ID CO5_HUMAN Reviewed; 1676 AA. AC P01031; Q14CJ0; Q27I61; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 4. DT 18-JUN-2025, entry version 251. DE RecName: Full=Complement C5 {ECO:0000305}; DE AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4; 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 C5b; DE AltName: Full=Complement C5 alpha' chain; DE Flags: Precursor; GN Name=C5 {ECO:0000303|PubMed:1984448, ECO:0000312|HGNC:HGNC:1331}; GN Synonyms=CPAMD4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-389 AND ILE-802. RX PubMed=1984448; RA Haviland D.L., Haviland J.C., Fleischer D.T., Hunt A., Wetsel R.A.; RT "Complete cDNA sequence of human complement pro-C5. Evidence of truncated RT transcripts derived from a single copy gene."; RL J. Immunol. 146:362-368(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-145; GLY-449; ILE-802; RP GLN-928; VAL-933; THR-1033; ASN-1037; LYS-1043; ASN-1310 AND ASP-1437. RG SeattleSNPs variation discovery resource; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-802. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-802. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 412-1676, AND VARIANT ILE-802. RX PubMed=3365401; DOI=10.1021/bi00405a012; RA Wetsel R.A., Lemons R.S., Lebeau M.M., Barnum S.R., Noack D., Tack B.F.; RT "Molecular analysis of human complement component C5: localization of the RT structural gene to chromosome 9."; RL Biochemistry 27:1474-1482(1988). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 412-1676, AND VARIANT ILE-802. RX PubMed=2579066; DOI=10.1016/s0021-9258(18)89523-0; RA Lundwall A.B., Wetsel R.A., Kristensen T., Whitehead A.S., Woods D.E., RA Ogden R.C., Colten H.R., Tack B.F.; RT "Isolation and sequence analysis of a cDNA clone encoding the fifth RT complement component."; RL J. Biol. Chem. 260:2108-2112(1985). RN [7] RP PROTEIN SEQUENCE OF 678-751, AND SUBCELLULAR LOCATION. RX PubMed=690134; DOI=10.1016/s0021-9258(17)38013-4; RA Fernandez H.N., Hugli T.E.; RT "Primary structural analysis of the polypeptide portion of human C5a RT anaphylatoxin. Polypeptide sequence determination and assignment of the RT oligosaccharide attachment site in C5a."; RL J. Biol. Chem. 253:6955-6964(1978). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 678-751. RX PubMed=1996961; DOI=10.1042/bj2730635; RA Bohnsack J.F., Mollison K.W., Buko A.M., Ashworth J.C., Hill H.R.; RT "Group B streptococci inactivate complement component C5a by enzymic RT cleavage at the C-terminus."; RL Biochem. J. 273:635-640(1991). RN [9] RP PROTEIN SEQUENCE OF 678-687, SUBCELLULAR LOCATION, AND PROTEOLYTIC RP CLEAVAGE. RX PubMed=106884; DOI=10.1021/bi00575a016; RA Tack B.F., Morris S.C., Prahl J.W.; RT "Fifth component of human complement: purification from plasma and RT polypeptide chain structure."; RL Biochemistry 18:1490-1497(1979). RN [10] RP PROTEIN SEQUENCE OF 752-764, AND PROTEOLYTIC CLEAVAGE. RX PubMed=6554279; DOI=10.1016/s0021-9258(17)44503-0; RA DiScipio R.G., Smith C.A., Muller-Eberhard H.J., Hugli T.E.; RT "The activation of human complement component C5 by a fluid phase C5 RT convertase."; RL J. Biol. Chem. 258:10629-10636(1983). RN [11] RP PROTEOLYTIC CLEAVAGE. RX PubMed=624565; RA Vogt W., Schmidt G., Von Buttlar B., Dieminger L.; RT "A new function of the activated third component of complement: binding to RT C5, an essential step for C5 activation."; RL Immunology 34:29-40(1978). RN [12] RP FUNCTION (C5A ANAPHYLATOXIN). RX PubMed=8182049; DOI=10.1016/s0021-9258(17)36643-7; RA DeMartino J.A., Van Riper G., Siciliano S.J., Molineaux C.J., RA Konteatis Z.D., Rosen H., Springer M.S.; RT "The amino terminus of the human C5a receptor is required for high affinity RT C5a binding and for receptor activation by C5a but not C5a analogs."; RL J. Biol. Chem. 269:14446-14450(1994). RN [13] RP FUNCTION (C5A ANAPHYLATOXIN). RX PubMed=9553099; DOI=10.1074/jbc.273.17.10411; RA Chen Z., Zhang X., Gonnella N.C., Pellas T.C., Boyar W.C., Ni F.; RT "Residues 21-30 within the extracellular N-terminal region of the C5a RT receptor represent a binding domain for the C5a anaphylatoxin."; RL J. Biol. Chem. 273:10411-10419(1998). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-741; ASN-911 AND ASN-1630. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [15] RP STRUCTURE BY NMR OF C5A. RX PubMed=3408713; DOI=10.1021/bi00410a007; RA Zuiderweg E.R.P., Mollison K.W., Henkin J., Carter G.W.; RT "Sequence-specific assignments in the 1H NMR spectrum of the human RT inflammatory protein C5a."; RL Biochemistry 27:3568-3580(1988). RN [16] RP STRUCTURE BY NMR OF C5A. RX PubMed=2784981; DOI=10.1021/bi00427a025; RA Zuiderweg E.R.P., Nettesheim D.G., Mollison K.W., Carter G.W.; RT "Tertiary structure of human complement component C5a in solution from RT nuclear magnetic resonance data."; RL Biochemistry 28:172-185(1989). RN [17] RP INVOLVEMENT IN C5D, AND VARIANTS C5D 19-GLN--CYS-1676 DEL AND RP 1476-ARG--CYS-1676 DEL. RX PubMed=7730648; RA Wang X., Fleischer D.T., Whitehead W.T., Haviland D.L., Rosenfeld S.I., RA Leddy J.P., Snyderman R., Wetsel R.A.; RT "Inherited human complement C5 deficiency. Nonsense mutations in exons 1 RT (Gln1 to Stop) and 36 (Arg1458 to Stop) and compound heterozygosity in RT three African-American families."; RL J. Immunol. 154:5464-5471(1995). RN [18] RP FUNCTION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=12878586; DOI=10.1074/jbc.m307017200; RA Rawal N., Pangburn M.K.; RT "Formation of high affinity C5 convertase of the classical pathway of RT complement."; RL J. Biol. Chem. 278:38476-38483(2003). RN [19] RP INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY. RX PubMed=15778377; DOI=10.4049/jimmunol.174.7.4172; RA Pfarr N., Prawitt D., Kirschfink M., Schroff C., Knuf M., Habermehl P., RA Mannhardt W., Zepp F., Fairbrother W., Loos M., Burge C.B., Pohlenz J.; RT "Linking C5 deficiency to an exonic splicing enhancer mutation."; RL J. Immunol. 174:4172-4177(2005). RN [20] RP INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY, AND VARIANTS ILE-389 AND ILE-802. RX PubMed=15488949; DOI=10.1016/j.molimm.2004.06.036; RA Delgado-Cervino E., Fontan G., Lopez-Trascasa M.; RT "C5 complement deficiency in a Spanish family. Molecular characterization RT of the double mutation responsible for the defect."; RL Mol. Immunol. 42:105-111(2005). RN [21] RP ASSOCIATION WITH SUSCEPTIBILITY TO LIVER FIBROSIS. RX PubMed=15995705; DOI=10.1038/ng1599; RA Hillebrandt S., Wasmuth H.E., Weiskirchen R., Hellerbrand C., Keppeler H., RA Werth A., Schirin-Sokhan R., Wilkens G., Geier A., Lorenzen J., Koehl J., RA Gressner A.M., Matern S., Lammert F.; RT "Complement factor 5 is a quantitative trait gene that modifies liver RT fibrogenesis in mice and humans."; RL Nat. Genet. 37:835-843(2005). RN [22] RP FUNCTION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=18204047; DOI=10.1074/jbc.m707591200; RA Rawal N., Rajagopalan R., Salvi V.P.; RT "Activation of complement component C5: comparison of C5 convertases of the RT lectin pathway and the classical pathway of complement."; RL J. Biol. Chem. 283:7853-7863(2008). RN [23] RP FUNCTION (COMPLEMENT C5B), AND SUBUNIT (COMPLEMENT C5B). RX PubMed=27052168; DOI=10.1016/j.celrep.2016.03.002; RA Sharp T.H., Koster A.J., Gros P.; RT "Heterogeneous MAC initiator and pore structures in a lipid bilayer by RT phase-plate cryo-electron tomography."; RL Cell Rep. 15:1-8(2016). RN [24] RP FUNCTION (COMPLEMENT C5B), AND SUBUNIT (COMPLEMENT C5B). RX PubMed=26841837; DOI=10.1038/ncomms10587; RA Serna M., Giles J.L., Morgan B.P., Bubeck D.; RT "Structural basis of complement membrane attack complex formation."; RL Nat. Commun. 7:10587-10587(2016). RN [25] RP FUNCTION (COMPLEMENT C5B), SUBUNIT (COMPLEMENT C5B), AND PROTEOLYTIC RP CLEAVAGE. RX PubMed=30643019; DOI=10.15252/embj.201899852; RA Heesterbeek D.A., Bardoel B.W., Parsons E.S., Bennett I., Ruyken M., RA Doorduijn D.J., Gorham R.D. Jr., Berends E.T., Pyne A.L., Hoogenboom B.W., RA Rooijakkers S.H.; RT "Bacterial killing by complement requires membrane attack complex formation RT via surface-bound C5 convertases."; RL EMBO J. 38:0-0(2019). RN [26] RP SUBUNIT (COMPLEMENT C5B), AND SUBCELLULAR LOCATION (COMPLEMENT C5B). RX PubMed=31061395; DOI=10.1038/s41467-019-10058-7; RA Parsons E.S., Stanley G.J., Pyne A.L.B., Hodel A.W., Nievergelt A.P., RA Menny A., Yon A.R., Rowley A., Richter R.P., Fantner G.E., Bubeck D., RA Hoogenboom B.W.; RT "Single-molecule kinetics of pore assembly by the membrane attack RT complex."; RL Nat. Commun. 10:2066-2066(2019). RN [27] RP FUNCTION (COMPLEMENT C5B), SUBUNIT (COMPLEMENT C5B), AND SUBCELLULAR RP LOCATION (COMPLEMENT C5B). RX PubMed=32569291; DOI=10.1371/journal.ppat.1008606; RA Doorduijn D.J., Bardoel B.W., Heesterbeek D.A.C., Ruyken M., Benn G., RA Parsons E.S., Hoogenboom B.W., Rooijakkers S.H.M.; RT "Bacterial killing by complement requires direct anchoring of membrane RT attack complex precursor C5b-7."; RL PLoS Pathog. 16:e1008606-e1008606(2020). RN [28] RP STRUCTURE BY NMR OF C5A. RX PubMed=2730871; DOI=10.1021/bi00432a008; RA Zuiderweg E.R.P., Fesik S.W.; RT "Heteronuclear three-dimensional NMR spectroscopy of the inflammatory RT protein C5a."; RL Biochemistry 28:2387-2391(1989). RN [29] RP STRUCTURE BY NMR OF 679-747 OF C5A, AND DISULFIDE BONDS. RX PubMed=9007977; DOI=10.1002/pro.5560060107; RA Zhang X., Boyar W., Galakatos N., Gonnella N.C.; RT "Solution structure of a unique C5a semi-synthetic antagonist: implications RT in receptor binding."; RL Protein Sci. 6:65-72(1997). RN [30] RP STRUCTURE BY NMR OF 679-751 OF C5A, AND DISULFIDE BONDS. RX PubMed=9188742; RX DOI=10.1002/(sici)1097-0134(199706)28:2<261::aid-prot13>3.0.co;2-g; RA Zhang X., Boyar W., Toth M.J., Wennogle L., Gonnella N.C.; RT "Structural definition of the C5a C-terminus by two-dimensional nuclear RT magnetic resonance spectroscopy."; RL Proteins 28:261-267(1997). RN [31] RP STRUCTURE BY NMR OF 1530-1676, AND DISULFIDE BONDS. RX PubMed=15598652; DOI=10.1074/jbc.m413126200; RA Bramham J., Thai C.-T., Soares D.C., Uhrin D., Ogata R.T., Barlow P.N.; RT "Functional insights from the structure of the multifunctional C345C domain RT of C5 of complement."; RL J. Biol. Chem. 280:10636-10645(2005). RN [32] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), INTERACTION WITH TICK COMPLEMENT RP INHIBITOR OMCI, GLYCOSYLATION AT ASN-741 AND ASN-911, AND DISULFIDE BONDS. RX PubMed=18536718; DOI=10.1038/ni.1625; RA Fredslund F., Laursen N.S., Roversi P., Jenner L., Oliveira C.L.P., RA Pedersen J.S., Nunn M.A., Lea S.M., Discipio R., Sottrup-Jensen L., RA Andersen G.R.; RT "Structure of and influence of a tick complement inhibitor on human RT complement component 5."; RL Nat. Immunol. 9:753-760(2008). RN [33] RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS), INTERACTION WITH STAPHYLOCOCCUS RP AUREUS PROTEIN SSL7 (MICROBIAL INFECTION), GLYCOSYLATION AT ASN-741 AND RP ASN-911, AND DISULFIDE BONDS. RX PubMed=20133685; DOI=10.1073/pnas.0910565107; RA Laursen N.S., Gordon N., Hermans S., Lorenz N., Jackson N., Wines B., RA Spillner E., Christensen J.B., Jensen M., Fredslund F., Bjerre M., RA Sottrup-Jensen L., Fraser J.D., Andersen G.R.; RT "Structural basis for inhibition of complement C5 by the SSL7 protein from RT Staphylococcus aureus."; RL Proc. Natl. Acad. Sci. U.S.A. 107:3681-3686(2010). RN [34] RP X-RAY CRYSTALLOGRAPHY (4.30 ANGSTROMS) OF 20-1676 IN COMPLEX WITH COBRA RP VENOM FACTOR, GLYCOSYLATION AT ASN-911, AND DISULFIDE BONDS. RX PubMed=21217642; DOI=10.1038/emboj.2010.341; RA Laursen N.S., Andersen K.R., Braren I., Spillner E., Sottrup-Jensen L., RA Andersen G.R.; RT "Substrate recognition by complement convertases revealed in the C5-cobra RT venom factor complex."; RL EMBO J. 30:606-616(2011). RN [35] {ECO:0007744|PDB:4A5W} RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 19-1676 IN COMPLEX WITH C6, AND RP SUBUNIT (COMPLEMENT C5B). RX PubMed=22832194; DOI=10.1016/j.celrep.2012.02.003; RA Hadders M.A., Bubeck D., Roversi P., Hakobyan S., Forneris F., Morgan B.P., RA Pangburn M.K., Llorca O., Lea S.M., Gros P.; RT "Assembly and regulation of the membrane attack complex based on structures RT of C5b6 and sC5b9."; RL Cell Rep. 1:200-207(2012). RN [36] {ECO:0007744|PDB:4E0S} RP X-RAY CRYSTALLOGRAPHY (4.21 ANGSTROMS) IN COMPLEX WITH C6, INTERACTION WITH RP C6, AND DISULFIDE BONDS. RX PubMed=22500023; DOI=10.1074/jbc.m112.361121; RA Aleshin A.E., DiScipio R.G., Stec B., Liddington R.C.; RT "Crystal structure of C5b-6 suggests structural basis for priming assembly RT of the membrane attack complex."; RL J. Biol. Chem. 287:19642-19652(2012). RN [37] {ECO:0000312|PDB:5HCC, ECO:0007744|PDB:5HCD, ECO:0007744|PDB:5HCE} RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH TICK COMPLEMENT RP INHIBITORS OMCI; RACI1; RACI2 AND RACI3, INTERACTION WITH TICK COMPLEMENT RP INHIBITORS OMCI; RACI1; RACI2 AND RACI3, GLYCOSYLATION AT ASN-911, AND RP DISULFIDE BONDS. RC TISSUE=Salivary gland; RX PubMed=27018802; DOI=10.1038/nsmb.3196; RA Jore M.M., Johnson S., Sheppard D., Barber N.M., Li Y.I., Nunn M.A., RA Elmlund H., Lea S.M.; RT "Structural basis for therapeutic inhibition of complement C5."; RL Nat. Struct. Mol. Biol. 23:378-386(2016). RN [38] {ECO:0007744|PDB:6H03, ECO:0007744|PDB:6H04} RP STRUCTURE BY ELECTRON MICROSCOPY (5.60 ANGSTROMS) OF 19-1676 OF MEMBRANE RP ATTACK COMPLEX, FUNCTION (COMPLEMENT C5B), SUBCELLULAR LOCATION (COMPLEMENT RP C5B), AND SUBUNIT (COMPLEMENT C5B). RX PubMed=30552328; DOI=10.1038/s41467-018-07653-5; RA Menny A., Serna M., Boyd C.M., Gardner S., Joseph A.P., Morgan B.P., RA Topf M., Brooks N.J., Bubeck D.; RT "CryoEM reveals how the complement membrane attack complex ruptures lipid RT bilayers."; RL Nat. Commun. 9:5316-5316(2018). RN [39] {ECO:0000312|PDB:6RPT, ECO:0000312|PDB:6RQJ} RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 348-460 IN COMPLEX WITH THE TICK RP COMPLEMENT INHBIBITORS OMCI; RACI1 AND CIRPT1, STRUCTURE BY ELECTRON RP MICROSCOPY (3.5 ANGSTROMS) OF 20-1676 IN COMPLEX WITH CIRPT1, INTERACTION RP WITH THE TICK COMPLEMENT INHIBITOR CIRPT1, BINDING REGION TO CIRPT1, AND RP DISULFIDE BOND. RX PubMed=31871188; DOI=10.1073/pnas.1909973116; RA Reichhardt M.P., Johnson S., Tang T., Morgan T., Tebeka N., Popitsch N., RA Deme J.C., Jore M.M., Lea S.M.; RT "An inhibitor of complement C5 provides structural insights into RT activation."; RL Proc. Natl. Acad. Sci. U.S.A. 117:362-370(2020). RN [40] {ECO:0007744|PDB:7NYC, ECO:0007744|PDB:7NYD} RP STRUCTURE BY ELECTRON MICROSCOPY (3.27 ANGSTROMS) OF 19-1976 OF MEMBRANE RP ATTACK COMPLEX, AND ACTIVITY REGULATION. RX PubMed=34667172; DOI=10.1038/s41467-021-26366-w; RA Menny A., Lukassen M.V., Couves E.C., Franc V., Heck A.J.R., Bubeck D.; RT "Structural basis of soluble membrane attack complex packaging for RT clearance."; RL Nat. Commun. 12:6086-6086(2021). RN [41] {ECO:0007744|PDB:8B0F, ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) IN COMPLEX WITH THE RP MEMBRANE ATTACK COMPLEX, AND ACTIVITY REGULATION (COMPLEMENT C5B). RX PubMed=36797260; DOI=10.1038/s41467-023-36441-z; RA Couves E.C., Gardner S., Voisin T.B., Bickel J.K., Stansfeld P.J., RA Tate E.W., Bubeck D.; RT "Structural basis for membrane attack complex inhibition by CD59."; RL Nat. Commun. 14:890-890(2023). RN [42] RP VARIANT TYR-966, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22028381; DOI=10.1093/jmcb/mjr024; RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., RA Zeng R., Wu J.R.; RT "Quantitative detection of single amino acid polymorphisms by targeted RT proteomics."; RL J. Mol. Cell Biol. 3:309-315(2011). RN [43] RP VARIANTS CYS-885 AND HIS-885, AND INVOLVEMENT IN POOR RESPONSE TO RP ECULIZUMAB. RX PubMed=24521109; DOI=10.1056/nejmoa1311084; RA Nishimura J., Yamamoto M., Hayashi S., Ohyashiki K., Ando K., Brodsky A.L., RA Noji H., Kitamura K., Eto T., Takahashi T., Masuko M., Matsumoto T., RA Wano Y., Shichishima T., Shibayama H., Hase M., Li L., Johnson K., RA Lazarowski A., Tamburini P., Inazawa J., Kinoshita T., Kanakura Y.; RT "Genetic variants in C5 and poor response to eculizumab."; RL N. Engl. J. Med. 370:632-639(2014). CC -!- FUNCTION: Precursor of the C5a anaphylatoxin and complement C5b CC components of the complement pathways, which consist in a cascade of CC proteins that leads to phagocytosis and breakdown of pathogens and CC signaling that strengthens the adaptive immune system (PubMed:12878586, CC PubMed:18204047, PubMed:30643019, PubMed:6554279). Activated downstream CC of classical, alternative, lectin and GZMK complement pathways CC (PubMed:12878586, PubMed:18204047, PubMed:30643019, PubMed:6554279). CC {ECO:0000269|PubMed:12878586, ECO:0000269|PubMed:18204047, CC ECO:0000269|PubMed:30643019, ECO:0000269|PubMed:6554279}. CC -!- FUNCTION: [Complement C5b]: Component of the membrane attack complex CC (MAC), a multiprotein complex activated by the complement cascade, CC which inserts into a target cell membrane and forms a pore, leading to CC target cell membrane rupture and cell lysis (PubMed:26841837, CC PubMed:27052168, PubMed:30552328, PubMed:30643019). Complement C5b is CC generated following cleavage by C5 convertase and initiates formation CC of the MAC complex: C5b binds sequentially C6, C7, C8 and multiple CC copies of the pore-forming subunit C9 (PubMed:30552328, CC PubMed:30643019). During MAC complex assembly, the C5b6 subcomplex, CC composed of complement C5b and C6, associates with the outer leaflet of CC target cell membrane, reducing the energy for membrane bending CC (PubMed:30552328, PubMed:32569291). {ECO:0000269|PubMed:26841837, CC ECO:0000269|PubMed:27052168, ECO:0000269|PubMed:30552328, CC ECO:0000269|PubMed:30643019, ECO:0000269|PubMed:32569291}. CC -!- FUNCTION: [C5a anaphylatoxin]: Mediator of local inflammatory process CC released following cleavage by C5 convertase (PubMed:8182049, CC PubMed:9553099). Acts by binding to its receptor (C5AR1 or C5AR2), CC activating G protein-coupled receptor signaling and inducing a variety CC of responses including intracellular calcium release, contraction of CC smooth muscle, increased vascular permeability, and histamine release CC from mast cells and basophilic leukocytes (PubMed:8182049, CC PubMed:9553099). C5a is also a potent chemokine which stimulates the CC locomotion of polymorphonuclear leukocytes and directs their migration CC toward sites of inflammation (PubMed:8182049, PubMed:9553099). CC {ECO:0000269|PubMed:8182049, ECO:0000269|PubMed:9553099}. CC -!- ACTIVITY REGULATION: [Complement C5b]: Membrane attack complex (MAC) CC assembly is inhibited by CD59, thereby protecting self-cells from CC damage during complement activation (PubMed:36797260). MAC assembly is CC also inhibited by clusterin (CLU) chaperones that inhibit CC polymerization of C9 (PubMed:34667172). {ECO:0000269|PubMed:34667172, CC ECO:0000269|PubMed:36797260}. CC -!- SUBUNIT: In absence of complement activation, the C5 precursor is first CC processed by the removal of 4 basic residues, forming two chains, beta CC and alpha, linked by a disulfide bond. {ECO:0000269|PubMed:106884}. CC -!- SUBUNIT: [Complement C5b]: Complement C5b is composed of complement C5b CC and complement C5 beta chains that are associated via disulfide bonds CC (PubMed:18536718, PubMed:21217642, PubMed:27018802). Component of the CC membrane attack complex (MAC), composed of complement C5b, C6, C7, C8A, CC C8B, C8G and multiple copies of the pore-forming subunit C9 CC (PubMed:22500023, PubMed:22832194, PubMed:26841837, PubMed:27052168, CC PubMed:30552328, PubMed:30643019, PubMed:31061395, PubMed:32569291). CC Interacts with the tick complement inhibitors OmCI, RaCI1 and CirpT1 CC (PubMed:18536718, PubMed:27018802, PubMed:31871188). Interacts with CC cobra venom factor (CVF) (PubMed:21217642). CC {ECO:0000269|PubMed:18536718, ECO:0000269|PubMed:21217642, CC ECO:0000269|PubMed:22500023, ECO:0000269|PubMed:22832194, CC ECO:0000269|PubMed:26841837, ECO:0000269|PubMed:27018802, CC ECO:0000269|PubMed:27052168, ECO:0000269|PubMed:30552328, CC ECO:0000269|PubMed:30643019, ECO:0000269|PubMed:31061395, CC ECO:0000269|PubMed:31871188, ECO:0000269|PubMed:32569291}. CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus CC protein SSL5. {ECO:0000269|PubMed:20133685}. CC -!- INTERACTION: CC P01031; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-8558308, EBI-7054139; CC P01031; Q13520: AQP6; NbExp=3; IntAct=EBI-8558308, EBI-13059134; CC P01031; Q03591: CFHR1; NbExp=3; IntAct=EBI-8558308, EBI-3935840; CC P01031; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-8558308, EBI-18013275; CC P01031; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-8558308, EBI-6942903; CC P01031; Q15125: EBP; NbExp=3; IntAct=EBI-8558308, EBI-3915253; CC P01031; P23276: KEL; NbExp=3; IntAct=EBI-8558308, EBI-746662; CC P01031; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-8558308, EBI-17272405; CC P01031; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-8558308, EBI-6163737; CC P01031; O14524-2: NEMP1; NbExp=3; IntAct=EBI-8558308, EBI-10969203; CC P01031; O15173: PGRMC2; NbExp=3; IntAct=EBI-8558308, EBI-1050125; CC P01031; P78424: POU6F2; NbExp=3; IntAct=EBI-8558308, EBI-12029004; CC P01031; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-8558308, EBI-17280858; CC P01031; Q91132; Xeno; NbExp=2; IntAct=EBI-8558308, EBI-7081824; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:106884}. CC -!- SUBCELLULAR LOCATION: [Complement C5b]: Secreted CC {ECO:0000269|PubMed:106884}. Target cell membrane CC {ECO:0000269|PubMed:30552328, ECO:0000269|PubMed:30643019, CC ECO:0000269|PubMed:31061395, ECO:0000269|PubMed:32569291}. CC Note=Secreted as soluble protein. Inserts into the cell membrane of CC target cells. {ECO:0000269|PubMed:30643019, CC ECO:0000269|PubMed:31061395}. CC -!- SUBCELLULAR LOCATION: [C5a anaphylatoxin]: Secreted CC {ECO:0000269|PubMed:690134}. CC -!- PTM: 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 (PubMed:106884). During activation of the complement systems, the CC alpha chain is cleaved into C5a and C5b by the C5 convertase: C5b stays CC linked to the beta chain, while C5a is released in the plasma CC (PubMed:12878586, PubMed:18204047, PubMed:30643019, PubMed:624565). The CC alpha chain is cleaved by the serine protease complement C2b component CC of the C5 convertase to generate C5a and C5b following activation by CC the classical, lectin and GZMK complement systems (PubMed:12878586, CC PubMed:18204047). The alpha chain is cleaved by CFB component of the C5 CC convertase to generate C5a and C5b following activation by the CC alternative complement system (PubMed:30643019, PubMed:624565, CC PubMed:6554279). {ECO:0000269|PubMed:106884, CC ECO:0000269|PubMed:12878586, ECO:0000269|PubMed:18204047, CC ECO:0000269|PubMed:30643019, ECO:0000269|PubMed:624565, CC ECO:0000269|PubMed:6554279}. CC -!- POLYMORPHISM: C5 variants are responsible for poor response to CC eculizumab [MIM:615749]. Eculizumab is a monoclonal antibody highly CC effective in reducing intravascular hemolysis in patients with CC paroxysmal nocturnal hemoglobinuria. It specifically binds to the CC terminal complement protein C5, inhibits its cleavage into C5a and C5b, CC and prevents the formations of the cytolytic complement pore CC (PubMed:24521109). {ECO:0000269|PubMed:24521109}. CC -!- DISEASE: Complement component 5 deficiency (C5D) [MIM:609536]: A rare CC defect of the complement classical pathway associated with CC susceptibility to severe recurrent infections, predominantly by CC Neisseria gonorrhoeae or Neisseria meningitidis. CC {ECO:0000269|PubMed:7730648}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Note=An association study of C5 haplotypes and genotypes in CC individuals with chronic hepatitis C virus infection shows that CC individuals homozygous for the C5_1 haplotype have a significantly CC higher stage of liver fibrosis than individuals carrying at least 1 CC other allele. {ECO:0000269|PubMed:15995705}. CC -!- WEB RESOURCE: Name=C5base; Note=C5 mutation db; CC URL="https://databases.lovd.nl/shared/genes/C5"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Complement C5 entry; CC URL="https://en.wikipedia.org/wiki/Complement_component_5"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M57729; AAA51925.1; -; mRNA. DR EMBL; DQ400449; ABD48959.1; -; Genomic_DNA. DR EMBL; CH471090; EAW87480.1; -; Genomic_DNA. DR EMBL; BC113738; AAI13739.1; -; mRNA. DR EMBL; BC113740; AAI13741.1; -; mRNA. DR EMBL; M65134; AAA51856.1; -; mRNA. DR CCDS; CCDS6826.1; -. DR PIR; A40075; C5HU. DR RefSeq; NP_001304092.1; NM_001317163.1. DR RefSeq; NP_001726.2; NM_001735.2. DR PDB; 1CFA; NMR; -; A=679-747. DR PDB; 1KJS; NMR; -; A=679-751. DR PDB; 1XWE; NMR; -; A=1530-1676. DR PDB; 3CU7; X-ray; 3.10 A; A/B=1-1676. DR PDB; 3HQA; X-ray; 2.59 A; A/B=679-750. DR PDB; 3HQB; X-ray; 3.30 A; A/B=679-750. DR PDB; 3KLS; X-ray; 3.60 A; A/B=1-1676. DR PDB; 3KM9; X-ray; 4.20 A; A/B=1-1676. DR PDB; 3PRX; X-ray; 4.30 A; A/C=1-1676. DR PDB; 3PVM; X-ray; 4.30 A; A/C=1-1676. DR PDB; 4A5W; X-ray; 3.50 A; A=19-1676. DR PDB; 4E0S; X-ray; 4.21 A; A=1-1676. DR PDB; 4P39; X-ray; 2.40 A; A/B/C/D=678-747. DR PDB; 4UU9; X-ray; 2.12 A; C/D=678-751. DR PDB; 5B4P; X-ray; 2.40 A; B/D=678-751. DR PDB; 5B71; X-ray; 2.11 A; E/F=20-124. DR PDB; 5HCC; X-ray; 2.59 A; A=679-1676, B=19-674. DR PDB; 5HCD; X-ray; 2.98 A; A=679-1676, B=19-674. DR PDB; 5HCE; X-ray; 3.12 A; A=679-1676, B=19-674. DR PDB; 5I5K; X-ray; 4.20 A; A/B=1-1676. DR PDB; 6H03; EM; 5.60 A; A=19-1676. DR PDB; 6H04; EM; 5.60 A; A=19-1676. DR PDB; 6RPT; X-ray; 2.70 A; A/C/E=348-460. DR PDB; 6RQJ; EM; 3.50 A; A/B=20-1676. DR PDB; 7AD6; X-ray; 2.75 A; A/B=1-1676. DR PDB; 7AD7; X-ray; 2.30 A; A/B=1-1676. DR PDB; 7NYC; EM; 3.50 A; A=19-1676. DR PDB; 7NYD; EM; 3.30 A; A=19-1676. DR PDB; 7Y64; EM; 2.90 A; E=678-751. DR PDB; 8B0F; EM; 3.00 A; A=1-1676. DR PDB; 8B0G; EM; 3.30 A; A=1-1676. DR PDB; 8B0H; EM; 3.30 A; A=1-1676. DR PDB; 8HK5; EM; 3.00 A; B=678-751. DR PDB; 8HQC; EM; 3.89 A; D=678-751. DR PDB; 8IA2; EM; 3.21 A; D=678-751. DR PDB; 8JZZ; EM; 3.31 A; D=678-751. DR PDBsum; 1CFA; -. DR PDBsum; 1KJS; -. DR PDBsum; 1XWE; -. DR PDBsum; 3CU7; -. DR PDBsum; 3HQA; -. DR PDBsum; 3HQB; -. DR PDBsum; 3KLS; -. DR PDBsum; 3KM9; -. DR PDBsum; 3PRX; -. DR PDBsum; 3PVM; -. DR PDBsum; 4A5W; -. DR PDBsum; 4E0S; -. DR PDBsum; 4P39; -. DR PDBsum; 4UU9; -. DR PDBsum; 5B4P; -. DR PDBsum; 5B71; -. DR PDBsum; 5HCC; -. DR PDBsum; 5HCD; -. DR PDBsum; 5HCE; -. DR PDBsum; 5I5K; -. DR PDBsum; 6H03; -. DR PDBsum; 6H04; -. DR PDBsum; 6RPT; -. DR PDBsum; 6RQJ; -. DR PDBsum; 7AD6; -. DR PDBsum; 7AD7; -. DR PDBsum; 7NYC; -. DR PDBsum; 7NYD; -. DR PDBsum; 7Y64; -. DR PDBsum; 8B0F; -. DR PDBsum; 8B0G; -. DR PDBsum; 8B0H; -. DR PDBsum; 8HK5; -. DR PDBsum; 8HQC; -. DR PDBsum; 8IA2; -. DR PDBsum; 8JZZ; -. DR AlphaFoldDB; P01031; -. DR BMRB; P01031; -. DR EMDB; EMD-0106; -. DR EMDB; EMD-0107; -. DR EMDB; EMD-12649; -. DR EMDB; EMD-12650; -. DR EMDB; EMD-12651; -. DR EMDB; EMD-15713; -. DR EMDB; EMD-15779; -. DR EMDB; EMD-15780; -. DR EMDB; EMD-15781; -. DR EMDB; EMD-16730; -. DR EMDB; EMD-33633; -. DR EMDB; EMD-34846; -. DR EMDB; EMD-34947; -. DR EMDB; EMD-35292; -. DR EMDB; EMD-36755; -. DR EMDB; EMD-4983; -. DR EMDB; EMD-8092; -. DR SASBDB; P01031; -. DR SMR; P01031; -. DR BioGRID; 107188; 40. DR ComplexPortal; CPX-6159; Membrane attack complex. DR ComplexPortal; CPX-677; C5b6 complement complex. DR FunCoup; P01031; 600. DR IntAct; P01031; 33. DR MINT; P01031; -. DR STRING; 9606.ENSP00000223642; -. DR BindingDB; P01031; -. DR ChEMBL; CHEMBL2364163; -. DR DrugBank; DB15165; Avacincaptad pegol. DR DrugBank; DB09130; Copper. DR DrugBank; DB16128; Crovalimab. DR DrugBank; DB01257; Eculizumab. DR DrugBank; DB00028; Human immunoglobulin G. DR DrugBank; DB15218; Pozelimab. DR DrugBank; DB11580; Ravulizumab. DR DrugBank; DB16416; Vilobelimab. DR DrugBank; DB15636; Zilucoplan. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR DrugCentral; P01031; -. DR MEROPS; I39.952; -. DR CarbonylDB; P01031; -. DR GlyConnect; 1147; 6 N-Linked glycans (3 sites). DR GlyCosmos; P01031; 4 sites, 7 glycans. DR GlyGen; P01031; 6 sites, 27 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P01031; -. DR PhosphoSitePlus; P01031; -. DR BioMuta; C5; -. DR DMDM; 166900096; -. DR CPTAC; non-CPTAC-1108; -. DR CPTAC; non-CPTAC-1109; -. DR jPOST; P01031; -. DR MassIVE; P01031; -. DR PaxDb; 9606-ENSP00000223642; -. DR PeptideAtlas; P01031; -. DR ProteomicsDB; 51309; -. DR ABCD; P01031; 19 sequenced antibodies. DR Antibodypedia; 15836; 977 antibodies from 44 providers. DR DNASU; 727; -. DR Ensembl; ENST00000223642.3; ENSP00000223642.1; ENSG00000106804.10. DR GeneID; 727; -. DR KEGG; hsa:727; -. DR MANE-Select; ENST00000223642.3; ENSP00000223642.1; NM_001735.3; NP_001726.2. DR UCSC; uc004bkv.4; human. DR AGR; HGNC:1331; -. DR CTD; 727; -. DR DisGeNET; 727; -. DR GeneCards; C5; -. DR HGNC; HGNC:1331; C5. DR HPA; ENSG00000106804; Tissue enriched (liver). DR MalaCards; C5; -. DR MIM; 120900; gene. DR MIM; 609536; phenotype. DR MIM; 615749; phenotype. DR neXtProt; NX_P01031; -. DR OpenTargets; ENSG00000106804; -. DR Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency. DR PharmGKB; PA25911; -. DR VEuPathDB; HostDB:ENSG00000106804; -. DR eggNOG; KOG1366; Eukaryota. DR GeneTree; ENSGT00940000155670; -. DR HOGENOM; CLU_001634_4_2_1; -. DR InParanoid; P01031; -. DR OMA; YKRIIAC; -. DR OrthoDB; 6359008at2759; -. DR PAN-GO; P01031; 0 GO annotations based on evolutionary models. DR PhylomeDB; P01031; -. DR TreeFam; TF313285; -. DR BRENDA; 3.4.21.43; 2681. DR PathwayCommons; P01031; -. DR Reactome; R-HSA-166665; Terminal pathway of complement. DR Reactome; R-HSA-174577; Activation of C3 and C5. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-977606; Regulation of Complement cascade. DR SignaLink; P01031; -. DR SIGNOR; P01031; -. DR BioGRID-ORCS; 727; 10 hits in 1156 CRISPR screens. DR ChiTaRS; C5; human. DR EvolutionaryTrace; P01031; -. DR GeneWiki; Complement_component_5; -. DR GenomeRNAi; 727; -. DR Pharos; P01031; Tclin. DR PRO; PR:P01031; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P01031; protein. DR Bgee; ENSG00000106804; Expressed in right lobe of liver and 158 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB. DR GO; GO:0008009; F:chemokine activity; TAS:ProtInc. DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro. DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc. 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:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IDA:BHF-UCL. DR GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL. DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL. DR CDD; cd00017; ANATO; 1. DR CDD; cd02896; complement_C3_C4_C5; 1. DR CDD; cd03582; NTR_complement_C5; 1. DR FunFam; 6.20.50.160:FF:000004; C5 isoform 3; 1. DR FunFam; 1.20.91.20:FF:000004; Complement C5; 1. DR FunFam; 1.50.10.20:FF:000020; Complement C5; 1. DR FunFam; 2.40.50.120:FF:000023; Complement C5; 1. DR FunFam; 2.60.40.10:FF:001901; Complement C5; 1. DR FunFam; 2.60.40.1930:FF:000011; Complement C5; 1. DR FunFam; 2.60.40.1930:FF:000012; Complement C5; 1. DR FunFam; 2.60.40.690:FF:000007; Complement C5; 1. DR FunFam; 2.60.40.1940:FF:000001; Complement component C3; 1. DR FunFam; 2.20.130.20:FF:000008; Complement component C5; 1. DR FunFam; 2.60.40.10:FF:001848; Complement component C5; 1. DR Gene3D; 1.50.10.20; -; 1. DR Gene3D; 2.20.130.20; -; 1. DR Gene3D; 2.40.50.120; -; 1. DR Gene3D; 2.60.120.1540; -; 1. DR Gene3D; 2.60.40.1930; -; 3. DR Gene3D; 2.60.40.1940; -; 1. DR Gene3D; 6.20.50.160; -; 1. DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1. DR Gene3D; 1.20.91.20; Anaphylotoxins (complement system); 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR009048; A-macroglobulin_rcpt-bd. DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf. DR InterPro; IPR050473; A2M/Complement_sys. 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; IPR001840; Anaphylatoxn_comp_syst_dom. DR InterPro; IPR041425; C3/4/5_MG1. DR InterPro; IPR048843; C5_CUB. 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; COMPLEMENT C5; 1. DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 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; PF21309; C5_CUB; 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 PRINTS; PR00004; ANAPHYLATOXN. 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; SSF49410; Alpha-macroglobulin receptor domain; 1. DR SUPFAM; SSF47686; Anaphylotoxins (complement system); 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. DR SUPFAM; SSF50242; TIMP-like; 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; Disease variant; Disulfide bond; Glycoprotein; KW Immunity; Inflammatory response; Innate immunity; Membrane; KW Membrane attack complex; Proteomics identification; Reference proteome; KW Secreted; Signal; Target cell membrane; Target membrane. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..673 FT /note="Complement C5 beta chain" FT /id="PRO_0000005985" FT PROPEP 674..677 FT /evidence="ECO:0000269|PubMed:690134" FT /id="PRO_0000005986" FT CHAIN 678..1676 FT /note="Complement C5 alpha chain" FT /evidence="ECO:0000305|PubMed:106884" FT /id="PRO_0000005987" FT CHAIN 678..751 FT /note="C5a anaphylatoxin" FT /evidence="ECO:0000269|PubMed:690134" FT /id="PRO_0000005988" FT CHAIN 752..1676 FT /note="Complement C5b" FT /id="PRO_0000005989" FT DOMAIN 698..732 FT /note="Anaphylatoxin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022" FT DOMAIN 1532..1676 FT /note="NTR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295" FT REGION 400..426 FT /note="Involved in the tick complement inhibitor CirpT1" FT /evidence="ECO:0000269|PubMed:31871188" FT REGION 692..721 FT /note="Involved in C5AR1 binding" FT /evidence="ECO:0000269|PubMed:9553099" FT SITE 751..752 FT /note="Cleavage; by C5 convertase" FT /evidence="ECO:0000269|PubMed:6554279" FT CARBOHYD 741 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:18536718, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT CARBOHYD 911 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:18536718, ECO:0000269|PubMed:21217642, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:3KM9" FT CARBOHYD 1115 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1630 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT DISULFID 567..810 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0000269|PubMed:30552328, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9, FT ECO:0007744|PDB:4E0S, ECO:0007744|PDB:6H03" FT DISULFID 634..669 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:3KM9, ECO:0007744|PDB:4E0S" FT DISULFID 698..724 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:9007977, FT ECO:0000269|PubMed:9188742, ECO:0007744|PDB:1CFA, FT ECO:0007744|PDB:1KJS, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT DISULFID 699..731 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:9007977, FT ECO:0000269|PubMed:9188742, ECO:0007744|PDB:1CFA, FT ECO:0007744|PDB:1KJS, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT DISULFID 711..732 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:9007977, FT ECO:0000269|PubMed:9188742, ECO:0007744|PDB:1CFA, FT ECO:0007744|PDB:1KJS, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT DISULFID 856..883 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0000269|PubMed:30552328, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9, FT ECO:0007744|PDB:4E0S, ECO:0007744|PDB:6H03" FT DISULFID 866..1527 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:4E0S" FT DISULFID 1101..1159 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0000269|PubMed:30552328, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9, FT ECO:0007744|PDB:4E0S, ECO:0007744|PDB:6H03" FT DISULFID 1375..1505 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:3KM9, ECO:0007744|PDB:4E0S" FT DISULFID 1405..1474 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:3KM9, ECO:0007744|PDB:4E0S" FT DISULFID 1520..1525 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:4E0S" FT DISULFID 1532..1606 FT /evidence="ECO:0000269|PubMed:15598652, FT ECO:0000269|PubMed:18536718, ECO:0000269|PubMed:20133685, FT ECO:0000269|PubMed:22500023, ECO:0007744|PDB:1XWE, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:4E0S" FT DISULFID 1553..1676 FT /evidence="ECO:0000269|PubMed:15598652, FT ECO:0000269|PubMed:18536718, ECO:0000269|PubMed:20133685, FT ECO:0000269|PubMed:22500023, ECO:0007744|PDB:1XWE, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:4E0S" FT DISULFID 1654..1657 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:22500023, FT ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, FT ECO:0007744|PDB:4E0S" FT VARIANT 19..1676 FT /note="Missing (in C5D)" FT /evidence="ECO:0000269|PubMed:7730648" FT /id="VAR_090455" FT VARIANT 145 FT /note="V -> I (in dbSNP:rs17216529)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_038735" FT VARIANT 354 FT /note="L -> M (in dbSNP:rs34552775)" FT /id="VAR_048822" FT VARIANT 389 FT /note="T -> I" FT /evidence="ECO:0000269|PubMed:15488949, FT ECO:0000269|PubMed:1984448" FT /id="VAR_023946" FT VARIANT 449 FT /note="R -> G (in dbSNP:rs2230213)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_038736" FT VARIANT 518 FT /note="F -> S" FT /id="VAR_001996" FT VARIANT 802 FT /note="V -> I (in dbSNP:rs17611)" FT /evidence="ECO:0000269|PubMed:15488949, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1984448, FT ECO:0000269|PubMed:2579066, ECO:0000269|PubMed:3365401, FT ECO:0000269|Ref.2, ECO:0000269|Ref.3" FT /id="VAR_014574" FT VARIANT 885 FT /note="R -> C (risk factor for poor response to eculizumab FT in PNH patients; dbSNP:rs373359894)" FT /evidence="ECO:0000269|PubMed:24521109" FT /id="VAR_071067" FT VARIANT 885 FT /note="R -> H (risk factor for poor response to eculizumab FT in PNH patients; dbSNP:rs56040400)" FT /evidence="ECO:0000269|PubMed:24521109" FT /id="VAR_071068" FT VARIANT 928 FT /note="R -> Q (in dbSNP:rs41309892)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_038737" FT VARIANT 933 FT /note="G -> V (in dbSNP:rs41309902)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_038738" FT VARIANT 966 FT /note="D -> Y (confirmed at protein level; FT dbSNP:rs2230212)" FT /evidence="ECO:0000269|PubMed:22028381" FT /id="VAR_048823" FT VARIANT 1033 FT /note="I -> T (in dbSNP:rs41311881)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_038739" FT VARIANT 1037 FT /note="D -> N (in dbSNP:rs41311883)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_038740" FT VARIANT 1043 FT /note="Q -> K (in dbSNP:rs41311887)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_038741" FT VARIANT 1053 FT /note="M -> L (in dbSNP:rs17609)" FT /id="VAR_014575" FT VARIANT 1310 FT /note="S -> N (in dbSNP:rs17610)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_014576" FT VARIANT 1365 FT /note="V -> A (in dbSNP:rs16910245)" FT /id="VAR_048824" FT VARIANT 1437 FT /note="E -> D (in dbSNP:rs17612)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_014577" FT VARIANT 1476..1676 FT /note="Missing (in C5D)" FT /evidence="ECO:0000269|PubMed:7730648" FT /id="VAR_090456" FT STRAND 22..26 FT /evidence="ECO:0007829|PDB:5B71" FT STRAND 29..45 FT /evidence="ECO:0007829|PDB:5B71" FT STRAND 50..58 FT /evidence="ECO:0007829|PDB:5B71" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:5B71" FT STRAND 65..73 FT /evidence="ECO:0007829|PDB:5B71" FT TURN 75..79 FT /evidence="ECO:0007829|PDB:5B71" FT STRAND 80..87 FT /evidence="ECO:0007829|PDB:5B71" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 101..107 FT /evidence="ECO:0007829|PDB:5B71" FT STRAND 112..120 FT /evidence="ECO:0007829|PDB:5B71" FT STRAND 124..131 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 159..164 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 170..176 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 179..184 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 197..208 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 212..219 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 226..234 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 246..253 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 261..273 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:5HCC" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:7AD6" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 296..301 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 303..306 FT /evidence="ECO:0007829|PDB:7AD7" FT TURN 307..311 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 315..318 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 322..331 FT /evidence="ECO:0007829|PDB:7AD7" FT TURN 332..334 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 337..347 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 349..351 FT /evidence="ECO:0007829|PDB:7AD6" FT STRAND 353..356 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:3CU7" FT STRAND 369..376 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 378..380 FT /evidence="ECO:0007829|PDB:4A5W" FT STRAND 387..396 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 407..410 FT /evidence="ECO:0007829|PDB:7AD7" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 417..422 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 428..437 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 440..442 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 449..456 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:6RQJ" FT STRAND 464..468 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 472..476 FT /evidence="ECO:0007829|PDB:3CU7" FT STRAND 480..489 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 493..495 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 498..505 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 508..516 FT /evidence="ECO:0007829|PDB:7AD7" FT TURN 519..521 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 522..529 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 532..534 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 536..547 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 548..550 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 552..563 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 571..577 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 580..582 FT /evidence="ECO:0007829|PDB:3CU7" FT STRAND 587..606 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 607..610 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 614..616 FT /evidence="ECO:0007829|PDB:4A5W" FT TURN 619..622 FT /evidence="ECO:0007829|PDB:7NYD" FT TURN 625..627 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 628..630 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 635..637 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 642..648 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 651..658 FT /evidence="ECO:0007829|PDB:7AD7" FT TURN 663..666 FT /evidence="ECO:0007829|PDB:5HCD" FT HELIX 678..687 FT /evidence="ECO:0007829|PDB:4UU9" FT TURN 690..692 FT /evidence="ECO:0007829|PDB:7AD6" FT HELIX 693..703 FT /evidence="ECO:0007829|PDB:4UU9" FT STRAND 707..709 FT /evidence="ECO:0007829|PDB:4UU9" FT HELIX 711..715 FT /evidence="ECO:0007829|PDB:4UU9" FT HELIX 722..740 FT /evidence="ECO:0007829|PDB:4UU9" FT TURN 744..746 FT /evidence="ECO:0007829|PDB:5B4P" FT TURN 753..755 FT /evidence="ECO:0007829|PDB:7AD6" FT STRAND 756..759 FT /evidence="ECO:0007829|PDB:7AD6" FT STRAND 764..766 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 777..789 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 796..805 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 808..811 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 815..819 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 822..828 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 831..834 FT /evidence="ECO:0007829|PDB:6RQJ" FT STRAND 838..847 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 849..851 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 853..859 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 863..866 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 874..877 FT /evidence="ECO:0007829|PDB:4A5W" FT STRAND 886..888 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 892..902 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 906..915 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 917..919 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 920..930 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 932..945 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 949..952 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 956..959 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 974..982 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 985..992 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 993..995 FT /evidence="ECO:0007829|PDB:7AD6" FT TURN 999..1002 FT /evidence="ECO:0007829|PDB:5HCC" FT HELIX 1008..1013 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1016..1027 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1031..1033 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1034..1036 FT /evidence="ECO:0007829|PDB:5HCC" FT HELIX 1038..1054 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1055..1059 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1066..1069 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1076..1089 FT /evidence="ECO:0007829|PDB:7AD7" FT TURN 1090..1092 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1097..1110 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1114..1116 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 1121..1123 FT /evidence="ECO:0007829|PDB:5HCC" FT HELIX 1133..1156 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1162..1178 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1179..1181 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1185..1196 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1203..1214 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1217..1219 FT /evidence="ECO:0007829|PDB:7AD7" FT TURN 1220..1223 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1224..1227 FT /evidence="ECO:0007829|PDB:7AD7" FT TURN 1233..1235 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1245..1260 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1264..1277 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1280..1282 FT /evidence="ECO:0007829|PDB:3CU7" FT HELIX 1287..1303 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1310..1320 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1322..1329 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1330..1332 FT /evidence="ECO:0007829|PDB:3CU7" FT STRAND 1338..1340 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1342..1344 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1346..1350 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1357..1368 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1371..1373 FT /evidence="ECO:0007829|PDB:3CU7" FT STRAND 1376..1386 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1399..1408 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1420..1427 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1432..1434 FT /evidence="ECO:0007829|PDB:7AD7" FT HELIX 1436..1444 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1451..1456 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1459..1465 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1469..1471 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1473..1481 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1485..1487 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1491..1497 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1500..1509 FT /evidence="ECO:0007829|PDB:7AD7" FT STRAND 1522..1524 FT /evidence="ECO:0007829|PDB:5HCC" FT TURN 1526..1529 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1530..1532 FT /evidence="ECO:0007829|PDB:5HCC" FT HELIX 1547..1550 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1554..1556 FT /evidence="ECO:0007829|PDB:7AD6" FT STRAND 1559..1571 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1574..1590 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1597..1605 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1616..1622 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1625..1629 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1632..1638 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1644..1647 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1650..1652 FT /evidence="ECO:0007829|PDB:5HCC" FT STRAND 1653..1656 FT /evidence="ECO:0007829|PDB:7NYD" FT HELIX 1657..1672 FT /evidence="ECO:0007829|PDB:5HCC" SQ SEQUENCE 1676 AA; 188305 MW; A7589E352F74672A CRC64; MGLLGILCFL IFLGKTWGQE QTYVISAPKI FRVGASENIV IQVYGYTEAF DATISIKSYP DKKFSYSSGH VHLSSENKFQ NSAILTIQPK QLPGGQNPVS YVYLEVVSKH FSKSKRMPIT YDNGFLFIHT DKPVYTPDQS VKVRVYSLND DLKPAKRETV LTFIDPEGSE VDMVEEIDHI GIISFPDFKI PSNPRYGMWT IKAKYKEDFS TTGTAYFEVK EYVLPHFSVS IEPEYNFIGY KNFKNFEITI KARYFYNKVV TEADVYITFG IREDLKDDQK EMMQTAMQNT MLINGIAQVT FDSETAVKEL SYYSLEDLNN KYLYIAVTVI ESTGGFSEEA EIPGIKYVLS PYKLNLVATP LFLKPGIPYP IKVQVKDSLD QLVGGVPVTL NAQTIDVNQE TSDLDPSKSV TRVDDGVASF VLNLPSGVTV LEFNVKTDAP DLPEENQARE GYRAIAYSSL SQSYLYIDWT DNHKALLVGE HLNIIVTPKS PYIDKITHYN YLILSKGKII HFGTREKFSD ASYQSINIPV TQNMVPSSRL LVYYIVTGEQ TAELVSDSVW LNIEEKCGNQ LQVHLSPDAD AYSPGQTVSL NMATGMDSWV ALAAVDSAVY GVQRGAKKPL ERVFQFLEKS DLGCGAGGGL NNANVFHLAG LTFLTNANAD DSQENDEPCK EILRPRRTLQ KKIEEIAAKY KHSVVKKCCY DGACVNNDET CEQRAARISL GPRCIKAFTE CCVVASQLRA NISHKDMQLG RLHMKTLLPV SKPEIRSYFP ESWLWEVHLV PRRKQLQFAL PDSLTTWEIQ GVGISNTGIC VADTVKAKVF KDVFLEMNIP YSVVRGEQIQ LKGTVYNYRT SGMQFCVKMS AVEGICTSES PVIDHQGTKS SKCVRQKVEG SSSHLVTFTV LPLEIGLHNI NFSLETWFGK EILVKTLRVV PEGVKRESYS GVTLDPRGIY GTISRRKEFP YRIPLDLVPK TEIKRILSVK GLLVGEILSA VLSQEGINIL THLPKGSAEA ELMSVVPVFY VFHYLETGNH WNIFHSDPLI EKQKLKKKLK EGMLSIMSYR NADYSYSVWK GGSASTWLTA FALRVLGQVN KYVEQNQNSI CNSLLWLVEN YQLDNGSFKE NSQYQPIKLQ GTLPVEAREN SLYLTAFTVI GIRKAFDICP LVKIDTALIK ADNFLLENTL PAQSTFTLAI SAYALSLGDK THPQFRSIVS ALKREALVKG NPPIYRFWKD NLQHKDSSVP NTGTARMVET TAYALLTSLN LKDINYVNPV IKWLSEEQRY GGGFYSTQDT INAIEGLTEY SLLVKQLRLS MDIDVSYKHK GALHNYKMTD KNFLGRPVEV LLNDDLIVST GFGSGLATVH VTTVVHKTST SEEVCSFYLK IDTQDIEASH YRGYGNSDYK RIVACASYKP SREESSSGSS HAVMDISLPT GISANEEDLK ALVEGVDQLF TDYQIKDGHV ILQLNSIPSS DFLCVRFRIF ELFEVGFLSP ATFTVYEYHR PDKQCTMFYS TSNIKIQKVC EGAACKCVEA DCGQMQEELD LTISAETRKQ TACKPEIAYA YKVSITSITV ENVFVKYKAT LLDIYKTGEA VAEKDSEITF IKKVTCTNAE LVKGRQYLIM GKEALQIKYN FSFRYIYPLD SLTWIEYWPR DTTCSSCQAF LANLDEFAED IFLNGC //