ID CO6_HUMAN Reviewed; 934 AA. AC P13671; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 3. DT 27-MAR-2024, entry version 221. DE RecName: Full=Complement component C6; DE Flags: Precursor; GN Name=C6; 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 PROTEIN SEQUENCE OF 22-31 AND 633-640. RX PubMed=2808363; DOI=10.1016/s0021-9258(19)84676-8; RA Haefliger J.-A., Tschopp J., Vial N., Jenne D.E.; RT "Complete primary structure and functional characterization of the sixth RT component of the human complement system. Identification of the C5b-binding RT domain in complement C6."; RL J. Biol. Chem. 264:18041-18051(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-119. RX PubMed=2789218; DOI=10.1016/s0021-9258(18)71607-4; RA Discipio R.G., Hugli T.E.; RT "The molecular architecture of human complement component C6."; RL J. Biol. Chem. 264:16197-16206(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-119. RC TISSUE=Blood; RX PubMed=8512929; DOI=10.1021/bi00075a012; RA Hobart M.J., Fernie B., Discipio R.G.; RT "Structure of the human C6 gene."; RL Biochemistry 32:6198-6205(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Soejima M., Koda Y.; RT "Sequence variation in C6 locus."; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-119. RC TISSUE=Ovary; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-491, AND VARIANT GLU-119. RX PubMed=2468158; DOI=10.1073/pnas.86.8.2799; RA Chakravarti D.N., Chakravarti B., Parra C.A., Mueller-Eberhard H.J.; RT "Structural homology of complement protein C6 with other channel-forming RT proteins of complement."; RL Proc. Natl. Acad. Sci. U.S.A. 86:2799-2803(1989). RN [8] RP DISULFIDE BONDS IN FACTOR I MODULE 1 REGION. RX PubMed=9366265; DOI=10.1016/s0167-4838(97)00072-1; RA Lengweiler S., Schaller J., DiScipio R.G., Rickli E.E.; RT "Elucidation of the disulfide-bonding pattern in the factor I modules of RT the sixth component (C6) of human complement."; RL Biochim. Biophys. Acta 1342:13-18(1997). RN [9] RP GLYCOSYLATION AT TRP-29; TRP-32; TRP-90; TRP-568; TRP-571 AND TRP-574. 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-324 AND ASN-855. 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 [11] 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 [12] RP X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 22-934, GLYCOSYLATION AT TRP-29; RP TRP-32; THR-38; ASN-324; THR-392; TRP-568 AND TRP-571, SUBUNIT, AND RP DISULFIDE BONDS. RX PubMed=22267737; DOI=10.1074/jbc.m111.327809; RA Aleshin A.E., Schraufstatter I.U., Stec B., Bankston L.A., Liddington R.C., RA DiScipio R.G.; RT "Structure of complement C6 suggests a mechanism for initiation and RT unidirectional, sequential assembly of membrane attack complex (MAC)."; RL J. Biol. Chem. 287:10210-10222(2012). RN [13] RP VARIANT ALLOTYPE C6 A GLU-119. RX PubMed=8101442; DOI=10.1006/bbrc.1993.1841; RA Dewald G., Nothen M.M., Cichon S.; RT "Polymorphism of human complement component C6: an amino acid substitution RT (Glu/Ala) within the second thrombospondin repeat differentiates between RT the two common allotypes C6 A and C6 B."; RL Biochem. Biophys. Res. Commun. 194:458-464(1993). RN [14] RP INVOLVEMENT IN COMPLEMENT COMPONENT 6 DEFICIENCY. RX PubMed=15565285; DOI=10.1007/s00431-004-1582-y; RA Ikinciogullari A., Tekin M., Dogu F., Reisli I., Tanir G., Yi Z., RA Garrison N., Brilliant M.H., Babacan E.; RT "Meningococccal meningitis and complement component 6 deficiency associated RT with oculocutaneous albinism."; RL Eur. J. Pediatr. 164:177-179(2005). 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. 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 12-14 copies of the pore-forming subunit CC C9. {ECO:0000269|PubMed:22267737}. CC -!- INTERACTION: CC P13671; P16333: NCK1; NbExp=2; IntAct=EBI-1753221, EBI-389883; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: All cysteine residues are assumed to be cross-linked to one CC another. Individual modules containing an even number of conserved CC cysteine residues are supposed to have disulfide linkages only within CC the same module. CC -!- POLYMORPHISM: The sequence shown is that of allotype C6 B. CC -!- DISEASE: Complement component 6 deficiency (C6D) [MIM:612446]: 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:15565285}. Note=Disease susceptibility is CC associated 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=C6base; Note=C6 mutation db; CC URL="http://structure.bmc.lu.se/idbase/C6base/"; 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; J05064; AAA51860.1; -; mRNA. DR EMBL; J05024; AAA59668.1; -; mRNA. DR EMBL; X72177; CAA50994.1; -; Genomic_DNA. DR EMBL; AB126592; BAD02321.1; -; mRNA. DR EMBL; AC008863; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091871; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC035723; AAH35723.1; -; mRNA. DR EMBL; J04506; AAB59433.1; -; mRNA. DR CCDS; CCDS3936.1; -. DR PIR; A34372; A34372. DR RefSeq; NP_000056.2; NM_000065.3. DR RefSeq; NP_001108603.2; NM_001115131.2. DR PDB; 3T5O; X-ray; 2.87 A; A=22-934. DR PDB; 4A5W; X-ray; 3.50 A; B=22-934. DR PDB; 4E0S; X-ray; 4.21 A; B=22-934. DR PDB; 6H03; EM; 5.60 A; B=22-934. DR PDB; 6H04; EM; 5.60 A; B=22-934. DR PDB; 7NYC; EM; 3.50 A; B=22-934. DR PDB; 7NYD; EM; 3.30 A; B=22-934. DR PDB; 7Q6C; X-ray; 2.29 A; A=769-934. DR PDB; 8B0F; EM; 3.00 A; B=1-934. DR PDB; 8B0G; EM; 3.30 A; B=1-934. DR PDB; 8B0H; EM; 3.30 A; B=1-934. DR PDBsum; 3T5O; -. DR PDBsum; 4A5W; -. DR PDBsum; 4E0S; -. DR PDBsum; 6H03; -. DR PDBsum; 6H04; -. DR PDBsum; 7NYC; -. DR PDBsum; 7NYD; -. DR PDBsum; 7Q6C; -. DR PDBsum; 8B0F; -. DR PDBsum; 8B0G; -. DR PDBsum; 8B0H; -. DR AlphaFoldDB; P13671; -. 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 SMR; P13671; -. DR BioGRID; 107190; 13. DR ComplexPortal; CPX-6159; Membrane attack complex. DR ComplexPortal; CPX-677; C5b6 complement complex. DR IntAct; P13671; 11. DR STRING; 9606.ENSP00000263413; -. DR TCDB; 1.C.39.3.3; the membrane attack complex/perforin (macpf) family. DR CarbonylDB; P13671; -. DR GlyConnect; 791; 7 N-Linked glycans (4 sites). DR GlyCosmos; P13671; 12 sites, 7 glycans. DR GlyGen; P13671; 12 sites, 7 N-linked glycans (4 sites). DR iPTMnet; P13671; -. DR PhosphoSitePlus; P13671; -. DR BioMuta; C6; -. DR DMDM; 146345396; -. DR EPD; P13671; -. DR jPOST; P13671; -. DR MassIVE; P13671; -. DR PaxDb; 9606-ENSP00000263413; -. DR PeptideAtlas; P13671; -. DR ProteomicsDB; 52956; -. DR ABCD; P13671; 9 sequenced antibodies. DR Antibodypedia; 10692; 358 antibodies from 33 providers. DR DNASU; 729; -. DR Ensembl; ENST00000263413.7; ENSP00000263413.3; ENSG00000039537.16. DR Ensembl; ENST00000337836.10; ENSP00000338861.5; ENSG00000039537.16. DR GeneID; 729; -. DR KEGG; hsa:729; -. DR MANE-Select; ENST00000337836.10; ENSP00000338861.5; NM_000065.5; NP_000056.2. DR UCSC; uc003jmk.4; human. DR AGR; HGNC:1339; -. DR CTD; 729; -. DR DisGeNET; 729; -. DR GeneCards; C6; -. DR HGNC; HGNC:1339; C6. DR HPA; ENSG00000039537; Tissue enriched (liver). DR MalaCards; C6; -. DR MIM; 217050; gene. DR MIM; 612446; phenotype. DR neXtProt; NX_P13671; -. DR OpenTargets; ENSG00000039537; -. DR Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency. DR PharmGKB; PA25921; -. DR VEuPathDB; HostDB:ENSG00000039537; -. DR eggNOG; ENOG502QPIM; Eukaryota. DR GeneTree; ENSGT00940000156814; -. DR HOGENOM; CLU_014082_0_0_1; -. DR InParanoid; P13671; -. DR OMA; CWGPWSR; -. DR OrthoDB; 5303272at2759; -. DR PhylomeDB; P13671; -. DR TreeFam; TF330498; -. DR PathwayCommons; P13671; -. DR Reactome; R-HSA-166665; Terminal pathway of complement. DR Reactome; R-HSA-977606; Regulation of Complement cascade. DR SignaLink; P13671; -. DR SIGNOR; P13671; -. DR BioGRID-ORCS; 729; 11 hits in 1152 CRISPR screens. DR ChiTaRS; C6; human. DR GeneWiki; Complement_component_6; -. DR GenomeRNAi; 729; -. DR Pharos; P13671; Tbio. DR PRO; PR:P13671; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P13671; Protein. DR Bgee; ENSG00000039537; Expressed in right lobe of liver and 107 other cell types or tissues. DR ExpressionAtlas; P13671; baseline and differential. 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; IBA:GO_Central. DR GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal. DR GO; GO:0006956; P:complement activation; IDA:ComplexPortal. DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0050778; P:positive regulation of immune response; NAS:ComplexPortal. DR CDD; cd00033; CCP; 2. DR CDD; cd00112; LDLa; 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; 3. DR InterPro; IPR048828; C6_KAZAL. DR InterPro; IPR048831; C8A_B_C6_EGF-like. DR InterPro; IPR003884; FacI_MAC. DR InterPro; IPR002350; Kazal_dom. 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:SF4; COMPLEMENT COMPONENT C6; 1. DR Pfam; PF21288; C6_KAZAL; 1. DR Pfam; PF21195; C8A_B_C6_EGF-like; 1. DR Pfam; PF00057; Ldl_recept_a; 1. DR Pfam; PF01823; MACPF; 1. DR Pfam; PF00084; Sushi; 2. DR Pfam; PF00090; TSP_1; 3. DR PRINTS; PR00764; COMPLEMENTC9. DR SMART; SM00032; CCP; 2. DR SMART; SM00057; FIMAC; 2. DR SMART; SM00192; LDLa; 1. DR SMART; SM00457; MACPF; 1. DR SMART; SM00209; TSP1; 3. DR SUPFAM; SSF57535; Complement control module/SCR domain; 2. DR SUPFAM; SSF57424; LDL receptor-like module; 1. DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS51465; KAZAL_2; 2. 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; 3. DR Genevisible; P13671; HS. PE 1: Evidence at protein level; KW 3D-structure; Complement pathway; Cytolysis; Direct protein sequencing; KW Disulfide bond; EGF-like domain; Glycoprotein; Immunity; Innate immunity; KW Membrane attack complex; Reference proteome; Repeat; Secreted; Signal; KW Sushi. FT SIGNAL 1..21 FT /evidence="ECO:0000269|PubMed:2808363" FT CHAIN 22..934 FT /note="Complement component C6" FT /id="PRO_0000023579" FT DOMAIN 22..79 FT /note="TSP type-1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT DOMAIN 81..134 FT /note="TSP type-1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT DOMAIN 138..175 FT /note="LDL-receptor class A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 176..522 FT /note="MACPF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745" FT DOMAIN 523..553 FT /note="EGF-like" FT DOMAIN 565..612 FT /note="TSP type-1 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT DOMAIN 642..701 FT /note="Sushi 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 702..763 FT /note="Sushi 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 780..839 FT /note="Kazal-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DOMAIN 876..934 FT /note="Kazal-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT REGION 611..688 FT /note="CCP 1" FT REGION 642..934 FT /note="C5b-binding domain" FT REGION 689..765 FT /note="CCP 2" FT REGION 766..840 FT /note="Factor I module (FIM) 1" FT REGION 858..934 FT /note="Factor I module (FIM) 2" FT CARBOHYD 29 FT /note="C-linked (Man) tryptophan" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 32 FT /note="C-linked (Man) tryptophan; partial" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 38 FT /note="O-linked (Fuc...) threonine" FT /evidence="ECO:0000305|PubMed:22267737" FT CARBOHYD 90 FT /note="C-linked (Man) tryptophan; partial" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 324 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:22267737" FT CARBOHYD 392 FT /note="O-linked (Fuc...) threonine" FT /evidence="ECO:0000305|PubMed:22267737" FT CARBOHYD 568 FT /note="C-linked (Man) tryptophan; partial" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 571 FT /note="C-linked (Man) tryptophan; partial" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 574 FT /note="C-linked (Man) tryptophan; partial" FT /evidence="ECO:0000269|PubMed:10551839" FT CARBOHYD 855 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT DISULFID 22..61 FT DISULFID 24..65 FT DISULFID 35..73 FT DISULFID 39..78 FT DISULFID 82..117 FT DISULFID 93..127 FT DISULFID 96..133 FT DISULFID 140..151 FT DISULFID 146..164 FT DISULFID 158..173 FT DISULFID 180..218 FT DISULFID 399..420 FT DISULFID 499..623 FT DISULFID 521..570 FT DISULFID 523..539 FT DISULFID 526..541 FT DISULFID 543..552 FT DISULFID 577..611 FT DISULFID 589..601 FT DISULFID 644..686 FT DISULFID 672..699 FT DISULFID 704..746 FT DISULFID 732..761 FT DISULFID 773..823 FT DISULFID 784..801 FT DISULFID 786..837 FT DISULFID 793..816 FT DISULFID 862..873 FT DISULFID 867..919 FT DISULFID 880..897 FT DISULFID 882..932 FT DISULFID 888..912 FT VARIANT 119 FT /note="A -> E (in allotype C6 A; dbSNP:rs1801033)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:2468158, ECO:0000269|PubMed:2789218, FT ECO:0000269|PubMed:8101442, ECO:0000269|PubMed:8512929" FT /id="VAR_006056" FT VARIANT 397 FT /note="K -> E (in dbSNP:rs6896011)" FT /id="VAR_027647" FT VARIANT 470 FT /note="S -> F (in dbSNP:rs10462014)" FT /id="VAR_027648" FT CONFLICT 567 FT /note="Q -> H (in Ref. 4; BAD02321)" FT /evidence="ECO:0000305" FT CONFLICT 616 FT /note="M -> I (in Ref. 4; BAD02321)" FT /evidence="ECO:0000305" FT CONFLICT 934 FT /note="A -> T (in Ref. 4; BAD02321)" FT /evidence="ECO:0000305" FT HELIX 24..26 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 42..48 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 54..58 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 61..64 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 99..103 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 141..145 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 179..182 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 190..194 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:3T5O" FT TURN 199..202 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 203..207 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:7NYC" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:7NYC" FT STRAND 236..240 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 250..256 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 258..262 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 279..282 FT /evidence="ECO:0007829|PDB:4A5W" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 298..307 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 309..327 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 336..341 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 351..361 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 367..382 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 383..389 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 393..407 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 418..420 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 426..429 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 434..436 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 437..442 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 445..447 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 449..455 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 461..465 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 466..478 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 481..486 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:4A5W" FT HELIX 490..493 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 500..516 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 520..522 FT /evidence="ECO:0007829|PDB:3T5O" FT TURN 527..529 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 530..535 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 538..542 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 547..549 FT /evidence="ECO:0007829|PDB:7NYD" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:4A5W" FT HELIX 559..561 FT /evidence="ECO:0007829|PDB:7NYC" FT STRAND 579..586 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 595..597 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 605..610 FT /evidence="ECO:0007829|PDB:3T5O" FT HELIX 628..630 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 631..633 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 643..645 FT /evidence="ECO:0007829|PDB:4A5W" FT STRAND 653..656 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 660..662 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 667..672 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 676..680 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 683..686 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 688..692 FT /evidence="ECO:0007829|PDB:4A5W" FT STRAND 698..701 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 703..705 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 711..714 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 715..717 FT /evidence="ECO:0007829|PDB:4A5W" FT STRAND 720..723 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 727..729 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 733..735 FT /evidence="ECO:0007829|PDB:7NYD" FT STRAND 737..740 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 742..745 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 747..749 FT /evidence="ECO:0007829|PDB:4A5W" FT STRAND 755..757 FT /evidence="ECO:0007829|PDB:4A5W" FT TURN 772..776 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 777..780 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 783..786 FT /evidence="ECO:0007829|PDB:7Q6C" FT TURN 789..791 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 799..804 FT /evidence="ECO:0007829|PDB:7Q6C" FT TURN 805..808 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 809..814 FT /evidence="ECO:0007829|PDB:7Q6C" FT HELIX 815..823 FT /evidence="ECO:0007829|PDB:7Q6C" FT HELIX 825..827 FT /evidence="ECO:0007829|PDB:3T5O" FT STRAND 829..836 FT /evidence="ECO:0007829|PDB:7Q6C" FT HELIX 841..852 FT /evidence="ECO:0007829|PDB:7Q6C" FT HELIX 853..855 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 860..862 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 865..867 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 871..873 FT /evidence="ECO:0007829|PDB:7Q6C" FT TURN 875..877 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 880..882 FT /evidence="ECO:0007829|PDB:7Q6C" FT HELIX 885..887 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 895..902 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 907..910 FT /evidence="ECO:0007829|PDB:7Q6C" FT HELIX 911..919 FT /evidence="ECO:0007829|PDB:7Q6C" FT STRAND 924..931 FT /evidence="ECO:0007829|PDB:7Q6C" SQ SEQUENCE 934 AA; 104786 MW; A88F4BED7CC349D3 CRC64; MARRSVLYFI LLNALINKGQ ACFCDHYAWT QWTSCSKTCN SGTQSRHRQI VVDKYYQENF CEQICSKQET RECNWQRCPI NCLLGDFGPW SDCDPCIEKQ SKVRSVLRPS QFGGQPCTAP LVAFQPCIPS KLCKIEEADC KNKFRCDSGR CIARKLECNG ENDCGDNSDE RDCGRTKAVC TRKYNPIPSV QLMGNGFHFL AGEPRGEVLD NSFTGGICKT VKSSRTSNPY RVPANLENVG FEVQTAEDDL KTDFYKDLTS LGHNENQQGS FSSQGGSSFS VPIFYSSKRS ENINHNSAFK QAIQASHKKD SSFIRIHKVM KVLNFTTKAK DLHLSDVFLK ALNHLPLEYN SALYSRIFDD FGTHYFTSGS LGGVYDLLYQ FSSEELKNSG LTEEEAKHCV RIETKKRVLF AKKTKVEHRC TTNKLSEKHE GSFIQGAEKS ISLIRGGRSE YGAALAWEKG SSGLEEKTFS EWLESVKENP AVIDFELAPI VDLVRNIPCA VTKRNNLRKA LQEYAAKFDP CQCAPCPNNG RPTLSGTECL CVCQSGTYGE NCEKQSPDYK SNAVDGQWGC WSSWSTCDAT YKRSRTRECN NPAPQRGGKR CEGEKRQEED CTFSIMENNG QPCINDDEEM KEVDLPEIEA DSGCPQPVPP ENGFIRNEKQ LYLVGEDVEI SCLTGFETVG YQYFRCLPDG TWRQGDVECQ RTECIKPVVQ EVLTITPFQR LYRIGESIEL TCPKGFVVAG PSRYTCQGNS WTPPISNSLT CEKDTLTKLK GHCQLGQKQS GSECICMSPE EDCSHHSEDL CVFDTDSNDY FTSPACKFLA EKCLNNQQLH FLHIGSCQDG RQLEWGLERT RLSSNSTKKE SCGYDTCYDW EKCSASTSKC VCLLPPQCFK GGNQLYCVKM GSSTSEKTLN ICEVGTIRCA NRKMEILHPG KCLA //