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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
 
 
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