UniProt UniProt http://www.uniprot.org Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Nature structural & molecular biology 2017 imex curation Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl 21-Nov-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl Accepted 2019-OCT-21 AT 09:30 BST AT 09:30 BST by MGT Nature structural & molecular biology 2017 Only protein-protein interactions imex curation imex curation Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Nature structural & molecular biology 2017 imex curation Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl 21-Nov-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl Accepted 2019-OCT-21 AT 09:30 BST AT 09:30 BST by MGT Nature structural & molecular biology 2017 Only protein-protein interactions imex curation imex curation Mock publication and experiment for abstract interactions that are not interaction evidences. Mock publication and experiment for abstract interactions that are not interaction evidences. unspecified method Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Nature structural & molecular biology 2017 imex curation Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl 21-Nov-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl Accepted 2019-OCT-21 AT 09:30 BST AT 09:30 BST by MGT Nature structural & molecular biology 2017 Only protein-protein interactions imex curation imex curation Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Nature structural & molecular biology 2017 imex curation Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl 21-Nov-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl Accepted 2019-OCT-21 AT 09:30 BST AT 09:30 BST by MGT Nature structural & molecular biology 2017 Only protein-protein interactions imex curation imex curation Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses. Nature structural & molecular biology 2017 imex curation Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl 21-Nov-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt CQ., Granneman J., Sharp TH., Lambris JD., Gros P. Supplementary figure legends in main text do not match the actual supp figs. p.gros@uu.nl Accepted 2019-OCT-21 AT 09:30 BST AT 09:30 BST by MGT Nature structural & molecular biology 2017 Only protein-protein interactions imex curation imex curation p01024-pro_0000005908 Complement C3 beta chain C3 CPAMD1 C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1 protein protein human Homo sapiens Human SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAA 23 667 C4754001F1A97259 p01024-pro_0000005911 Complement C3b alpha' chain C3 CPAMD1 C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1 protein protein human Homo sapiens Human SNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN 749 1663 1E32EA0CEA20EA81 p05156-pro_0000027569 Complement factor I heavy chain C3B/C4B inactivator CFI IF protein protein human Homo sapiens Human KVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHI 19 335 FF4F124994A70525 cfah_human Complement factor H CFH HF HF1 HF2 H factor 1 protein protein human Homo sapiens Human MRLLAKIICLMLWAICVAEDCNELPPRRNTEILTGSWSDQTYPEGTQAIYKCRPGYRSLGNVIMVCRKGEWVALNPLRKCQKRPCGHPGDTPFGTFTLTGGNVFEYGVKAVYTCNEGYQLLGEINYRECDTDGWTNDIPICEVVKCLPVTAPENGKIVSSAMEPDREYHFGQAVRFVCNSGYKIEGDEEMHCSDDGFWSKEKPKCVEISCKSPDVINGSPISQKIIYKENERFQYKCNMGYEYSERGDAVCTESGWRPLPSCEEKSCDNPYIPNGDYSPLRIKHRTGDEITYQCRNGFYPATRGNTAKCTSTGWIPAPRCTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDGWSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCIRVKTCSKSSIDIENGFISESQYTYALKEKAKYQCKLGYVTADGETSGSITCGKDGWSAQPTCIKSCDIPVFMNARTKNDFTWFKLNDTLDYECHDGYESNTGSTTGSIVCGYNGWSDLPICYERECELPKIDVHLVPDRKKDQYKVGEVLKFSCKPGFTIVGPNSVQCYHFGLSPDLPICKEQVQSCGPPPELLNGNVKEKTKEEYGHSEVVEYYCNPRFLMKGPNKIQCVDGEWTTLPVCIVEESTCGDIPELEHGWAQLSSPPYYYGDSVEFNCSESFTMIGHRSITCIHGVWTQLPQCVAIDKLKKCKSSNLIILEEHLKNKKEFDHNSNIRYRCRGKEGWIHTVCINGRWDPEVNCSMAQIQLCPPPPQIPNSHNMTTTLNYRDGEKVSVLCQENYLIQEGEEITCKDGRWQSIPLCVEKIPCSQPPQIEHGTINSSRSSQESYAHGTKLSYTCEGGFRISEENETTCYMGKWSSPPQCEGLPCKSPPEISHGVVAHMSDSYQYGEEVTYKCFEGFGIDGPAIAKCLGEKWSHPPSCIKTDCLSLPSFENAIPMGEKKDVYKAGEQVTYTCATYYKMDGASNVTCINSRWTGRPTCRDTSCVNPPTVQNAYIVSRQMSKYPSGERVRYQCRSPYEMFGDEEVMCLNGNWTEPPQCKDSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAKQKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAKR DIP protein P08603 original sequence version: 161 DIP protein P08603-1 original sequence version: 149 3C26D62A2BF9BFEE p01024-pro_0000005912 Complement C3c alpha' chain fragment 1 C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1 C3 CPAMD1 protein protein human Homo sapiens Human SNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGR 749 954 0276608B22698C7C p01024-pro_0000273948 Complement C3c alpha' chain fragment 2 C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1 C3 CPAMD1 protein protein human Homo sapiens Human SEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN 1321 1663 E1E1CA28F655650D mcp_human Membrane cofactor protein MCP MIC10 TLX Trophoblast leukocyte common antigen CD46 protein protein human Homo sapiens Human MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL DIP protein P15529 original sequence version: 143 85FE0CF100EA703E p05156-pro_0000027570 Complement factor I light chain C3B/C4B inactivator CFI IF protein protein human Homo sapiens Human IVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV 340 583 3CA07FF7750BB0D1 cr1_human Complement receptor type 1 CR1 C3BR C3b/C4b receptor protein protein human Homo sapiens Human MGASSPRSPEPVGPPAPGLPFCCGGSLLAVVVLLALPVAWGQCNAPEWLPFARPTNLTDEFEFPIGTYLNYECRPGYSGRPFSIICLKNSVWTGAKDRCRRKSCRNPPDPVNGMVHVIKGIQFGSQIKYSCTKGYRLIGSSSATCIISGDTVIWDNETPICDRIPCGLPPTITNGDFISTNRENFHYGSVVTYRCNPGSGGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPDVLHAERTQRDKDNFSPGQEVFYSCEPGYDLRGAASMRCTPQGDWSPAAPTCEVKSCDDFMGQLLNGRVLFPVNLQLGAKVDFVCDEGFQLKGSSASYCVLAGMESLWNSSVPVCEQIFCPSPPVIPNGRHTGKPLEVFPFGKTVNYTCDPHPDRGTSFDLIGESTIRCTSDPQGNGVWSSPAPRCGILGHCQAPDHFLFAKLKTQTNASDFPIGTSLKYECRPEYYGRPFSITCLDNLVWSSPKDVCKRKSCKTPPDPVNGMVHVITDIQVGSRINYSCTTGHRLIGHSSAECILSGNAAHWSTKPPICQRIPCGLPPTIANGDFISTNRENFHYGSVVTYRCNPGSGGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPDVLHAERTQRDKDNFSPGQEVFYSCEPGYDLRGAASMRCTPQGDWSPAAPTCEVKSCDDFMGQLLNGRVLFPVNLQLGAKVDFVCDEGFQLKGSSASYCVLAGMESLWNSSVPVCEQIFCPSPPVIPNGRHTGKPLEVFPFGKAVNYTCDPHPDRGTSFDLIGESTIRCTSDPQGNGVWSSPAPRCGILGHCQAPDHFLFAKLKTQTNASDFPIGTSLKYECRPEYYGRPFSITCLDNLVWSSPKDVCKRKSCKTPPDPVNGMVHVITDIQVGSRINYSCTTGHRLIGHSSAECILSGNTAHWSTKPPICQRIPCGLPPTIANGDFISTNRENFHYGSVVTYRCNLGSRGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPEILHGEHTPSHQDNFSPGQEVFYSCEPGYDLRGAASLHCTPQGDWSPEAPRCAVKSCDDFLGQLPHGRVLFPLNLQLGAKVSFVCDEGFRLKGSSVSHCVLVGMRSLWNNSVPVCEHIFCPNPPAILNGRHTGTPSGDIPYGKEISYTCDPHPDRGMTFNLIGESTIRCTSDPHGNGVWSSPAPRCELSVRAGHCKTPEQFPFASPTIPINDFEFPVGTSLNYECRPGYFGKMFSISCLENLVWSSVEDNCRRKSCGPPPEPFNGMVHINTDTQFGSTVNYSCNEGFRLIGSPSTTCLVSGNNVTWDKKAPICEIISCEPPPTISNGDFYSNNRTSFHNGTVVTYQCHTGPDGEQLFELVGERSIYCTSKDDQVGVWSSPPPRCISTNKCTAPEVENAIRVPGNRSFFSLTEIIRFRCQPGFVMVGSHTVQCQTNGRWGPKLPHCSRVCQPPPEILHGEHTLSHQDNFSPGQEVFYSCEPSYDLRGAASLHCTPQGDWSPEAPRCTVKSCDDFLGQLPHGRVLLPLNLQLGAKVSFVCDEGFRLKGRSASHCVLAGMKALWNSSVPVCEQIFCPNPPAILNGRHTGTPFGDIPYGKEISYACDTHPDRGMTFNLIGESSIRCTSDPQGNGVWSSPAPRCELSVPAACPHPPKIQNGHYIGGHVSLYLPGMTISYICDPGYLLVGKGFIFCTDQGIWSQLDHYCKEVNCSFPLFMNGISKELEMKKVYHYGDYVTLKCEDGYTLEGSPWSQCQADDRWDPPLAKCTSRTHDALIVGTLSGTIFFILLIIFLSWIILKHRKGNNAHENPKEVAIHLHSQGGSSVHPRTLQTNEENSRVLP FB01870F19D5E6DD c3-c3-1 1 10 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain picpa Pichia pastoris (Yeast) Yeast Pichia pastoris 8 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma 7 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma physical association physical association Table 1 c3-c3-2 1 9 unspecified role unspecified role neutral component neutral component purified purified human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 10 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain picpa Pichia pastoris (Yeast) Yeast Pichia pastoris 8 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma 7 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma 14 unspecified role unspecified role neutral component neutral component purified purified P05156-PRO_0000027570:p.Ser186Ala mutation mutation certain certain sequence position certain certain certain sequence position certain S A Tue Mar 19 11:43:08 GMT 2019 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser220Ala' Tue Jun 30 20:09:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser186Ala' human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. physical association physical association Table 1 c3-c3-3 6 8 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind range range range range human-plasma homo sapiens blood plasma plasma blood plasma 7 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma direct interaction direct interaction Fig. 4A iC3b is formed by the cleavage of C3b by Factor I in the presence of Factor H, CR1, or membrane cofactor protein. Factor I cleavage of C3b to iC3b inactivates C3b from functioning in the C3 or C5 convertase enzymes. The iC3b fragment thus produced is a glycoprotein composed of two C3alpha-prime polypeptides of M.W. 43,000 and M.W. 63,000 which are disulfide bonded to the intact C3 beta-chain . c3-c3-4 6 8 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-plasma homo sapiens blood plasma plasma blood plasma 7 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma direct interaction direct interaction Fig. 4A C3b cleaved between Arg1281-Ser1282 (iC3b1) (Arg1303-Ser1304 including signal sequence) c3-c3-5 4 39 unspecified role unspecified role bait bait purified purified human-plasma homo sapiens blood plasma plasma blood plasma 10 unspecified role unspecified role prey prey purified purified region required to bind necessary binding region required to bind range range range range region sufficient to bind sufficient binding region sufficient to bind range range range range human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. physical association physical association Fig. 5, Supp. fig 8B c3-c3-6 6 7 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma 8 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma direct interaction direct interaction Fig. 4A c3-c3-7 2 8 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-plasma homo sapiens blood plasma plasma blood plasma 7 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma direct interaction direct interaction Fig. 4B C3b cleaved between Arg1281-Ser1282 (iC3b1) (Arg1303-Ser1304 including signal sequence) c3-c3-8 2 8 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind range range range range human-plasma homo sapiens blood plasma plasma blood plasma 7 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma direct interaction direct interaction Fig. 4B iC3b is formed by the cleavage of C3b by Factor I in the presence of Factor H, CR1, or membrane cofactor protein. Factor I cleavage of C3b to iC3b inactivates C3b from functioning in the C3 or C5 convertase enzymes. The iC3b fragment thus produced is a glycoprotein composed of two C3alpha-prime polypeptides of M.W. 43,000 and M.W. 63,000 which are disulfide bonded to the intact C3 beta-chain . c3-c3-9 2 7 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma 8 unspecified role unspecified role neutral component neutral component purified purified human-plasma homo sapiens blood plasma plasma blood plasma direct interaction direct interaction Fig. 4B c3-10 4 39 unspecified role unspecified role bait bait purified purified human-plasma homo sapiens blood plasma plasma blood plasma 13 unspecified role unspecified role prey prey purified purified region sufficient to bind sufficient binding region sufficient to bind range range range range human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. physical association physical association Fig. 5, Supp. fig 8B. c3-cr1-1 4 39 unspecified role unspecified role bait bait purified purified human-plasma homo sapiens blood plasma plasma blood plasma 15 unspecified role unspecified role prey prey purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. physical association physical association Fig 5, Supp. Fig 8B c3-cr1-2 4 7 unspecified role unspecified role bait bait human-plasma homo sapiens blood plasma plasma blood plasma 15 unspecified role unspecified role prey prey purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 8 unspecified role unspecified role bait bait purified purified region sufficient to bind sufficient binding region sufficient to bind range range range range human-plasma homo sapiens blood plasma plasma blood plasma physical association physical association Fig. 5, Supp. Fig 8B. iC3b is formed by the cleavage of C3b by Factor I in the presence of Factor H, CR1, or membrane cofactor protein. Factor I cleavage of C3b to iC3b inactivates C3b from functioning in the C3 or C5 convertase enzymes. The iC3b fragment thus produced is a glycoprotein composed of two C3alpha-prime polypeptides of M.W. 43,000 and M.W. 63,000 which are disulfide bonded to the intact C3 beta-chain . c3-cfb-5 4 15 unspecified role unspecified role prey prey purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 7 unspecified role unspecified role bait bait purified purified human-plasma homo sapiens blood plasma plasma blood plasma 12 unspecified role unspecified role bait bait purified purified human-plasma homo sapiens blood plasma plasma blood plasma 11 unspecified role unspecified role bait bait purified purified human-plasma homo sapiens blood plasma plasma blood plasma physical association physical association Supp Fig. 8B c3-c3-17 5 8 enzyme target enzyme target substrate substrate unspecified role unspecified role purified purified human-plasma homo sapiens blood plasma plasma blood plasma 9 enzyme enzyme neutral component neutral component purified purified p05156-pro_0000027570 binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 10 enzyme regulator enzyme regulator neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain range range picpa Pichia pastoris (Yeast) Yeast Pichia pastoris 14 enzyme enzyme neutral component neutral component purified purified P05156-PRO_0000027570:p.Ser186Ala mutation mutation certain certain sequence position certain certain certain sequence position certain S A Tue Mar 19 11:43:08 GMT 2019 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser220Ala' Tue Jun 30 17:46:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser186Ala' p05156-pro_0000027569 binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 80 85 protein cleavage protein cleavage Supp Fig. 8A c3b_human-cd46-1 5 8 enzyme target enzyme target substrate substrate unspecified role unspecified role purified purified human-plasma homo sapiens blood plasma plasma blood plasma 9 enzyme enzyme neutral component neutral component purified purified p05156-pro_0000027570 binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 14 enzyme enzyme neutral component neutral component purified purified P05156-PRO_0000027570:p.Ser186Ala mutation mutation certain certain sequence position certain certain certain sequence position certain S A Tue Mar 19 11:43:08 GMT 2019 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser220Ala' Tue Jun 30 18:41:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser186Ala' p05156-pro_0000027569 binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain picpa Pichia pastoris (Yeast) Yeast Pichia pastoris 89 92 protein cleavage protein cleavage Supp Fig. 8A c3b_human Complement C3b complex C3b dimer 8 unspecified role unspecified role C3 beta chain binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 unspecified role unspecified role C3b alpha(prime) chain binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 96 98 physical association physical association human Homo sapiens Human stable complex stable complex physical interaction evidence used in manual assertion physical interaction evidence used in manual assertion IPI inferred from physical interaction A protein complex of the alternative pathway of complement activation of the innate immune system. Complement C3 precurser is activated by cleavage into C3a and C3b by C3 convertases, either C4bC2a in the classical and lectin pathways or C3(H2O)Bb, C3bBb, C3bBbC3b, C3bBbP or C3bBbC3bP in the alternative pathway. C3b acts as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex (CPX-6159) assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response. Activation of C3b leads to an amplification cascade that generates more C3 convertase, deposits more C3b at the local site and switches C3 convertases to C5 convertases. To protect host cells from inadvertent complement activation the activation of C3b is tightly regulated by either disrupting the C3 convertases or aiding in the proteolytic degradation of C3b. Bacteria and viruses possess C3b proteases to evade the complement response. Lack of protection, due to familial mutations in the complement genes or the presence of autoantibodies against regulators has been linked to atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathies (C3G) in kidneys and age-related macular degeneration (AMD) in eyes. Conditions of chronic and acute inflammations, as in rheumatoid arthritis, strokes, and heart attacks, become aggravated by complement activation against the disturbed tissue. The alternative pathway is continuously activated at a low level. C3 precursor is first processed by the removal of 4 Arg residues and spontaneous hydrolysis due to the breakdown of the internal thioester bond forms C3(H2O) (disulfide bonded P01024-PRO_0000005909 & P01024-PRO_0000005908). C3(H2O) subsequently binds factor B that is cleaved by Factor D (P00746) into 2 fragments: CFBa and CFBb. CFBb, a serine protease, then combines with complement factor C3(H2O) or C3b to generate the C3 or C5 convertases. Proteolytic cleavage of C3 to C3b is accompanied by large conformational changes that result in the exposure of cryptic binding sites required for convertase assembly and regulation. This includes a significant movement of the thioester-bond-containing domain through which C3b attaches to target surfaces. Heterodimer Complement component 3 (C3) deficiency [Orphanet:280133]: a rare, autosomal recessive 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. Atypical hemolytic-uremic syndrome with C3 anomaly [Orphanet:2134 & Orphanet:93575]: an autosomal dominant, atypical form of hemolytic-uremic syndrome (aHUS, a thrombotic microangiopathy) characterized by mechanical hemolytic anemia, thrombocytopenia, and renal dysfunction. Age-related macular degeneration [EFO:0001365]: age-related macular degeneration usually in older adults which results in a loss of vision in the center of the visual field (the macula lutea) because of damage to the retina. Manifests 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. Occurs in dry and wet forms. Most common cause of irreversible vision loss in the developed world. Accepted 2017-JAN-19 by ORCHARD coronavirus