GenomeNet

Database: UniProt
Entry: P02748
LinkDB: P02748
Original site: P02748 
ID   CO9_HUMAN               Reviewed;         559 AA.
AC   P02748;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   29-SEP-2021, entry version 211.
DE   RecName: Full=Complement component C9;
DE   Contains:
DE     RecName: Full=Complement component C9a;
DE   Contains:
DE     RecName: Full=Complement component C9b;
DE   Flags: Precursor;
GN   Name=C9;
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].
RX   PubMed=4018030; DOI=10.1002/j.1460-2075.1985.tb03639.x;
RA   Stanley K.K., Kocher H.-P., Luzio J.P., Jackson P., Tschopp J.;
RT   "The sequence and topology of human complement component C9.";
RL   EMBO J. 4:375-382(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-559, AND PROTEIN SEQUENCE OF N-TERMINUS.
RX   PubMed=6095282; DOI=10.1073/pnas.81.23.7298;
RA   Discipio R.G., Gehring M.R., Podack E.R., Kan C.C., Hugli T.E., Fey G.H.;
RT   "Nucleotide sequence of cDNA and derived amino acid sequence of human
RT   complement component C9.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:7298-7302(1984).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-159.
RX   PubMed=3219351; DOI=10.1021/bi00417a050;
RA   Marazziti D., Eggertsen G., Fey G.H., Stanley K.K.;
RT   "Relationships between the gene and protein structure in human complement
RT   component C9.";
RL   Biochemistry 27:6529-6534(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-559, VARIANT C9D GLY-119, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9634479; DOI=10.1007/s002510050415;
RA   Witzel-Schloemp K., Hobart M.J., Fernie B.A., Orren A., Wuerzner R.,
RA   Rittner C., Kaufmann T., Schneider P.M.;
RT   "Heterogeneity in the genetic basis of human complement C9 deficiency.";
RL   Immunogenetics 48:144-147(1998).
RN   [6]
RP   PARTIAL PROTEIN SEQUENCE, ELECTRON MICROSCOPY, FUNCTION, SUBCELLULAR
RP   LOCATION, PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION AT ASN-277 AND ASN-415.
RX   PubMed=4055801;
RA   DiScipio R.G., Hugli T.E.;
RT   "The architecture of complement component C9 and poly(C9).";
RL   J. Biol. Chem. 260:14802-14809(1985).
RN   [7]
RP   DISULFIDE BONDS, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=8603752; DOI=10.1016/0014-5793(95)01541-8;
RA   Lengweiler S., Schaller J., Rickli E.E.;
RT   "Identification of disulfide bonds in the ninth component (C9) of human
RT   complement.";
RL   FEBS Lett. 380:8-12(1996).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9212048; DOI=10.1203/00006450-199707000-00021;
RA   Lassiter H.A., Walz B.M., Wilson J.L., Jung E., Calisi C.R.,
RA   Goldsmith L.J., Wilson R.A., Morgan B.P., Feldhoff R.C.;
RT   "The administration of complement component C9 enhances the survival of
RT   neonatal rats with Escherichia coli sepsis.";
RL   Pediatr. Res. 42:128-136(1997).
RN   [9]
RP   GLYCOSYLATION AT TRP-48 AND TRP-51.
RX   PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
RA   Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
RT   "The four terminal components of the complement system are C-mannosylated
RT   on multiple tryptophan residues.";
RL   J. Biol. Chem. 274:32786-32794(1999).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
RC   TISSUE=Platelet;
RX   PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA   Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT   "Elucidation of N-glycosylation sites on human platelet proteins: a
RT   glycoproteomic approach.";
RL   Mol. Cell. Proteomics 5:226-233(2006).
RN   [13]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [14]
RP   GLYCOSYLATION AT ASN-415.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
RP   3D-STRUCTURE MODELING OF MEMBRANE-SPANNING DOMAIN (MSB).
RX   PubMed=2395434; DOI=10.1016/0161-5890(90)90001-g;
RA   Peitsch M.C., Amiguet P., Guy R., Brunner J., Maizel J.V. Jr., Tschopp J.;
RT   "Localization and molecular modelling of the membrane-inserted domain of
RT   the ninth component of human complement and perforin.";
RL   Mol. Immunol. 27:589-602(1990).
RN   [17]
RP   ELECTRON MICROSCOPY, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=22832194; DOI=10.1016/j.celrep.2012.02.003;
RA   Hadders M.A., Bubeck D., Roversi P., Hakobyan S., Forneris F., Morgan B.P.,
RA   Pangburn M.K., Llorca O., Lea S.M., Gros P.;
RT   "Assembly and regulation of the membrane attack complex based on structures
RT   of C5b6 and sC5b9.";
RL   Cell Rep. 1:200-207(2012).
RN   [18]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.70 ANGSTROMS) OF 39-544, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=26841934; DOI=10.1038/ncomms10588;
RA   Dudkina N.V., Spicer B.A., Reboul C.F., Conroy P.J., Lukoyanova N.,
RA   Elmlund H., Law R.H., Ekkel S.M., Kondos S.C., Goode R.J., Ramm G.,
RA   Whisstock J.C., Saibil H.R., Dunstone M.A.;
RT   "Structure of the poly-C9 component of the complement membrane attack
RT   complex.";
RL   Nat. Commun. 7:10588-10588(2016).
RN   [19] {ECO:0007744|PDB:6DLW}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 22-559, FUNCTION,
RP   SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF PHE-283
RP   AND VAL-426.
RX   PubMed=30111885; DOI=10.1038/s41467-018-05717-0;
RA   Spicer B.A., Law R.H.P., Caradoc-Davies T.T., Ekkel S.M., Bayly-Jones C.,
RA   Pang S.S., Conroy P.J., Ramm G., Radjainia M., Venugopal H.,
RA   Whisstock J.C., Dunstone M.A.;
RT   "The first transmembrane region of complement component-9 acts as a brake
RT   on its self-assembly.";
RL   Nat. Commun. 9:3266-3266(2018).
RN   [20]
RP   VARIANT ARMD15 SER-167.
RX   PubMed=24036952; DOI=10.1038/ng.2741;
RA   Seddon J.M., Yu Y., Miller E.C., Reynolds R., Tan P.L., Gowrisankar S.,
RA   Goldstein J.I., Triebwasser M., Anderson H.E., Zerbib J., Kavanagh D.,
RA   Souied E., Katsanis N., Daly M.J., Atkinson J.P., Raychaudhuri S.;
RT   "Rare variants in CFI, C3 and C9 are associated with high risk of advanced
RT   age-related macular degeneration.";
RL   Nat. Genet. 45:1366-1370(2013).
CC   -!- FUNCTION: Constituent of the membrane attack complex (MAC) that plays a
CC       key role in the innate and adaptive immune response by forming pores in
CC       the plasma membrane of target cells (PubMed:9634479, PubMed:9212048,
CC       PubMed:26841934). C9 is the pore-forming subunit of the MAC
CC       (PubMed:4055801, PubMed:26841934, PubMed:30111885).
CC       {ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885,
CC       ECO:0000269|PubMed:4055801, ECO:0000269|PubMed:9212048,
CC       ECO:0000269|PubMed:9634479}.
CC   -!- SUBUNIT: Component of the membrane attack complex (MAC). MAC assembly
CC       is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b binds
CC       sequentially C6, C7, C8 and multiple copies of the pore-forming subunit
CC       C9 (PubMed:22832194). About 20 C9 chains oligomerize to give rise to a
CC       huge beta-barrel that forms a 100 Angstrom diameter pore in target
CC       membranes (PubMed:26841934, PubMed:30111885).
CC       {ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841934,
CC       ECO:0000269|PubMed:30111885}.
CC   -!- INTERACTION:
CC       P02748; P00441: SOD1; NbExp=3; IntAct=EBI-6677628, EBI-990792;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22832194,
CC       ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:8603752,
CC       ECO:0000269|PubMed:9212048, ECO:0000269|PubMed:9634479}. Target cell
CC       membrane {ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885,
CC       ECO:0000269|PubMed:9212048}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:26841934}. Note=Secreted as soluble monomer.
CC       Oligomerizes at target membranes, forming a pre-pore. A conformation
CC       change then leads to the formation of a 100 Angstrom diameter pore.
CC       {ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885,
CC       ECO:0000269|PubMed:4055801, ECO:0000269|PubMed:9634479}.
CC   -!- TISSUE SPECIFICITY: Plasma (at protein level).
CC       {ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841934,
CC       ECO:0000269|PubMed:8603752, ECO:0000269|PubMed:9212048,
CC       ECO:0000269|PubMed:9634479}.
CC   -!- PTM: Thrombin cleaves factor C9 to produce C9a and C9b.
CC       {ECO:0000269|PubMed:4055801}.
CC   -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC   -!- PTM: Initially, positions and connectivity of disulfide bonds were
CC       based on peptide sequencing done for the human protein
CC       (PubMed:8603752). The crystal structures for the human and mouse
CC       proteins corrected the positions and connectivities of the disulfide
CC       bonds (PubMed:30111885). The distance between Cys-57 and Cys-94 in the
CC       monomeric mouse protein precludes formation of a disulfide bond,
CC       contrary to what is seen in the structure of the human polymeric form
CC       of the protein (Probable). {ECO:0000269|PubMed:30111885,
CC       ECO:0000269|PubMed:8603752, ECO:0000305|PubMed:30111885}.
CC   -!- DISEASE: Complement component 9 deficiency (C9D) [MIM:613825]: 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. Some patients may
CC       develop dermatomyositis. {ECO:0000269|PubMed:9634479}. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Macular degeneration, age-related, 15 (ARMD15) [MIM:615591]: A
CC       form of age-related macular degeneration, a multifactorial eye disease
CC       and the most common cause of irreversible vision loss in the developed
CC       world. In most patients, the disease is manifest as ophthalmoscopically
CC       visible yellowish accumulations of protein and lipid that lie beneath
CC       the retinal pigment epithelium and within an elastin-containing
CC       structure known as Bruch membrane. {ECO:0000269|PubMed:24036952}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=C9base; Note=C9 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/C9base/";
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; X02176; CAA26117.1; -; mRNA.
DR   EMBL; BC020721; AAH20721.1; -; mRNA.
DR   EMBL; K02766; AAA51889.1; -; mRNA.
DR   EMBL; J02833; AAA51890.1; -; Genomic_DNA.
DR   EMBL; Y08545; CAA69849.1; -; Genomic_DNA.
DR   EMBL; Y08546; CAA69849.1; JOINED; Genomic_DNA.
DR   EMBL; Y08547; CAA69849.1; JOINED; Genomic_DNA.
DR   EMBL; Y08548; CAA69849.1; JOINED; Genomic_DNA.
DR   EMBL; Y08549; CAA69849.1; JOINED; Genomic_DNA.
DR   EMBL; Y08550; CAA69849.1; JOINED; Genomic_DNA.
DR   EMBL; Y08551; CAA69849.1; JOINED; Genomic_DNA.
DR   EMBL; Y08552; CAA69849.1; JOINED; Genomic_DNA.
DR   EMBL; Y08553; CAA69849.1; JOINED; Genomic_DNA.
DR   EMBL; Y08554; CAA69849.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS3929.1; -.
DR   PIR; A59363; C9HU.
DR   RefSeq; NP_001728.1; NM_001737.4.
DR   PDB; 5FMW; EM; 6.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=39-544.
DR   PDB; 6DLW; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=22-559.
DR   PDB; 6H03; EM; 5.60 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=22-559.
DR   PDB; 6H04; EM; 5.60 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=22-559.
DR   PDBsum; 5FMW; -.
DR   PDBsum; 6DLW; -.
DR   PDBsum; 6H03; -.
DR   PDBsum; 6H04; -.
DR   SMR; P02748; -.
DR   BioGRID; 107196; 7.
DR   ComplexPortal; CPX-6159; Membrane attack complex.
DR   DIP; DIP-1124N; -.
DR   ELM; P02748; -.
DR   IntAct; P02748; 5.
DR   STRING; 9606.ENSP00000263408; -.
DR   BindingDB; P02748; -.
DR   ChEMBL; CHEMBL4295693; -.
DR   DrugBank; DB09130; Copper.
DR   GlyConnect; 1150; 8 N-Linked glycans (2 sites).
DR   GlyGen; P02748; 11 sites, 10 N-linked glycans (2 sites), 4 O-linked glycans (5 sites).
DR   iPTMnet; P02748; -.
DR   PhosphoSitePlus; P02748; -.
DR   BioMuta; C9; -.
DR   DMDM; 1352108; -.
DR   CPTAC; non-CPTAC-1110; -.
DR   CPTAC; non-CPTAC-1111; -.
DR   CPTAC; non-CPTAC-2656; -.
DR   jPOST; P02748; -.
DR   MassIVE; P02748; -.
DR   MaxQB; P02748; -.
DR   PaxDb; P02748; -.
DR   PeptideAtlas; P02748; -.
DR   PRIDE; P02748; -.
DR   ProteomicsDB; 51564; -.
DR   Antibodypedia; 3685; 530 antibodies.
DR   DNASU; 735; -.
DR   Ensembl; ENST00000263408; ENSP00000263408; ENSG00000113600.
DR   GeneID; 735; -.
DR   KEGG; hsa:735; -.
DR   UCSC; uc003jlv.5; human.
DR   CTD; 735; -.
DR   DisGeNET; 735; -.
DR   GeneCards; C9; -.
DR   HGNC; HGNC:1358; C9.
DR   HPA; ENSG00000113600; Tissue enriched (liver).
DR   MalaCards; C9; -.
DR   MIM; 120940; gene.
DR   MIM; 613825; phenotype.
DR   MIM; 615591; phenotype.
DR   neXtProt; NX_P02748; -.
DR   OpenTargets; ENSG00000113600; -.
DR   Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency.
DR   Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
DR   PharmGKB; PA25968; -.
DR   VEuPathDB; HostDB:ENSG00000113600; -.
DR   eggNOG; ENOG502QWHM; Eukaryota.
DR   GeneTree; ENSGT00940000159777; -.
DR   HOGENOM; CLU_032453_2_0_1; -.
DR   InParanoid; P02748; -.
DR   OMA; WASSIND; -.
DR   OrthoDB; 787014at2759; -.
DR   PhylomeDB; P02748; -.
DR   TreeFam; TF330498; -.
DR   PathwayCommons; P02748; -.
DR   Reactome; R-HSA-166665; Terminal pathway of complement.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SIGNOR; P02748; -.
DR   BioGRID-ORCS; 735; 6 hits in 1003 CRISPR screens.
DR   ChiTaRS; C9; human.
DR   GenomeRNAi; 735; -.
DR   Pharos; P02748; Tbio.
DR   PRO; PR:P02748; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P02748; protein.
DR   Bgee; ENSG00000113600; Expressed in liver and 82 other tissues.
DR   Genevisible; P02748; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0001906; P:cell killing; IDA:UniProtKB.
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:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.20.100.10; -; 1.
DR   Gene3D; 4.10.400.10; -; 1.
DR   InterPro; IPR037567; Complement_C9.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001862; MAC_perforin.
DR   InterPro; IPR020864; MACPF.
DR   InterPro; IPR020863; MACPF_CS.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR45742:SF3; PTHR45742:SF3; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00457; MACPF; 1.
DR   SMART; SM00209; TSP1; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   SUPFAM; SSF82895; SSF82895; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS00279; MACPF_1; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
DR   PROSITE; PS50092; TSP1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Age-related macular degeneration;
KW   Complement alternate pathway; Complement pathway; Cytolysis;
KW   Direct protein sequencing; Disease variant; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Immunity; Innate immunity; Membrane;
KW   Membrane attack complex; Phosphoprotein; Reference proteome; Secreted;
KW   Signal; Target cell membrane; Target membrane; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:6095282"
FT   CHAIN           22..559
FT                   /note="Complement component C9"
FT                   /id="PRO_0000023602"
FT   CHAIN           22..265
FT                   /note="Complement component C9a"
FT                   /id="PRO_0000023603"
FT   CHAIN           266..559
FT                   /note="Complement component C9b"
FT                   /id="PRO_0000023604"
FT   TRANSMEM        314..330
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..354
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..95
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          99..136
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          138..509
FT                   /note="MACPF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT   DOMAIN          510..540
FT                   /note="EGF-like"
FT   SITE            265..266
FT                   /note="Cleavage; by thrombin"
FT   CARBOHYD        48
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000269|PubMed:10551839"
FT   CARBOHYD        51
FT                   /note="C-linked (Man) tryptophan; partial"
FT                   /evidence="ECO:0000269|PubMed:10551839"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:4055801"
FT   DISULFID        43..78
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0000269|PubMed:8603752, ECO:0007744|PDB:6DLW"
FT   DISULFID        54..88
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0007744|PDB:6DLW"
FT   DISULFID        57..94
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0007744|PDB:6DLW"
FT   DISULFID        101..112
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0000269|PubMed:8603752, ECO:0007744|PDB:6DLW"
FT   DISULFID        107..125
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0000269|PubMed:8603752, ECO:0007744|PDB:6DLW"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0000269|PubMed:8603752, ECO:0007744|PDB:6DLW"
FT   DISULFID        142..181
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0000269|PubMed:8603752, ECO:0007744|PDB:6DLW"
FT   DISULFID        510..526
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0000269|PubMed:8603752, ECO:0007744|PDB:6DLW"
FT   DISULFID        513..528
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0000269|PubMed:8603752, ECO:0007744|PDB:6DLW"
FT   DISULFID        530..539
FT                   /evidence="ECO:0000269|PubMed:30111885,
FT                   ECO:0000269|PubMed:8603752, ECO:0007744|PDB:6DLW"
FT   VARIANT         5
FT                   /note="R -> W (in dbSNP:rs700233)"
FT                   /id="VAR_022024"
FT   VARIANT         119
FT                   /note="C -> G (in C9D; dbSNP:rs121909593)"
FT                   /evidence="ECO:0000269|PubMed:9634479"
FT                   /id="VAR_012648"
FT   VARIANT         127
FT                   /note="D -> Y (in dbSNP:rs696763)"
FT                   /id="VAR_050481"
FT   VARIANT         167
FT                   /note="P -> S (in ARMD15; dbSNP:rs34882957)"
FT                   /evidence="ECO:0000269|PubMed:24036952"
FT                   /id="VAR_070940"
FT   VARIANT         203
FT                   /note="I -> V (in dbSNP:rs13361416)"
FT                   /id="VAR_027651"
FT   VARIANT         279
FT                   /note="T -> S (in dbSNP:rs34625111)"
FT                   /id="VAR_033802"
FT   VARIANT         427
FT                   /note="S -> T (in dbSNP:rs34421659)"
FT                   /id="VAR_061503"
FT   MUTAGEN         283
FT                   /note="F->C: Creates an artifactual disulfide bond that
FT                   prevents the conformation change required for
FT                   oligomerization and pore formation; when associated with C-
FT                   427."
FT                   /evidence="ECO:0000269|PubMed:30111885"
FT   MUTAGEN         426
FT                   /note="V->C: Creates an artifactual disulfide bond that
FT                   prevents the conformation change required for
FT                   oligomerization and pore formation; when associated with C-
FT                   283."
FT                   /evidence="ECO:0000269|PubMed:30111885"
FT   CONFLICT        43
FT                   /note="C -> R (in Ref. 3; AAA51889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="Missing (in Ref. 3; AAA51889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        417
FT                   /note="T -> P (in Ref. 3; AAA51889)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   559 AA;  63173 MW;  7403F6AD77B3ECE1 CRC64;
     MSACRSFAVA ICILEISILT AQYTTSYDPE LTESSGSASH IDCRMSPWSE WSQCDPCLRQ
     MFRSRSIEVF GQFNGKRCTD AVGDRRQCVP TEPCEDAEDD CGNDFQCSTG RCIKMRLRCN
     GDNDCGDFSD EDDCESEPRP PCRDRVVEES ELARTAGYGI NILGMDPLST PFDNEFYNGL
     CNRDRDGNTL TYYRRPWNVA SLIYETKGEK NFRTEHYEEQ IEAFKSIIQE KTSNFNAAIS
     LKFTPTETNK AEQCCEETAS SISLHGKGSF RFSYSKNETY QLFLSYSSKK EKMFLHVKGE
     IHLGRFVMRN RDVVLTTTFV DDIKALPTTY EKGEYFAFLE TYGTHYSSSG SLGGLYELIY
     VLDKASMKRK GVELKDIKRC LGYHLDVSLA FSEISVGAEF NKDDCVKRGE GRAVNITSEN
     LIDDVVSLIR GGTRKYAFEL KEKLLRGTVI DVTDFVNWAS SINDAPVLIS QKLSPIYNLV
     PVKMKNAHLK KQNLERAIED YINEFSVRKC HTCQNGGTVI LMDGKCLCAC PFKFEGIACE
     ISKQKISEGL PALEFPNEK
//
DBGET integrated database retrieval system