Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Silaffin-1

Gene

SIL1

Organism
Cylindrotheca fusiformis (Marine diatom)
Status
Reviewed-Annotation score: 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

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000003259720 – 107Acidic1 PublicationAdd BLAST88
PeptideiPRO_0000032598108 – 136Silaffin-1BCuratedAdd BLAST29
PropeptideiPRO_0000032599137 – 140Curated4
PeptideiPRO_0000032600141 – 158Silaffin-1A2Add BLAST18
PropeptideiPRO_0000032601159 – 162Curated4
PeptideiPRO_0000032602163 – 177Silaffin-1A1Add BLAST15
PropeptideiPRO_0000032603178 – 181Curated4
PeptideiPRO_0000032604182 – 196Silaffin-1A1Add BLAST15
PropeptideiPRO_0000032605197 – 200Curated4
PeptideiPRO_0000032606201 – 215Silaffin-1A1Add BLAST15
PropeptideiPRO_0000032607216 – 219Curated4
PeptideiPRO_0000032608220 – 234Silaffin-1A1Add BLAST15
PropeptideiPRO_0000032609235 – 238Curated4
PeptideiPRO_0000032610239 – 253Silaffin-1A1Add BLAST15
PropeptideiPRO_0000032611254 – 265CuratedAdd BLAST12

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei110N6-poly(methylaminopropyl)lysine1 Publication1
Modified residuei111N6,N6-dimethyllysine1 Publication1
Modified residuei143N6-poly(methylaminopropyl)lysine2 Publications1
Modified residuei144N6,N6-dimethyllysine2 Publications1
Modified residuei154N6-poly(methylaminopropyl)lysine1 Publication1
Modified residuei155N6,N6-dimethyllysine1 Publication1
Modified residuei163Phosphoserine1 Publication1
Modified residuei164Phosphoserine1 Publication1
Modified residuei165N6-poly(methylaminopropyl)lysine2 Publications1
Modified residuei166N6,N6-dimethyllysine2 Publications1
Modified residuei167Phosphoserine1 Publication1
Modified residuei169Phosphoserine1 Publication1
Modified residuei171Phosphoserine1 Publication1
Modified residuei173Phosphoserine1 Publication1
Modified residuei174N6,N6,N6-trimethyl-5-hydroxylysine2 Publications1
Modified residuei176Phosphoserine1 Publication1
Modified residuei177N6-poly(methylaminopropyl)lysine1 Publication1
Modified residuei182Phosphoserine1 Publication1
Modified residuei183Phosphoserine1 Publication1
Modified residuei184N6-poly(methylaminopropyl)lysine2 Publications1
Modified residuei185N6,N6-dimethyllysine2 Publications1
Modified residuei186Phosphoserine1 Publication1
Modified residuei188Phosphoserine1 Publication1
Modified residuei190Phosphoserine1 Publication1
Modified residuei192Phosphoserine1 Publication1
Modified residuei193N6,N6,N6-trimethyl-5-hydroxylysine2 Publications1
Modified residuei195Phosphoserine1 Publication1
Modified residuei196N6-poly(methylaminopropyl)lysine1 Publication1
Modified residuei201Phosphoserine1 Publication1
Modified residuei202Phosphoserine1 Publication1
Modified residuei203N6-poly(methylaminopropyl)lysine2 Publications1
Modified residuei204N6,N6-dimethyllysine2 Publications1
Modified residuei205Phosphoserine1 Publication1
Modified residuei207Phosphoserine1 Publication1
Modified residuei209Phosphoserine1 Publication1
Modified residuei211Phosphoserine1 Publication1
Modified residuei212N6,N6,N6-trimethyl-5-hydroxylysine2 Publications1
Modified residuei214Phosphoserine1 Publication1
Modified residuei215N6-poly(methylaminopropyl)lysine1 Publication1
Modified residuei220Phosphoserine1 Publication1
Modified residuei221Phosphoserine1 Publication1
Modified residuei222N6-poly(methylaminopropyl)lysine2 Publications1
Modified residuei223N6,N6-dimethyllysine2 Publications1
Modified residuei224Phosphoserine1 Publication1
Modified residuei226Phosphoserine1 Publication1
Modified residuei228Phosphoserine1 Publication1
Modified residuei230Phosphoserine1 Publication1
Modified residuei231N6,N6,N6-trimethyl-5-hydroxylysine2 Publications1
Modified residuei233Phosphoserine1 Publication1
Modified residuei234N6-poly(methylaminopropyl)lysine1 Publication1
Modified residuei239Phosphoserine1 Publication1
Modified residuei240Phosphoserine1 Publication1
Modified residuei241N6-poly(methylaminopropyl)lysine2 Publications1
Modified residuei242N6,N6-dimethyllysine2 Publications1
Modified residuei243Phosphoserine1 Publication1
Modified residuei245Phosphoserine1 Publication1
Modified residuei247Phosphoserine1 Publication1
Modified residuei249Phosphoserine1 Publication1
Modified residuei250N6,N6,N6-trimethyl-5-hydroxylysine2 Publications1
Modified residuei252Phosphoserine1 Publication1
Modified residuei253N6-poly(methylaminopropyl)lysine1 Publication1

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

PTM databases

iPTMnetiQ9SE35.

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

Structurei

3D structure databases

ProteinModelPortaliQ9SE35.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati108 – 140R1; atypicalAdd BLAST33
Repeati141 – 162R2; atypicalAdd BLAST22
Repeati163 – 181R3Add BLAST19
Repeati182 – 200R4Add BLAST19
Repeati201 – 219R5Add BLAST19
Repeati220 – 238R6Add BLAST19
Repeati239 – 257R7Add BLAST19

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni108 – 2577 X 19 AA repeat of S-S-K-K-S-G-S-Y-S-G-S-K-G-S-K-R-R-[IL]-LAdd BLAST150

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

« Hide

        10         20         30         40         50
MKLTAIFPLL FTAVGYCAAQ SIADLAAANL STEDSKSAQL ISADSSDDAS
60 70 80 90 100
DSSVESVDAA SSDVSGSSVE SVDVSGSSLE SVDVSGSSLE SVDDSSEDSE
110 120 130 140 150
EEELRILSSK KSGSYYSYGT KKSGSYSGYS TKKSASRRIL SSKKSGSYSG
160 170 180 190 200
YSTKKSGSRR ILSSKKSGSY SGSKGSKRRI LSSKKSGSYS GSKGSKRRNL
210 220 230 240 250
SSKKSGSYSG SKGSKRRILS SKKSGSYSGS KGSKRRNLSS KKSGSYSGSK
260
GSKRRILSGG LRGSM
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF191634 Genomic DNA. Translation: AAF16940.1.
PIRiA59141.

3D structure databases

ProteinModelPortaliQ9SE35.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ9SE35.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

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: November 2, 2016
This is version 50 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.