UniProtKB - P01025 (CO3_PIG)
Complement C3
C3
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 1661 | Coordinates Mg2+ for interaction with Complement factor B Bb fragmentBy similarity | 1 |
GO - Molecular functioni
- C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
- endopeptidase inhibitor activity Source: InterPro
GO - Biological processi
- complement activation, alternative pathway Source: UniProtKB-KW
- complement activation, classical pathway Source: UniProtKB-KW
- fatty acid metabolic process Source: UniProtKB-KW
- inflammatory response Source: UniProtKB-KW
- innate immune response Source: AgBase
- positive regulation of glucose transmembrane transport Source: UniProtKB
- positive regulation of G protein-coupled receptor signaling pathway Source: UniProtKB
- positive regulation of lipid storage Source: UniProtKB
- positive regulation of protein phosphorylation Source: UniProtKB
- regulation of triglyceride biosynthetic process Source: UniProtKB
Keywordsi
Biological process | Complement alternate pathway, Complement pathway, Fatty acid metabolism, Immunity, Inflammatory response, Innate immunity, Lipid metabolism |
Protein family/group databases
MEROPSi | I39.950 |
Names & Taxonomyi
Protein namesi | Recommended name: Complement C3Cleaved into the following 12 chains: Alternative name(s): C3adesArg |
Gene namesi | Name:C3 |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular space Source: InterPro
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 22 | By similarityAdd BLAST | 22 | |
ChainiPRO_0000419922 | 23 – 1661 | Complement C3Add BLAST | 1639 | |
ChainiPRO_0000419923 | 23 – 665 | Complement C3 beta chainBy similarityAdd BLAST | 643 | |
ChainiPRO_0000430432 | 567 – 665 | C3-beta-cBy similarityAdd BLAST | 99 | |
ChainiPRO_0000419924 | 670 – 1661 | Complement C3 alpha chainBy similarityAdd BLAST | 992 | |
ChainiPRO_0000419925 | 670 – 746 | C3a anaphylatoxinAdd BLAST | 77 | |
ChainiPRO_0000419926 | 670 – 745 | Acylation stimulating proteinBy similarityAdd BLAST | 76 | |
ChainiPRO_0000419927 | 747 – 1661 | Complement C3b alpha' chainBy similarityAdd BLAST | 915 | |
ChainiPRO_0000419928 | 747 – 953 | Complement C3c alpha' chain fragment 1By similarityAdd BLAST | 207 | |
ChainiPRO_0000419929 | 954 – 1302 | Complement C3dg fragmentBy similarityAdd BLAST | 349 | |
ChainiPRO_0000419930 | 954 – 1000 | Complement C3g fragmentBy similarityAdd BLAST | 47 | |
ChainiPRO_0000419931 | 1001 – 1302 | Complement C3d fragmentBy similarityAdd BLAST | 302 | |
PeptideiPRO_0000419932 | 1303 – 1319 | Complement C3f fragmentBy similarityAdd BLAST | 17 | |
ChainiPRO_0000419933 | 1320 – 1661 | Complement C3c alpha' chain fragment 2By similarityAdd BLAST | 342 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 38 | PhosphoserineBy similarity | 1 | |
Modified residuei | 70 | PhosphoserineBy similarity | 1 | |
Modified residuei | 302 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 557 ↔ 814 | Interchain (between beta and alpha chains)PROSITE-ProRule annotation | ||
Disulfide bondi | 625 ↔ 660 | By similarity | ||
Modified residuei | 670 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 691 ↔ 718 | By similarity | ||
Disulfide bondi | 692 ↔ 725 | By similarity | ||
Disulfide bondi | 705 ↔ 726 | By similarity | ||
Disulfide bondi | 871 ↔ 1511 | By similarity | ||
Glycosylationi | 937 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 966 | PhosphoserineBy similarity | 1 | |
Cross-linki | 1008 ↔ 1011 | Isoglutamyl cysteine thioester (Cys-Gln)By similarity | ||
Disulfide bondi | 1099 ↔ 1156 | By similarity | ||
Modified residuei | 1319 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 1356 ↔ 1487 | By similarity | ||
Disulfide bondi | 1387 ↔ 1456 | By similarity | ||
Disulfide bondi | 1504 ↔ 1509 | By similarity | ||
Disulfide bondi | 1516 ↔ 1588 | By similarity | ||
Disulfide bondi | 1535 ↔ 1659 | By similarity | ||
Modified residuei | 1571 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 1615 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1635 ↔ 1644 | By similarity |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 745 – 746 | Cleavage; by carboxypeptidasesBy similarity | 2 | |
Sitei | 746 – 747 | Cleavage; by C3 convertaseBy similarity | 2 | |
Sitei | 1301 – 1302 | Cleavage; by factor IBy similarity | 2 | |
Sitei | 1318 – 1319 | Cleavage; by factor IBy similarity | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Thioester bondProteomic databases
PaxDbi | P01025 |
PeptideAtlasi | P01025 |
PRIDEi | P01025 |
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). Forms the pro-C3-convertase enzyme complex by binding to Complement factor B Bb fragment (Bb), which is then stabilized by binding CFP, allowing the complex to become active (By similarity). The interaction with Bb is dependent on Mg2+ (By similarity). C3b interacts with CR1 (via Sushi 8 and Sushi 9 domains). C3b interacts with CFH. C3d interacts with CFH. 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.
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.
By similarityBinary interactionsi
P01025
With | #Exp. | IntAct |
---|---|---|
gC [C7EYC8] from Suid alphaherpesvirus 1. | 2 | EBI-11688674,EBI-11688666 |
GO - Molecular functioni
- C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
Protein-protein interaction databases
IntActi | P01025, 1 interactor |
STRINGi | 9823.ENSSSCP00000014399 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 691 – 726 | Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 1516 – 1659 | NTRPROSITE-ProRule annotationAdd BLAST | 144 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1632 – 1657 | Interaction with CFP/properdinBy similarityAdd BLAST | 26 |
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG1366, Eukaryota |
InParanoidi | P01025 |
OrthoDBi | 23785at2759 |
Family and domain databases
CDDi | cd00017, ANATO, 1 hit cd03583, NTR_complement_C3, 1 hit |
Gene3Di | 2.40.50.120, 1 hit 2.60.40.10, 2 hits 2.60.40.690, 1 hit |
InterProi | View protein in InterPro IPR009048, A-macroglobulin_rcpt-bd IPR036595, A-macroglobulin_rcpt-bd_sf IPR011625, A2M_N_BRD IPR011626, Alpha-macroglobulin_TED IPR000020, Anaphylatoxin/fibulin IPR018081, Anaphylatoxin_comp_syst IPR001840, Anaphylatoxn_comp_syst_dom IPR041425, C3/4/5_MG1 IPR035711, Complement_C3-like IPR013783, Ig-like_fold IPR001599, Macroglobln_a2 IPR019742, MacrogloblnA2_CS IPR002890, MG2 IPR041555, MG3 IPR040839, MG4 IPR001134, Netrin_domain IPR018933, Netrin_module_non-TIMP IPR035815, NTR_complement_C3 IPR008930, Terpenoid_cyclase/PrenylTrfase IPR008993, TIMP-like_OB-fold |
PANTHERi | PTHR11412:SF81, PTHR11412:SF81, 1 hit |
Pfami | View protein in Pfam PF00207, A2M, 1 hit PF07703, A2M_BRD, 1 hit PF07677, A2M_recep, 1 hit PF01821, ANATO, 1 hit PF17790, MG1, 1 hit PF01835, MG2, 1 hit PF17791, MG3, 1 hit PF17789, MG4, 1 hit PF01759, NTR, 1 hit PF07678, TED_complement, 1 hit |
PRINTSi | PR00004, ANAPHYLATOXN |
SMARTi | View protein in SMART SM01360, A2M, 1 hit SM01359, A2M_N_2, 1 hit SM01361, A2M_recep, 1 hit SM00104, ANATO, 1 hit SM00643, C345C, 1 hit |
SUPFAMi | SSF47686, SSF47686, 1 hit SSF48239, SSF48239, 1 hit SSF49410, SSF49410, 1 hit SSF50242, SSF50242, 1 hit |
PROSITEi | View protein in PROSITE PS00477, ALPHA_2_MACROGLOBULIN, 1 hit PS01177, ANAPHYLATOXIN_1, 1 hit PS01178, ANAPHYLATOXIN_2, 1 hit PS50189, NTR, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 679 | D → N AA sequence (PubMed:956663).Curated | 1 | |
Sequence conflicti | 687 – 688 | DV → EL AA sequence (PubMed:956663).Curated | 2 | |
Sequence conflicti | 698 | D → N AA sequence (PubMed:956663).Curated | 1 | |
Sequence conflicti | 713 – 716 | QHGD → HQGN AA sequence (PubMed:956663).Curated | 4 | |
Sequence conflicti | 724 | D → N AA sequence (PubMed:956663).Curated | 1 |
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 |
PIRi | A01259 |
RefSeqi | NP_999174.1, NM_214009.1 |
Genome annotation databases
GeneIDi | 397072 |
KEGGi | ssc:397072 |
Similar proteinsi
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 |
PIRi | A01259 |
RefSeqi | NP_999174.1, NM_214009.1 |
3D structure databases
SMRi | P01025 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | P01025, 1 interactor |
STRINGi | 9823.ENSSSCP00000014399 |
Protein family/group databases
MEROPSi | I39.950 |
Proteomic databases
PaxDbi | P01025 |
PeptideAtlasi | P01025 |
PRIDEi | P01025 |
Genome annotation databases
GeneIDi | 397072 |
KEGGi | ssc:397072 |
Organism-specific databases
CTDi | 718 |
Phylogenomic databases
eggNOGi | KOG1366, Eukaryota |
InParanoidi | P01025 |
OrthoDBi | 23785at2759 |
Family and domain databases
CDDi | cd00017, ANATO, 1 hit cd03583, NTR_complement_C3, 1 hit |
Gene3Di | 2.40.50.120, 1 hit 2.60.40.10, 2 hits 2.60.40.690, 1 hit |
InterProi | View protein in InterPro IPR009048, A-macroglobulin_rcpt-bd IPR036595, A-macroglobulin_rcpt-bd_sf IPR011625, A2M_N_BRD IPR011626, Alpha-macroglobulin_TED IPR000020, Anaphylatoxin/fibulin IPR018081, Anaphylatoxin_comp_syst IPR001840, Anaphylatoxn_comp_syst_dom IPR041425, C3/4/5_MG1 IPR035711, Complement_C3-like IPR013783, Ig-like_fold IPR001599, Macroglobln_a2 IPR019742, MacrogloblnA2_CS IPR002890, MG2 IPR041555, MG3 IPR040839, MG4 IPR001134, Netrin_domain IPR018933, Netrin_module_non-TIMP IPR035815, NTR_complement_C3 IPR008930, Terpenoid_cyclase/PrenylTrfase IPR008993, TIMP-like_OB-fold |
PANTHERi | PTHR11412:SF81, PTHR11412:SF81, 1 hit |
Pfami | View protein in Pfam PF00207, A2M, 1 hit PF07703, A2M_BRD, 1 hit PF07677, A2M_recep, 1 hit PF01821, ANATO, 1 hit PF17790, MG1, 1 hit PF01835, MG2, 1 hit PF17791, MG3, 1 hit PF17789, MG4, 1 hit PF01759, NTR, 1 hit PF07678, TED_complement, 1 hit |
PRINTSi | PR00004, ANAPHYLATOXN |
SMARTi | View protein in SMART SM01360, A2M, 1 hit SM01359, A2M_N_2, 1 hit SM01361, A2M_recep, 1 hit SM00104, ANATO, 1 hit SM00643, C345C, 1 hit |
SUPFAMi | SSF47686, SSF47686, 1 hit SSF48239, SSF48239, 1 hit SSF49410, SSF49410, 1 hit SSF50242, SSF50242, 1 hit |
PROSITEi | View protein in PROSITE PS00477, ALPHA_2_MACROGLOBULIN, 1 hit PS01177, ANAPHYLATOXIN_1, 1 hit PS01178, ANAPHYLATOXIN_2, 1 hit PS50189, NTR, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CO3_PIG | |
Accessioni | P01025Primary (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: | December 2, 2020 | |
This is version 114 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |