Silaffin-1 precursor - Cylindrotheca fusiformis (Marine diatom)

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Q9SE35 (SIL1_CYLFU) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 43. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Silaffin-1

Alternative name(s):
natSil-1

Gene names

Name:

SIL1

Organism

Cylindrotheca fusiformis (Marine diatom)

Taxonomic identifier

2853 [NCBI]

Taxonomic lineage

Eukaryota › stramenopiles › Bacillariophyta › Bacillariophyceae › Bacillariophycidae › Bacillariales › Bacillariaceae › Cylindrotheca

Protein attributes

Sequence length	265 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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. Ref.1 Ref.3 Ref.4
Subunit structure	Silaffin-1A peptides form large aggregates via electrostatic interactions due to intermolecular interactions between the negatively charged phosphate groups and the polyamine moities. Ref.4
Domain	It is unknown whether the acidic chain located at the N-terminus is functional or whether it represents a propeptide.
Post-translational modification	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). 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. Ref.4
Biotechnological use	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. Ref.5 Ref.6
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). 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.
Mass spectrometry	Molecular mass is 2485.7 Da from positions 163 - 177. Determined by ESI. Ref.2 Molecular mass is 2557.1±71.4 Da from positions 163 - 177. Determined by ESI. Ref.2 Molecular mass is 2628.2±71.1 Da from positions 163 - 177. Determined by ESI. Ref.2 Molecular mass is 2699.3±71.1 Da from positions 163 - 177. Determined by ESI. Ref.2 Molecular mass is 2770.4±71.1 Da from positions 163 - 177. Determined by ESI. Ref.2 Molecular mass is 2878.3 Da from positions 141 - 158. Determined by ESI. Ref.2 Molecular mass is 2949.4±71.1 Da from positions 141 - 158. Determined by ESI. Ref.2 Molecular mass is 3020.8±71.4 Da from positions 141 - 158. Determined by ESI. Ref.2 Molecular mass is 3091.8±71 Da from positions 141 - 158. Determined by ESI. Ref.2 Molecular mass is 3162.9±71.1 Da from positions 141 - 158. Determined by ESI. Ref.2

Ontologies

Keywords
Biological process	Biomineralization
Domain	Repeat Signal
PTM	Cleavage on pair of basic residues Hydroxylation Methylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	biomineral tissue development Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Potential

Propeptide

20 – 107

Acidic

PRO_0000032597

Peptide

108 – 136

Silaffin-1B Probable

PRO_0000032598

Propeptide

137 – 140

Probable

PRO_0000032599

Peptide

141 – 158

Silaffin-1A2 Ref.2

PRO_0000032600

Propeptide

159 – 162

Probable

PRO_0000032601

Peptide

163 – 177

Silaffin-1A1

PRO_0000032602

Propeptide

178 – 181

Probable

PRO_0000032603

Peptide

182 – 196

Silaffin-1A1

PRO_0000032604

Propeptide

197 – 200

Probable

PRO_0000032605

Peptide

201 – 215

Silaffin-1A1

PRO_0000032606

Propeptide

216 – 219

Probable

PRO_0000032607

Peptide

220 – 234

Silaffin-1A1

PRO_0000032608

Propeptide

235 – 238

Probable

PRO_0000032609

Peptide

239 – 253

Silaffin-1A1

PRO_0000032610

Propeptide

254 – 265

Probable

PRO_0000032611

Regions

Repeat

108 – 140

R1; atypical

Repeat

141 – 162

R2; atypical

Repeat

Repeat

Repeat

Repeat

Repeat

Region

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

Amino acid modifications

Modified residue

110

N6-poly(methylaminopropyl)lysine Probable

Modified residue

111

N6,N6-dimethyllysine Probable

Modified residue

143

N6-poly(methylaminopropyl)lysine Ref.1

Modified residue

144

N6,N6-dimethyllysine Ref.1 Ref.2

Modified residue

154

N6-poly(methylaminopropyl)lysine

Modified residue

155

N6,N6-dimethyllysine Ref.2

Modified residue

163

Phosphoserine Ref.4

Modified residue

164

Phosphoserine Ref.4

Modified residue

165

N6-poly(methylaminopropyl)lysine Ref.1

Modified residue

166

N6,N6-dimethyllysine Ref.1 Ref.2

Modified residue

167

Phosphoserine Ref.4

Modified residue

169

Phosphoserine Ref.4

Modified residue

171

Phosphoserine Ref.4

Modified residue

173

Phosphoserine Ref.4

Modified residue

174

N6,N6,N6-trimethyl-5-hydroxylysine

Modified residue

176

Phosphoserine Ref.4

Modified residue

177

N6-poly(methylaminopropyl)lysine

Modified residue

182

Phosphoserine Ref.4

Modified residue

183

Phosphoserine Ref.4

Modified residue

184

N6-poly(methylaminopropyl)lysine Ref.1

Modified residue

185

N6,N6-dimethyllysine Ref.1 Ref.2

Modified residue

186

Phosphoserine Ref.4

Modified residue

188

Phosphoserine Ref.4

Modified residue

190

Phosphoserine Ref.4

Modified residue

192

Phosphoserine Ref.4

Modified residue

193

N6,N6,N6-trimethyl-5-hydroxylysine

Modified residue

195

Phosphoserine Ref.4

Modified residue

196

N6-poly(methylaminopropyl)lysine

Modified residue

201

Phosphoserine Ref.4

Modified residue

202

Phosphoserine Ref.4

Modified residue

203

N6-poly(methylaminopropyl)lysine Ref.1

Modified residue

204

N6,N6-dimethyllysine Ref.1 Ref.2

Modified residue

205

Phosphoserine Ref.4

Modified residue

207

Phosphoserine Ref.4

Modified residue

209

Phosphoserine Ref.4

Modified residue

211

Phosphoserine Ref.4

Modified residue

212

N6,N6,N6-trimethyl-5-hydroxylysine

Modified residue

214

Phosphoserine Ref.4

Modified residue

215

N6-poly(methylaminopropyl)lysine

Modified residue

220

Phosphoserine Ref.4

Modified residue

221

Phosphoserine Ref.4

Modified residue

222

N6-poly(methylaminopropyl)lysine Ref.1

Modified residue

223

N6,N6-dimethyllysine Ref.1 Ref.2

Modified residue

224

Phosphoserine Ref.4

Modified residue

226

Phosphoserine Ref.4

Modified residue

228

Phosphoserine Ref.4

Modified residue

230

Phosphoserine Ref.4

Modified residue

231

N6,N6,N6-trimethyl-5-hydroxylysine

Modified residue

233

Phosphoserine Ref.4

Modified residue

234

N6-poly(methylaminopropyl)lysine

Modified residue

239

Phosphoserine Ref.4

Modified residue

240

Phosphoserine Ref.4

Modified residue

241

N6-poly(methylaminopropyl)lysine Ref.1

Modified residue

242

N6,N6-dimethyllysine Ref.1 Ref.2

Modified residue

243

Phosphoserine Ref.4

Modified residue

245

Phosphoserine Ref.4

Modified residue

247

Phosphoserine Ref.4

Modified residue

249

Phosphoserine Ref.4

Modified residue

250

N6,N6,N6-trimethyl-5-hydroxylysine

Modified residue

252

Phosphoserine Ref.4

Modified residue

253

N6-poly(methylaminopropyl)lysine

Sequences

Sequence

Length

Mass (Da)

Tools

Q9SE35 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E628FAF40E1B051B
Show »

FASTA

265

27,500

        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

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References

[1]	"Polycationic peptides from diatom biosilica that direct silica nanosphere formation." Kroeger N., Deutzmann R., Sumper M. Science 286:1129-1132(1999) [PubMed: 10550045] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 108-120; 141-151 AND 163-173, FUNCTION, METHYLATION AT LYS-144 AND LYS-166, METHYLAMINOPROPYLATION AT LYS-143 AND LYS-165.
[2]	"Silica-precipitating peptides from diatoms. The chemical structure of silaffin-A from Cylindrotheca fusiformis." Kroeger N., Deutzmann R., Sumper M. J. Biol. Chem. 276:26066-26070(2001) [PubMed: 11349130] [Abstract] Cited for: 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, METHYLHYDROXYLATION AT LYS-174; LYS-193; LYS-212; LYS-231 AND LYS-250.
[3]	"Species-specific polyamines from diatoms control silica morphology." Kroeger N., Deutzmann R., Bergsdorf C., Sumper M. Proc. Natl. Acad. Sci. U.S.A. 97:14133-14138(2000) [PubMed: 11106386] [Abstract] Cited for: FUNCTION.
[4]	"Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis." Kroeger N., Lorenz S., Brunner E., Sumper M. Science 298:584-586(2002) [PubMed: 12386330] [Abstract] Cited for: 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, METHYLHYDROXYLATION AT LYS-174; LYS-193; LYS-212; LYS-231 AND LYS-250.
[5]	"Ultrafast holographic nanopatterning of biocatalytically formed silica." Brott L.L., Naik R.R., Pikas D.J., Kirkpatrick S.M., Tomlin D.W., Whitlock P.W., Clarson S.J., Stone M.O. Nature 413:291-293(2001) [PubMed: 11565027] [Abstract] Cited for: BIOTECHNOLOGICAL RELEVANCE.
[6]	"Enzyme immobilization in a biomimetic silica support." Luckarift H.R., Spain J.C., Naik R.R., Stone M.O. Nat. Biotechnol. 22:211-213(2004) [PubMed: 14716316] [Abstract] Cited for: BIOTECHNOLOGICAL RELEVANCE.

Web resources

Protein Spotlight

Miniature masonry - Issue 43 of February 2004

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF191634 Genomic DNA. Translation: AAF16940.1.
PIR	A59141.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

SIL1_CYLFU

Accession

Primary (citable) accession number: Q9SE35

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	May 1, 2000
Last modified:	September 21, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 3 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents