P01024 (CO3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement C3

Alternative name(s):
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1

Cleaved into the following 11 chains:

1. Complement C3 beta chain
2. Complement C3 alpha chain
3. C3a anaphylatoxin
4. Acylation stimulating protein
   Short name=ASP
   Alternative name(s):
   C3adesArg
5. Complement C3b alpha' chain
6. Complement C3c alpha' chain fragment 1
7. Complement C3dg fragment
8. Complement C3g fragment
9. Complement C3d fragment
10. Complement C3f fragment
11. Complement C3c alpha' chain fragment 2

Gene names

Name:	C3
Synonyms:	CPAMD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.11 Ref.14 Ref.15 Ref.16 Ref.22 Ref.25 Ref.29 Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. Ref.5 Ref.11 Ref.14 Ref.15 Ref.16 Ref.22 Ref.25 Ref.29 Acylation stimulating protein (ASP): 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 GPR77. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of GPR77. Ref.5 Ref.11 Ref.14 Ref.15 Ref.16 Ref.22 Ref.25 Ref.29
Subunit structure	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 GPR77; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of GPR77, recruitment of ARRB2 to the cell surface and endocytosis of GRP77. Ref.7 Ref.10 Ref.17 Ref.18 Ref.30 Ref.31 Ref.43 Ref.44
Subcellular location	Secreted.
Tissue specificity	Plasma. The acylation stimulating protein (ASP) is expressed in adiopocytes and released into the plasma during both the fasting and postprandial periods. Ref.15 Ref.22
Post-translational modification	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.
Polymorphism	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.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32 Ref.35 Ref.36 Ref.37 Ref.48 Ref.49 Age-related macular degeneration 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.32 Ref.50 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype. Ref.32 Ref.51 Ref.52 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. Ref.32
Sequence similarities	Contains 1 anaphylatoxin-like domain. Contains 1 NTR domain.
Caution	According to Ref.44, the interaction surface between C3 and CR2 reported in Ref.36 is artifactual and can be ascribed to the presence of zinc acetate in the buffer.

Ontologies

Keywords
Biological process	Complement alternate pathway Complement pathway Fatty acid metabolism Immunity Inflammatory response Innate immunity Lipid metabolism
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Age-related macular degeneration Disease mutation Hemolytic uremic syndrome
Domain	Signal
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Thioester bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Traceable author statement PubMed 9164946. Source: ProtInc complement activation, alternative pathway Traceable author statement. Source: Reactome complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of endopeptidase activity Inferred from electronic annotation. Source: GOC positive regulation of G-protein coupled receptor protein signaling pathway Inferred from direct assay Ref.22. Source: UniProtKB positive regulation of activation of membrane attack complex Inferred from electronic annotation. Source: Compara positive regulation of angiogenesis Inferred from electronic annotation. Source: Compara positive regulation of glucose transport Inferred from direct assay Ref.22Ref.14. Source: UniProtKB positive regulation of lipid storage Inferred from direct assay Ref.15. Source: UniProtKB positive regulation of phagocytosis Inferred from electronic annotation. Source: Compara positive regulation of protein phosphorylation Inferred from direct assay Ref.22. Source: UniProtKB positive regulation of type IIa hypersensitivity Inferred from electronic annotation. Source: Compara positive regulation vascular endothelial growth factor production Inferred from direct assay PubMed 16452172. Source: BHF-UCL regulation of complement activation Traceable author statement. Source: Reactome regulation of triglyceride biosynthetic process Inferred from direct assay Ref.16. Source: UniProtKB
Cellular_component	extracellular space Inferred from electronic annotation. Source: InterPro extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Molecular_function	C5L2 anaphylatoxin chemotactic receptor binding Inferred from direct assay Ref.22. Source: UniProtKB endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VSIG4	Q9Y279-1	5	EBI-905851,EBI-903144
VSIG4	Q9Y279-2	2	EBI-905851,EBI-903148

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.5

Chain

23 – 1663

1641

Complement C3

PRO_0000005907

Chain

23 – 667

645

Complement C3 beta chain

PRO_0000005908

Chain

672 – 1663

992

Complement C3 alpha chain

PRO_0000005909

Chain

672 – 748

77

C3a anaphylatoxin

PRO_0000005910

Chain

672 – 747

76

Acylation stimulating protein

PRO_0000419935

Chain

749 – 1663

915

Complement C3b alpha' chain

PRO_0000005911

Chain

749 – 954

206

Complement C3c alpha' chain fragment 1

PRO_0000005912

Chain

955 – 1303

349

Complement C3dg fragment

PRO_0000005913

Chain

955 – 1001

47

Complement C3g fragment

PRO_0000005914

Chain

1002 – 1303

302

Complement C3d fragment

PRO_0000005915

Peptide

1304 – 1320

17

Complement C3f fragment

PRO_0000005916

Chain

1321 – 1663

343

Complement C3c alpha' chain fragment 2

PRO_0000273948

Regions

Domain

693 – 728

36

Anaphylatoxin-like

Domain

1518 – 1661

144

NTR

Region

1424 – 1456

33

Properdin-binding

Sites

Site

747 – 748

2

Cleavage; by carboxypeptidases

Site

748 – 749

2

Cleavage; by C3 convertase

Site

954 – 955

2

Cleavage; by factor I Potential

Site

1303 – 1304

2

Cleavage; by factor I

Site

1320 – 1321

2

Cleavage; by factor I

Amino acid modifications

Modified residue

489

1

Phosphotyrosine By similarity

Glycosylation

85

1

N-linked (GlcNAc...) Ref.1 Ref.19 Ref.23 Ref.26 Ref.28 Ref.40 Ref.41

Glycosylation

939

1

N-linked (GlcNAc...) Ref.20 Ref.23 Ref.40

Glycosylation

1617

1

N-linked (GlcNAc...) Ref.23

Disulfide bond

559 ↔ 816

Interchain (between beta and alpha chains) Ref.13 Ref.41

Disulfide bond

627 ↔ 662

Ref.13 Ref.41

Disulfide bond

693 ↔ 720

Ref.13 Ref.41

Disulfide bond

694 ↔ 727

Ref.13 Ref.41

Disulfide bond

707 ↔ 728

Ref.13 Ref.41

Disulfide bond

873 ↔ 1513

Ref.13 Ref.41

Disulfide bond

1101 ↔ 1158

Ref.13 Ref.41

Disulfide bond

1358 ↔ 1489

Ref.13 Ref.41

Disulfide bond

1389 ↔ 1458

Ref.13 Ref.41

Disulfide bond

1506 ↔ 1511

Ref.13 Ref.41

Disulfide bond

1518 ↔ 1590

Ref.13 Ref.41

Disulfide bond

1537 ↔ 1661

Ref.13 Ref.41

Disulfide bond

1637 ↔ 1646

Ref.13 Ref.41

Cross-link

1010 ↔ 1013

Isoglutamyl cysteine thioester (Cys-Gln)

Natural variations

Natural variant

102

1

R → G in allele C3F; associated with ARMD9. Ref.2 Ref.47 Ref.50
Corresponds to variant rs2230199 [ dbSNP | Ensembl ].

VAR_001983

Natural variant

314

1

P → L. Ref.1 Ref.2 Ref.47
Corresponds to variant rs1047286 [ dbSNP | Ensembl ].

VAR_001984

Natural variant

469

1

E → D.
Corresponds to variant rs11569422 [ dbSNP | Ensembl ].

VAR_020262

Natural variant

549

1

D → N in C3D; impairs secretion; variant confirmed at protein level. Ref.48 Ref.53

VAR_001985

Natural variant

592

1

R → Q in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. Ref.51

VAR_063213

Natural variant

592

1

R → W in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. Ref.51

VAR_063214

Natural variant

603

1

F → V in AHUS5. Ref.52

VAR_063654

Natural variant

735

1

R → W in AHUS5. Ref.51

VAR_063215

Natural variant

863

1

R → K. Ref.2
Corresponds to variant rs11569472 [ dbSNP | Ensembl ].

VAR_019206

Natural variant

1042

1

R → L in AHUS5. Ref.52

VAR_063655

Natural variant

1094

1

A → V in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. Ref.51

VAR_063216

Natural variant

1115

1

D → N in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. Ref.51

VAR_063217

Natural variant

1158

1

C → W in AHUS5. Ref.51

VAR_063218

Natural variant

1161

1

Q → K in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I. Ref.51

VAR_063219

Natural variant

1216

1

D → N in C3S. Ref.45

VAR_022761

Natural variant

1224

1

G → D. Ref.2
Corresponds to variant rs11569534 [ dbSNP | Ensembl ].

VAR_019207

Natural variant

1320

1

R → Q in C3D; allotype C3'F02'; may inhibit IC3B synthesis. Ref.49

VAR_001986

Natural variant

1367

1

I → T. Ref.2
Corresponds to variant rs11569541 [ dbSNP | Ensembl ].

VAR_019208

Natural variant

1464

1

H → D in AHUS5. Ref.51

VAR_063220

Natural variant

1521

1

Q → R.
Corresponds to variant rs7256789 [ dbSNP | Ensembl ].

VAR_029792

Natural variant

1601

1

H → N.
Corresponds to variant rs1803225 [ dbSNP | Ensembl ].

VAR_029793

Natural variant

1619

1

S → R.
Corresponds to variant rs2230210 [ dbSNP | Ensembl ].

VAR_029326

Experimental info

Mutagenesis

1029

1

D → A: Minor effect on binding of C3d to CR2. Ref.12 Ref.30 Ref.31

Mutagenesis

1030

1

E → A: Impaired binding of C3d to CR2. Ref.12 Ref.30 Ref.31

Mutagenesis

1032

1

E → A: Impaired binding of C3d to CR2. Ref.12 Ref.30 Ref.31

Mutagenesis

1035

1

E → A: No effect on binding of C3d to CR2. Ref.12 Ref.30

Mutagenesis

1042

1

R → M: Impaired binding of C3d to CR2. Ref.12 Ref.30

Mutagenesis

1108 – 1109

2

IL → RR: Impaired binding of C3d to CR2; when associated with A-1163. Ref.12

Mutagenesis

1110

1

E → A: No effect on binding of C3d to CR2. Ref.12 Ref.31

Mutagenesis

1115

1

D → A: No effect on binding of C3d to CR2. Ref.12 Ref.31

Mutagenesis

1121

1

D → A: No effect on binding of C3d to CR2. Ref.12 Ref.31

Mutagenesis

1140

1

D → A: No effect on binding of C3d to CR2. Ref.12 Ref.30 Ref.31

Mutagenesis

1153

1

E → A: Impaired binding of C3d to CR2. Ref.12 Ref.30 Ref.31

Mutagenesis

1156

1

D → A: Impaired binding of C3d to CR2. Ref.12 Ref.30 Ref.31

Mutagenesis

1159

1

E → A: Impaired binding of C3d to CR2. Ref.12 Ref.30 Ref.31

Mutagenesis

1160

1

E → A: Minor effect on binding of C3d to CR2. Ref.12 Ref.30 Ref.31

Mutagenesis

1163

1

N → A: No effect on binding of C3d to CR2. Impaired binding of C3d to CR2; when associated with 1108-R-R-1109. Ref.12 Ref.30 Ref.31 Ref.36

Mutagenesis

1163

1

N → R: Impaired binding of C3d to CR2. Ref.12 Ref.30 Ref.31 Ref.36

Mutagenesis

1284

1

K → A: Impaired binding of C3d to CR2. Ref.12 Ref.30

Sequence conflict

681

1

D → N AA sequence Ref.6

Sequence conflict

700

1

E → Q AA sequence Ref.6

Sequence conflict

1026

1

H → S AA sequence Ref.8

Secondary structure

1

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1663

Helix Strand Turn

Details...

Helix

675 – 684

10

Helix

688 – 697

10

Helix

707 – 710

4

Turn

712 – 714

3

Helix

718 – 743

26

Helix

997 – 999

3

Helix

1001 – 1003

3

Helix

1013 – 1031

19

Helix

1034 – 1037

4

Helix

1041 – 1057

17

Beta strand

1068 – 1072

5

Helix

1076 – 1089

14

Turn

1090 – 1092

3

Helix

1097 – 1111

15

Turn

1114 – 1116

3

Helix

1127 – 1133

7

Helix

1139 – 1158

20

Turn

1159 – 1161

3

Helix

1165 – 1179

15

Helix

1180 – 1182

3

Helix

1186 – 1198

13

Helix

1204 – 1213

10

Turn

1216 – 1218

3

Beta strand

1223 – 1225

3

Helix

1226 – 1243

18

Turn

1246 – 1248

3

Helix

1249 – 1258

10

Helix

1269 – 1285

17

Sequences

	Sequence		Length	Mass (Da)
	P01024 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 30C2832A9E75FFC4	FASTA	1,663	187,148
	10 20 30 40 50 60 MGPTSGPSLL LLLLTHLPLA LGSPMYSIIT PNILRLESEE TMVLEAHDAQ GDVPVTVTVH 70 80 90 100 110 120 DFPGKKLVLS SEKTVLTPAT NHMGNVTFTI PANREFKSEK GRNKFVTVQA TFGTQVVEKV 130 140 150 160 170 180 VLVSLQSGYL FIQTDKTIYT PGSTVLYRIF TVNHKLLPVG RTVMVNIENP EGIPVKQDSL 190 200 210 220 230 240 SSQNQLGVLP LSWDIPELVN MGQWKIRAYY ENSPQQVFST EFEVKEYVLP SFEVIVEPTE 250 260 270 280 290 300 KFYYIYNEKG LEVTITARFL YGKKVEGTAF VIFGIQDGEQ RISLPESLKR IPIEDGSGEV 310 320 330 340 350 360 VLSRKVLLDG VQNPRAEDLV GKSLYVSATV ILHSGSDMVQ AERSGIPIVT SPYQIHFTKT 370 380 390 400 410 420 PKYFKPGMPF DLMVFVTNPD GSPAYRVPVA VQGEDTVQSL TQGDGVAKLS INTHPSQKPL 430 440 450 460 470 480 SITVRTKKQE LSEAEQATRT MQALPYSTVG NSNNYLHLSV LRTELRPGET LNVNFLLRMD 490 500 510 520 530 540 RAHEAKIRYY TYLIMNKGRL LKAGRQVREP GQDLVVLPLS ITTDFIPSFR LVAYYTLIGA 550 560 570 580 590 600 SGQREVVADS VWVDVKDSCV GSLVVKSGQS EDRQPVPGQQ MTLKIEGDHG ARVVLVAVDK 610 620 630 640 650 660 GVFVLNKKNK LTQSKIWDVV EKADIGCTPG SGKDYAGVFS DAGLTFTSSS GQQTAQRAEL 670 680 690 700 710 720 QCPQPAARRR RSVQLTEKRM DKVGKYPKEL RKCCEDGMRE NPMRFSCQRR TRFISLGEAC 730 740 750 760 770 780 KKVFLDCCNY ITELRRQHAR ASHLGLARSN LDEDIIAEEN IVSRSEFPES WLWNVEDLKE 790 800 810 820 830 840 PPKNGISTKL MNIFLKDSIT TWEILAVSMS DKKGICVADP FEVTVMQDFF IDLRLPYSVV 850 860 870 880 890 900 RNEQVEIRAV LYNYRQNQEL KVRVELLHNP AFCSLATTKR RHQQTVTIPP KSSLSVPYVI 910 920 930 940 950 960 VPLKTGLQEV EVKAAVYHHF ISDGVRKSLK VVPEGIRMNK TVAVRTLDPE RLGREGVQKE 970 980 990 1000 1010 1020 DIPPADLSDQ VPDTESETRI LLQGTPVAQM TEDAVDAERL KHLIVTPSGC GEQNMIGMTP 1030 1040 1050 1060 1070 1080 TVIAVHYLDE TEQWEKFGLE KRQGALELIK KGYTQQLAFR QPSSAFAAFV KRAPSTWLTA 1090 1100 1110 1120 1130 1140 YVVKVFSLAV NLIAIDSQVL CGAVKWLILE KQKPDGVFQE DAPVIHQEMI GGLRNNNEKD 1150 1160 1170 1180 1190 1200 MALTAFVLIS LQEAKDICEE QVNSLPGSIT KAGDFLEANY MNLQRSYTVA IAGYALAQMG 1210 1220 1230 1240 1250 1260 RLKGPLLNKF LTTAKDKNRW EDPGKQLYNV EATSYALLAL LQLKDFDFVP PVVRWLNEQR 1270 1280 1290 1300 1310 1320 YYGGGYGSTQ ATFMVFQALA QYQKDAPDHQ ELNLDVSLQL PSRSSKITHR IHWESASLLR 1330 1340 1350 1360 1370 1380 SEETKENEGF TVTAEGKGQG TLSVVTMYHA KAKDQLTCNK FDLKVTIKPA PETEKRPQDA 1390 1400 1410 1420 1430 1440 KNTMILEICT RYRGDQDATM SILDISMMTG FAPDTDDLKQ LANGVDRYIS KYELDKAFSD 1450 1460 1470 1480 1490 1500 RNTLIIYLDK VSHSEDDCLA FKVHQYFNVE LIQPGAVKVY AYYNLEESCT RFYHPEKEDG 1510 1520 1530 1540 1550 1560 KLNKLCRDEL CRCAEENCFI QKSDDKVTLE ERLDKACEPG VDYVYKTRLV KVQLSNDFDE 1570 1580 1590 1600 1610 1620 YIMAIEQTIK SGSDEVQVGQ QRTFISPIKC REALKLEEKK HYLMWGLSSD FWGEKPNLSY 1630 1640 1650 1660 IIGKDTWVEH WPEEDECQDE ENQKQCQDLG AFTESMVVFG CPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY, FUNCTION OF ACYLATION STIMULATING PROTEIN.
[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 OF ACYLATION STIMULATING PROTEIN.
[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 OF ACYLATION STIMULATING PROTEIN.
[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 OF ACYLATION STIMULATING PROTEIN 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 OF ACYLATION STIMULATING PROTEIN.
[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 GPR77.
[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 OF ACYLATION STIMULATING PROTEIN WITH GPR77.
[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, MASS SPECTROMETRY. 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 ON ACYLATION STIMULATING PROTEIN PRODUCTION.
[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 OF ACYLATION STIMULATING PROTEIN AS LIGAND FOR GPR77, 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, MASS SPECTROMETRY. 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 OF ACYLATION STIMULATING PROTEIN BY MASS SPECTROMETRY, FUNCTION OF ACYLATION STIMULATING PROTEIN.
[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, MASS SPECTROMETRY. 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 OF ACYLATION STIMULATING PROTEIN 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, MASS SPECTROMETRY. 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 OF ACYLATION STIMULATING PROTEIN AS LIGAND FOR GPR77.
[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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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]	"Complement C3 variant and the risk of age-related macular degeneration." Yates J.R.W., Sepp T., Matharu B.K., Khan J.C., Thurlby D.A., Shahid H., Clayton D.G., Hayward C., Morgan J., Wright A.F., Armbrecht A.M., Dhillon B., Deary I.J., Redmond E., Bird A.C., Moore A.T. N. Engl. J. Med. 357:553-561(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF VARIANT GLY-102 WITH ARMD9.
[51]	"Mutations in complement C3 predispose to development of atypical hemolytic uremic syndrome." Fremeaux-Bacchi V., Miller E.C., Liszewski M.K., Strain L., Blouin J., Brown A.L., Moghal N., Kaplan B.S., Weiss R.A., Lhotta K., Kapur G., Mattoo T., Nivet H., Wong W., Gie S., Hurault de Ligny B., Fischbach M., Gupta R. , Hauhart R., Meunier V., Loirat C., Dragon-Durey M.A., Fridman W.H., Janssen B.J., Goodship T.H., Atkinson J.P. Blood 112:4948-4952(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

C3base

C3 mutation db

GeneReviews

Wikipedia

Complement C3 entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00783987.

PIR

C3HU. A94065.

RefSeq

NP_000055.2. NM_000064.2.

UniGene

Hs.529053.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P01024.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35180N.

IntAct

P01024. 5 interactions.

MINT

MINT-5003988.

STRING

9606.ENSP00000245907.

Protein family/group databases

MEROPS

I39.950.

PTM databases

GlycoSuiteDB

P01024.

PhosphoSite

P01024.

Polymorphism databases

DMDM

119370332.

2D gel databases

DOSAC-COBS-2DPAGE

P01024.

SWISS-2DPAGE

P01024.

Proteomic databases

PaxDb

P01024.

PeptideAtlas

P01024.

PRIDE

P01024.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000245907; ENSP00000245907; ENSG00000125730.

GeneID

718.

KEGG

hsa:718.

UCSC

uc002mfm.3. human.

Organism-specific databases

CTD

718.

GeneCards

GC19M006677.

H-InvDB

HIX0020036.

HGNC

HGNC:1318. C3.

HPA

CAB004209.
HPA003563.
HPA020432.

MIM

120700. gene.
611378. phenotype.
612925. phenotype.
613779. phenotype.

neXtProt

NX_P01024.

Orphanet

279. Age-related macular degeneration.
93575. Atypical hemolytic uremic syndrome with C3 anomaly.
280133. Complement component 3 deficiency.

PharmGKB

PA25897.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG241555.

HOGENOM

HOG000286028.

HOVERGEN

HBG005110.

InParanoid

P01024.

KO

K03990.

OMA

AYYTLIG.

OrthoDB

EOG41G337.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P01024.

Bgee

P01024.

CleanEx

HS_C3.

Genevestigator

P01024.

GermOnline

ENSG00000125730. Homo sapiens.

Family and domain databases

Gene3D

1.20.91.20. 1 hit.
2.60.40.690. 1 hit.

InterPro

IPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_.
IPR001840. Anaphylatoxn.
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]

Pfam

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]

PRINTS

PR00004. ANAPHYLATOXN.

SMART

SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]

SUPFAM

SSF49410. AM_receptor_bind. 1 hit.
SSF47686. Anaphylatoxin. 1 hit.
SSF48239. Terp_cyc_toroid. 1 hit.
SSF50242. TIMP_like. 1 hit.

PROSITE

PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P01024.

ChEMBL

CHEMBL4917.

ChiTaRS

C3. human.

EvolutionaryTrace

P01024.

GenomeRNAi

718.

NextBio

2922.

PMAP-CutDB

P01024.

SOURCE

Search...

Entry information

Entry name

CO3_HUMAN

Accession

Primary (citable) accession number: P01024
Secondary accession number(s): A7E236

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 12, 2006
Last modified:	May 29, 2013
This is version 172 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.