.
  10. "Complement component C3b binds directly to purified glycoprotein C of herpes simplex virus types 1 and 2."
    Eisenberg R.J., Ponce de Leon M., Friedman H.M., Fries L.F., Frank M.M., Hastings J.C., Cohen G.H.
    Microb. Pathog. 3:423-435(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERPES SIMPLEX VIRUS HHV-1 AND HHV-2 GYCOPROTEIN C.
  11. "Purification and characterization of acylation stimulating protein."
    Cianflone K.M., Sniderman A.D., Walsh M.J., Vu H.T., Gagnon J., Rodriguez M.A.
    J. Biol. Chem. 264:426-430(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Structural requirements for thioester bond formation in human complement component C3. Reassessment of the role of thioester bond integrity on the conformation of C3."
    Isaac L., Isenman D.E.
    J. Biol. Chem. 267:10062-10069(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THE THIOESTER BOND REGION.
  13. "Disulfide bridges in human complement component C3b."
    Dolmer K., Sottrup-Jensen L.
    FEBS Lett. 315:85-90(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  14. "Acylation-stimulating protein (ASP) regulates glucose transport in the rat L6 muscle cell line."
    Tao Y., Cianflone K., Sniderman A.D., Colby-Germinario S.P., Germinario R.J.
    Biochim. Biophys. Acta 1344:221-229(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Coordinated release of acylation stimulating protein (ASP) and triacylglycerol clearance by human adipose tissue in vivo in the postprandial period."
    Saleh J., Summers L.K., Cianflone K., Fielding B.A., Sniderman A.D., Frayn K.N.
    J. Lipid Res. 39:884-891(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, FUNCTION.
  16. "Acylation-stimulating protein (ASP): structure-function determinants of cell surface binding and triacylglycerol synthetic activity."
    Murray I., Kohl J., Cianflone K.
    Biochem. J. 342:41-48(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "The orphan receptor C5L2 has high affinity binding sites for complement fragments C5a and C5a des Arg(74)."
    Cain S.A., Monk P.N.
    J. Biol. Chem. 277:7165-7169(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C5AR2.
  18. "The chemoattractant receptor-like protein C5L2 binds the C3a des-Arg77/acylation-stimulating protein."
    Kalant D., Cain S.A., Maslowska M., Sniderman A.D., Cianflone K., Monk P.N.
    J. Biol. Chem. 278:11123-11129(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C5AR2.
  19. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-85.
  20. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-939.
    Tissue: Plasma.
  21. "Acylation-stimulating protein: effect of acute exercise and endurance training."
    Schrauwen P., Hesselink M.K., Jain M., Cianflone K.
    Int. J. Obes. Relat. Metab. Disord. 29:632-638(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFFECTS OF EXERCISE.
  22. "C5L2 is a functional receptor for acylation-stimulating protein."
    Kalant D., MacLaren R., Cui W., Samanta R., Monk P.N., Laporte S.A., Cianflone K.
    J. Biol. Chem. 280:23936-23944(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  23. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85; ASN-939 AND ASN-1617.
    Tissue: Plasma.
  24. "Relationships among acylation stimulating protein, adiponectin and complement C3 in lean vs obese type 2 diabetes."
    Yang Y., Lu H.L., Zhang J., Yu H.Y., Wang H.W., Zhang M.X., Cianflone K.
    Int. J. Obes. Relat. Metab. Disord. 30:439-446(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH TYPE 2 DIABETES.
  25. "Targeting the signaling pathway of acylation stimulating protein."
    Maslowska M., Legakis H., Assadi F., Cianflone K.
    J. Lipid Res. 47:643-652(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  26. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
    Tissue: Platelet.
  27. "Acylation stimulating protein but not complement C3 associates with metabolic syndrome components in Chinese children and adolescents."
    Wamba P.C., Mi J., Zhao X.Y., Zhang M.X., Wen Y., Cheng H., Hou D.Q., Cianflone K.
    Eur. J. Endocrinol. 159:781-790(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH OBESITY.
  28. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
    Tissue: Liver.
  29. "C5a- and ASP-mediated C5L2 activation, endocytosis and recycling are lost in S323I-C5L2 mutation."
    Cui W., Simaan M., Laporte S., Lodge R., Cianflone K.
    Mol. Immunol. 46:3086-3098(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "Mutational analyses reveal that the staphylococcal immune evasion molecule Sbi and complement receptor 2 (CR2) share overlapping contact residues on C3d: implications for the controversy regarding the CR2/C3d cocrystal structure."
    Isenman D.E., Leung E., Mackay J.D., Bagby S., van den Elsen J.M.
    J. Immunol. 184:1946-1955(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-1029; GLU-1030; GLU-1032; GLU-1035; ARG-1042; ASP-1140; GLU-1153; ASP-1156; GLU-1159; GLU-1160; ASN-1163 AND LYS-1284, INTERACTION WITH CR2 AND S.AUREUS SBI.
  31. "Delineation of the complement receptor type 2-C3d complex by site-directed mutagenesis and molecular docking."
    Shaw C.D., Storek M.J., Young K.A., Kovacs J.M., Thurman J.M., Holers V.M., Hannan J.P.
    J. Mol. Biol. 404:697-710(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-1029; GLU-1030; GLU-1032; GLU-1110; ASP-1115; ASP-1121; ASP-1140; GLU-1153; ASP-1156; GLU-1159; GLU-1160 AND ASN-1163, INTERACTION WITH CR2.
  32. "Serum complement C3: a determinant of cardiometabolic risk, additive to the metabolic syndrome, in middle-aged population."
    Onat A., Hergenc G., Can G., Kaya Z., Yuksel H.
    Metabolism 59:628-634(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH CORONARY HEART DISEASE.
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: differences between crystal and solution conformations."
    Nettesheim D.G., Edalji R.P., Mollison K.W., Greer J., Zuiderweg E.R.P.
    Proc. Natl. Acad. Sci. U.S.A. 85:5036-5040(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF C3A.
  35. "X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2."
    Nagar B., Jones R.G., Diefenbach R.J., Isenman D.E., Rini J.M.
    Science 280:1277-1281(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF C3D.
  36. "Structure of complement receptor 2 in complex with its C3d ligand."
    Szakonyi G., Guthridge J.M., Li D., Young K., Holers V.M., Chen X.S.
    Science 292:1725-1728(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF C3D IN COMPLEX WITH CR2, MUTAGENESIS OF 1108-ILE-LEU-1109 AND ASN-1163.
  37. "Solution structure of the complex between CR2 SCR 1-2 and C3d of human complement: an X-ray scattering and sedimentation modelling study."
    Gilbert H.E., Eaton J.T., Hannan J.P., Holers V.M., Perkins S.J.
    J. Mol. Biol. 346:859-873(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY SCATTERING SOLUTION STRUCTURE OF C3D IN COMPLEX WITH CR2.
  38. "Structures of complement component C3 provide insights into the function and evolution of immunity."
    Janssen B.J.C., Huizinga E.G., Raaijmakers H.C.A., Roos A., Daha M.R., Nilsson-Ekdahl K., Nilsson B., Gros P.
    Nature 437:505-511(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF C3C, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF C3.
  39. "Structure of C3b reveals conformational changes that underlie complement activity."
    Janssen B.J.C., Christodoulidou A., McCarthy A., Lambris J.D., Gros P.
    Nature 444:213-216(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF C3B.
  40. "Structure of C3b in complex with CRIg gives insights into regulation of complement activation."
    Wiesmann C., Katschke K.J., Yin J., Helmy K.Y., Steffek M., Fairbrother W.J., McCallum S.A., Embuscado L., DeForge L., Hass P.E., van Lookeren Campagne M.
    Nature 444:217-220(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF C3C IN COMPLEX WITH VSIG4, X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF C3B IN COMPLEX WITH VSIG4, GLYCOSYLATION AT ASN-85 AND ASN-939.
  41. "Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition."
    Janssen B.J., Halff E.F., Lambris J.D., Gros P.
    J. Biol. Chem. 282:29241-29247(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-936 AND 1321-1663 IN COMPLEX WITH INHIBITOR COMPSTATIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-85.
  42. "A structural basis for complement inhibition by Staphylococcus aureus."
    Hammel M., Sfyroera G., Ricklin D., Magotti P., Lambris J.D., Geisbrecht B.V.
    Nat. Immunol. 8:430-437(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 996-1287 IN COMPLEX WITH S.AUREUS FIB.
  43. "A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d."
    Clark E.A., Crennell S., Upadhyay A., Zozulya A.V., Mackay J.D., Svergun D.I., Bagby S., van den Elsen J.M.
    Mol. Immunol. 48:452-462(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 996-1303 IN COMPLEX WITH S.AUREUS SBI, SUBUNIT.
  44. "A crystal structure of the complex between human complement receptor 2 and its ligand C3d."
    van den Elsen J.M., Isenman D.E.
    Science 332:608-611(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 996-1303 IN COMPLEX WITH CR2, INTERACTION WITH CR2.
  45. "The difference between human C3F and C3S results from a single amino acid change from an asparagine to an aspartate residue at position 1216 on the alpha-chain of the complement component, C3."
    Poznansky M.C., Clissold P.M., Lachmann P.J.
    J. Immunol. 143:1254-1258(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT C3S ASN-1216.
  46. Erratum
    Poznansky M.C., Clissold P.M., Lachmann P.J.
    J. Immunol. 143:3860-3862(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: RETRACTION.
  47. "Molecular basis of polymorphisms of human complement component C3."
    Botto M., Yong Fong K., So A.K., Koch C., Walport M.J.
    J. Exp. Med. 172:1011-1017(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLY-102 AND LEU-314.
  48. "Inherited human complement C3 deficiency. An amino acid substitution in the beta-chain (Asp549 to Asn) impairs C3 secretion."
    Singer L., Whitehead W.T., Akama H., Katz Y., Fishelson Z., Wetsel R.A.
    J. Biol. Chem. 269:28494-28499(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT C3D ASN-549.
  49. "A novel C3 allotype C3'F02'has an amino acid substitution that may inhibit iC3b synthesis and cause C3-hypocomplementemia."
    Watanabe Y., Matsui N., Yan K., Nishimukai H., Tokunaga K., Juji T., Kobayashi N., Kohsaka T.
    Mol. Immunol. 30:62-62(1993)
    Cited for: VARIANT C3D GLN-1320.
  50. Cited for: ASSOCIATION OF VARIANT GLY-102 WITH ARMD9.
  51. Cited for: VARIANTS AHUS5 GLN-592; TRP-592; TRP-735; VAL-1094; ASN-1115; TRP-1158; LYS-1161 AND ASP-1464, CHARACTERIZATION OF VARIANTS AHUS5 GLN-592; TRP-592; VAL-1094; ASN-1115 AND LYS-1161.
  52. "Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome."
    Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.
    Hum. Mutat. 31:E1445-E1460(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AHUS5 VAL-603 AND LEU-1042.
  53. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."
    Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
    J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-549, IDENTIFICATION BY MASS SPECTROMETRY.
  54. "Common polymorphisms in C3, factor B, and factor H collaborate to determine systemic complement activity and disease risk."
    Heurich M., Martinez-Barricarte R., Francis N.J., Roberts D.L., Rodriguez de Cordoba S., Morgan B.P., Harris C.L.
    Proc. Natl. Acad. Sci. U.S.A. 108:8761-8766(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT GLY-102.
  55. Cited for: VARIANT ARMD9 GLN-155, CHARACTERIZATION OF VARIANT ARMD9 GLN-155.

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: October 29, 2014
This is version 188 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

External Data

Dasty 3