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 02-OCT-2024, entry version 247. DE RecName: Full=Complement C5; 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 C5 alpha' chain; DE Flags: Precursor; GN Name=C5; 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. 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 FUNCTION, AND INTERACTION WITH C5AR1. 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 [10] RP INTERACTION WITH C5AR1. 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] RP INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY. 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 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] {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 [26] {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 [27] 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 [28] 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: 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 (PubMed:8182049). C5a is also a potent CC chemokine which stimulates the locomotion of polymorphonuclear CC leukocytes and directs their migration toward sites of inflammation. CC {ECO:0000269|PubMed:8182049}. 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 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:27018802}. CC -!- SUBUNIT: [C5a anaphylatoxin]: Interacts with C5AR1. CC {ECO:0000269|PubMed:8182049, ECO:0000269|PubMed:9553099}. 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. 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. Note=The disease is CC caused by variants 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-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; 38. DR ComplexPortal; CPX-6159; Membrane attack complex. DR ComplexPortal; CPX-677; C5b6 complement complex. 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; 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; 4 sites, 8 N-linked glycans (3 sites). 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; 1000 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; 4033541at2759; -. 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 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; Disulfide bond; Glycoprotein; Immunity; KW Inflammatory response; Innate immunity; Membrane attack complex; KW Proteomics identification; Reference proteome; Secreted; Signal. 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 /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 C5 alpha' chain" 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 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:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT DISULFID 634..669 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" 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:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT DISULFID 866..1527 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS" FT DISULFID 1101..1159 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT DISULFID 1375..1505 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT DISULFID 1405..1474 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9" FT DISULFID 1520..1525 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS" FT DISULFID 1532..1606 FT /evidence="ECO:0000269|PubMed:15598652, FT ECO:0000269|PubMed:18536718, ECO:0000269|PubMed:20133685, FT ECO:0007744|PDB:1XWE, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS" FT DISULFID 1553..1676 FT /evidence="ECO:0000269|PubMed:15598652, FT ECO:0000269|PubMed:18536718, ECO:0000269|PubMed:20133685, FT ECO:0007744|PDB:1XWE, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS" FT DISULFID 1654..1657 FT /evidence="ECO:0000269|PubMed:18536718, FT ECO:0000269|PubMed:20133685, ECO:0007744|PDB:3CU7, FT ECO:0007744|PDB:3KLS" 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 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 397..399 FT /evidence="ECO:0007829|PDB:7NYC" 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 965..967 FT /evidence="ECO:0007829|PDB:7NYC" 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 TURN 1028..1030 FT /evidence="ECO:0007829|PDB:7NYC" 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 1445..1447 FT /evidence="ECO:0007829|PDB:7NYC" 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 HELIX 1607..1609 FT /evidence="ECO:0007829|PDB:7NYC" 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 //