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UniProtKB/Swiss-Prot entry Q9SE35

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SIL1_CYLFU
Primary accession number Q9SE35
Secondary accession numbers None
Integrated into Swiss-Prot on February 16, 2004
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 39)
Name and origin of the protein
Protein name Silaffin-1 [Precursor]
Synonym natSil-1
Contains Silaffin-1B
Silaffin-1A2
Silaffin-1A1
Gene name
Name: SIL1
From
Cylindrotheca fusiformis (Marine diatom) [TaxID: 2853] 
Taxonomy Eukaryota; stramenopiles; Bacillariophyta; Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae; Cylindrotheca.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 108-120; 141-151 AND 163-173, FUNCTION, METHYLATION AT LYS-144 AND LYS-166, AND METHYLAMINOPROPYLATION AT LYS-143 AND LYS-165.
DOI=10.1126/science.286.5442.1129; PubMed=10550045 [NCBI, ExPASy, EBI, Israel, Japan]
Kroeger N., Deutzmann R., Sumper M.;
"Polycationic peptides from diatom biosilica that direct silica nanosphere formation.";
Science 286:1129-1132(1999).
[2]
 PROTEIN SEQUENCE OF 141-158 AND 163-177, MASS SPECTROMETRY, METHYLATION AT LYS-111; LYS-144; LYS-155; LYS-166; LYS-185; LYS-204; LYS-223 AND LYS-242, METHYLAMINOPROPYLATION AT LYS-110; LYS-143; LYS-154; LYS-165; LYS-177; LYS-184; LYS-196; LYS-203; LYS-215; LYS-222; LYS-234; LYS-241 AND LYS-253, AND METHYLHYDROXYLATION AT LYS-174; LYS-193; LYS-212; LYS-231 AND LYS-250.
DOI=10.1074/jbc.M102093200; PubMed=11349130 [NCBI, ExPASy, EBI, Israel, Japan]
Kroeger N., Deutzmann R., Sumper M.;
"Silica-precipitating peptides from diatoms. The chemical structure of silaffin-A from Cylindrotheca fusiformis.";
J. Biol. Chem. 276:26066-26070(2001).
[3]
 FUNCTION.
DOI=10.1073/pnas.260496497; PubMed=11106386 [NCBI, ExPASy, EBI, Israel, Japan]
Kroeger N., Deutzmann R., Bergsdorf C., Sumper M.;
"Species-specific polyamines from diatoms control silica morphology.";
Proc. Natl. Acad. Sci. U.S.A. 97:14133-14138(2000).
[4]
 FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-163; SER-164; SER-167; SER-169; SER-171; SER-173; SER-176; SER-182; SER-183; SER-186; SER-188; SER-190; SER-192; SER-195; SER-201; SER-202; SER-205; SER-207; SER-209; SER-211; SER-214; SER-220; SER-221; SER-224; SER-226; SER-228; SER-230; SER-233; SER-239; SER-240; SER-243; SER-245; SER-247; SER-249 AND SER-252, AND METHYLHYDROXYLATION AT LYS-174; LYS-193; LYS-212; LYS-231 AND LYS-250.
DOI=10.1126/science.1076221; PubMed=12386330 [NCBI, ExPASy, EBI, Israel, Japan]
Kroeger N., Lorenz S., Brunner E., Sumper M.;
"Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis.";
Science 298:584-586(2002).
[5]
 BIOTECHNOLOGICAL RELEVANCE.
DOI=10.1038/35095031; PubMed=11565027 [NCBI, ExPASy, EBI, Israel, Japan]
Brott L.L., Naik R.R., Pikas D.J., Kirkpatrick S.M., Tomlin D.W., Whitlock P.W., Clarson S.J., Stone M.O.;
"Ultrafast holographic nanopatterning of biocatalytically formed silica.";
Nature 413:291-293(2001).
[6]
 BIOTECHNOLOGICAL RELEVANCE.
DOI=10.1038/nbt931; PubMed=14716316 [NCBI, ExPASy, EBI, Israel, Japan]
Luckarift H.R., Spain J.C., Naik R.R., Stone M.O.;
"Enzyme immobilization in a biomimetic silica support.";
Nat. Biotechnol. 22:211-213(2004).
Comments
  • FUNCTION: Catalyzes the polymerization of silica spheres from a silicilic acid solution. It therefore plays a central role in the formation of silica cell wall of diatoms.
  • SUBUNIT: Silaffin-1A peptides form large aggregates via electrostatic interactions due to intermolecular interactions between the negatively charged phosphate groups and the polyamine moities.
  • DOMAIN: It is unknown whether the acidic chain located at the N-terminus is functional or whether it represents a propeptide.
  • PTM: N6-polymethylaminopropylated. Two lysine residues of each peptide bears 6 to 11 repeats of methyl-propylamine, which gives a possible template for nucleation, and may also control the silica colloid size within the silica deposition vesicle (SDV).
  • PTM: Phosphorylated. All serine residues of the Silaffin-1A1 peptide are phosphorylated. Only minor amounts of the Silaffin-1A2 peptide are phosphorylated. Phosphorylation is essential for the activity. It may represent a source of anions required for silica formation of diatoms.
  • MASS SPECTROMETRY: Mass=2485.7; Method=Electrospray; Range=163-177; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=2557.1; Mass_error=71.4; Method=Electrospray; Range=163-177; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=2628.2; Mass_error=71.1; Method=Electrospray; Range=163-177; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=2699.3; Mass_error=71.1; Method=Electrospray; Range=163-177; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=2770.4; Mass_error=71.1; Method=Electrospray; Range=163-177; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=2878.3; Method=Electrospray; Range=141-158; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=2949.4; Mass_error=71.1; Method=Electrospray; Range=141-158; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=3020.8; Mass_error=71.4; Method=Electrospray; Range=141-158; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=3091.8; Mass_error=71; Method=Electrospray; Range=141-158; Source=PubMed:11349130;.
  • MASS SPECTROMETRY: Mass=3162.9; Mass_error=71.1; Method=Electrospray; Range=141-158; Source=PubMed:11349130;.
  • BIOTECHNOLOGY: Due to its ability to synthesize simple silica nanospheres in vitro from silanes at nearly neutral pH and at ambient temperatures and pressures, it is of great interest in nanotechnology. May be of practical use for the fabrication of photonic devices.
  • MISCELLANEOUS: The results of the mass spectrometry differ for the same peptide due to the length of the methyl-propylamine chains that vary from 14 to 18 units for the Silaffin-1A2 peptide (141-158) and from 13 to 17 units for the Silaffin-1A1 peptide (163-177).
  • MISCELLANEOUS: The species-specific pattern of biosilica pattern of diatoms may be generated by polyamines of different chain lengths as well as by a synergistic action of long-chain polyamines and silaffins.
  • WEB RESOURCE: Name=Protein Spotlight; Note=Miniature masonry -Issue 43 of February 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt043.shtml";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF191634; AAF16940.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A59141; A59141.
3D structure databases
ModBase Q9SE35.
Family and domain databases
BLOCKS Q9SE35.
Other
ProtoNet Q9SE35.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Biomineralization; Cleavage on pair of basic residues; Direct protein sequencing; Hydroxylation; Methylation; Phosphoprotein; Repeat; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    19  19     Potential. 
PROPEP   20   107  88     Acidic. PRO_0000032597
PEPTIDE   108   136  29     Silaffin-1B (Probable). PRO_0000032598
PROPEP   137   140  4     Probable. PRO_0000032599
PEPTIDE   141   158  18     Silaffin-1A2. PRO_0000032600
PROPEP   159   162  4     Probable. PRO_0000032601
PEPTIDE   163   177  15     Silaffin-1A1. PRO_0000032602
PROPEP   178   181  4     Probable. PRO_0000032603
PEPTIDE   182   196  15     Silaffin-1A1. PRO_0000032604
PROPEP   197   200  4     Probable. PRO_0000032605
PEPTIDE   201   215  15     Silaffin-1A1. PRO_0000032606
PROPEP   216   219  4     Probable. PRO_0000032607
PEPTIDE   220   234  15     Silaffin-1A1. PRO_0000032608
PROPEP   235   238  4     Probable. PRO_0000032609
PEPTIDE   239   253  15     Silaffin-1A1. PRO_0000032610
PROPEP   254   265  12     Probable. PRO_0000032611
REPEAT   108   140  33     R1; atypical. 
REPEAT   141   162  22     R2; atypical. 
REPEAT   163   181  19     R3. 
REPEAT   182   200  19     R4. 
REPEAT   201   219  19     R5. 
REPEAT   220   238  19     R6. 
REPEAT   239   257  19     R7. 
REGION   108   257  150     7 X 19 AA repeat of S-S-K-K-S-G-S-Y-S-G-S-K-G-S-K-R-R-[IL]-L. 
MOD_RES   110   110        N6-poly(methylaminopropyl)lysine (Probable). 
MOD_RES   111   111        N6,N6-dimethyllysine (Probable). 
MOD_RES   143   143        N6-poly(methylaminopropyl)lysine. 
MOD_RES   144   144        N6,N6-dimethyllysine. 
MOD_RES   154   154        N6-poly(methylaminopropyl)lysine. 
MOD_RES   155   155        N6,N6-dimethyllysine. 
MOD_RES   163   163        Phosphoserine. 
MOD_RES   164   164        Phosphoserine. 
MOD_RES   165   165        N6-poly(methylaminopropyl)lysine. 
MOD_RES   166   166        N6,N6-dimethyllysine. 
MOD_RES   167   167        Phosphoserine. 
MOD_RES   169   169        Phosphoserine. 
MOD_RES   171   171        Phosphoserine. 
MOD_RES   173   173        Phosphoserine. 
MOD_RES   174   174        N6,N6,N6-trimethyl-5-hydroxylysine. 
MOD_RES   176   176        Phosphoserine. 
MOD_RES   177   177        N6-poly(methylaminopropyl)lysine. 
MOD_RES   182   182        Phosphoserine. 
MOD_RES   183   183        Phosphoserine. 
MOD_RES   184   184        N6-poly(methylaminopropyl)lysine. 
MOD_RES   185   185        N6,N6-dimethyllysine. 
MOD_RES   186   186        Phosphoserine. 
MOD_RES   188   188        Phosphoserine. 
MOD_RES   190   190        Phosphoserine. 
MOD_RES   192   192        Phosphoserine. 
MOD_RES   193   193        N6,N6,N6-trimethyl-5-hydroxylysine. 
MOD_RES   195   195        Phosphoserine. 
MOD_RES   196   196        N6-poly(methylaminopropyl)lysine. 
MOD_RES   201   201        Phosphoserine. 
MOD_RES   202   202        Phosphoserine. 
MOD_RES   203   203        N6-poly(methylaminopropyl)lysine. 
MOD_RES   204   204        N6,N6-dimethyllysine. 
MOD_RES   205   205        Phosphoserine. 
MOD_RES   207   207        Phosphoserine. 
MOD_RES   209   209        Phosphoserine. 
MOD_RES   211   211        Phosphoserine. 
MOD_RES   212   212        N6,N6,N6-trimethyl-5-hydroxylysine. 
MOD_RES   214   214        Phosphoserine. 
MOD_RES   215   215        N6-poly(methylaminopropyl)lysine. 
MOD_RES   220   220        Phosphoserine. 
MOD_RES   221   221        Phosphoserine. 
MOD_RES   222   222        N6-poly(methylaminopropyl)lysine. 
MOD_RES   223   223        N6,N6-dimethyllysine. 
MOD_RES   224   224        Phosphoserine. 
MOD_RES   226   226        Phosphoserine. 
MOD_RES   228   228        Phosphoserine. 
MOD_RES   230   230        Phosphoserine. 
MOD_RES   231   231        N6,N6,N6-trimethyl-5-hydroxylysine. 
MOD_RES   233   233        Phosphoserine. 
MOD_RES   234   234        N6-poly(methylaminopropyl)lysine. 
MOD_RES   239   239        Phosphoserine. 
MOD_RES   240   240        Phosphoserine. 
MOD_RES   241   241        N6-poly(methylaminopropyl)lysine. 
MOD_RES   242   242        N6,N6-dimethyllysine. 
MOD_RES   243   243        Phosphoserine. 
MOD_RES   245   245        Phosphoserine. 
MOD_RES   247   247        Phosphoserine. 
MOD_RES   249   249        Phosphoserine. 
MOD_RES   250   250        N6,N6,N6-trimethyl-5-hydroxylysine. 
MOD_RES   252   252        Phosphoserine. 
MOD_RES   253   253        N6-poly(methylaminopropyl)lysine. 
Sequence information
Length: 265 AA [This is the length of the unprocessed precursor] Molecular weight: 27500 Da [This is the MW of the unprocessed precursor] CRC64: E628FAF40E1B051B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKLTAIFPLL FTAVGYCAAQ SIADLAAANL STEDSKSAQL ISADSSDDAS DSSVESVDAA 

        70         80         90        100        110        120 
SSDVSGSSVE SVDVSGSSLE SVDVSGSSLE SVDDSSEDSE EEELRILSSK KSGSYYSYGT 

       130        140        150        160        170        180 
KKSGSYSGYS TKKSASRRIL SSKKSGSYSG YSTKKSGSRR ILSSKKSGSY SGSKGSKRRI 

       190        200        210        220        230        240 
LSSKKSGSYS GSKGSKRRNL SSKKSGSYSG SKGSKRRILS SKKSGSYSGS KGSKRRNLSS 

       250        260 
KKSGSYSGSK GSKRRILSGG LRGSM
Q9SE35 in FASTA format

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