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Protein

Complement C3

Gene

C3

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates (By similarity).By similarity
Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity).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 post-prandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-internalization and recycling of C5AR2 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Protein family/group databases

MEROPSiI39.950.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:C3
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 16611639Complement C3PRO_0000419922Add
BLAST
Chaini23 – 665643Complement C3 beta chainBy similarityPRO_0000419923Add
BLAST
Chaini567 – 66599C3-beta-cBy similarityPRO_0000430432Add
BLAST
Chaini670 – 1661992Complement C3 alpha chainBy similarityPRO_0000419924Add
BLAST
Chaini670 – 74677C3a anaphylatoxinPRO_0000419925Add
BLAST
Chaini670 – 74576Acylation stimulating proteinBy similarityPRO_0000419926Add
BLAST
Chaini747 – 1661915Complement C3b alpha' chainBy similarityPRO_0000419927Add
BLAST
Chaini747 – 953207Complement C3c alpha' chain fragment 1By similarityPRO_0000419928Add
BLAST
Chaini954 – 1302349Complement C3dg fragmentBy similarityPRO_0000419929Add
BLAST
Chaini954 – 100047Complement C3g fragmentBy similarityPRO_0000419930Add
BLAST
Chaini1001 – 1302302Complement C3d fragmentBy similarityPRO_0000419931Add
BLAST
Peptidei1303 – 131917Complement C3f fragmentBy similarityPRO_0000419932Add
BLAST
Chaini1320 – 1661342Complement C3c alpha' chain fragment 2By similarityPRO_0000419933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei70 – 701PhosphoserineBy similarity
Modified residuei302 – 3021PhosphoserineBy similarity
Disulfide bondi557 ↔ 814Interchain (between beta and alpha chains)PROSITE-ProRule annotation
Disulfide bondi625 ↔ 660By similarity
Modified residuei670 – 6701PhosphoserineBy similarity
Disulfide bondi691 ↔ 718By similarity
Disulfide bondi692 ↔ 725By similarity
Disulfide bondi705 ↔ 726By similarity
Disulfide bondi871 ↔ 1511By similarity
Glycosylationi937 – 9371N-linked (GlcNAc...)Sequence analysis
Modified residuei966 – 9661PhosphoserineBy similarity
Cross-linki1008 ↔ 1011Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Disulfide bondi1099 ↔ 1156By similarity
Modified residuei1319 – 13191PhosphoserineBy similarity
Disulfide bondi1356 ↔ 1487By similarity
Disulfide bondi1387 ↔ 1456By similarity
Disulfide bondi1504 ↔ 1509By similarity
Disulfide bondi1516 ↔ 1588By similarity
Disulfide bondi1535 ↔ 1659By similarity
Modified residuei1571 – 15711PhosphoserineBy similarity
Glycosylationi1615 – 16151N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1635 ↔ 1644By similarity

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 carboxylases to release the C-termianl 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 (By similarity).By similarity
Phosphorylated by FAM20C in the extracellular medium.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei745 – 7462Cleavage; by carboxypeptidasesBy similarity
Sitei746 – 7472Cleavage; by C3 convertaseBy similarity
Sitei1301 – 13022Cleavage; by factor IBy similarity
Sitei1318 – 13192Cleavage; by factor IBy similarity

Keywords - PTMi

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

Proteomic databases

PeptideAtlasiP01025.

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). Interacts with VSIG4. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
gCC7EYC82EBI-11688674,EBI-11688666From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

IntActiP01025. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP01025.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini691 – 72636Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini1516 – 1659144NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1422 – 145433Properdin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP01025.
KOiK03990.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P01025-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTSGPRLL LLLLTSLPLA LGDPIYTIIT PNVLRLESEE MVVLEAHEGQ
60 70 80 90 100
GDIRVSVTVH DFPAKRQVLS SETTTLNNAN NYLSTVNIKI PASKEFKSEK
110 120 130 140 150
GHKFVTVQAL FGNVQVEKVV LVSLQSGYLF IQTDKTIYTP GSTVLYRIFT
160 170 180 190 200
VDHKLLPVGQ TIVVTIETPE GIDIKRDSLS SHNQFGILAL SWNIPELVNM
210 220 230 240 250
GQWKIRAHYE DAPQQVFSAE FEVKEYVLPS FEVQVEPSEK FYYIDDPNGL
260 270 280 290 300
TVNIIARFLY GESVDGTAFV IFGVQDGDQR ISLSQSLTRV PIIDGTGEAT
310 320 330 340 350
LSQGVLLNGV HYSSVNDLVG KSIYVSVTVI LNSGSDMVEA ERTGIPIVTS
360 370 380 390 400
PYQIHFTKTP KFFKPAMPFD LMVYVTNPDG SPARHIPVVT EDFKVRSLTQ
410 420 430 440 450
EDGVAKLSIN TPDNRNSLPI TVRTEKDGIP AARQASKTMH VLPYNTQGNS
460 470 480 490 500
KNYLHLSLPR VELKPGENLN VNFHLRTDPG YQDKIRYFTY LIMNKGKLLK
510 520 530 540 550
VGRQPRESGQ VVVVLPLTIT TDFIPSFRLV AYYTLIAANG QREVVADSVW
560 570 580 590 600
VDVKDSCVGT LVVKGGGKQD KQHRPGQQMT LEIQGERGAR VGLVAVDKGV
610 620 630 640 650
FVLNKKNKLT QRRIWDVVEK ADIGCTPGSG KDFAGVFTDA GLAFKSSKGL
660 670 680 690 700
QTPQRADLEC PKPAARKRRS VQLMEKRMDK LGQYSKDVRR CCEHGMRDNP
710 720 730 740 750
MKFSCQRRAQ FIQHGDACVK AFLDCCEYIA KLRQQHSRNK PLGLARSDLD
760 770 780 790 800
EEIIPEEDII SRSQFPESWL WTIEEFKEPD KNGISTKTMN VFLKDSITTW
810 820 830 840 850
EILAVSLSDK KGICVADPYE VVVKQDFFID LRLPYSVVRN EQVEIRAILY
860 870 880 890 900
NYREAEDLKV RVELLYNPAF CSLATAKKRH QQTLTVPAKS SVPVPYIIVP
910 920 930 940 950
LKTGLQEVEV KAAVYNHFIS DGVKKTLKVV PEGMRVNKTV VTRTLDPEHK
960 970 980 990 1000
GQQGVQREEI PPADLSDQVP DTESETKILL QGTPVAQMVE DAIDGDRLKH
1010 1020 1030 1040 1050
LIQTPSGCGE QNMIGMTPTV IAVHYLDSTE QWEKFGLEKR QEALELIKKG
1060 1070 1080 1090 1100
YTQQLAFRQK NSAFAAFQDR LSSTLLTAYV VKVFAMAANL IAIDSQVLCG
1110 1120 1130 1140 1150
AVKWLILEKQ KPDGVFEENG PVIHQEMIGG FKNTEEKDVS LTAFVLIALQ
1160 1170 1180 1190 1200
EAKDICEPQV NSLLRSINKA RDFLADYYLE LKRPYTVAIA GYALALSDKL
1210 1220 1230 1240 1250
DEPFLNKLLS TAKERNRWEE PGQKLHNVEA TSYALLALLV VKDFDSVPPI
1260 1270 1280 1290 1300
VRWLNEQRYY GGGYGSTQAT FMVFQALAQY QKDVPDHKDL NLDVSIHLPS
1310 1320 1330 1340 1350
RSAPVRHRIL WESASLLRSE ETKENEGFTL IAEGKGQGTL SVVTMYHGKA
1360 1370 1380 1390 1400
KGKTTCKKFD LKVSIHPAPE PVKKPQEAKS SMVLDICTRY LGNQDATMSI
1410 1420 1430 1440 1450
LDISMMTGFS PDTEDLKLLS TGVDRYISKY ELNKALSNKN TLIIYLDKIS
1460 1470 1480 1490 1500
HTLEDCISFK VHQYFNVGLI QPGSVKVYSY YNLDESCTRF YHPEKEDGML
1510 1520 1530 1540 1550
NKLCHKEMCR CAEENCFMHH DEEEVTLDDR LERACEPGVD YVYKTRLLKK
1560 1570 1580 1590 1600
ELSDDFDDYI MVIEQIIKSG SDEVQVGQER RFISHIKCRE ALKLKEGGHY
1610 1620 1630 1640 1650
LVWGVSSDLW GEKPNISYII GKDTWVELWP DGDVCQDEEN QKQCQDLANF
1660
SENMVVFGCP N
Length:1,661
Mass (Da):186,807
Last modified:October 31, 2012 - v2
Checksum:i4899D0914BE3310C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti679 – 6791D → N AA sequence (PubMed:956663).Curated
Sequence conflicti687 – 6882DV → EL AA sequence (PubMed:956663).Curated
Sequence conflicti698 – 6981D → N AA sequence (PubMed:956663).Curated
Sequence conflicti713 – 7164QHGD → HQGN AA sequence (PubMed:956663).Curated
Sequence conflicti724 – 7241D → N AA sequence (PubMed:956663).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF154933 mRNA. Translation: AAG40565.1.
AJ494748 Genomic DNA. Translation: CAD38823.2.
AF110278 mRNA. Translation: AAC99785.1.
PIRiA01259.
RefSeqiNP_999174.1. NM_214009.1.
UniGeneiSsc.61.

Genome annotation databases

GeneIDi397072.
KEGGissc:397072.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF154933 mRNA. Translation: AAG40565.1.
AJ494748 Genomic DNA. Translation: CAD38823.2.
AF110278 mRNA. Translation: AAC99785.1.
PIRiA01259.
RefSeqiNP_999174.1. NM_214009.1.
UniGeneiSsc.61.

3D structure databases

ProteinModelPortaliP01025.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01025. 1 interaction.

Protein family/group databases

MEROPSiI39.950.

Proteomic databases

PeptideAtlasiP01025.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397072.
KEGGissc:397072.

Organism-specific databases

CTDi718.

Phylogenomic databases

InParanoidiP01025.
KOiK03990.

Family and domain databases

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

Entry informationi

Entry nameiCO3_PIG
AccessioniPrimary (citable) accession number: P01025
Secondary accession number(s): O97940, Q9GKP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 31, 2012
Last modified: September 7, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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