GenomeNet

Database: UniProt
Entry: P13671
LinkDB: P13671
Original site: P13671 
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   13-FEB-2019, entry version 195.
DE   RecName: Full=Complement component C6;
DE   Flags: Precursor;
GN   Name=C6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-31 AND 633-640.
RX   PubMed=2808363;
RA   Haefliger J.-A., Tschopp J., Vial N., Jenne D.E.;
RT   "Complete primary structure and functional characterization of the
RT   sixth component of the human complement system. Identification of the
RT   C5b-binding 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;
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.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   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
RT   project: 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-
RT   forming 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
RT   of 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-
RT   mannosylated 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.,
RA   Moore R.J., 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 22-934, GLYCOSYLATION AT
RP   TRP-29; TRP-32; THR-38; ASN-324; THR-392; TRP-568 AND TRP-571,
RP   SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=22267737; DOI=10.1074/jbc.M111.327809;
RA   Aleshin A.E., Schraufstatter I.U., Stec B., Bankston L.A.,
RA   Liddington R.C., DiScipio R.G.;
RT   "Structure of complement C6 suggests a mechanism for initiation and
RT   unidirectional, sequential assembly of membrane attack complex
RT   (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
RT   substitution (Glu/Ala) within the second thrombospondin repeat
RT   differentiates between 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
RT   associated with oculocutaneous albinism.";
RL   Eur. J. Pediatr. 164:177-179(2005).
CC   -!- FUNCTION: Constituent of the membrane attack complex (MAC) that
CC       plays a key role in the innate and adaptive immune response by
CC       forming pores in the plasma membrane of target cells.
CC   -!- SUBUNIT: Component of the membrane attack complex (MAC). MAC
CC       assembly is initiated by proteolytic cleavage of C5 into C5a and
CC       C5b. C5b binds sequentially C6, C7, C8 and 12-14 copies of the
CC       pore-forming subunit C9. {ECO:0000269|PubMed:22267737}.
CC   -!- INTERACTION:
CC       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
CC       within the same module.
CC   -!- POLYMORPHISM: The sequence shown is that of allotype C6 B.
CC   -!- DISEASE: Complement component 6 deficiency (C6D) [MIM:612446]: A
CC       rare 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 variations affecting the gene represented in this
CC       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/";
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   UniGene; Hs.481992; -.
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   PDBsum; 3T5O; -.
DR   PDBsum; 4A5W; -.
DR   PDBsum; 4E0S; -.
DR   PDBsum; 6H03; -.
DR   PDBsum; 6H04; -.
DR   ProteinModelPortal; P13671; -.
DR   SMR; P13671; -.
DR   BioGrid; 107190; 8.
DR   IntAct; P13671; 5.
DR   STRING; 9606.ENSP00000263413; -.
DR   TCDB; 1.C.39.3.3; the membrane attack complex/perforin (macpf) family.
DR   CarbonylDB; P13671; -.
DR   GlyConnect; 791; -.
DR   iPTMnet; P13671; -.
DR   PhosphoSitePlus; P13671; -.
DR   BioMuta; C6; -.
DR   DMDM; 146345396; -.
DR   EPD; P13671; -.
DR   jPOST; P13671; -.
DR   PaxDb; P13671; -.
DR   PeptideAtlas; P13671; -.
DR   PRIDE; P13671; -.
DR   ProteomicsDB; 52956; -.
DR   DNASU; 729; -.
DR   Ensembl; ENST00000263413; ENSP00000263413; ENSG00000039537.
DR   Ensembl; ENST00000337836; ENSP00000338861; ENSG00000039537.
DR   GeneID; 729; -.
DR   KEGG; hsa:729; -.
DR   UCSC; uc003jmk.4; human.
DR   CTD; 729; -.
DR   DisGeNET; 729; -.
DR   EuPathDB; HostDB:ENSG00000039537.13; -.
DR   GeneCards; C6; -.
DR   H-InvDB; HIX0024838; -.
DR   HGNC; HGNC:1339; C6.
DR   HPA; CAB069427; -.
DR   HPA; HPA043823; -.
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   eggNOG; ENOG410IDXP; Eukaryota.
DR   eggNOG; ENOG410YJ70; LUCA.
DR   GeneTree; ENSGT00940000156814; -.
DR   HOGENOM; HOG000111865; -.
DR   HOVERGEN; HBG005366; -.
DR   InParanoid; P13671; -.
DR   KO; K03995; -.
DR   OMA; CKNKFRC; -.
DR   OrthoDB; 100680at2759; -.
DR   PhylomeDB; P13671; -.
DR   TreeFam; TF330498; -.
DR   Reactome; R-HSA-166665; Terminal pathway of complement.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   ChiTaRS; C6; human.
DR   GeneWiki; Complement_component_6; -.
DR   GenomeRNAi; 729; -.
DR   PRO; PR:P13671; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000039537; Expressed in 117 organ(s), highest expression level in liver.
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:0005579; C:membrane attack complex; IDA:UniProtKB.
DR   GO; GO:0006956; P:complement activation; TAS:ProtInc.
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:0001970; P:positive regulation of activation of membrane attack complex; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.20.100.10; -; 3.
DR   InterPro; IPR037563; Complement_C6.
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; PTHR19325:SF23; PTHR19325:SF23; 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; 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; Complete proteome; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Immunity; Innate immunity; Membrane attack complex;
KW   Polymorphism; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL        1     21       {ECO:0000269|PubMed:2808363}.
FT   CHAIN        22    934       Complement component C6.
FT                                /FTId=PRO_0000023579.
FT   DOMAIN       22     79       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN       81    134       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      138    175       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      176    522       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      523    553       EGF-like.
FT   DOMAIN      565    612       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      642    701       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      702    763       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      780    839       Kazal-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      876    934       Kazal-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   REGION      611    688       CCP 1.
FT   REGION      642    934       C5b-binding domain.
FT   REGION      689    765       CCP 2.
FT   REGION      766    840       Factor I module (FIM) 1.
FT   REGION      858    934       Factor I module (FIM) 2.
FT   CARBOHYD     29     29       C-linked (Man) tryptophan.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD     32     32       C-linked (Man) tryptophan; partial.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD     38     38       O-linked (Fuc...) threonine.
FT                                {ECO:0000305|PubMed:22267737}.
FT   CARBOHYD     90     90       C-linked (Man) tryptophan; partial.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    324    324       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:22267737}.
FT   CARBOHYD    392    392       O-linked (Fuc...) threonine.
FT                                {ECO:0000305|PubMed:22267737}.
FT   CARBOHYD    568    568       C-linked (Man) tryptophan; partial.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    571    571       C-linked (Man) tryptophan; partial.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    574    574       C-linked (Man) tryptophan; partial.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    855    855       N-linked (GlcNAc...) asparagine.
FT                                {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    119       A -> E (in allotype C6 A;
FT                                dbSNP:rs1801033).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:2468158,
FT                                ECO:0000269|PubMed:2789218,
FT                                ECO:0000269|PubMed:8101442,
FT                                ECO:0000269|PubMed:8512929}.
FT                                /FTId=VAR_006056.
FT   VARIANT     397    397       K -> E (in dbSNP:rs6896011).
FT                                /FTId=VAR_027647.
FT   VARIANT     470    470       S -> F (in dbSNP:rs10462014).
FT                                /FTId=VAR_027648.
FT   CONFLICT    567    567       Q -> H (in Ref. 4; BAD02321).
FT                                {ECO:0000305}.
FT   CONFLICT    616    616       M -> I (in Ref. 4; BAD02321).
FT                                {ECO:0000305}.
FT   CONFLICT    934    934       A -> T (in Ref. 4; BAD02321).
FT                                {ECO:0000305}.
FT   HELIX        24     26       {ECO:0000244|PDB:3T5O}.
FT   STRAND       38     40       {ECO:0000244|PDB:3T5O}.
FT   STRAND       42     48       {ECO:0000244|PDB:3T5O}.
FT   HELIX        54     58       {ECO:0000244|PDB:3T5O}.
FT   HELIX        61     64       {ECO:0000244|PDB:3T5O}.
FT   STRAND       68     73       {ECO:0000244|PDB:3T5O}.
FT   STRAND       95     97       {ECO:0000244|PDB:3T5O}.
FT   STRAND      100    104       {ECO:0000244|PDB:4A5W}.
FT   STRAND      106    108       {ECO:0000244|PDB:3T5O}.
FT   STRAND      121    125       {ECO:0000244|PDB:4A5W}.
FT   STRAND      130    133       {ECO:0000244|PDB:3T5O}.
FT   STRAND      141    145       {ECO:0000244|PDB:3T5O}.
FT   STRAND      151    153       {ECO:0000244|PDB:3T5O}.
FT   HELIX       154    156       {ECO:0000244|PDB:3T5O}.
FT   STRAND      157    161       {ECO:0000244|PDB:3T5O}.
FT   STRAND      164    167       {ECO:0000244|PDB:3T5O}.
FT   HELIX       168    170       {ECO:0000244|PDB:3T5O}.
FT   STRAND      179    182       {ECO:0000244|PDB:3T5O}.
FT   HELIX       190    194       {ECO:0000244|PDB:3T5O}.
FT   STRAND      195    198       {ECO:0000244|PDB:3T5O}.
FT   TURN        199    202       {ECO:0000244|PDB:3T5O}.
FT   STRAND      203    207       {ECO:0000244|PDB:3T5O}.
FT   STRAND      226    228       {ECO:0000244|PDB:3T5O}.
FT   STRAND      236    240       {ECO:0000244|PDB:3T5O}.
FT   HELIX       247    249       {ECO:0000244|PDB:3T5O}.
FT   STRAND      250    256       {ECO:0000244|PDB:3T5O}.
FT   HELIX       258    262       {ECO:0000244|PDB:3T5O}.
FT   STRAND      279    282       {ECO:0000244|PDB:4A5W}.
FT   TURN        287    289       {ECO:0000244|PDB:3T5O}.
FT   HELIX       298    307       {ECO:0000244|PDB:3T5O}.
FT   STRAND      309    327       {ECO:0000244|PDB:3T5O}.
FT   STRAND      329    331       {ECO:0000244|PDB:3T5O}.
FT   HELIX       336    341       {ECO:0000244|PDB:3T5O}.
FT   HELIX       351    361       {ECO:0000244|PDB:3T5O}.
FT   STRAND      363    365       {ECO:0000244|PDB:3T5O}.
FT   STRAND      367    382       {ECO:0000244|PDB:3T5O}.
FT   HELIX       383    389       {ECO:0000244|PDB:3T5O}.
FT   HELIX       393    407       {ECO:0000244|PDB:3T5O}.
FT   HELIX       418    420       {ECO:0000244|PDB:3T5O}.
FT   HELIX       426    429       {ECO:0000244|PDB:3T5O}.
FT   HELIX       434    436       {ECO:0000244|PDB:3T5O}.
FT   STRAND      437    442       {ECO:0000244|PDB:3T5O}.
FT   STRAND      445    447       {ECO:0000244|PDB:3T5O}.
FT   HELIX       449    455       {ECO:0000244|PDB:3T5O}.
FT   STRAND      461    465       {ECO:0000244|PDB:3T5O}.
FT   HELIX       466    478       {ECO:0000244|PDB:3T5O}.
FT   STRAND      481    486       {ECO:0000244|PDB:3T5O}.
FT   STRAND      487    489       {ECO:0000244|PDB:4A5W}.
FT   HELIX       490    493       {ECO:0000244|PDB:3T5O}.
FT   HELIX       500    516       {ECO:0000244|PDB:3T5O}.
FT   HELIX       520    522       {ECO:0000244|PDB:3T5O}.
FT   TURN        527    529       {ECO:0000244|PDB:3T5O}.
FT   STRAND      530    535       {ECO:0000244|PDB:3T5O}.
FT   STRAND      538    542       {ECO:0000244|PDB:3T5O}.
FT   STRAND      547    549       {ECO:0000244|PDB:4A5W}.
FT   HELIX       550    552       {ECO:0000244|PDB:4A5W}.
FT   STRAND      579    586       {ECO:0000244|PDB:3T5O}.
FT   STRAND      595    597       {ECO:0000244|PDB:3T5O}.
FT   STRAND      605    610       {ECO:0000244|PDB:3T5O}.
FT   STRAND      643    645       {ECO:0000244|PDB:4A5W}.
FT   STRAND      653    656       {ECO:0000244|PDB:3T5O}.
FT   STRAND      660    663       {ECO:0000244|PDB:4A5W}.
FT   STRAND      667    672       {ECO:0000244|PDB:3T5O}.
FT   STRAND      676    680       {ECO:0000244|PDB:3T5O}.
FT   STRAND      683    686       {ECO:0000244|PDB:3T5O}.
FT   STRAND      688    692       {ECO:0000244|PDB:4A5W}.
FT   STRAND      698    701       {ECO:0000244|PDB:3T5O}.
FT   STRAND      703    705       {ECO:0000244|PDB:3T5O}.
FT   STRAND      711    714       {ECO:0000244|PDB:3T5O}.
FT   STRAND      715    717       {ECO:0000244|PDB:4A5W}.
FT   STRAND      720    723       {ECO:0000244|PDB:3T5O}.
FT   STRAND      727    729       {ECO:0000244|PDB:3T5O}.
FT   STRAND      734    736       {ECO:0000244|PDB:4A5W}.
FT   STRAND      737    740       {ECO:0000244|PDB:3T5O}.
FT   STRAND      742    745       {ECO:0000244|PDB:3T5O}.
FT   STRAND      747    749       {ECO:0000244|PDB:4A5W}.
FT   STRAND      755    757       {ECO:0000244|PDB:4A5W}.
FT   TURN        772    776       {ECO:0000244|PDB:3T5O}.
FT   STRAND      778    783       {ECO:0000244|PDB:4A5W}.
FT   HELIX       789    792       {ECO:0000244|PDB:3T5O}.
FT   STRAND      798    804       {ECO:0000244|PDB:3T5O}.
FT   TURN        805    808       {ECO:0000244|PDB:3T5O}.
FT   STRAND      809    814       {ECO:0000244|PDB:3T5O}.
FT   HELIX       815    822       {ECO:0000244|PDB:3T5O}.
FT   HELIX       825    827       {ECO:0000244|PDB:3T5O}.
FT   STRAND      829    836       {ECO:0000244|PDB:3T5O}.
FT   HELIX       841    851       {ECO:0000244|PDB:3T5O}.
FT   STRAND      853    857       {ECO:0000244|PDB:4A5W}.
FT   STRAND      862    864       {ECO:0000244|PDB:3T5O}.
FT   STRAND      875    877       {ECO:0000244|PDB:3T5O}.
FT   STRAND      879    881       {ECO:0000244|PDB:3T5O}.
FT   HELIX       885    891       {ECO:0000244|PDB:4A5W}.
FT   STRAND      897    899       {ECO:0000244|PDB:3T5O}.
FT   STRAND      901    903       {ECO:0000244|PDB:3T5O}.
FT   STRAND      905    907       {ECO:0000244|PDB:3T5O}.
FT   HELIX       911    920       {ECO:0000244|PDB:3T5O}.
FT   STRAND      925    930       {ECO:0000244|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
//
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