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Complement component C6

 CO6_HUMAN               Reviewed;         934 AA.
P13671;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 3.
25-OCT-2017, entry version 186.
RecName: Full=Complement component C6;
Flags: Precursor;
Name=C6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-31 AND 633-640.
PubMed=2808363;
Haefliger J.-A., Tschopp J., Vial N., Jenne D.E.;
"Complete primary structure and functional characterization of the
sixth component of the human complement system. Identification of the
C5b-binding domain in complement C6.";
J. Biol. Chem. 264:18041-18051(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-119.
PubMed=2789218;
Discipio R.G., Hugli T.E.;
"The molecular architecture of human complement component C6.";
J. Biol. Chem. 264:16197-16206(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-119.
TISSUE=Blood;
PubMed=8512929; DOI=10.1021/bi00075a012;
Hobart M.J., Fernie B., Discipio R.G.;
"Structure of the human C6 gene.";
Biochemistry 32:6198-6205(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Soejima M., Koda Y.;
"Sequence variation in C6 locus.";
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-119.
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-491, AND VARIANT GLU-119.
PubMed=2468158; DOI=10.1073/pnas.86.8.2799;
Chakravarti D.N., Chakravarti B., Parra C.A., Mueller-Eberhard H.J.;
"Structural homology of complement protein C6 with other channel-
forming proteins of complement.";
Proc. Natl. Acad. Sci. U.S.A. 86:2799-2803(1989).
[8]
DISULFIDE BONDS IN FACTOR I MODULE 1 REGION.
PubMed=9366265; DOI=10.1016/S0167-4838(97)00072-1;
Lengweiler S., Schaller J., DiScipio R.G., Rickli E.E.;
"Elucidation of the disulfide-bonding pattern in the factor I modules
of the sixth component (C6) of human complement.";
Biochim. Biophys. Acta 1342:13-18(1997).
[9]
GLYCOSYLATION AT TRP-29; TRP-32; TRP-90; TRP-568; TRP-571 AND TRP-574.
PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
"The four terminal components of the complement system are C-
mannosylated on multiple tryptophan residues.";
J. Biol. Chem. 274:32786-32794(1999).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-324 AND ASN-855.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 22-934, GLYCOSYLATION AT
TRP-29; TRP-32; THR-38; ASN-324; THR-392; TRP-568 AND TRP-571,
SUBUNIT, AND DISULFIDE BONDS.
PubMed=22267737; DOI=10.1074/jbc.M111.327809;
Aleshin A.E., Schraufstatter I.U., Stec B., Bankston L.A.,
Liddington R.C., DiScipio R.G.;
"Structure of complement C6 suggests a mechanism for initiation and
unidirectional, sequential assembly of membrane attack complex
(MAC).";
J. Biol. Chem. 287:10210-10222(2012).
[13]
VARIANT ALLOTYPE C6 A GLU-119.
PubMed=8101442; DOI=10.1006/bbrc.1993.1841;
Dewald G., Nothen M.M., Cichon S.;
"Polymorphism of human complement component C6: an amino acid
substitution (Glu/Ala) within the second thrombospondin repeat
differentiates between the two common allotypes C6 A and C6 B.";
Biochem. Biophys. Res. Commun. 194:458-464(1993).
[14]
INVOLVEMENT IN COMPLEMENT COMPONENT 6 DEFICIENCY.
PubMed=15565285; DOI=10.1007/s00431-004-1582-y;
Ikinciogullari A., Tekin M., Dogu F., Reisli I., Tanir G., Yi Z.,
Garrison N., Brilliant M.H., Babacan E.;
"Meningococccal meningitis and complement component 6 deficiency
associated with oculocutaneous albinism.";
Eur. J. Pediatr. 164:177-179(2005).
-!- FUNCTION: Constituent of the membrane attack complex (MAC) that
plays a key role in the innate and adaptive immune response by
forming pores in the plasma membrane of target cells.
-!- SUBUNIT: Component of the membrane attack complex (MAC). MAC
assembly is initiated by proteolytic cleavage of C5 into C5a and
C5b. C5b binds sequentially C6, C7, C8 and 12-14 copies of the
pore-forming subunit C9. {ECO:0000269|PubMed:22267737}.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-1753221, EBI-389883;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: All cysteine residues are assumed to be cross-linked to one
another. Individual modules containing an even number of conserved
cysteine residues are supposed to have disulfide linkages only
within the same module.
-!- POLYMORPHISM: The sequence shown is that of allotype C6 B.
-!- DISEASE: Complement component 6 deficiency (C6D) [MIM:612446]: A
rare defect of the complement classical pathway associated with
susceptibility to severe recurrent infections, predominantly by
Neisseria gonorrhoeae or Neisseria meningitidis.
{ECO:0000269|PubMed:15565285}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=C6base; Note=C6 mutation db;
URL="http://structure.bmc.lu.se/idbase/C6base/";
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EMBL; J05064; AAA51860.1; -; mRNA.
EMBL; J05024; AAA59668.1; -; mRNA.
EMBL; X72177; CAA50994.1; -; Genomic_DNA.
EMBL; AB126592; BAD02321.1; -; mRNA.
EMBL; AC008863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC035723; AAH35723.1; -; mRNA.
EMBL; J04506; AAB59433.1; -; mRNA.
CCDS; CCDS3936.1; -.
PIR; A34372; A34372.
RefSeq; NP_000056.2; NM_000065.3.
RefSeq; NP_001108603.2; NM_001115131.2.
UniGene; Hs.481992; -.
PDB; 3T5O; X-ray; 2.87 A; A=22-934.
PDB; 4A5W; X-ray; 3.50 A; B=22-934.
PDB; 4E0S; X-ray; 4.21 A; B=22-934.
PDBsum; 3T5O; -.
PDBsum; 4A5W; -.
PDBsum; 4E0S; -.
ProteinModelPortal; P13671; -.
SMR; P13671; -.
BioGrid; 107190; 8.
IntAct; P13671; 5.
STRING; 9606.ENSP00000263413; -.
TCDB; 1.C.39.3.3; the membrane attack complex/perforin (macpf) family.
iPTMnet; P13671; -.
PhosphoSitePlus; P13671; -.
DMDM; 146345396; -.
EPD; P13671; -.
PaxDb; P13671; -.
PeptideAtlas; P13671; -.
PRIDE; P13671; -.
DNASU; 729; -.
Ensembl; ENST00000263413; ENSP00000263413; ENSG00000039537.
Ensembl; ENST00000337836; ENSP00000338861; ENSG00000039537.
GeneID; 729; -.
KEGG; hsa:729; -.
UCSC; uc003jmk.4; human.
CTD; 729; -.
DisGeNET; 729; -.
EuPathDB; HostDB:ENSG00000039537.13; -.
GeneCards; C6; -.
H-InvDB; HIX0024838; -.
HGNC; HGNC:1339; C6.
HPA; CAB069427; -.
HPA; HPA043823; -.
MalaCards; C6; -.
MIM; 217050; gene.
MIM; 612446; phenotype.
neXtProt; NX_P13671; -.
OpenTargets; ENSG00000039537; -.
Orphanet; 169150; Immunodeficiency due to a late component of complements deficiency.
PharmGKB; PA25921; -.
eggNOG; ENOG410IDXP; Eukaryota.
eggNOG; ENOG410YJ70; LUCA.
GeneTree; ENSGT00550000074478; -.
HOGENOM; HOG000111865; -.
HOVERGEN; HBG005366; -.
InParanoid; P13671; -.
KO; K03995; -.
OMA; CKNKFRC; -.
OrthoDB; EOG091G07LK; -.
PhylomeDB; P13671; -.
TreeFam; TF330498; -.
Reactome; R-HSA-166665; Terminal pathway of complement.
Reactome; R-HSA-977606; Regulation of Complement cascade.
ChiTaRS; C6; human.
GeneWiki; Complement_component_6; -.
GenomeRNAi; 729; -.
PRO; PR:P13671; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000039537; -.
CleanEx; HS_C6; -.
ExpressionAtlas; P13671; baseline and differential.
Genevisible; P13671; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
GO; GO:0006956; P:complement activation; TAS:ProtInc.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0001970; P:positive regulation of activation of membrane attack complex; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00033; CCP; 2.
CDD; cd00112; LDLa; 1.
Gene3D; 2.20.100.10; -; 2.
InterPro; IPR003884; FacI_MAC.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR001862; MAC_perforin.
InterPro; IPR020864; MACPF.
InterPro; IPR020863; MACPF_CS.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF01823; MACPF; 1.
Pfam; PF00084; Sushi; 2.
Pfam; PF00090; TSP_1; 3.
PRINTS; PR00764; COMPLEMENTC9.
SMART; SM00032; CCP; 2.
SMART; SM00057; FIMAC; 2.
SMART; SM00192; LDLa; 1.
SMART; SM00457; MACPF; 1.
SMART; SM00209; TSP1; 3.
SUPFAM; SSF57424; SSF57424; 1.
SUPFAM; SSF57535; SSF57535; 2.
SUPFAM; SSF82895; SSF82895; 3.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS51465; KAZAL_2; 2.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 1.
PROSITE; PS00279; MACPF_1; 1.
PROSITE; PS51412; MACPF_2; 1.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50092; TSP1; 3.
1: Evidence at protein level;
3D-structure; Complement pathway; Complete proteome; Cytolysis;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Glycoprotein; Immunity; Innate immunity; Membrane attack complex;
Polymorphism; Reference proteome; Repeat; Secreted; Signal; Sushi.
SIGNAL 1 21 {ECO:0000269|PubMed:2808363}.
CHAIN 22 934 Complement component C6.
/FTId=PRO_0000023579.
DOMAIN 22 79 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 81 134 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 138 175 LDL-receptor class A.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 176 522 MACPF. {ECO:0000255|PROSITE-
ProRule:PRU00745}.
DOMAIN 523 553 EGF-like.
DOMAIN 565 612 TSP type-1 3. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 642 701 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 702 763 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 780 839 Kazal-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 876 934 Kazal-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
REGION 611 688 CCP 1.
REGION 642 934 C5b-binding domain.
REGION 689 765 CCP 2.
REGION 766 840 Factor I module (FIM) 1.
REGION 858 934 Factor I module (FIM) 2.
CARBOHYD 29 29 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 32 32 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 38 38 O-linked (Fuc...) threonine.
{ECO:0000305|PubMed:22267737}.
CARBOHYD 90 90 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:22267737}.
CARBOHYD 392 392 O-linked (Fuc...) threonine.
{ECO:0000305|PubMed:22267737}.
CARBOHYD 568 568 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 571 571 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 574 574 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 855 855 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 22 61
DISULFID 24 65
DISULFID 35 73
DISULFID 39 78
DISULFID 82 117
DISULFID 93 127
DISULFID 96 133
DISULFID 140 151
DISULFID 146 164
DISULFID 158 173
DISULFID 180 218
DISULFID 399 420
DISULFID 499 623
DISULFID 521 570
DISULFID 523 539
DISULFID 526 541
DISULFID 543 552
DISULFID 577 611
DISULFID 589 601
DISULFID 644 686
DISULFID 672 699
DISULFID 704 746
DISULFID 732 761
DISULFID 773 823
DISULFID 784 801
DISULFID 786 837
DISULFID 793 816
DISULFID 862 873
DISULFID 867 919
DISULFID 880 897
DISULFID 882 932
DISULFID 888 912
VARIANT 119 119 A -> E (in allotype C6 A;
dbSNP:rs1801033).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2468158,
ECO:0000269|PubMed:2789218,
ECO:0000269|PubMed:8101442,
ECO:0000269|PubMed:8512929}.
/FTId=VAR_006056.
VARIANT 397 397 K -> E (in dbSNP:rs6896011).
/FTId=VAR_027647.
VARIANT 470 470 S -> F (in dbSNP:rs10462014).
/FTId=VAR_027648.
CONFLICT 567 567 Q -> H (in Ref. 4; BAD02321).
{ECO:0000305}.
CONFLICT 616 616 M -> I (in Ref. 4; BAD02321).
{ECO:0000305}.
CONFLICT 934 934 A -> T (in Ref. 4; BAD02321).
{ECO:0000305}.
HELIX 24 26 {ECO:0000244|PDB:3T5O}.
STRAND 38 40 {ECO:0000244|PDB:3T5O}.
STRAND 42 48 {ECO:0000244|PDB:3T5O}.
HELIX 54 58 {ECO:0000244|PDB:3T5O}.
HELIX 61 64 {ECO:0000244|PDB:3T5O}.
STRAND 68 73 {ECO:0000244|PDB:3T5O}.
STRAND 95 97 {ECO:0000244|PDB:3T5O}.
STRAND 100 104 {ECO:0000244|PDB:4A5W}.
STRAND 106 108 {ECO:0000244|PDB:3T5O}.
STRAND 121 125 {ECO:0000244|PDB:4A5W}.
STRAND 130 133 {ECO:0000244|PDB:3T5O}.
STRAND 141 145 {ECO:0000244|PDB:3T5O}.
STRAND 151 153 {ECO:0000244|PDB:3T5O}.
HELIX 154 156 {ECO:0000244|PDB:3T5O}.
STRAND 157 161 {ECO:0000244|PDB:3T5O}.
STRAND 164 167 {ECO:0000244|PDB:3T5O}.
HELIX 168 170 {ECO:0000244|PDB:3T5O}.
STRAND 179 182 {ECO:0000244|PDB:3T5O}.
HELIX 190 194 {ECO:0000244|PDB:3T5O}.
STRAND 195 198 {ECO:0000244|PDB:3T5O}.
TURN 199 202 {ECO:0000244|PDB:3T5O}.
STRAND 203 207 {ECO:0000244|PDB:3T5O}.
STRAND 226 228 {ECO:0000244|PDB:3T5O}.
STRAND 236 240 {ECO:0000244|PDB:3T5O}.
HELIX 247 249 {ECO:0000244|PDB:3T5O}.
STRAND 250 256 {ECO:0000244|PDB:3T5O}.
HELIX 258 262 {ECO:0000244|PDB:3T5O}.
STRAND 279 282 {ECO:0000244|PDB:4A5W}.
TURN 287 289 {ECO:0000244|PDB:3T5O}.
HELIX 298 307 {ECO:0000244|PDB:3T5O}.
STRAND 309 327 {ECO:0000244|PDB:3T5O}.
STRAND 329 331 {ECO:0000244|PDB:3T5O}.
HELIX 336 341 {ECO:0000244|PDB:3T5O}.
HELIX 351 361 {ECO:0000244|PDB:3T5O}.
STRAND 363 365 {ECO:0000244|PDB:3T5O}.
STRAND 367 382 {ECO:0000244|PDB:3T5O}.
HELIX 383 389 {ECO:0000244|PDB:3T5O}.
HELIX 393 407 {ECO:0000244|PDB:3T5O}.
HELIX 418 420 {ECO:0000244|PDB:3T5O}.
HELIX 426 429 {ECO:0000244|PDB:3T5O}.
HELIX 434 436 {ECO:0000244|PDB:3T5O}.
STRAND 437 442 {ECO:0000244|PDB:3T5O}.
STRAND 445 447 {ECO:0000244|PDB:3T5O}.
HELIX 449 455 {ECO:0000244|PDB:3T5O}.
STRAND 461 465 {ECO:0000244|PDB:3T5O}.
HELIX 466 478 {ECO:0000244|PDB:3T5O}.
STRAND 481 486 {ECO:0000244|PDB:3T5O}.
STRAND 487 489 {ECO:0000244|PDB:4A5W}.
HELIX 490 493 {ECO:0000244|PDB:3T5O}.
HELIX 500 516 {ECO:0000244|PDB:3T5O}.
HELIX 520 522 {ECO:0000244|PDB:3T5O}.
TURN 527 529 {ECO:0000244|PDB:3T5O}.
STRAND 530 535 {ECO:0000244|PDB:3T5O}.
STRAND 538 542 {ECO:0000244|PDB:3T5O}.
STRAND 547 549 {ECO:0000244|PDB:4A5W}.
HELIX 550 552 {ECO:0000244|PDB:4A5W}.
STRAND 579 586 {ECO:0000244|PDB:3T5O}.
STRAND 595 597 {ECO:0000244|PDB:3T5O}.
STRAND 605 610 {ECO:0000244|PDB:3T5O}.
STRAND 643 645 {ECO:0000244|PDB:4A5W}.
STRAND 653 656 {ECO:0000244|PDB:3T5O}.
STRAND 660 663 {ECO:0000244|PDB:4A5W}.
STRAND 667 672 {ECO:0000244|PDB:3T5O}.
STRAND 676 680 {ECO:0000244|PDB:3T5O}.
STRAND 683 686 {ECO:0000244|PDB:3T5O}.
STRAND 688 692 {ECO:0000244|PDB:4A5W}.
STRAND 698 701 {ECO:0000244|PDB:3T5O}.
STRAND 703 705 {ECO:0000244|PDB:3T5O}.
STRAND 711 714 {ECO:0000244|PDB:3T5O}.
STRAND 715 717 {ECO:0000244|PDB:4A5W}.
STRAND 720 723 {ECO:0000244|PDB:3T5O}.
STRAND 727 729 {ECO:0000244|PDB:3T5O}.
STRAND 734 736 {ECO:0000244|PDB:4A5W}.
STRAND 737 740 {ECO:0000244|PDB:3T5O}.
STRAND 742 745 {ECO:0000244|PDB:3T5O}.
STRAND 747 749 {ECO:0000244|PDB:4A5W}.
STRAND 755 757 {ECO:0000244|PDB:4A5W}.
TURN 772 776 {ECO:0000244|PDB:3T5O}.
STRAND 778 783 {ECO:0000244|PDB:4A5W}.
HELIX 789 792 {ECO:0000244|PDB:3T5O}.
STRAND 798 804 {ECO:0000244|PDB:3T5O}.
TURN 805 808 {ECO:0000244|PDB:3T5O}.
STRAND 809 814 {ECO:0000244|PDB:3T5O}.
HELIX 815 822 {ECO:0000244|PDB:3T5O}.
HELIX 825 827 {ECO:0000244|PDB:3T5O}.
STRAND 829 836 {ECO:0000244|PDB:3T5O}.
HELIX 841 851 {ECO:0000244|PDB:3T5O}.
STRAND 853 857 {ECO:0000244|PDB:4A5W}.
STRAND 862 864 {ECO:0000244|PDB:3T5O}.
STRAND 875 877 {ECO:0000244|PDB:3T5O}.
STRAND 879 881 {ECO:0000244|PDB:3T5O}.
HELIX 885 891 {ECO:0000244|PDB:4A5W}.
STRAND 897 899 {ECO:0000244|PDB:3T5O}.
STRAND 901 903 {ECO:0000244|PDB:3T5O}.
STRAND 905 907 {ECO:0000244|PDB:3T5O}.
HELIX 911 920 {ECO:0000244|PDB:3T5O}.
STRAND 925 930 {ECO:0000244|PDB:3T5O}.
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


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