ID CO7_HUMAN Reviewed; 843 AA. AC P10643; A8K2T4; Q6P3T5; Q92489; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 2. DT 02-SEP-2026, entry version 233. DE RecName: Full=Complement component C7 {ECO:0000305}; DE Flags: Precursor; GN Name=C7 {ECO:0000303|PubMed:3335508, ECO:0000312|HGNC:HGNC:1346}; 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], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND VARIANT RP PRO-587. RX PubMed=3335508; DOI=10.1016/s0021-9258(19)57427-0; RA Discipio R.G., Chakravari D.N., Mueller-Eberhard H.J., Fey G.H.; RT "The structure of human complement component C7 and the C5b-7 complex."; RL J. Biol. Chem. 263:549-560(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-222. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=PNS; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-822, AND VARIANT THR-389. RX PubMed=7730625; DOI=10.4049/jimmunol.154.10.5188; RA Hobart M.J., Fernie B.A., DiScipio R.G.; RT "Structure of the human C7 gene and comparison with the C6, C8A, C8B and C9 RT genes."; RL J. Immunol. 154:5188-5194(1995). RN [5] RP GLYCOSYLATION AT TRP-36; TRP-503; TRP-506 AND TRP-509. 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 [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202. 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 [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202 AND ASN-754. 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 [8] RP GLYCOSYLATION AT ASN-754. 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 [9] RP FUNCTION, AND SUBUNIT. 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 [10] RP GLYCOSYLATION AT THR-696, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.m111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of N- and RT O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 11:1-17(2012). RN [11] RP FUNCTION, AND SUBUNIT. RX PubMed=27052168; DOI=10.1016/j.celrep.2016.03.002; RA Sharp T.H., Koster A.J., Gros P.; RT "Heterogeneous MAC initiator and pore structures in a lipid bilayer by RT phase-plate cryo-electron tomography."; RL Cell Rep. 15:1-8(2016). RN [12] RP FUNCTION, AND SUBUNIT. RX PubMed=26841837; DOI=10.1038/ncomms10587; RA Serna M., Giles J.L., Morgan B.P., Bubeck D.; RT "Structural basis of complement membrane attack complex formation."; RL Nat. Commun. 7:10587-10587(2016). RN [13] RP FUNCTION, AND SUBUNIT. RX PubMed=31061395; DOI=10.1038/s41467-019-10058-7; RA Parsons E.S., Stanley G.J., Pyne A.L.B., Hodel A.W., Nievergelt A.P., RA Menny A., Yon A.R., Rowley A., Richter R.P., Fantner G.E., Bubeck D., RA Hoogenboom B.W.; RT "Single-molecule kinetics of pore assembly by the membrane attack RT complex."; RL Nat. Commun. 10:2066-2066(2019). RN [14] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=32569291; DOI=10.1371/journal.ppat.1008606; RA Doorduijn D.J., Bardoel B.W., Heesterbeek D.A.C., Ruyken M., Benn G., RA Parsons E.S., Hoogenboom B.W., Rooijakkers S.H.M.; RT "Bacterial killing by complement requires direct anchoring of membrane RT attack complex precursor C5b-7."; RL PLoS Pathog. 16:e1008606-e1008606(2020). RN [15] RP FUNCTION. RX PubMed=39914456; DOI=10.1038/s41586-025-08713-9; RG Accelerating Medicines Partnership RA/SLE Network; RA Donado C.A., Theisen E., Zhang F., Nathan A., Fairfield M.L., Rupani K.V., RA Jones D., Johannes K.P., Raychaudhuri S., Dwyer D.F., Jonsson A.H., RA Brenner M.B.; RT "Granzyme K activates the entire complement cascade."; RL Nature 0:0-0(2025). RN [16] RP FUNCTION. RX PubMed=39814882; DOI=10.1038/s41586-024-08395-9; RA Lan F., Li J., Miao W., Sun F., Duan S., Song Y., Yao J., Wang X., Wang C., RA Liu X., Wang J., Zhang L., Qi H.; RT "GZMK-expressing CD8+ T cells promote recurrent airway inflammatory RT diseases."; RL Nature 638:490-498(2025). RN [17] {ECO:0007744|PDB:2WCY} RP STRUCTURE BY NMR OF 693-843, AND DISULFIDE BONDS. RX PubMed=19419965; DOI=10.1074/jbc.m901993200; RA Phelan M.M., Thai C.-T., Soares D.C., Ogata R.T., Barlow P.N., Bramham J.; RT "Solution structure of factor I-like modules from complement C7 reveals a RT pair of follistatin domains in compact pseudosymmetric arrangement."; RL J. Biol. Chem. 284:19637-19649(2009). RN [18] {ECO:0007744|PDB:6H03, ECO:0007744|PDB:6H04} RP STRUCTURE BY ELECTRON MICROSCOPY (5.60 ANGSTROMS) OF 23-843 OF MEMBRANE RP ATTACK COMPLEX, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE RP BONDS. RX PubMed=30552328; DOI=10.1038/s41467-018-07653-5; RA Menny A., Serna M., Boyd C.M., Gardner S., Joseph A.P., Morgan B.P., RA Topf M., Brooks N.J., Bubeck D.; RT "CryoEM reveals how the complement membrane attack complex ruptures lipid RT bilayers."; RL Nat. Commun. 9:5316-5316(2018). RN [19] {ECO:0007744|PDB:7NYC, ECO:0007744|PDB:7NYD} RP STRUCTURE BY ELECTRON MICROSCOPY (3.27 ANGSTROMS) OF 23-843 OF MEMBRANE RP ATTACK COMPLEX, AND ACTIVITY REGULATION. RX PubMed=34667172; DOI=10.1038/s41467-021-26366-w; RA Menny A., Lukassen M.V., Couves E.C., Franc V., Heck A.J.R., Bubeck D.; RT "Structural basis of soluble membrane attack complex packaging for RT clearance."; RL Nat. Commun. 12:6086-6086(2021). RN [20] {ECO:0007744|PDB:8B0F, ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) IN COMPLEX WITH THE RP MEMBRANE ATTACK COMPLEX, ACTIVITY REGULATION, AND DISULFIDE BONDS. RX PubMed=36797260; DOI=10.1038/s41467-023-36441-z; RA Couves E.C., Gardner S., Voisin T.B., Bickel J.K., Stansfeld P.J., RA Tate E.W., Bubeck D.; RT "Structural basis for membrane attack complex inhibition by CD59."; RL Nat. Commun. 14:890-890(2023). RN [21] RP VARIANT C7D SER-521. RX PubMed=8871666; DOI=10.4049/jimmunol.157.8.3648; RA Fernie B.A., Wurzner R., Orren A., Morgan B.P., Potter P.C., Platonov A.E., RA Vershinina I.V., Shipulin G.A., Lachmann P.J., Hobart M.J.; RT "Molecular bases of combined subtotal deficiencies of C6 and C7: their RT effects in combination with other C6 and C7 deficiencies."; RL J. Immunol. 157:3648-3657(1996). RN [22] RP VARIANT C7D ARG-379. RX PubMed=9218625; DOI=10.4049/jimmunol.159.2.1019; RA Fernie B.A., Orren A., Sheehan G., Schlesinger M., Hobart M.J.; RT "Molecular bases of C7 deficiency: three different defects."; RL J. Immunol. 159:1019-1026(1997). RN [23] RP VARIANTS C7D GLN-220; GLN-682 AND HIS-687. RX PubMed=9856499; DOI=10.1007/s004390050859; RA Fernie B.A., Hobart M.J.; RT "Complement C7 deficiency: seven further molecular defects and their RT associated marker haplotypes."; RL Hum. Genet. 103:513-519(1998). RN [24] RP VARIANTS THR-389 AND PRO-587, 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). CC -!- FUNCTION: Component of the membrane attack complex (MAC), a CC multiprotein complex activated by the complement cascade, which inserts CC into a target cell membrane and forms a pore, leading to target cell CC membrane rupture and cell lysis (PubMed:22832194, PubMed:26841837, CC PubMed:27052168, PubMed:30552328, PubMed:3335508). The MAC is initiated CC by proteolytic cleavage of C5 into complement C5b in response to the CC classical, alternative, lectin and GZMK complement pathways CC (PubMed:22832194, PubMed:30552328, PubMed:3335508, PubMed:39914456, CC PubMed:39814882). The complement pathways consist in a cascade of CC proteins that leads to phagocytosis and breakdown of pathogens and CC signaling that strengthens the adaptive immune system (PubMed:22832194, CC PubMed:30552328, PubMed:3335508). C7 serves as a membrane anchor CC (PubMed:30552328). During MAC assembly, associates with C5b and C6 to CC form the C5b-7 complex, a key lipophilic precursor of the MAC complex, CC which associates with the outer leaflet and reduces the energy for CC membrane bending (PubMed:30552328, PubMed:32569291). CC {ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841837, CC ECO:0000269|PubMed:27052168, ECO:0000269|PubMed:30552328, CC ECO:0000269|PubMed:32569291, ECO:0000269|PubMed:3335508, CC ECO:0000269|PubMed:39814882, ECO:0000269|PubMed:39914456}. CC -!- ACTIVITY REGULATION: Membrane attack complex (MAC) assembly is CC inhibited by CD59, thereby protecting self-cells from damage during CC complement activation (PubMed:36797260). MAC assembly is also inhibited CC by clusterin (CLU) chaperones that inhibit polymerization of C9 CC (PubMed:34667172). {ECO:0000269|PubMed:34667172, CC ECO:0000269|PubMed:36797260}. CC -!- SUBUNIT: Monomer or dimer; as a C5b-7 complex it can also form CC multimeric rosettes (PubMed:22832194, PubMed:30552328). Component of CC the membrane attack complex (MAC), composed of complement C5b, C6, C7, CC C8A, C8B, C8G and multiple copies of the pore-forming subunit C9 CC (PubMed:22832194, PubMed:26841837, PubMed:27052168, PubMed:30552328, CC PubMed:31061395, PubMed:32569291, PubMed:3335508). CC {ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841837, CC ECO:0000269|PubMed:27052168, ECO:0000269|PubMed:30552328, CC ECO:0000269|PubMed:31061395, ECO:0000269|PubMed:32569291, CC ECO:0000269|PubMed:3335508}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3335508}. Target CC cell membrane {ECO:0000269|PubMed:30552328, CC ECO:0000269|PubMed:31061395, ECO:0000269|PubMed:32569291}. CC Note=Secreted as soluble protein (PubMed:3335508). Inserts into the CC cell membrane of target cells (PubMed:30552328, PubMed:31061395). CC {ECO:0000269|PubMed:30552328, ECO:0000269|PubMed:31061395, CC ECO:0000269|PubMed:3335508}. CC -!- PTM: C-, N- and O-glycosylated. O-glycosylated with core 1 or possibly CC core 8 glycans. {ECO:0000269|PubMed:10551839, CC ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:22171320}. CC -!- DISEASE: Complement component 7 deficiency (C7D) [MIM:610102]: A rare CC defect of the complement classical pathway associated with CC susceptibility to severe recurrent infections, predominantly by CC Neisseria gonorrhoeae or Neisseria meningitidis. CC {ECO:0000269|PubMed:8871666, ECO:0000269|PubMed:9218625, CC ECO:0000269|PubMed:9856499}. Note=Disease susceptibility is associated CC with variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=C7; Note=complement component 7; CC URL="https://databases.lovd.nl/shared/genes/C7"; 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; J03507; AAA51861.1; -; mRNA. DR EMBL; AK290349; BAF83038.1; -; mRNA. DR EMBL; BC063851; AAH63851.1; -; mRNA. DR EMBL; X86328; CAA60121.1; -; Genomic_DNA. DR EMBL; X86329; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86330; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86331; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86332; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86333; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86334; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86335; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86336; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86337; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86338; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86339; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86340; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86341; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86342; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86343; CAA60121.1; JOINED; Genomic_DNA. DR EMBL; X86344; CAA60121.1; JOINED; Genomic_DNA. DR CCDS; CCDS47201.1; -. DR PIR; A27340; A27340. DR RefSeq; NP_000578.2; NM_000587.4. DR PDB; 2WCY; NMR; -; A=693-843. DR PDB; 6H03; EM; 5.60 A; D=23-843. DR PDB; 6H04; EM; 5.60 A; D=23-843. DR PDB; 7NYC; EM; 3.50 A; C=23-843. DR PDB; 7NYD; EM; 3.30 A; C=23-843. DR PDB; 8B0F; EM; 3.00 A; C=1-843. DR PDB; 8B0G; EM; 3.30 A; C=1-843. DR PDB; 8B0H; EM; 3.30 A; C=1-843. DR AlphaFoldDB; P10643; -. DR BMRB; P10643; -. DR EMDB; EMD-0106; -. DR EMDB; EMD-0107; -. DR EMDB; EMD-12649; -. DR EMDB; EMD-12650; -. DR EMDB; EMD-12651; -. DR EMDB; EMD-15779; -. DR EMDB; EMD-15780; -. DR EMDB; EMD-15781; -. DR EMDB; EMD-3289; -. DR SMR; P10643; -. DR BioGRID; 107191; 9. DR ComplexPortal; CPX-6159; Membrane attack complex. DR FunCoup; P10643; 110. DR IntAct; P10643; 9. DR MINT; P10643; -. DR NDEx; IQUERY-CP-C7; 9 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000322061; -. DR GlyConnect; P10643; 5 N-Linked glycans (2 sites), 1 O-Linked glycan (1 site). DR GlyCosmos; P10643; 7 sites, 5 glycans. DR GlyGen; P10643; 8 sites, 1 C-linked glycan (4 sites), 33 N-linked glycans (2 sites), 3 O-linked glycans (2 sites). DR iPTMnet; P10643; -. DR PhosphoSitePlus; P10643; -. DR SwissPalm; P10643; -. DR BioMuta; C7; -. DR DMDM; 61252057; -. DR CPTAC; non-CPTAC-2655; -. DR jPOST; P10643; -. DR MassIVE; P10643; -. DR PaxDb; 9606-ENSP00000322061; -. DR PeptideAtlas; P10643; -. DR ProteomicsDB; 52633; -. DR Antibodypedia; 709; 334 antibodies from 38 providers. DR DNASU; 730; -. DR Ensembl; ENST00000313164.10; ENSP00000322061.9; ENSG00000112936.22. DR Ensembl; ENST00000696333.1; ENSP00000512566.1; ENSG00000112936.22. DR GeneID; 730; -. DR KEGG; hsa:730; -. DR MANE-Select; ENST00000313164.10; ENSP00000322061.9; NM_000587.4; NP_000578.2. DR UCSC; uc003jmh.5; human. DR AGR; HGNC:1346; -. DR ClinPGx; PA25941; -. DR CTD; 730; -. DR DisGeNET; 730; -. DR GeneCards; C7; -. DR HGNC; HGNC:1346; C7. DR HPA; ENSG00000112936; Tissue enhanced (adrenal). DR MalaCards; C7; -. DR MIM; 217070; gene. DR MIM; 610102; phenotype. DR OpenTargets; ENSG00000112936; -. DR Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency. DR VEuPathDB; HostDB:ENSG00000112936; -. DR eggNOG; ENOG502QU3G; Eukaryota. DR GeneTree; ENSGT00940000156804; -. DR HOGENOM; CLU_014082_0_0_1; -. DR InParanoid; P10643; -. DR OMA; CQNGGQP; -. DR OrthoDB; 504708at2759; -. DR PAN-GO; P10643; 3 GO annotations based on evolutionary models. DR PhylomeDB; P10643; -. DR PathwayCommons; P10643; -. DR Reactome; R-HSA-166665; Terminal pathway of complement. DR Reactome; R-HSA-977606; Regulation of Complement cascade. DR SignaLink; P10643; -. DR SIGNOR; P10643; -. DR Agora; ENSG00000112936; -. DR BioGRID-ORCS; 730; 13 hits in 1149 CRISPR screens. DR ChiTaRS; C7; human. DR EvolutionaryTrace; P10643; -. DR GenomeRNAi; 730; -. DR Pharos; P10643; Tbio. DR PRO; PR:P10643; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P10643; protein. DR Bgee; ENSG00000112936; Expressed in right ovary and 168 other cell types or tissues. DR ExpressionAtlas; P10643; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; EXP:UniProtKB. DR GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB. DR GO; GO:0044218; C:other organism cell membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal. DR GO; GO:0006956; P:complement activation; IDA:UniProtKB. DR GO; GO:0160257; P:complement activation, GZMK pathway; IDA:UniProtKB. DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProt. DR GO; GO:0050778; P:positive regulation of immune response; NAS:ComplexPortal. DR GO; GO:0055085; P:transmembrane transport; IEA:GOC. DR CDD; cd00033; CCP; 2. DR CDD; cd00112; LDLa; 1. DR FunFam; 2.10.70.10:FF:000075; Complement component C7; 1. DR FunFam; 2.10.70.10:FF:000077; Complement component C7; 1. DR FunFam; 3.30.60.30:FF:000053; Complement component C7; 1. DR FunFam; 3.30.60.30:FF:000095; Complement component C7; 1. DR FunFam; 4.10.400.10:FF:000099; Complement component C7; 1. DR FunFam; 2.20.100.10:FF:000002; Unc-5 netrin receptor C; 1. DR Gene3D; 3.30.60.30; -; 2. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2. DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1. DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2. DR InterPro; IPR048827; C7_FIM2_N. DR InterPro; IPR048825; C7_KAZAL. DR InterPro; IPR003884; FacI_MAC. DR InterPro; IPR040729; Kazal_3. 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; IPR035976; Sushi/SCR/CCP_sf. DR InterPro; IPR000436; Sushi_SCR_CCP_dom. DR InterPro; IPR000884; TSP1_rpt. DR InterPro; IPR036383; TSP1_rpt_sf. DR PANTHER; PTHR45742; COMPLEMENT COMPONENT C6; 1. DR PANTHER; PTHR45742:SF2; COMPLEMENT COMPONENT C7; 1. DR Pfam; PF21284; C7_FIM2_N; 1. DR Pfam; PF18434; Kazal_3; 1. DR Pfam; PF21330; Kazal_C7; 1. DR Pfam; PF00057; Ldl_recept_a; 1. DR Pfam; PF01823; MACPF; 1. DR Pfam; PF00084; Sushi; 2. DR Pfam; PF00090; TSP_1; 2. DR PRINTS; PR00764; COMPLEMENTC9. DR PRINTS; PR01705; TSP1REPEAT. DR SMART; SM00032; CCP; 2. DR SMART; SM00057; FIMAC; 2. DR SMART; SM00192; LDLa; 1. DR SMART; SM00457; MACPF; 1. DR SMART; SM00209; TSP1; 2. DR SUPFAM; SSF57535; Complement control module/SCR domain; 2. DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2. 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; PS50923; SUSHI; 2. DR PROSITE; PS50092; TSP1; 2. DR PDBsum; 2WCY; -. DR PDBsum; 6H03; -. DR PDBsum; 6H04; -. DR PDBsum; 7NYC; -. DR PDBsum; 7NYD; -. DR PDBsum; 8B0F; -. DR PDBsum; 8B0G; -. DR PDBsum; 8B0H; -. PE 1: Evidence at protein level; KW 3D-structure; 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; Proteomics identification; Reference proteome; KW Repeat; Secreted; Signal; Sushi; Target cell membrane; Target membrane. FT SIGNAL 1..22 FT /evidence="ECO:0000305|PubMed:3335508" FT CHAIN 23..843 FT /note="Complement component C7" FT /id="PRO_0000023583" FT DOMAIN 27..80 FT /note="TSP type-1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT DOMAIN 83..121 FT /note="LDL-receptor class A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 124..456 FT /note="MACPF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745" FT DOMAIN 457..487 FT /note="EGF-like" FT DOMAIN 500..549 FT /note="TSP type-1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT DOMAIN 569..628 FT /note="Sushi 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 629..690 FT /note="Sushi 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT REGION 108..143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 219..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 516..538 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 545..615 FT /note="CCP 1" FT REGION 616..693 FT /note="CCP 2" FT REGION 695..770 FT /note="Factor I module (FIM) 1" FT REGION 771..843 FT /note="Factor I module (FIM) 2" FT COMPBIAS 108..120 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..132 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 225..234 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 36 FT /note="C-linked (Man) tryptophan" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 202 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952" FT CARBOHYD 503 FT /note="C-linked (Man) tryptophan; partial" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 506 FT /note="C-linked (Man) tryptophan; partial" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 509 FT /note="C-linked (Man) tryptophan; partial" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 696 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:22171320" FT CARBOHYD 754 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490" FT DISULFID 28..63 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 39..73 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 42..79 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 85..96 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 91..109 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 103..119 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 128..165 FT /evidence="ECO:0000269|PubMed:36797260, FT ECO:0007744|PDB:8B0F, ECO:0007744|PDB:8B0G, FT ECO:0007744|PDB:8B0H" FT DISULFID 337..353 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0000269|PubMed:30552328, ECO:0000269|PubMed:36797260, FT ECO:0007744|PDB:2WCY, ECO:0007744|PDB:6H04, FT ECO:0007744|PDB:8B0F, ECO:0007744|PDB:8B0G, FT ECO:0007744|PDB:8B0H" FT DISULFID 433..560 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:7NYC, FT ECO:0007744|PDB:7NYD, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 455..505 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 457..473 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:8B0F, ECO:0007744|PDB:8B0G, FT ECO:0007744|PDB:8B0H" FT DISULFID 460..475 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 477..486 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 512..545 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 523..535 FT /evidence="ECO:0000269|PubMed:36797260, FT ECO:0007744|PDB:7NYC, ECO:0007744|PDB:7NYD, FT ECO:0007744|PDB:8B0F, ECO:0007744|PDB:8B0G, FT ECO:0007744|PDB:8B0H" FT DISULFID 571..613 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 599..626 FT /evidence="ECO:0000269|PubMed:36797260, FT ECO:0007744|PDB:7NYC, ECO:0007744|PDB:7NYD, FT ECO:0007744|PDB:8B0F, ECO:0007744|PDB:8B0G, FT ECO:0007744|PDB:8B0H" FT DISULFID 631..673 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:6H04, ECO:0007744|PDB:8B0F, FT ECO:0007744|PDB:8B0G, ECO:0007744|PDB:8B0H" FT DISULFID 659..688 FT /evidence="ECO:0000269|PubMed:30552328, FT ECO:0000269|PubMed:36797260, ECO:0007744|PDB:6H03, FT ECO:0007744|PDB:8B0F, ECO:0007744|PDB:8B0G, FT ECO:0007744|PDB:8B0H" FT DISULFID 702..713 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT DISULFID 715..750 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT DISULFID 721..743 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT DISULFID 728..763 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT DISULFID 773..782 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT DISULFID 776..789 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT DISULFID 791..825 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT DISULFID 797..818 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT DISULFID 805..838 FT /evidence="ECO:0000269|PubMed:19419965, FT ECO:0007744|PDB:2WCY" FT VARIANT 128 FT /note="C -> R (in dbSNP:rs2271708)" FT /id="VAR_050480" FT VARIANT 220 FT /note="R -> Q (in C7D; dbSNP:rs369349760)" FT /evidence="ECO:0000269|PubMed:9856499" FT /id="VAR_012643" FT VARIANT 222 FT /note="R -> H (in dbSNP:rs75345202)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_081726" FT VARIANT 379 FT /note="G -> R (in C7D; dbSNP:rs121964921)" FT /evidence="ECO:0000269|PubMed:9218625" FT /id="VAR_012644" FT VARIANT 389 FT /note="S -> T (confirmed at protein level; FT dbSNP:rs1063499)" FT /evidence="ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:7730625" FT /id="VAR_033798" FT VARIANT 420 FT /note="K -> Q (in dbSNP:rs3792646)" FT /id="VAR_022023" FT VARIANT 521 FT /note="R -> S (in C7D; dbSNP:rs121964920)" FT /evidence="ECO:0000269|PubMed:8871666" FT /id="VAR_012645" FT VARIANT 587 FT /note="T -> P (confirmed at protein level; FT dbSNP:rs13157656)" FT /evidence="ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:3335508" FT /id="VAR_033799" FT VARIANT 682 FT /note="E -> Q (in C7D; dbSNP:rs541873000)" FT /evidence="ECO:0000269|PubMed:9856499" FT /id="VAR_012646" FT VARIANT 687 FT /note="R -> H (in C7D; dbSNP:rs113187203)" FT /evidence="ECO:0000269|PubMed:9856499" FT /id="VAR_012647" FT CONFLICT 18 FT /note="S -> G (in Ref. 2; BAF83038)" FT /evidence="ECO:0000305" FT CONFLICT 123 FT /note="E -> G (in Ref. 2; BAF83038)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="R -> V (in Ref. 4; CAA60121)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="S -> P (in Ref. 2; BAF83038)" FT /evidence="ECO:0000305" FT CONFLICT 821..822 FT /note="GA -> AL (in Ref. 4; CAA60121)" FT /evidence="ECO:0000305" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:8B0F" FT TURN 41..43 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 44..54 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 67..72 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:8B0F" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:8B0F" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 137..141 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:8B0F" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 151..154 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:8B0F" FT TURN 171..174 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 184..187 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 191..263 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:8B0F" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 274..282 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 289..299 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 301..342 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 344..346 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 348..380 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 382..389 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 400..409 FT /evidence="ECO:0007829|PDB:8B0F" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 415..423 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 424..427 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 434..451 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 454..456 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 458..460 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 465..469 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 472..476 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 481..483 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 503..510 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 513..515 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 516..520 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 532..534 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 539..544 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 548..556 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 558..560 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 574..576 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 580..582 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 594..599 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 603..607 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 610..613 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 617..621 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 624..631 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 632..634 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 641..644 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 647..649 FT /evidence="ECO:0007829|PDB:8B0G" FT STRAND 654..658 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 669..675 FT /evidence="ECO:0007829|PDB:8B0F" FT STRAND 678..681 FT /evidence="ECO:0007829|PDB:8B0F" FT HELIX 699..701 FT /evidence="ECO:0007829|PDB:2WCY" FT STRAND 706..709 FT /evidence="ECO:0007829|PDB:2WCY" FT STRAND 712..715 FT /evidence="ECO:0007829|PDB:2WCY" FT TURN 718..723 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 726..730 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 732..735 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 737..741 FT /evidence="ECO:0007829|PDB:7NYD" FT HELIX 742..750 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 755..757 FT /evidence="ECO:0007829|PDB:2WCY" FT STRAND 766..769 FT /evidence="ECO:0007829|PDB:2WCY" FT STRAND 780..782 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 787..791 FT /evidence="ECO:0007829|PDB:7NYD" FT HELIX 794..796 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 803..808 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 811..816 FT /evidence="ECO:0007829|PDB:7NYD" FT HELIX 817..825 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 830..836 FT /evidence="ECO:0007829|PDB:7NYD" SQ SEQUENCE 843 AA; 93518 MW; DBD5D7C92DF71FA5 CRC64; MKVISLFILV GFIGEFQSFS SASSPVNCQW DFYAPWSECN GCTKTQTRRR SVAVYGQYGG QPCVGNAFET QSCEPTRGCP TEEGCGERFR CFSGQCISKS LVCNGDSDCD EDSADEDRCE DSERRPSCDI DKPPPNIELT GNGYNELTGQ FRNRVINTKS FGGQCRKVFS GDGKDFYRLS GNVLSYTFQV KINNDFNYEF YNSTWSYVKH TSTEHTSSSR KRSFFRSSSS SSRSYTSHTN EIHKGKSYQL LVVENTVEVA QFINNNPEFL QLAEPFWKEL SHLPSLYDYS AYRRLIDQYG THYLQSGSLG GEYRVLFYVD SEKLKQNDFN SVEEKKCKSS GWHFVVKFSS HGCKELENAL KAASGTQNNV LRGEPFIRGG GAGFISGLSY LELDNPAGNK RRYSAWAESV TNLPQVIKQK LTPLYELVKE VPCASVKKLY LKWALEEYLD EFDPCHCRPC QNGGLATVEG THCLCHCKPY TFGAACEQGV LVGNQAGGVD GGWSCWSSWS PCVQGKKTRS RECNNPPPSG GGRSCVGETT ESTQCEDEEL EHLRLLEPHC FPLSLVPTEF CPSPPALKDG FVQDEGTMFP VGKNVVYTCN EGYSLIGNPV ARCGEDLRWL VGEMHCQKIA CVLPVLMDGI QSHPQKPFYT VGEKVTVSCS GGMSLEGPSA FLCGSSLKWS PEMKNARCVQ KENPLTQAVP KCQRWEKLQN SRCVCKMPYE CGPSLDVCAQ DERSKRILPL TVCKMHVLHC QGRNYTLTGR DSCTLPASAE KACGACPLWG KCDAESSKCV CREASECEEE GFSICVEVNG KEQTMSECEA GALRCRGQSI SVTSIRPCAA ETQ //