CO6_HUMAN
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 03-AUG-2022, entry version 212.
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 PDBsum; 3T5O; -.
DR PDBsum; 4A5W; -.
DR PDBsum; 4E0S; -.
DR PDBsum; 6H03; -.
DR PDBsum; 6H04; -.
DR PDBsum; 7NYC; -.
DR PDBsum; 7NYD; -.
DR AlphaFoldDB; P13671; -.
DR SMR; P13671; -.
DR BioGRID; 107190; 11.
DR ComplexPortal; CPX-6159; Membrane attack complex.
DR ComplexPortal; CPX-677; C5b6 complement complex.
DR IntAct; P13671; 10.
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 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; P13671; -.
DR PeptideAtlas; P13671; -.
DR PRIDE; P13671; -.
DR ProteomicsDB; 52956; -.
DR ABCD; P13671; 9 sequenced antibodies.
DR Antibodypedia; 10692; 311 antibodies from 33 providers.
DR DNASU; 729; -.
DR Ensembl; ENST00000263413.7; ENSP00000263413.3; ENSG00000039537.14.
DR Ensembl; ENST00000337836.10; ENSP00000338861.5; ENSG00000039537.14.
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 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; FRPCIPS; -.
DR OrthoDB; 100680at2759; -.
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; 9 hits in 1068 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 105 other tissues.
DR ExpressionAtlas; P13671; baseline and differential.
DR Genevisible; P13671; 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; IBA:GO_Central.
DR GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC: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:0019835; P:cytolysis; 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:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 4.10.400.10; -; 1.
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 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; SSF57424; SSF57424; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR SUPFAM; SSF82895; SSF82895; 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.
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 778..783
FT /evidence="ECO:0007829|PDB:4A5W"
FT HELIX 789..792
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 798..804
FT /evidence="ECO:0007829|PDB:3T5O"
FT TURN 805..808
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 809..814
FT /evidence="ECO:0007829|PDB:3T5O"
FT HELIX 815..822
FT /evidence="ECO:0007829|PDB:3T5O"
FT HELIX 825..827
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 829..836
FT /evidence="ECO:0007829|PDB:3T5O"
FT HELIX 841..851
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 853..857
FT /evidence="ECO:0007829|PDB:4A5W"
FT STRAND 862..864
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 879..881
FT /evidence="ECO:0007829|PDB:3T5O"
FT HELIX 885..891
FT /evidence="ECO:0007829|PDB:4A5W"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 905..907
FT /evidence="ECO:0007829|PDB:3T5O"
FT HELIX 911..920
FT /evidence="ECO:0007829|PDB:3T5O"
FT STRAND 925..930
FT /evidence="ECO:0007829|PDB:3T5O"
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
