CO3_ONCMY
ID CO3_ONCMY Reviewed; 1640 AA.
AC P98093;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Complement C3;
DE Contains:
DE RecName: Full=Complement C3 beta chain;
DE Contains:
DE RecName: Full=Complement C3 alpha chain;
DE Contains:
DE RecName: Full=C3a anaphylatoxin;
DE Contains:
DE RecName: Full=Complement C3b alpha' chain;
DE Contains:
DE RecName: Full=Complement C3c alpha' chain fragment 1;
DE Contains:
DE RecName: Full=Complement C3dg fragment;
DE Contains:
DE RecName: Full=Complement C3g fragment;
DE Contains:
DE RecName: Full=Complement C3d fragment;
DE Contains:
DE RecName: Full=Complement C3f fragment;
DE Contains:
DE RecName: Full=Complement C3c alpha' chain fragment 2;
DE Flags: Fragment;
GN Name=c3;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-23; 647-666; 723-733;
RP 946-960; 1034-1046; 1296-1312 AND 1310-1329.
RC TISSUE=Liver;
RX PubMed=8245455;
RA Lambris J.D., Lao Z., Pang J., Alsenz J.;
RT "Third component of trout complement. cDNA cloning and conservation of
RT functional sites.";
RL J. Immunol. 151:6123-6134(1993).
CC -!- FUNCTION: C3 plays a central role in the activation of the complement
CC system. Its processing by C3 convertase is the central reaction in both
CC classical and alternative complement pathways. After activation C3b can
CC bind covalently, via its reactive thioester, to cell surface
CC carbohydrates or immune aggregates.
CC -!- SUBUNIT: C3 precursor is first processed by the removal of 4 Arg
CC residues, forming two chains, beta and alpha, linked by a disulfide
CC bond. C3 convertase activates C3 by cleaving the alpha chain, releasing
CC C3a anaphylatoxin and generating C3b (beta chain + alpha' chain) (By
CC similarity). FForms the pro-C3-convertase enzyme complex by binding to
CC C3b, which is then stabilized by binding CFP, allowing the complex to
CC become active (By similarity). The interaction with CFB Bb fragment is
CC dependent on Mg2+ (By similarity). C3b interacts with CR1 (via Sushi 8
CC and Sushi 9 domains). C3b interacts with CFH. C3d interacts with CFH.
CC C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2).
CC During pregnancy, C3dg exists as a complex (probably a 2:2:2
CC heterohexamer) with AGT and the proform of PRG2. Interacts with VSIG4.
CC Interacts with S.aureus immunoglobulin-binding protein sbi, this
CC prevents interaction between C3dg and CR2. Interacts with S.aureus fib.
CC Interacts (both C3a and ASP) with C5AR2; the interaction occurs with
CC higher affinity for ASP, enhancing the phosphorylation and activation
CC of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of
CC GRP77 (By similarity). {ECO:0000250|UniProtKB:P01024}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: C3b is rapidly split in two positions by factor I and a cofactor
CC to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is
CC slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha'
CC chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other
CC proteases produce other fragments such as C3d or C3g.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB05029.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L24433; AAB05029.1; ALT_INIT; mRNA.
DR PIR; I51339; I51339.
DR AlphaFoldDB; P98093; -.
DR SMR; P98093; -.
DR MEROPS; I39.950; -.
DR PRIDE; P98093; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:AgBase.
DR GO; GO:0003823; F:antigen binding; IDA:AgBase.
DR GO; GO:0001848; F:complement binding; IDA:AgBase.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:AgBase.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd03583; NTR_complement_C3; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR035711; Complement_C3-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR035815; NTR_complement_C3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SUPFAM; SSF47686; SSF47686; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Complement alternate pathway;
KW Complement pathway; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunity; Inflammatory response; Innate immunity; Secreted;
KW Thioester bond.
FT CHAIN 1..1640
FT /note="Complement C3"
FT /id="PRO_0000005952"
FT CHAIN 1..642
FT /note="Complement C3 beta chain"
FT /id="PRO_0000005953"
FT CHAIN 647..1640
FT /note="Complement C3 alpha chain"
FT /id="PRO_0000005954"
FT CHAIN 647..722
FT /note="C3a anaphylatoxin"
FT /id="PRO_0000005955"
FT CHAIN 723..1640
FT /note="Complement C3b alpha' chain"
FT /id="PRO_0000005956"
FT CHAIN 723..931
FT /note="Complement C3c alpha' chain fragment 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005957"
FT CHAIN 932..1278
FT /note="Complement C3dg fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005958"
FT CHAIN 932..1033
FT /note="Complement C3g fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005959"
FT CHAIN 1034..1278
FT /note="Complement C3d fragment"
FT /id="PRO_0000005960"
FT PEPTIDE 1279..1295
FT /note="Complement C3f fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005961"
FT CHAIN 1296..1640
FT /note="Complement C3c alpha' chain fragment 2"
FT /id="PRO_0000273956"
FT DOMAIN 668..703
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1493..1638
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 1420..1430
FT /note="Properdin-binding"
FT SITE 722..723
FT /note="Cleavage; by C3 convertase"
FT SITE 931..932
FT /note="Cleavage; by factor I"
FT /evidence="ECO:0000250"
FT SITE 1278..1279
FT /note="Cleavage; by factor I"
FT /evidence="ECO:0000250"
FT SITE 1295..1296
FT /note="Cleavage; by factor I"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 536..797
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022,
FT ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 603..638
FT /evidence="ECO:0000250"
FT DISULFID 668..695
FT /evidence="ECO:0000250"
FT DISULFID 669..702
FT /evidence="ECO:0000250"
FT DISULFID 682..703
FT /evidence="ECO:0000250"
FT DISULFID 853..1488
FT /evidence="ECO:0000250"
FT DISULFID 1079..1135
FT /evidence="ECO:0000250"
FT DISULFID 1335..1464
FT /evidence="ECO:0000250"
FT DISULFID 1481..1486
FT /evidence="ECO:0000250"
FT DISULFID 1493..1563
FT /evidence="ECO:0000250"
FT DISULFID 1510..1638
FT /evidence="ECO:0000250"
FT DISULFID 1614..1623
FT /evidence="ECO:0000250"
FT CROSSLNK 988..991
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 1640 AA; 182105 MW; 0965B4FAF1E87812 CRC64;
AALQVLSAPN LLRVGSNENI FVESQDHVGG PLNVKIMVKN HPTQSKELAS KSVVLDQANN
FQAMTQLVIQ RGPLVDDPKQ KQYVVLQAQF PDRLLEKVVL VSFQSGYIFI QTDKTIYTPA
STVHYRVFSM TPGLEPLTRE IFEDQEVAKN KEIAVSVEIM TPENITIFRE IVNPDKGVKS
GQFKLPDIVS FGTWHVVTRF QSTPQKTFSS EFEVKEYVLP SFEVSLTPAK AFFYVDDNDL
TVDITARYLY GKEVTGTGYV VFGVITTESE KKSFPASLQR VEIKDGKGVA CLKKEHITQT
FPKIHDLVKQ SIFVSVSVLT EGGGEMVEAE KRGIQIVTSP YSILFKRTPK YFKPGMPFDV
SVYITNPDNS PAIGVEVEVT PDHAKGVTRA NGFAKIPLNT VASATELVIT VKTKDPGDPR
QQTGGGTMKA LPYRTSTKNF LHVGVDSNEL KIGDPIKIDL NLGPTTIPNH DLTYMFLSRG
QLVKVGRFKR QGNALVTLSV PVSKELLPSF RIVAYYHVGA ADLVADSVWV DIKVSCMGSL
KVTSTRPKAS YEPRRAFSLT ITGDPGAKVG LVAVDKGVYV LNSKHRLTQT KIWDTIEKHD
TGCTAGGGAD NMGVFYDAGL VFETNTAKGT GIRTDPSCPV SSRRRRAVTI SDVITSMASK
YHGLAKECCV DGMRDNTMGY TCDRRAQYIS DGDVCVQAFL VCCTEMASKK IESKQDALLL
SRSEEDDDDD AYMRSEDIVS RSQFPESWMW EDTNLPECPA QNKHCESTSV IRNNFLKDSI
TTWQITAISL SKTHGICVAD PFEMIVLKEF FIDLKLPYSA VRNEQLEVKA ILHNYSEDPI
IVRVELMENG EVCSSASKKG KYRQEVNMDP MSTRVVPYVI IPMKLGLHSI EVKASVKNSG
SNDGVKRDLR VVAEGVLVKK ETNVLLNPVK HGGEQTSHIP SGVPRNQVPN SDADTLISVT
AGEQTSVLVE QAISGDSLGS LIVQPVGCGE QNMIYMTLPV IATHYLDNTK KWEDIGLDKR
NTAIKYINIG YQRQLAYRKE DGSYAAWVSR QSSTWLTAYV VKVFAMSSTL ISVQENVLCT
AVKWLILNTQ QPDGIFNEFA PVIHAEMTGN VRGSDNDASM TAFVLIAMQE ASSVCEQSVN
SLPGSMAKAV AYLEKRLPHL TNPYAVAMTS YALANAGKLN KETLLKFASP QLDHWPVPGG
YQYTLEATSY ALLALVKVKA FEEAGPIVRW LNKQKKVGGG YGSTQSTIMV FQAVAEYWSH
VKDLKDFDLN INLEVAGRAS VTKWSINNKN QFHTRTDKVN SIDKDLTVKA SGNGEATLSV
VTLYYALPEE KDSDCESFDL SVTLTKMDKT SHEDAKESFM LTIEVLYKNS ERDATMSILD
IGLLTGFIVD TDDLNQLSKG RERYIEKFEM DKVLSERGSL ILYLDKVSHK LEDRISFKIH
RVQEVGVLQP AAVSVYEYYN QKRCVKFYHP QREGGTLSRL CLGDVCTCAE ESCSMQKKGE
PDVQRIDKAC GAGLDYVYKA TVVDSKLTTH TDTYTVKIDL VIKPGTDEGV EGKNRDFMGL
AYCREALGLM QGKTYMIMGK SEDLHRVEDK GLLQYKYVLG EQTWIEYWPS QQECTSRDYR
EVCLGIDEFI NQITTFGCPV
