CO5_RAT
ID CO5_RAT Reviewed; 1681 AA.
AC P08650; A0A096P6L9; Q63078;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Complement C5;
DE Contains:
DE RecName: Full=Complement C5 beta chain;
DE Contains:
DE RecName: Full=Complement C5 alpha chain;
DE Contains:
DE RecName: Full=C5a anaphylatoxin;
DE Contains:
DE RecName: Full=Complement C5 alpha' chain;
DE Flags: Precursor;
GN Name=C5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 679-755.
RC STRAIN=Lewis; TISSUE=Liver;
RX PubMed=9116048; DOI=10.1016/s0167-4781(97)00006-7;
RA Rothermel E., Rolf O., Goetze O., Zwirner J.;
RT "Nucleotide and corrected amino acid sequence of the functional recombinant
RT rat anaphylatoxin C5a.";
RL Biochim. Biophys. Acta 1351:9-12(1997).
RN [3]
RP PROTEIN SEQUENCE OF 679-755.
RA Cui L.-X., Ferreri K., Hugli T.E.;
RT "Characterization of rat C5a, a uniquely active spasmogen.";
RL Complement 2:18-19(1985).
RN [4]
RP PROTEIN SEQUENCE OF 679-755, AND SUBCELLULAR LOCATION.
RC TISSUE=Serum;
RX PubMed=7987212; DOI=10.1002/pro.5560030803;
RA Cui L.-X., Carney D.F., Hugli T.E.;
RT "Primary structure and functional characterization of rat C5a: an
RT anaphylatoxin with unusually high potency.";
RL Protein Sci. 3:1169-1177(1994).
RN [5] {ECO:0007744|PDB:6JV7, ECO:0007744|PDB:6JV8}
RP X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 679-749, AND DISULFIDE BONDS.
RA Zuo C.;
RT "Chimeric protein probes for C5a receptors through fusion of anaphylatoxin
RT C5a core region with a small-molecule antagonist.";
RL Submitted (APR-2019) to the PDB data bank.
CC -!- FUNCTION: Activation of C5 by a C5 convertase initiates the spontaneous
CC assembly of the late complement components, C5-C9, into the membrane
CC attack complex. C5b has a transient binding site for C6. The C5b-C6
CC complex is the foundation upon which the lytic complex is assembled.
CC -!- FUNCTION: [C5a anaphylatoxin]: Derived from proteolytic degradation of
CC complement C5, C5a anaphylatoxin is a mediator of local inflammatory
CC process. Binding to the receptor C5AR1 induces a variety of responses
CC including intracellular calcium release, contraction of smooth muscle,
CC increased vascular permeability, and histamine release from mast cells
CC and basophilic leukocytes. C5a is also a potent chemokine which
CC stimulates the locomotion of polymorphonuclear leukocytes and directs
CC their migration toward sites of inflammation.
CC {ECO:0000250|UniProtKB:P01031}.
CC -!- SUBUNIT: C5 precursor is first processed by the removal of 4 basic
CC residues, forming two chains, beta and alpha, linked by a disulfide
CC bond. C5 convertase activates C5 by cleaving the alpha chain, releasing
CC C5a anaphylatoxin and generating C5b (beta chain + alpha' chain).
CC {ECO:0000250|UniProtKB:P01031}.
CC -!- SUBUNIT: [C5a anaphylatoxin]: Interacts with C5AR1.
CC {ECO:0000250|UniProtKB:P01031}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7987212}.
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DR EMBL; AABR07051491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X91892; CAA62994.1; -; mRNA.
DR PIR; A57689; A57689.
DR PDB; 6JV7; X-ray; 1.31 A; A=679-749.
DR PDB; 6JV8; X-ray; 1.58 A; A=680-755.
DR PDBsum; 6JV7; -.
DR PDBsum; 6JV8; -.
DR AlphaFoldDB; P08650; -.
DR SMR; P08650; -.
DR STRING; 10116.ENSRNOP00000025534; -.
DR iPTMnet; A0A096P6L9; -.
DR PaxDb; P08650; -.
DR PRIDE; P08650; -.
DR UCSC; RGD:2237; rat.
DR RGD; 2237; C5.
DR VEuPathDB; HostDB:ENSRNOG00000018899; -.
DR eggNOG; KOG1366; Eukaryota.
DR HOGENOM; CLU_001634_4_2_1; -.
DR InParanoid; P08650; -.
DR OMA; YVEQNQN; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000018899; Expressed in liver and 4 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005579; C:membrane attack complex; ISO:RGD.
DR GO; GO:0031714; F:C5a anaphylatoxin chemotactic receptor binding; IDA:RGD.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:RGD.
DR GO; GO:0006935; P:chemotaxis; IDA:RGD.
DR GO; GO:0006956; P:complement activation; ISO:RGD.
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:0097273; P:creatinine homeostasis; ISO:RGD.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0032835; P:glomerulus development; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; IDA:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IDA:RGD.
DR GO; GO:0090594; P:inflammatory response to wounding; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:RGD.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IDA:RGD.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; ISO:RGD.
DR GO; GO:0010700; P:negative regulation of norepinephrine secretion; IDA:RGD.
DR GO; GO:0001780; P:neutrophil homeostasis; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
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; IPR041425; C3/4/5_MG1.
DR InterPro; IPR037562; Complement_C5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
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; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF83; PTHR11412:SF83; 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; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW Complement alternate pathway; Complement pathway; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Membrane attack complex;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..674
FT /note="Complement C5 beta chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000453364"
FT PROPEP 675..678
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT /id="PRO_0000453365"
FT CHAIN 679..1681
FT /note="Complement C5 alpha chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000453366"
FT CHAIN 679..755
FT /note="C5a anaphylatoxin"
FT /evidence="ECO:0000269|PubMed:7987212, ECO:0000269|Ref.3"
FT /id="PRO_0000005996"
FT CHAIN 756..1681
FT /note="Complement C5 alpha' chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000453367"
FT DOMAIN 702..736
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1536..1680
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 696..725
FT /note="Involved in C5AR1 binding"
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 567..814
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 635..670
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 702..728
FT /evidence="ECO:0007744|PDB:6JV7, ECO:0007744|PDB:6JV8"
FT DISULFID 703..735
FT /evidence="ECO:0007744|PDB:6JV7, ECO:0007744|PDB:6JV8"
FT DISULFID 715..736
FT /evidence="ECO:0007744|PDB:6JV7, ECO:0007744|PDB:6JV8"
FT DISULFID 860..887
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 870..1531
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 1105..1163
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 1379..1509
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 1409..1478
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 1524..1529
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 1536..1610
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 1557..1680
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT DISULFID 1658..1661
FT /evidence="ECO:0000250|UniProtKB:P01031"
FT CONFLICT 733
FT /note="N -> K (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 739..741
FT /note="ADK -> DP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="K -> H (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 745..747
FT /note="ESH -> NES (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 745..747
FT /note="ESH -> NQS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 683..691
FT /evidence="ECO:0007829|PDB:6JV7"
FT HELIX 697..707
FT /evidence="ECO:0007829|PDB:6JV7"
FT HELIX 715..719
FT /evidence="ECO:0007829|PDB:6JV7"
FT HELIX 726..749
FT /evidence="ECO:0007829|PDB:6JV7"
SQ SEQUENCE 1681 AA; 189081 MW; 56D466A91F0D153C CRC64;
MGLWGLLCLL IFLDKTWGQE QTYVISAPKI FRVGSSENVV IQAHGYTEAF DATISLKSYP
DKKVTYSSGY VNLSPENKFQ NSALLTLPPK QFPRDENPVS HVYLEVVSMH FSKSKKIPIT
YDNGFLFIHT DKPVYTPDQS VKIRVYSLSD DLKPAKRETV LTFVDPEGTE VDIVEENDYT
GIISFPDFKI PSNPKYGVWT IKAKYKKDFT TTGTAYFEVK EYVLPRFSVS IEPESNFIGY
KNFKNFEITV KARYFYNKMV PDAEVYIFFG LREDIKEDEK QMMHKAMQAA TLMDGAAQTC
WLAETEVREI NYNMFEDRNN NYSYIACTVT ESSGGFSEEA EIPGIKYVLS PYTLNLVATP
LFLKPGIPFS IKVQVKDSLE QLVGGVPVTL MAQTVNVNQE TSDLEPKRSI THSADGVASF
VVNLPSEVTS LKFEVKTDAP ELPEENQASK EYEAVTYSSL SQSYIYIGWT ENYKPMLVGE
YLNIIVTPKS PYIDKITHYN YLILSKGKIV QYGTKEKLLY SSYQNINIPV TQDMVPSARL
LVYYIVTGEQ TAELVADAVW INIEEKCGNQ LQVHLSPDKD VYSPGQTVSL DMVTEADSWV
ALSAVDSAVY GVRGKAKRAM QRVFQAFDDK SDLGCGAGGG RDNVDVFHLA GLTFLTNANA
DDSQYHDDSC KEILRPKRDL QLLHQKVEEQ AAKYKHRVPK KCCYDGAREN KYETCEQRVA
RVTIGPHCIR AFNECCTIAD KIRKESHHKG MLLGRIQIKA LLPVMKAEIR SYFPESWLWE
VHRVPKRNQL QVALPDSLTT WEIQGIGISD NGICVADTLK AKVFKDVFLE MNIPYSVVRG
EQIQLKGTVY NYRTSGTMFC VKMSAVEGIC TPGSSAASPQ TSRSSRCVRQ RIEGSSSHLV
TFSLLPLEIG LHSINFSLET SFGKEILVKT LRVVPEGIKR ESYAGVTLDP RGVYGIVNRR
KEFPYRIPLD LVPKTNVKRI LSVKGLLIGE FLSTVLSKEG IDILTHLPKG SAEAELMSIV
PVFYVFHYLE AGNHWNIFHP DTLARKQSLQ KKIKEGLVSV MSYRNADYSY SMWKGASSSA
WLTAFALRVL GQVNKYVKQD QYSICNSLLW LIEKCQLENG SFKENSQYLP IKLQGTLPAE
AQENTLYLTA FSVIGIRKAI GICPTEKIYT ALAKADSFLL ERTLPSKSTF TLAIVAYALS
LGDRTHPKFR SIVSALKREA LVKGDPPIYR FWRDTLQRPD SSAPNSGTAG MVETTAYALL
TSLNLKETSY VNPIIKWLSE EQRYGGGFYS TQDTINAIEG LTEYSLLVKQ LHLDMDINVS
YKHKGDFYQY KVTEKNFLGR PVEVPLNDDL IVTTGYSSGL ATVYVKTVVH KTSVAEEFCS
FYLKIDTQEV EASSYLSYSD SGHKRIIACA SYKPSKEESA SGSSHAVMDI LLPTGIGANQ
EDLRALVEGV DQLLTDYQIK DSHVILQLNS IPSRDFLCVR FRIFELFQVG FLNPATFTVY
EYHRPDKQCT MIYSTSDTNL QRVCEGAACK CVEADCGQLQ AELDLAISAD TRKETACKPE
IAYAYKVRIT SATEENIFVK YTATLLDIYK TGEAAAEKDS EITFIKKISC TNANLVKGKQ
YLIMGKEALQ IKHNFSFKYI YPLDSSTWIE YWPTDTTCPS CQAFVANLDE FAEDIFLNGC
E
