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Q9SE35

- SIL1_CYLFU

UniProt

Q9SE35 - SIL1_CYLFU

Protein

Silaffin-1

Gene

SIL1

Organism
Cylindrotheca fusiformis (Marine diatom)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    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 – 1919Sequence AnalysisAdd
    BLAST
    Propeptidei20 – 10788Acidic1 PublicationPRO_0000032597Add
    BLAST
    Peptidei108 – 13629Silaffin-1BCuratedPRO_0000032598Add
    BLAST
    Propeptidei137 – 1404CuratedPRO_0000032599
    Peptidei141 – 15818Silaffin-1A2PRO_0000032600Add
    BLAST
    Propeptidei159 – 1624CuratedPRO_0000032601
    Peptidei163 – 17715Silaffin-1A1PRO_0000032602Add
    BLAST
    Propeptidei178 – 1814CuratedPRO_0000032603
    Peptidei182 – 19615Silaffin-1A1PRO_0000032604Add
    BLAST
    Propeptidei197 – 2004CuratedPRO_0000032605
    Peptidei201 – 21515Silaffin-1A1PRO_0000032606Add
    BLAST
    Propeptidei216 – 2194CuratedPRO_0000032607
    Peptidei220 – 23415Silaffin-1A1PRO_0000032608Add
    BLAST
    Propeptidei235 – 2384CuratedPRO_0000032609
    Peptidei239 – 25315Silaffin-1A1PRO_0000032610Add
    BLAST
    Propeptidei254 – 26512CuratedPRO_0000032611Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101N6-poly(methylaminopropyl)lysineCurated
    Modified residuei111 – 1111N6,N6-dimethyllysine1 Publication
    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-hydroxylysine2 Publications
    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-hydroxylysine2 Publications
    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-hydroxylysine2 Publications
    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-hydroxylysine2 Publications
    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-hydroxylysine2 Publications
    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; atypicalAdd
    BLAST
    Repeati141 – 16222R2; atypicalAdd
    BLAST
    Repeati163 – 18119R3Add
    BLAST
    Repeati182 – 20019R4Add
    BLAST
    Repeati201 – 21919R5Add
    BLAST
    Repeati220 – 23819R6Add
    BLAST
    Repeati239 – 25719R7Add
    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]-LAdd
    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: October 1, 2014
    This is version 47 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