GenomeNet

Database: UniProt
Entry: P98094
LinkDB: P98094
Original site: P98094 
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   14-MAY-2014, entry version 80.
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;
OC   Hyperotreti; Myxiniformes; 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   Gene3D; 1.20.91.20; -; 1.
DR   Gene3D; 1.50.10.20; -; 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_comp_syst.
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; 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   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
//
DBGET integrated database retrieval system