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Database: UniProt
Entry: P01031
LinkDB: P01031
Original site: P01031 
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   29-SEP-2021, entry version 232.
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;
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;
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;
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, 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]
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   [26]
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 tick complement inhibitor. {ECO:0000269|PubMed:18536718,
CC       ECO:0000269|PubMed:21217642}.
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; 7AD6; X-ray; 2.75 A; A/B=1-1676.
DR   PDB; 7AD7; X-ray; 2.30 A; A/B=1-1676.
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; 7AD6; -.
DR   PDBsum; 7AD7; -.
DR   BMRB; P01031; -.
DR   SASBDB; P01031; -.
DR   SMR; P01031; -.
DR   BioGRID; 107188; 26.
DR   ComplexPortal; CPX-6159; Membrane attack complex.
DR   ComplexPortal; CPX-677; C5b6 complement complex.
DR   IntAct; P01031; 25.
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; 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; 12624; -.
DR   ProteomicsDB; 51309; -.
DR   ABCD; P01031; 18 sequenced antibodies.
DR   Antibodypedia; 15836; 876 antibodies.
DR   DNASU; 727; -.
DR   Ensembl; ENST00000223642; ENSP00000223642; ENSG00000106804.
DR   GeneID; 727; -.
DR   KEGG; hsa:727; -.
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; LTWIEYW; -.
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   SIGNOR; P01031; -.
DR   BioGRID-ORCS; 727; 3 hits in 1005 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 liver and 192 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: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:0000187; P:activation of MAPK activity; 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: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: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          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:5HCC"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:5HCC"
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:5HCC"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          143..148
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          159..164
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          170..176
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          179..184
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          197..208
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          212..219
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          226..234
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            241..244
FT                   /evidence="ECO:0007829|PDB:4A5W"
FT   STRAND          246..254
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          262..273
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          281..283
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          289..293
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          296..301
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           303..307
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          314..318
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          322..331
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            332..334
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          337..347
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          353..356
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          361..363
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          365..367
FT                   /evidence="ECO:0007829|PDB:3CU7"
FT   STRAND          369..376
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          378..380
FT                   /evidence="ECO:0007829|PDB:4A5W"
FT   STRAND          387..396
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          401..403
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          407..410
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            413..415
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          416..422
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          428..437
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           444..446
FT                   /evidence="ECO:0007829|PDB:6RPT"
FT   STRAND          449..456
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          464..468
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          472..476
FT                   /evidence="ECO:0007829|PDB:3CU7"
FT   STRAND          480..492
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           493..495
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          498..505
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          508..516
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          519..522
FT                   /evidence="ECO:0007829|PDB:3CU7"
FT   STRAND          524..529
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           532..534
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          536..546
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          548..550
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          553..563
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          571..577
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          580..582
FT                   /evidence="ECO:0007829|PDB:3CU7"
FT   STRAND          587..606
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           607..610
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           614..616
FT                   /evidence="ECO:0007829|PDB:4A5W"
FT   HELIX           623..627
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           628..630
FT                   /evidence="ECO:0007829|PDB:4A5W"
FT   STRAND          635..637
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           642..648
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          651..657
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            663..666
FT                   /evidence="ECO:0007829|PDB:5HCD"
FT   HELIX           678..687
FT                   /evidence="ECO:0007829|PDB:4UU9"
FT   TURN            689..692
FT                   /evidence="ECO:0007829|PDB:3HQB"
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   STRAND          764..767
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          777..789
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          795..805
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          808..811
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          815..819
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          822..828
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          838..847
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          849..851
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          853..859
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          863..869
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          874..877
FT                   /evidence="ECO:0007829|PDB:4A5W"
FT   STRAND          886..888
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          892..902
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          906..916
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          919..930
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          932..945
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          949..952
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          956..959
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          974..982
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           985..992
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          993..996
FT                   /evidence="ECO:0007829|PDB:3CU7"
FT   TURN            999..1002
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1008..1013
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1016..1027
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1031..1033
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1034..1036
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1038..1054
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1055..1059
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1066..1069
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1076..1089
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            1090..1092
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1097..1110
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1121..1123
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1133..1154
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1155..1158
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1162..1178
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1185..1196
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1203..1214
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1217..1219
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            1220..1223
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1224..1227
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   TURN            1233..1235
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1245..1260
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1264..1277
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1280..1282
FT                   /evidence="ECO:0007829|PDB:3CU7"
FT   HELIX           1287..1303
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1310..1317
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1324..1332
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1338..1340
FT                   /evidence="ECO:0007829|PDB:4A5W"
FT   STRAND          1342..1344
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1346..1350
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1357..1368
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1371..1373
FT                   /evidence="ECO:0007829|PDB:3CU7"
FT   STRAND          1376..1384
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1401..1408
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1420..1427
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1432..1434
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   HELIX           1436..1443
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1451..1456
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1459..1465
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1469..1471
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1473..1483
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1485..1487
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1491..1497
FT                   /evidence="ECO:0007829|PDB:5HCC"
FT   STRAND          1500..1509
FT                   /evidence="ECO:0007829|PDB:5HCC"
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          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   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
//
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