CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001862
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Complement C3 
Protein Synonyms/Alias
 HSE-MSF; Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein; ASP; C3adesArg; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2 
Gene Name
 C3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
74RQVLTSEKTVLTGASubiquitination[1]
95SIKIPASKEFNSDKEubiquitination[1]
306GDAVLTRKVLMEGVRubiquitination[1]
360PYQIHFTKTPKFFKPubiquitination[1]
398VTQGSNAKALTQDDGubiquitination[1]
408TQDDGVAKLSINTPNubiquitination[1]
466SVSRMELKPGDNLNVubiquitination[1]
566CIGTLVVKGDPRDNHubiquitination[1]
599VGLVAVDKGVFVLNKubiquitination[1]
879FCSMATAKNRYFQTIubiquitination[1]
1215GKFLNTAKDRNRWEEubiquitination[1]
1325LLRSEETKQNEAFSLubiquitination[1]
1335EAFSLTAKGKGRGTLubiquitination[1]
1431GVDRYISKYEMNKAFubiquitination[1]
1535NLNVRLDKACEPGVDubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 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. 
Sequence Annotation
 DOMAIN 693 728 Anaphylatoxin-like.
 DOMAIN 1518 1661 NTR.
 REGION 1424 1456 Properdin-binding (By similarity).
 MOD_RES 489 489 Phosphotyrosine.
 CARBOHYD 939 939 N-linked (GlcNAc...).
 CARBOHYD 1617 1617 N-linked (GlcNAc...).
 DISULFID 559 816 Interchain (between beta and alpha
 DISULFID 626 661 By similarity.
 DISULFID 693 720 By similarity.
 DISULFID 694 727 By similarity.
 DISULFID 707 728 By similarity.
 DISULFID 873 1513 By similarity.
 DISULFID 1101 1158 By similarity.
 DISULFID 1358 1489 By similarity.
 DISULFID 1389 1458 By similarity.
 DISULFID 1506 1511 By similarity.
 DISULFID 1518 1590 By similarity.
 DISULFID 1537 1661 By similarity.
 DISULFID 1637 1646 By similarity.
 CROSSLNK 1010 1013 Isoglutamyl cysteine thioester (Cys-Gln)  
Keyword
 Alternative initiation; Cleavage on pair of basic residues; Complement alternate pathway; Complement pathway; Complete proteome; Direct protein sequencing; Disulfide bond; Fatty acid metabolism; Glycoprotein; Immunity; Inflammatory response; Innate immunity; Lipid metabolism; Phosphoprotein; Reference proteome; Secreted; Signal; Thioester bond. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1663 AA 
Protein Sequence
MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD AQGDIPVTVT 60
VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD KEGHKYVTVV ANFGETVVEK 120
AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI FTVDNNLLPV GKTVVILIET PDGIPVKRDI 180
LSSNNQHGIL PLSWNIPELV NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT 240
ETFYYIDDPN GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD 300
AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV TSPYQIHFTK 360
TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL TQDDGVAKLS INTPNSRQPL 420
TITVRTKKDT LPESRQATKT MEAHPYSTMH NSNNYLHLSV SRMELKPGDN LNVNFHLRTD 480
PGHEAKIRYY TYLVMNKGKL LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA 540
SGQREVVADS VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG 600
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG LQTEQRADLE 660
CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD IPMRYSCQRR ARLITQGENC 720
IKAFIDCCNH ITKLREQHRR DHVLGLARSE LEEDIIPEED IISRSHFPQS WLWTIEELKE 780
PEKNGISTKV MNIFLKDSIT TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV 840
RNEQVEIRAV LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI 900
VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE KLGQGGVQKV 960
DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL KHLIVTPAGC GEQNMIGMTP 1020
TVIAVHYLDQ TEQWEKFGIE KRQEALELIK KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA 1080
YVVKVFSLAA NLIAIDSHVL CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD 1140
VSLTAFVLIA LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN 1200
KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP PVVRWLNEQR 1260
YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL PSRSSATTFR LLWENGNLLR 1320
SEETKQNEAF SLTAKGKGRG TLSVVAVYHA KLKSKVTCKK FDLRVSIRPA PETAKKPEEA 1380
KNTMFLEICT KYLGDVDATM SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN 1440
KNTLIIYLEK ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG 1500
MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT NIELLDDFDE 1560
YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK KYLMWGLSSD LWGEKPNTSY 1620
IIGKDTWVEH WPEAEECQDQ KYQKQCEELG AFTESMVVYG CPN 1663 
Gene Ontology
 GO:0005615; C:extracellular space; IEA:InterPro.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; ISS:UniProtKB.
 GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
 GO:0006956; P:complement activation; IDA:MGI.
 GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
 GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
 GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
 GO:0010951; P:negative regulation of endopeptidase activity; IEA:GOC.
 GO:0001970; P:positive regulation of activation of membrane attack complex; IMP:BHF-UCL.
 GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
 GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
 GO:0010828; P:positive regulation of glucose transport; ISS:UniProtKB.
 GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
 GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
 GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
 GO:0001798; P:positive regulation of type IIa hypersensitivity; IMP:MGI.
 GO:0010575; P:positive regulation vascular endothelial growth factor production; IEA:Compara.
 GO:0010866; P:regulation of triglyceride biosynthetic process; ISS:UniProtKB. 
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. 
Pfam
 PF00207; A2M
 PF07678; A2M_comp
 PF01835; A2M_N
 PF07703; A2M_N_2
 PF07677; A2M_recep
 PF01821; ANATO
 PF01759; NTR
 PF10569; Thiol-ester_cl 
SMART
 SM00104; ANATO
 SM00643; C345C 
PROSITE
 PS00477; ALPHA_2_MACROGLOBULIN
 PS01177; ANAPHYLATOXIN_1
 PS01178; ANAPHYLATOXIN_2
 PS50189; NTR 
PRINTS
 PR00004; ANAPHYLATOXN.