CO5_HUMAN
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 03-AUG-2022, entry version 235.
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="http://structure.bmc.lu.se/idbase/C5base/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Complement C5 entry;
CC URL="https://en.wikipedia.org/wiki/Complement_component_5";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/c5/";
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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 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 AlphaFoldDB; P01031; -.
DR BMRB; P01031; -.
DR SASBDB; P01031; -.
DR SMR; P01031; -.
DR BioGRID; 107188; 33.
DR ComplexPortal; CPX-6159; Membrane attack complex.
DR ComplexPortal; CPX-677; C5b6 complement complex.
DR IntAct; P01031; 27.
DR MINT; P01031; -.
DR STRING; 9606.ENSP00000223642; -.
DR BindingDB; P01031; -.
DR ChEMBL; CHEMBL2364163; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01257; Eculizumab.
DR DrugBank; DB00028; Human immunoglobulin G.
DR DrugBank; DB11580; Ravulizumab.
DR DrugBank; DB16416; Vilobelimab.
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 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 EPD; P01031; -.
DR jPOST; P01031; -.
DR MassIVE; P01031; -.
DR MaxQB; P01031; -.
DR PaxDb; P01031; -.
DR PeptideAtlas; P01031; -.
DR PRIDE; P01031; -.
DR ProteomicsDB; 51309; -.
DR ABCD; P01031; 19 sequenced antibodies.
DR Antibodypedia; 15836; 763 antibodies from 41 providers.
DR DNASU; 727; -.
DR Ensembl; ENST00000223642.3; ENSP00000223642.1; ENSG00000106804.8.
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 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; YVEQNQN; -.
DR OrthoDB; 20179at2759; -.
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; 8 hits in 1069 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 156 other tissues.
DR Genevisible; P01031; HS.
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:0005886; C:plasma membrane; IC:ComplexPortal.
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:0006956; P:complement activation; IDA:ComplexPortal.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IDA:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
DR GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
DR CDD; cd00017; ANATO; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR037562; Complement_C5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF83; PTHR11412:SF83; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR 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; SSF47686; SSF47686; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW Complement alternate pathway; Complement pathway; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Membrane attack complex;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..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 (associated with 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 (associated with 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 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:7NYC"
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
