CO3_EPTBU
ID CO3_EPTBU Reviewed; 1620 AA.
AC P98094;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 C3 gamma chain;
DE Flags: Fragment;
GN Name=C3;
OS Eptatretus burgeri (Inshore hagfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC Myxiniformes; Myxinidae; Eptatretinae; Eptatretus.
OX NCBI_TaxID=7764;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1372251; DOI=10.1002/j.1460-2075.1992.tb05120.x;
RA Ishiguro H., Kobayashi K., Suzuki M., Titani K., Tomonaga S., Kurosawa Y.;
RT "Isolation of a hagfish gene that encodes a complement component.";
RL EMBO J. 11:829-837(1992).
CC -!- FUNCTION: C3 plays a central role in the activation of the complement
CC system. After activation (C3b), it can bind covalently, via its
CC reactive thioester, to cell surface carbohydrates or immune aggregates.
CC Cyclostomates C3 appears to represent the common ancestor of mammalian
CC C3 and C4, showing similarities to both proteins.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; Z11595; CAA77677.1; -; mRNA.
DR EMBL; Z11596; CAB63257.1; ALT_SEQ; Genomic_DNA.
DR PIR; S21045; S21045.
DR AlphaFoldDB; P98094; -.
DR SMR; P98094; -.
DR Proteomes; UP000694388; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd00017; ANATO; 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; IPR035711; Complement_C3-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
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; 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 Complement pathway; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW Reference proteome; Secreted; Thioester bond.
FT CHAIN <1..1620
FT /note="Complement C3"
FT /id="PRO_0000005942"
FT CHAIN <1..633
FT /note="Complement C3 beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005943"
FT CHAIN 634..1336
FT /note="Complement C3 alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005944"
FT CHAIN 634..714
FT /note="C3a anaphylatoxin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005945"
FT CHAIN 1343..1620
FT /note="Complement C3 gamma chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005946"
FT DOMAIN 658..694
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1479..1616
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 1406..1416
FT /note="Properdin-binding"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 526..780
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022,
FT ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 593..628
FT /evidence="ECO:0000250"
FT DISULFID 658..686
FT /evidence="ECO:0000250"
FT DISULFID 659..693
FT /evidence="ECO:0000250"
FT DISULFID 672..694
FT /evidence="ECO:0000250"
FT DISULFID 836..1474
FT /evidence="ECO:0000250"
FT DISULFID 1062..1114
FT /evidence="ECO:0000250"
FT DISULFID 1321..1451
FT /evidence="ECO:0000250"
FT DISULFID 1356..1420
FT /evidence="ECO:0000250"
FT DISULFID 1467..1472
FT /evidence="ECO:0000250"
FT DISULFID 1479..1551
FT /evidence="ECO:0000250"
FT DISULFID 1499..1616
FT /evidence="ECO:0000250"
FT DISULFID 1598..1607
FT /evidence="ECO:0000250"
FT CROSSLNK 970..973
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 1620 AA; 181747 MW; 21F30FAB72417358 CRC64;
VLVIAPAATS SYDDLAVAIL MVDQKKITEV HVLLVNPHTG ATLDEKKVKL QWDNKFIAFT
KLQVTPKEVE KWKEDFVRLM VKWDGGQHME IDIPLTSRRG LVFAQTDQPI YTPNNDVNIR
LFPVTRQLNP ILSSLVVDIM NPDGVVVDRI EKNAFEVEKV MELRPFHVPA ITSLGDWKIV
SWMKDKPQFN YTSGFKVEEY VLPTFDVSIT SEQPYLHVYD KAFTIHIKAM HIYGKPVMGR
AYVRYGVKHQ SKRTLLSTSS ALARFEQGEA MHTLRQKHIL EQYPDPKLLL GQSLYVEASV
ISSDAGEIEN SILDDIPIVA SPYSIKSKWT VPFFKPGVPY IYKVLVLNPD GSPASGVPIK
VSFSFDSSGN WITQKRKTMD NGIAMQTINT ARNSKKLNIK VQTEDERLEQ SQQAEASFTI
ASYSSPSGSF IHLNAHREVK SPGEHIVFDV FIKSAAKDHV LHFNYLMISN GKIHNFLQEG
RKGDTTSVSL LLTPELVPQF RLVAFFILPS GELVADSIII DVKDSCHAKL SLDVAGGKRL
FSPRDNVNFD LSGESDSWVA VGVVDKAAYV LDKKNKLTAN KVYKAMEASD LGCSVGSGKT
GPLVFRDAGL AIMAKEISGM DDVKDPGCPN GHTRRKRELV LEIAIEKAST YPAELRKCCR
DAAIESPLRL SCEERTKHIH DEGEGCQETF LECCKHVEEE LLIAMEEEDE DLGRSQGEDF
MIQESQVVIR SHFPESFMWE IIKLSRSAEN GKSRITKKMP DSITTWDIQA VEVSQSKGLC
VGPSLELTVF KQFFLKVHTP YALKQYEQVE LRVVIYNYMN QDVKGEIQVK CGDGICTDAE
QNEPLKSRFA VEKNSATSFS FMVVPLSSSD SSVSVLARVF GSDVHDAVEK DLRVMPEGNY
EEMSRSWSVQ PRRHGGQQVI VVDNETPQNV VPGTEMSAFL SAQGNLVAET IQNTLKGSKI
SNLLRLPRGC GEQNMMYTSI TVMVARYLNR SDQWNKMGDP QLKKRSFDFI TSGFASQLTY
RKPDYSYAAW LHRASSTWLT AFVAKVFSQA RQLVFIPVSE ICGSVRWLMR KQDKDGSFLE
SKPVVHLNMM GQVTGKVVLT SFVFIALLEA RESCINEVEG FTVVVEKAHG YLTSQAMNGL
EDFPLAITAY ALSLWKVSDG AAKVTMHTLK TSGLQTEELI HWGSNKGKAA AVESTAYGLL
AAIQHEEGEI AEKATNWLSQ SATFGGYFQS TQDTVMALQA LTGFESCQSR MKKMDLSFKI
RAEENGVFDK EFQITNDNAF VQKPFKVPVH GQLTVTASGT GQGILTFVKK YREKVVIKKD
CKGFSLEITT NLDNQVKQRR RQSINPEFNV YRFIGCFRYL RNQEPGMVVM DISLPTGFEA
KKKDLDDMKN LVDNYIVQYE IRPGRVFLYL DKVNKDEKNC VGFRLNQVFE SNLVLPVTAT
VFEYYEPDFR CSKSYHPKME VNPDASCHGN ICNCLQRHCV ELKGMADEDR NADRNGNACR
AEYVFIIGVT KVTKTASYIN INAALKTVLK KGMDQAINVG ARRSFVIPMH CGKNLNVSPG
DIYLVMGMHN AHWRNSDRTQ YVLTSDTWFE KFPLESVCRL PSPPASCQVS ENFKGCSLKG
