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-APR-2013, entry version 76.
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; Hyperotreti; Myxiniformes;
OC Myxinidae; Eptatretinae; Eptatretus.
OX NCBI_TaxID=7764;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=1372251;
RA Ishiguro H., Kobayashi K., Suzuki M., Titani K., Tomonaga S.,
RA 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
CC complement system. After activation (C3b), it can bind covalently,
CC via its reactive thioester, to cell surface carbohydrates or
CC immune aggregates. Cyclostomates C3 appears to represent the
CC common ancestor of mammalian C3 and C4, showing similarities to
CC both proteins.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Contains 1 anaphylatoxin-like domain.
CC -!- SIMILARITY: Contains 1 NTR domain.
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DR EMBL; Z11595; CAA77677.1; -; mRNA.
DR EMBL; Z11596; CAB63257.1; ALT_SEQ; Genomic_DNA.
DR PIR; S21045; S21045.
DR ProteinModelPortal; P98094; -.
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 GO; GO:0010951; P:negative regulation of endopeptidase activity; IEA:GOC.
DR Gene3D; 1.20.91.20; -; 1.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR011626; A2M_comp.
DR InterPro; IPR002890; A2M_N.
DR InterPro; IPR011625; A2M_N_2.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
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 Pfam; PF00207; A2M; 1.
DR Pfam; PF07678; A2M_comp; 1.
DR Pfam; PF01835; A2M_N; 1.
DR Pfam; PF07703; A2M_N_2; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF10569; Thiol-ester_cl; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SUPFAM; SSF49410; AM_receptor_bind; 1.
DR SUPFAM; SSF47686; Anaphylatoxin; 1.
DR SUPFAM; SSF48239; Terp_cyc_toroid; 1.
DR SUPFAM; SSF50242; TIMP_like; 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 Secreted; Thioester bond.
FT CHAIN <1 1620 Complement C3.
FT /FTId=PRO_0000005942.
FT CHAIN <1 633 Complement C3 beta chain (By similarity).
FT /FTId=PRO_0000005943.
FT CHAIN 634 1336 Complement C3 alpha chain (By
FT similarity).
FT /FTId=PRO_0000005944.
FT CHAIN 634 714 C3a anaphylatoxin (By similarity).
FT /FTId=PRO_0000005945.
FT CHAIN 1343 1620 Complement C3 gamma chain (By
FT similarity).
FT /FTId=PRO_0000005946.
FT DOMAIN 658 694 Anaphylatoxin-like.
FT DOMAIN 1479 1616 NTR.
FT REGION 1406 1416 Properdin-binding.
FT CARBOHYD 190 190 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 989 989 N-linked (GlcNAc...) (Potential).
FT DISULFID 526 780 Interchain (between beta and alpha
FT chains) (By similarity).
FT DISULFID 593 628 By similarity.
FT DISULFID 658 686 By similarity.
FT DISULFID 659 693 By similarity.
FT DISULFID 672 694 By similarity.
FT DISULFID 836 1474 By similarity.
FT DISULFID 1062 1114 By similarity.
FT DISULFID 1321 1451 By similarity.
FT DISULFID 1356 1420 By similarity.
FT DISULFID 1467 1472 By similarity.
FT DISULFID 1479 1551 By similarity.
FT DISULFID 1499 1616 By similarity.
FT DISULFID 1598 1607 By similarity.
FT CROSSLNK 970 973 Isoglutamyl cysteine thioester (Cys-Gln)
FT (By similarity).
FT NON_TER 1 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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