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Q9SE35

- SIL1_CYLFU

UniProt

Q9SE35 - SIL1_CYLFU

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Protein
Silaffin-1
Gene
SIL1
Organism
Cylindrotheca fusiformis (Marine diatom)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Biomineralization

Names & Taxonomyi

Protein namesi
Recommended name:
Silaffin-1
Alternative name(s):
natSil-1
Cleaved into the following 3 chains:
Gene namesi
Name:SIL1
OrganismiCylindrotheca fusiformis (Marine diatom)
Taxonomic identifieri2853 [NCBI]
Taxonomic lineageiEukaryotaStramenopilesBacillariophytaBacillariophyceaeBacillariophycidaeBacillarialesBacillariaceaeCylindrotheca

Pathology & Biotechi

Biotechnological usei

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.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Propeptidei20 – 10788Acidic
PRO_0000032597Add
BLAST
Peptidei108 – 13629Silaffin-1B Inferred
PRO_0000032598Add
BLAST
Propeptidei137 – 1404 Inferred
PRO_0000032599
Peptidei141 – 15818Silaffin-1A21 Publication
PRO_0000032600Add
BLAST
Propeptidei159 – 1624 Inferred
PRO_0000032601
Peptidei163 – 17715Silaffin-1A1
PRO_0000032602Add
BLAST
Propeptidei178 – 1814 Inferred
PRO_0000032603
Peptidei182 – 19615Silaffin-1A1
PRO_0000032604Add
BLAST
Propeptidei197 – 2004 Inferred
PRO_0000032605
Peptidei201 – 21515Silaffin-1A1
PRO_0000032606Add
BLAST
Propeptidei216 – 2194 Inferred
PRO_0000032607
Peptidei220 – 23415Silaffin-1A1
PRO_0000032608Add
BLAST
Propeptidei235 – 2384 Inferred
PRO_0000032609
Peptidei239 – 25315Silaffin-1A1
PRO_0000032610Add
BLAST
Propeptidei254 – 26512 Inferred
PRO_0000032611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101N6-poly(methylaminopropyl)lysine Inferred
Modified residuei111 – 1111N6,N6-dimethyllysine Inferred
Modified residuei143 – 1431N6-poly(methylaminopropyl)lysine1 Publication
Modified residuei144 – 1441N6,N6-dimethyllysine2 Publications
Modified residuei154 – 1541N6-poly(methylaminopropyl)lysine
Modified residuei155 – 1551N6,N6-dimethyllysine1 Publication
Modified residuei163 – 1631Phosphoserine1 Publication
Modified residuei164 – 1641Phosphoserine1 Publication
Modified residuei165 – 1651N6-poly(methylaminopropyl)lysine1 Publication
Modified residuei166 – 1661N6,N6-dimethyllysine2 Publications
Modified residuei167 – 1671Phosphoserine1 Publication
Modified residuei169 – 1691Phosphoserine1 Publication
Modified residuei171 – 1711Phosphoserine1 Publication
Modified residuei173 – 1731Phosphoserine1 Publication
Modified residuei174 – 1741N6,N6,N6-trimethyl-5-hydroxylysine
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei177 – 1771N6-poly(methylaminopropyl)lysine
Modified residuei182 – 1821Phosphoserine1 Publication
Modified residuei183 – 1831Phosphoserine1 Publication
Modified residuei184 – 1841N6-poly(methylaminopropyl)lysine1 Publication
Modified residuei185 – 1851N6,N6-dimethyllysine2 Publications
Modified residuei186 – 1861Phosphoserine1 Publication
Modified residuei188 – 1881Phosphoserine1 Publication
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei192 – 1921Phosphoserine1 Publication
Modified residuei193 – 1931N6,N6,N6-trimethyl-5-hydroxylysine
Modified residuei195 – 1951Phosphoserine1 Publication
Modified residuei196 – 1961N6-poly(methylaminopropyl)lysine
Modified residuei201 – 2011Phosphoserine1 Publication
Modified residuei202 – 2021Phosphoserine1 Publication
Modified residuei203 – 2031N6-poly(methylaminopropyl)lysine1 Publication
Modified residuei204 – 2041N6,N6-dimethyllysine2 Publications
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei207 – 2071Phosphoserine1 Publication
Modified residuei209 – 2091Phosphoserine1 Publication
Modified residuei211 – 2111Phosphoserine1 Publication
Modified residuei212 – 2121N6,N6,N6-trimethyl-5-hydroxylysine
Modified residuei214 – 2141Phosphoserine1 Publication
Modified residuei215 – 2151N6-poly(methylaminopropyl)lysine
Modified residuei220 – 2201Phosphoserine1 Publication
Modified residuei221 – 2211Phosphoserine1 Publication
Modified residuei222 – 2221N6-poly(methylaminopropyl)lysine1 Publication
Modified residuei223 – 2231N6,N6-dimethyllysine2 Publications
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei226 – 2261Phosphoserine1 Publication
Modified residuei228 – 2281Phosphoserine1 Publication
Modified residuei230 – 2301Phosphoserine1 Publication
Modified residuei231 – 2311N6,N6,N6-trimethyl-5-hydroxylysine
Modified residuei233 – 2331Phosphoserine1 Publication
Modified residuei234 – 2341N6-poly(methylaminopropyl)lysine
Modified residuei239 – 2391Phosphoserine1 Publication
Modified residuei240 – 2401Phosphoserine1 Publication
Modified residuei241 – 2411N6-poly(methylaminopropyl)lysine1 Publication
Modified residuei242 – 2421N6,N6-dimethyllysine2 Publications
Modified residuei243 – 2431Phosphoserine1 Publication
Modified residuei245 – 2451Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei250 – 2501N6,N6,N6-trimethyl-5-hydroxylysine
Modified residuei252 – 2521Phosphoserine1 Publication
Modified residuei253 – 2531N6-poly(methylaminopropyl)lysine

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Hydroxylation, Methylation, Phosphoprotein

Interactioni

Subunit structurei

Silaffin-1A peptides form large aggregates via electrostatic interactions due to intermolecular interactions between the negatively charged phosphate groups and the polyamine moities.1 Publication

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati108 – 14033R1; atypical
Add
BLAST
Repeati141 – 16222R2; atypical
Add
BLAST
Repeati163 – 18119R3
Add
BLAST
Repeati182 – 20019R4
Add
BLAST
Repeati201 – 21919R5
Add
BLAST
Repeati220 – 23819R6
Add
BLAST
Repeati239 – 25719R7
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 2571507 X 19 AA repeat of S-S-K-K-S-G-S-Y-S-G-S-K-G-S-K-R-R-[IL]-L
Add
BLAST

Domaini

It is unknown whether the acidic chain located at the N-terminus is functional or whether it represents a propeptide.

Keywords - Domaini

Repeat, Signal

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SE35-1 [UniParc]FASTAAdd to Basket

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MKLTAIFPLL FTAVGYCAAQ SIADLAAANL STEDSKSAQL ISADSSDDAS    50
DSSVESVDAA SSDVSGSSVE SVDVSGSSLE SVDVSGSSLE SVDDSSEDSE 100
EEELRILSSK KSGSYYSYGT KKSGSYSGYS TKKSASRRIL SSKKSGSYSG 150
YSTKKSGSRR ILSSKKSGSY SGSKGSKRRI LSSKKSGSYS GSKGSKRRNL 200
SSKKSGSYSG SKGSKRRILS SKKSGSYSGS KGSKRRNLSS KKSGSYSGSK 250
GSKRRILSGG LRGSM 265
Length:265
Mass (Da):27,500
Last modified:May 1, 2000 - v1
Checksum:iE628FAF40E1B051B
GO

Mass spectrometryi

Molecular mass is 2485.7 Da from positions 163 - 177. Determined by ESI. 1 Publication
Molecular mass is 2557.1±71.4 Da from positions 163 - 177. Determined by ESI. 1 Publication
Molecular mass is 2628.2±71.1 Da from positions 163 - 177. Determined by ESI. 1 Publication
Molecular mass is 2699.3±71.1 Da from positions 163 - 177. Determined by ESI. 1 Publication
Molecular mass is 2770.4±71.1 Da from positions 163 - 177. Determined by ESI. 1 Publication
Molecular mass is 2878.3 Da from positions 141 - 158. Determined by ESI. 1 Publication
Molecular mass is 2949.4±71.1 Da from positions 141 - 158. Determined by ESI. 1 Publication
Molecular mass is 3020.8±71.4 Da from positions 141 - 158. Determined by ESI. 1 Publication
Molecular mass is 3091.8±71 Da from positions 141 - 158. Determined by ESI. 1 Publication
Molecular mass is 3162.9±71.1 Da from positions 141 - 158. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF191634 Genomic DNA. Translation: AAF16940.1.
PIRiA59141.

Cross-referencesi

Web resourcesi

Protein Spotlight

Miniature masonry - Issue 43 of February 2004

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF191634 Genomic DNA. Translation: AAF16940.1 .
PIRi A59141.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  1. "Polycationic peptides from diatom biosilica that direct silica nanosphere formation."
    Kroeger N., Deutzmann R., Sumper M.
    Science 286:1129-1132(1999) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGICAL RELEVANCE.

Entry informationi

Entry nameiSIL1_CYLFU
AccessioniPrimary (citable) accession number: Q9SE35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

External Data

Dasty 3